ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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Q9QZU4 | MAVNDCFSLTYPHNPHPGDLIEVFRPCYQHWALYLGDGYVINIAPIDGIRSSFTSAKSVFSTKALVKMQLLKDVVGNDTYRINNKYDTTYPPLPVEEVIQRSEFPIGQEVAYDLLVNNCEHFVTLLRYGEGVSEQANRAIGTIGLVAAGIDIFTFLGLFPKRQRTKY | Function: Exhibits both phospholipase A1/2 and acyltransferase activities (By similarity). Shows phospholipase A1 (PLA1) and A2 (PLA2) activity, catalyzing the calcium-independent release of fatty acids from the sn-1 or sn-2 position of glycerophospholipids . Shows O-acyltransferase activity, catalyzing the transfer of a fatty acyl group from glycerophospholipid to the hydroxyl group of lysophospholipid (By similarity). Shows N-acyltransferase activity, catalyzing the calcium-independent transfer of a fatty acyl group at the sn-1 position of phosphatidylcholine (PC) and other glycerophospholipids to the primary amine of phosphatidylethanolamine (PE), forming N-acylphosphatidylethanolamine (NAPE), which serves as precursor for N-acylethanolamines (NAEs) (By similarity).
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+)
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 18810
Sequence Length: 167
Subcellular Location: Membrane
EC: 2.3.1.-
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D2KX21 | MAVNDCFSLTYPHNPHPGDLIEVFRPCYQHWALYLGDGYVINIAPVDGIPSSFSSAKSVFSTKALVKMQLLKDVVGNDTYRINNKYDTTYPPLPVEEVIQRSEFAIGQEVTYDLLVNNCEHFVTLLRYGEGVSEQANRAIGTIGLVAAGIDIFTFLGLFPKRQGAKS | Function: Exhibits both phospholipase A1/2 and acyltransferase activities (By similarity). Shows phospholipase A1 (PLA1) and A2 (PLA2) activity, catalyzing the calcium-independent release of fatty acids from the sn-1 or sn-2 position of glycerophospholipids (By similarity). Shows O-acyltransferase activity, catalyzing the transfer of a fatty acyl group from glycerophospholipid to the hydroxyl group of lysophospholipid (By similarity).
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+)
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 18521
Sequence Length: 167
Subcellular Location: Membrane
EC: 2.3.1.-
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P53816 | MRAPIPEPKPGDLIEIFRPFYRHWAIYVGDGYVVHLAPPSEVAGAGAASVMSALTDKAIVKKELLYDVAGSDKYQVNNKHDDKYSPLPCSKIIQRAEELVGQEVLYKLTSENCEHFVNELRYGVARSDQVRDVIIAASVAGMGLAAMSLIGVMFSRNKRQKQ | Function: Exhibits both phospholipase A1/2 and acyltransferase activities . Shows phospholipase A1 (PLA1) and A2 (PLA2) activity, catalyzing the calcium-independent release of fatty acids from the sn-1 or sn-2 position of glycerophospholipids . For most substrates, PLA1 activity is much higher than PLA2 activity . Shows O-acyltransferase activity,catalyzing the transfer of a fatty acyl group from glycerophospholipid to the hydroxyl group of lysophospholipid . Shows N-acyltransferase activity, catalyzing the calcium-independent transfer of a fatty acyl group at the sn-1 position of phosphatidylcholine (PC) and other glycerophospholipids to the primary amine of phosphatidylethanolamine (PE), forming N-acylphosphatidylethanolamine (NAPE), which serves as precursor for N-acylethanolamines (NAEs) . Exhibits high N-acyltransferase activity and low phospholipase A1/2 activity . Required for complete organelle rupture and degradation that occur during eye lens terminal differentiation, when fiber cells that compose the lens degrade all membrane-bound organelles in order to provide lens with transparency to allow the passage of light. Organelle membrane degradation is probably catalyzed by the phospholipase activity (By similarity).
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+)
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 17937
Sequence Length: 162
Domain: The C-terminal transmembrane domain is required for the targeting of the protein to damaged organelles.
Subcellular Location: Cell membrane
EC: 2.3.1.-
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Q8R3U1 | MLAPIPEPKPGDLIEIFRPMYRHWAIYVGDGYVIHLAPPSEIAGAGAASIMSALTDKAIVKKELLCHVAGKDKYQVNNKHDEEYTPLPLSKIIQRAERLVGQEVLYRLTSENCEHFVNELRYGVPRSDQVRDAVKAVGIAGVGLAALGLVGVMLSRNKKQKQ | Function: Exhibits both phospholipase A1/2 and acyltransferase activities . Shows phospholipase A1 (PLA1) and A2 (PLA2), catalyzing the calcium-independent release of fatty acids from the sn-1 or sn-2 position of glycerophospholipids . For most substrates, PLA1 activity is much higher than PLA2 activity (By similarity). Shows O-acyltransferase activity, catalyzing the transfer of a fatty acyl group from glycerophospholipid to the hydroxyl group of lysophospholipid (By similarity). Shows N-acyltransferase activity,catalyzing the calcium-independent transfer of a fatty acyl group at the sn-1 position of phosphatidylcholine (PC) and other glycerophospholipids to the primary amine of phosphatidylethanolamine (PE), forming N-acylphosphatidylethanolamine (NAPE), which serves as precursor for N-acylethanolamines (NAEs) . Exhibits high N-acyltransferase activity and low phospholipase A1/2 activity (By similarity). Required for complete organelle rupture and degradation that occur during eye lens terminal differentiation, when fiber cells that compose the lens degrade all membrane-bound organelles in order to provide lens with transparency to allow the passage of light . Organelle membrane degradation is probably catalyzed by the phospholipase activity .
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+)
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 17872
Sequence Length: 162
Domain: The C-terminal transmembrane domain is required for the targeting of the protein to damaged organelles.
Subcellular Location: Cell membrane
EC: 2.3.1.-
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Q9UL19 | MASPHQEPKPGDLIEIFRLGYEHWALYIGDGYVIHLAPPSEYPGAGSSSVFSVLSNSAEVKRERLEDVVGGCCYRVNNSLDHEYQPRPVEVIISSAKEMVGQKMKYSIVSRNCEHFVTQLRYGKSRCKQVEKAKVEVGVATALGILVVAGCSFAIRRYQKKATA | Function: Exhibits both phospholipase A1/2 and acyltransferase activities . Shows phospholipase A1 (PLA1) and A2 (PLA2), catalyzing the calcium-independent release of fatty acids from the sn-1 or sn-2 position of glycerophospholipids . For most substrates, PLA1 activity is much higher than PLA2 activity . Shows O-acyltransferase activity, catalyzing the transfer of a fatty acyl group from glycerophospholipid to the hydroxyl group of lysophospholipid . Shows N-acyltransferase activity, catalyzing the calcium-independent transfer of a fatty acyl group at the sn-1 position of phosphatidylcholine (PC) and other glycerophospholipids to the primary amine of phosphatidylethanolamine (PE), forming N-acylphosphatidylethanolamine (NAPE), which serves as precursor for N-acylethanolamines (NAEs) . Promotes keratinocyte differentiation via activation of TGM1 .
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+)
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 18179
Sequence Length: 164
Subcellular Location: Membrane
EC: 2.3.1.-
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Q96KN8 | MGLSPGAEGEYALRLPRIPPPLPKPASRTASTGPKDQPPALRRSAVPHSGLNSISPLELEESVGFAALVQLPAKQPPPGTLEQGRSIQQGEKAVVSLETTPSQKADWSSIPKPENEGKLIKQAAEGKPRPRPGDLIEIFRIGYEHWAIYVEDDCVVHLAPPSEEFEVGSITSIFSNRAVVKYSRLEDVLHGCSWKVNNKLDGTYLPLPVDKIIQRTKKMVNKIVQYSLIEGNCEHFVNGLRYGVPRSQQVEHALMEGAKAAGAVISAVVDSIKPKPITA | Function: Exhibits both phospholipase A1/2 and acyltransferase activities . Shows phospholipase A1 (PLA1) and A2 (PLA2) activity, catalyzing the calcium-independent release of fatty acids from the sn-1 or sn-2 position of glycerophospholipids . Shows N-acyltransferase activity, catalyzing the calcium-independent transfer of a fatty acyl group at the sn-1 position of phosphatidylcholine (PC) and other glycerophospholipids to the primary amine of phosphatidylethanolamine (PE), forming N-acylphosphatidylethanolamine (NAPE), which serves as precursor for N-acylethanolamines (NAEs) .
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+)
Sequence Mass (Da): 30312
Sequence Length: 279
Subcellular Location: Cytoplasm
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B0Y665 | MKTTTVACAVAGLLFSCVSGAPDPVHVEIQQRALPNAPDGYTPSTVGCPASRPTIRSAASLSPNETSWLETRRGKTTSAMKDFFNHVKIQDFDAAGYIDRHSSNSSDLPNIGIAVSGGGYRALMNGAGAIKAFDSRTPNSTSAGQLGGLLQSATYLSGLSGGSWLVGSIYINNFTTISALQTHQKGTVWQFQNSIFEGPDGGSIQILDSATYYRDISNAVSGKSDAGYPTSITDYWGRALSYQMINATNGGPSYTWSSIALTDAFQKAEMPMPLVVADGRYPGELLISSNATVYEFNPWEFGTFDPTVFGFAPLEYLGTKFNGGSVPSNESCVRGFDNVGFVMGTSSTLFNQFLLQINSTALPDWLKSVFTDILKDIGENDEDIAQYAPNPFYHFSNTTNPSAAELELDLVDGGEDLQNIPLHPLIQPERHVDVIFAVDSSADTTYSWPNGTALVATYERSLNSSGIANGTSFPAIPDQNTFVNKGLNTRPTFFGCNSSNTTGPSPLIVYLPNYPYTAYSNFSTFQPDYTEQERDSTILNGYDVVTMGNSTRDGNWSTCVGCAILSRSLERTNTNVPEICKQCFQRYCWDGSLNSTTPAGYEPVTILDSAASGIIPSISTVAMAVVFAAWTIF | Function: Catalyzes the release of fatty acids from lysophospholipids.
PTM: The GPI-like anchor contains a phosphoceramide lipid group. The anchor position has not been determined.
Location Topology: Lipid-anchor
Catalytic Activity: a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid + H(+) + sn-glycerol 3-phosphocholine
Sequence Mass (Da): 68144
Sequence Length: 633
Subcellular Location: Cell membrane
EC: 3.1.1.5
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Q500W4 | MAAFTGTTDKCKACDKTVYVMDLMTLEGMPYHKSCFRCSHCNGTLVICNYSSMDGVLYCKTHFEQLFKESGNFSKNFQTAGKTEKSNDATKAPNRLSSFFSGTQDKCAACKKTVYPLEKMTMEGESYHKTCFRCAHSGCPLTHSSYAALDGVLYCKVHFSQLFLEKGNYNHVLQAAANHRRSTAEEDKTEPKEDEANPTEEETSDAAAEEHES | Function: Binds to actin filaments and promotes cross-linking into thick bundles. Has an actin-stabilizing activity. Associates predominantly with long and dynamic actin bundles in the shank of growing pollen tubes. The actin regulatory activities are inhibited by pH > 6.8 and/or high [Ca(2+)].
Sequence Mass (Da): 23765
Sequence Length: 213
Domain: The C-terminal domain (159-213) is required for the ability to respond to pH and calcium variations.
Subcellular Location: Cytoplasm
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P34331 | MNRLPNIAKPPQKSNQRKEKAPPEVPALIADKDRGTYYEKGRFLGKGGFAHCYELTNRATREVVAGKVVPKSMLVKQYQRDKVDNERILIHRELGHINIVKLFNFFEDNLNVYITLELCARRSLMELHKRRKAVTEPEARYFTHQIVDGVLYLHDLNIIHRDMKLGNLFLNDDLVVKIGDFGLATTVNGDERKKTLCGTPNYIAPEVLNKAGHSFEVDIWAVGCILYILLFGQPPFESKSLEETYSRIRHNNYTIPSIATQPAASLIRKMLDPEPTRRPTAKQVQRDGFFKSGFMPTRLPVSCLTMVPKFGGHETSMMEENVAPRGVDARSQRPLNGRAGLSALPQHIVSNNADRERAQQQAAEATFREPEDAYLSQLFHQVAVLLEQRIPGLEEEEAALDGYQSPECLPVFWISKWVDYSDKYGIGYQLCDNSVGVLFNDNSRIMLDQAGNELTYIEKSNKEHYFSMHSGEMPGLLNKKVTLLKYFRSYMNDHLVKAGEGSEQRAGDDLARLPTLRVWFRTKSAIVLHLSNGTVQINFFNDHVKMMMCPLMQAVTFIDQNKRMLTYKLNNLQRNGCPEKFLHRLKYAKTMIERLMSDANVVSQNPARQPDMPRSMAAARSASAGSRGPNQAASHLPQSASGSNIHPRR | Function: Required for oocyte nuclear envelope breakdown before entry of oocyte into spermatheca . In meiotic cells, required for spindle dynamics and probably for spindle attachment to the chromosomes . Zygotic role in the development of the germline and nerve cord . In mitotic cells, plays a role in spindle organization and centrosome maturation . Involved in asymmetric nuclear localization of cdc-25.1 during embryogenesis which affects cell division timing . Together with plk-2, regulates cytoplasm polarity in early embryos . May play a minor role in chromosome pairing and synapsis during oocyte meiosis I .
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 73633
Sequence Length: 649
Domain: The POLO box domains are involved in the asymmetric cytoplasmic localization.
Subcellular Location: Cytoplasm
EC: 2.7.11.21
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P53350 | MSAAVTAGKLARAPADPGKAGVPGVAAPGAPAAAPPAKEIPEVLVDPRSRRRYVRGRFLGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTARPTINELLNDEFFTSGYIPARLPITCLTIPPRFSIAPSSLDPSNRKPLTVLNKGLENPLPERPREKEEPVVRETGEVVDCHLSDMLQQLHSVNASKPSERGLVRQEEAEDPACIPIFWVSKWVDYSDKYGLGYQLCDNSVGVLFNDSTRLILYNDGDSLQYIERDGTESYLTVSSHPNSLMKKITLLKYFRNYMSEHLLKAGANITPREGDELARLPYLRTWFRTRSAIILHLSNGSVQINFFQDHTKLILCPLMAAVTYIDEKRDFRTYRLSLLEEYGCCKELASRLRYARTMVDKLLSSRSASNRLKAS | Function: Serine/threonine-protein kinase that performs several important functions throughout M phase of the cell cycle, including the regulation of centrosome maturation and spindle assembly, the removal of cohesins from chromosome arms, the inactivation of anaphase-promoting complex/cyclosome (APC/C) inhibitors, and the regulation of mitotic exit and cytokinesis. Polo-like kinase proteins acts by binding and phosphorylating proteins are that already phosphorylated on a specific motif recognized by the POLO box domains. Phosphorylates BORA, BUB1B/BUBR1, CCNB1, CDC25C, CEP55, ECT2, ERCC6L, FBXO5/EMI1, FOXM1, KIF20A/MKLP2, CENPU, NEDD1, NINL, NPM1, NUDC, PKMYT1/MYT1, KIZ, PPP1R12A/MYPT1, PRC1, RACGAP1/CYK4, SGO1, STAG2/SA2, TEX14, TOPORS, p73/TP73, TPT1, WEE1 and HNRNPU. Plays a key role in centrosome functions and the assembly of bipolar spindles by phosphorylating KIZ, NEDD1 and NINL. NEDD1 phosphorylation promotes subsequent targeting of the gamma-tubulin ring complex (gTuRC) to the centrosome, an important step for spindle formation. Phosphorylation of NINL component of the centrosome leads to NINL dissociation from other centrosomal proteins. Involved in mitosis exit and cytokinesis by phosphorylating CEP55, ECT2, KIF20A/MKLP2, CENPU, PRC1 and RACGAP1. Recruited at the central spindle by phosphorylating and docking PRC1 and KIF20A/MKLP2; creates its own docking sites on PRC1 and KIF20A/MKLP2 by mediating phosphorylation of sites subsequently recognized by the POLO box domains. Phosphorylates RACGAP1, thereby creating a docking site for the Rho GTP exchange factor ECT2 that is essential for the cleavage furrow formation. Promotes the central spindle recruitment of ECT2. Plays a central role in G2/M transition of mitotic cell cycle by phosphorylating CCNB1, CDC25C, FOXM1, CENPU, PKMYT1/MYT1, PPP1R12A/MYPT1 and WEE1. Part of a regulatory circuit that promotes the activation of CDK1 by phosphorylating the positive regulator CDC25C and inhibiting the negative regulators WEE1 and PKMYT1/MYT1. Also acts by mediating phosphorylation of cyclin-B1 (CCNB1) on centrosomes in prophase. Phosphorylates FOXM1, a key mitotic transcription regulator, leading to enhance FOXM1 transcriptional activity. Involved in kinetochore functions and sister chromatid cohesion by phosphorylating BUB1B/BUBR1, FBXO5/EMI1 and STAG2/SA2. PLK1 is high on non-attached kinetochores suggesting a role of PLK1 in kinetochore attachment or in spindle assembly checkpoint (SAC) regulation. Required for kinetochore localization of BUB1B. Regulates the dissociation of cohesin from chromosomes by phosphorylating cohesin subunits such as STAG2/SA2. Phosphorylates SGO1: required for spindle pole localization of isoform 3 of SGO1 and plays a role in regulating its centriole cohesion function. Mediates phosphorylation of FBXO5/EMI1, a negative regulator of the APC/C complex during prophase, leading to FBXO5/EMI1 ubiquitination and degradation by the proteasome. Acts as a negative regulator of p53 family members: phosphorylates TOPORS, leading to inhibit the sumoylation of p53/TP53 and simultaneously enhance the ubiquitination and subsequent degradation of p53/TP53. Phosphorylates the transactivation domain of the transcription factor p73/TP73, leading to inhibit p73/TP73-mediated transcriptional activation and pro-apoptotic functions. Phosphorylates BORA, and thereby promotes the degradation of BORA. Contributes to the regulation of AURKA function. Also required for recovery after DNA damage checkpoint and entry into mitosis. Phosphorylates MISP, leading to stabilization of cortical and astral microtubule attachments required for proper spindle positioning . Together with MEIKIN, acts as a regulator of kinetochore function during meiosis I: required both for mono-orientation of kinetochores on sister chromosomes and protection of centromeric cohesin from separase-mediated cleavage (By similarity). Phosphorylates CEP68 and is required for its degradation . Regulates nuclear envelope breakdown during prophase by phosphorylating DCTN1 resulting in its localization in the nuclear envelope . Phosphorylates the heat shock transcription factor HSF1, promoting HSF1 nuclear translocation upon heat shock . Phosphorylates HSF1 also in the early mitotic period; this phosphorylation regulates HSF1 localization to the spindle pole, the recruitment of the SCF(BTRC) ubiquitin ligase complex induicing HSF1 degradation, and hence mitotic progression . Regulates mitotic progression by phosphorylating RIOK2 . Through the phosphorylation of DZIP1 regulates the localization during mitosis of the BBSome, a ciliary protein complex involved in cilium biogenesis .
PTM: Catalytic activity is enhanced by phosphorylation of Thr-210. Phosphorylation at Thr-210 is first detected on centrosomes in the G2 phase of the cell cycle, peaks in prometaphase and gradually disappears from centrosomes during anaphase. Dephosphorylation at Thr-210 at centrosomes is probably mediated by protein phosphatase 1C (PP1C), via interaction with PPP1R12A/MYPT1. Autophosphorylation and phosphorylation of Ser-137 may not be significant for the activation of PLK1 during mitosis, but may enhance catalytic activity during recovery after DNA damage checkpoint. Phosphorylated in vitro by STK10.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 68255
Sequence Length: 603
Domain: The POLO box domains act as phosphopeptide-binding module that recognize and bind serine-[phosphothreonine/phosphoserine]-(proline/X) motifs. PLK1 recognizes and binds docking proteins that are already phosphorylated on these motifs, and then phosphorylates them. PLK1 can also create its own docking sites by mediating phosphorylation of serine-[phosphothreonine/phosphoserine]-(proline/X) motifs subsequently recognized by the POLO box domains.
Subcellular Location: Nucleus
EC: 2.7.11.21
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Q07832 | MNAAAKAGKLARAPADLGKGGVPGDAVPGAPVAAPLAKEIPEVLVDPRSRRQYVRGRFLGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQKEKMSMEISIHRSLAHQHVVGFHDFFEDSDFVFVVLELCRRRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNQVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYEGERKKTLCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTARPTIHELLNDEFFTSGYIPARLPITCLTIPPRFSIAPSSLDPSSRKPLKVLNKGVENPLPDRPREKEEPVVRETNEAIECHLSDLLQQLTSVNASKPSERGLVRQEEAEDPACIPIFWVSKWVDYSDKYGLGYQLCDNSVGVLFNDSTRLILYNDGDSLQYIERDGTESYLTVSSHPNSLMKKITLLNYFRNYMSEHLLKAGANITPREGDELARLPYLRTWFRTRSAIILHLSNGTVQINFFQDHTKLILCPLMAAVTYINEKRDFQTYRLSLLEEYGCCKELASRLRYARTMVDKLLSSRSASNRLKAS | Function: Serine/threonine-protein kinase that performs several important functions throughout M phase of the cell cycle, including the regulation of centrosome maturation and spindle assembly, the removal of cohesins from chromosome arms, the inactivation of anaphase-promoting complex/cyclosome (APC/C) inhibitors, and the regulation of mitotic exit and cytokinesis. Polo-like kinase proteins acts by binding and phosphorylating proteins are that already phosphorylated on a specific motif recognized by the POLO box domains. Phosphorylates BORA, BUB1B/BUBR1, CCNB1, CDC25C, CEP55, ECT2, ERCC6L, FBXO5/EMI1, FOXM1, KIF20A/MKLP2, CENPU, NEDD1, NINL, NPM1, NUDC, PKMYT1/MYT1, KIZ, PPP1R12A/MYPT1, PRC1, RACGAP1/CYK4, SGO1, STAG2/SA2, TEX14, TOPORS, p73/TP73, TPT1, WEE1 and HNRNPU. Plays a key role in centrosome functions and the assembly of bipolar spindles by phosphorylating KIZ, NEDD1 and NINL. NEDD1 phosphorylation promotes subsequent targeting of the gamma-tubulin ring complex (gTuRC) to the centrosome, an important step for spindle formation. Phosphorylation of NINL component of the centrosome leads to NINL dissociation from other centrosomal proteins. Involved in mitosis exit and cytokinesis by phosphorylating CEP55, ECT2, KIF20A/MKLP2, CENPU, PRC1 and RACGAP1. Recruited at the central spindle by phosphorylating and docking PRC1 and KIF20A/MKLP2; creates its own docking sites on PRC1 and KIF20A/MKLP2 by mediating phosphorylation of sites subsequently recognized by the POLO box domains. Phosphorylates RACGAP1, thereby creating a docking site for the Rho GTP exchange factor ECT2 that is essential for the cleavage furrow formation. Promotes the central spindle recruitment of ECT2. Plays a central role in G2/M transition of mitotic cell cycle by phosphorylating CCNB1, CDC25C, FOXM1, CENPU, PKMYT1/MYT1, PPP1R12A/MYPT1 and WEE1. Part of a regulatory circuit that promotes the activation of CDK1 by phosphorylating the positive regulator CDC25C and inhibiting the negative regulators WEE1 and PKMYT1/MYT1. Also acts by mediating phosphorylation of cyclin-B1 (CCNB1) on centrosomes in prophase. Phosphorylates FOXM1, a key mitotic transcription regulator, leading to enhance FOXM1 transcriptional activity. Involved in kinetochore functions and sister chromatid cohesion by phosphorylating BUB1B/BUBR1, FBXO5/EMI1 and STAG2/SA2. PLK1 is high on non-attached kinetochores suggesting a role of PLK1 in kinetochore attachment or in spindle assembly checkpoint (SAC) regulation. Required for kinetochore localization of BUB1B. Regulates the dissociation of cohesin from chromosomes by phosphorylating cohesin subunits such as STAG2/SA2. Phosphorylates SGO1: required for spindle pole localization of isoform 3 of SGO1 and plays a role in regulating its centriole cohesion function. Mediates phosphorylation of FBXO5/EMI1, a negative regulator of the APC/C complex during prophase, leading to FBXO5/EMI1 ubiquitination and degradation by the proteasome. Acts as a negative regulator of p53 family members: phosphorylates TOPORS, leading to inhibit the sumoylation of p53/TP53 and simultaneously enhance the ubiquitination and subsequent degradation of p53/TP53. Phosphorylates the transactivation domain of the transcription factor p73/TP73, leading to inhibit p73/TP73-mediated transcriptional activation and pro-apoptotic functions. Phosphorylates BORA, and thereby promotes the degradation of BORA. Contributes to the regulation of AURKA function. Also required for recovery after DNA damage checkpoint and entry into mitosis.Phosphorylates MISP, leading to stabilization of cortical and astral microtubule attachments required for proper spindle positioning (By similarity). Together with MEIKIN, acts as a regulator of kinetochore function during meiosis I: required both for mono-orientation of kinetochores on sister chromosomes and protection of centromeric cohesin from separase-mediated cleavage . Phosphorylates CEP68 and is required for its degradation. Regulates nuclear envelope breakdown during prophase by phosphorylating DCTN1 resulting in its localization in the nuclear envelope (By similarity). Phosphorylates the heat shock transcription factor HSF1, promoting HSF1 nuclear translocation upon heat shock (By similarity). Phosphorylates HSF1 also in the early mitotic period; this phosphorylation regulates HSF1 localization to the spindle pole, the recruitment of the SCF(BTRC) ubiquitin ligase complex induicing HSF1 degradation, and hence mitotic progression (By similarity). Regulates mitotic progression by phosphorylating RIOK2 (By similarity). Through the phosphorylation of DZIP1 regulates the localization during mitosis of the BBSome, a ciliary protein complex involved in cilium biogenesis .
PTM: Catalytic activity is enhanced by phosphorylation of Thr-210. Phosphorylation at Thr-210 is first detected on centrosomes in the G2 phase of the cell cycle, peaks in prometaphase and gradually disappears from centrosomes during anaphase. Dephosphorylation at Thr-210 at centrosomes is probably mediated by protein phosphatase 1C (PP1C), via interaction with PPP1R12A/MYPT1. Autophosphorylation and phosphorylation of Ser-137 may not be significant for the activation of PLK1 during mitosis, but may enhance catalytic activity during recovery after DNA damage checkpoint. Phosphorylated in vitro by STK10 (By similarity).
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 68301
Sequence Length: 603
Domain: The POLO box domains act as phosphopeptide-binding module that recognize and bind serine-[phosphothreonine/phosphoserine]-(proline/X) motifs. PLK1 recognizes and binds docking proteins that are already phosphorylated on these motifs, and then phosphorylates them. PLK1 can also create its own docking sites by mediating phosphorylation of serine-[phosphothreonine/phosphoserine]-(proline/X) motifs subsequently recognized by the POLO box domains (By similarity).
Subcellular Location: Nucleus
EC: 2.7.11.21
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P58606 | AEKDCIAPGAPCFGTDKPCCNPRAWCSSYANKCL | Function: Binds reversibly and blocks N-type voltage-gated calcium channels (Cav).
Sequence Mass (Da): 3621
Sequence Length: 34
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
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P70032 | MAQVAGKKLTVAPEAAKPPGIPGSSSAVKEIPEILVDPRTRRRYLRGRFLGKGGFAKCYEITDLESREVFAGKIVPKTMLLKPHQKDKMTMEIAIQRSLDHRHVVGFHGFFEDNDFVYVVLELCRRRSLLELHKRRKAVTEPEARYYLKQTISGCQYLHSNRVIHRDLKLGNLFLNDEMEVKIGDFGLATKVEYDGERKKTLCGTPNYIAPEVLGKKGHSFEVDIWSIGCIMYTLLVGKPPFETSCLKETYMRIKKNEYSIPKHINPVAAALIQKMLRSDPTSRPTIDDLLNDEFFTSGYIPSRLPTTCLTVPPRFSIAPSTIDQSLRKPLTAINKGQDSPLVEKQVAPAKEEEMQQPEFTEPADCYLSEMLQQLTCLNAVKPSERALIRQEEAEDPASIPIFWISKWVDYSDKYGLGYQLCDNSVGVLFNDSTRLIMYNDGDSLQYIERNNTESYLNVRSYPTTLTKKITLLKYFRNYMSEHLLKAGANTTPREGDELARLPFLRTWFRTRSAIILHLSNGTVQINFFQDHTKIILCPLMAAVSYIDEKREFRTYKLSLIQEFGCCKELASRLRYARTMVEKLQSSKSAVAHVKASA | Function: Serine/threonine-protein kinase that performs several important functions throughout M phase of the cell cycle, including the regulation of centrosome maturation and spindle assembly, the removal of cohesins from chromosome arms, the inactivation of anaphase-promoting complex/cyclosome (APC/C) inhibitors, and the regulation of mitotic exit and cytokinesis. Polo-like kinase proteins acts by binding and phosphorylating proteins are that already phosphorylated on a specific motif recognized by the POLO box domains. Phosphorylates cdc25, pkmyt1/myt1, stag2/sa2, tpx2. Plays multiple essential roles during mitosis. Phosphorylates the N-terminal domain of cdc25, which leads to cyclin b-cdc2 activation and mitotic entry. Also required for organization of bipolar spindles, and for exit from mitosis. Involved in kinetochore functions and sister chromatid cohesion by phosphorylating stag2/sa2.
PTM: Activated by phosphorylation on Thr-201 during M phase. Phosphorylated by stk10, leading to activation during oocyte maturation.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 68212
Sequence Length: 598
Domain: The POLO box domains act as phosphopeptide-binding module that recognize and bind serine-[phosphothreonine/phosphoserine]-(proline/X) motifs. plk1 recognizes and binds docking proteins that are already phosphorylated on these motifs, and then phosphorylates them (By similarity).
Subcellular Location: Nucleus
EC: 2.7.11.21
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A0A6B9L3U7 | MMKFLLVLFLITITLITMAYSEEHGCIPPFQPCEGVNSRCCGLYVCFNKICLATP | Function: Binds reversibly and blocks P/Q-type voltage-gated calcium channels (Cav).
Sequence Mass (Da): 6175
Sequence Length: 55
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
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Q9R012 | MELLRTITYQPAAGTKMCEQALGKACGGDSKKKRPQQPSEDGQSQAQVTPAAPHHHHHHSHSGPEISRIIVDPTTGKRYCRGKVLGKGGFAKCYEMTDLTNNKVYAAKIIPHSRVAKPHQREKIDKEIELHRILHHKHVVQFYHYFEDKENIYILLEYCSRRSMAHILKARKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINEAMELKVGDFGLAARLEPLEHRRRTICGTPNYLSPEVLNKQGHGCESDIWALGCVMYTMLLGRPPFETTNLKETYRCIREARYTMPSSLLAPAKHLIASMLSKNPEDRPSLDDIIRHDFFLQGFTPDRLSSSCCHTVPDFHLSSPAKNFFKKAAAALFGGKKDKARYNDTHNKVSKEDEDIYKLRHDLKKTSITQQPSKHRTDEELQPPPTTFAKSGTSAVENKQQIGDAIRMIVRGTLGSCSSSSECLEDSTMGSVADTVARVLRGCLENMPEADCIPKEQLSTSFQWVTKWVDYSNKYGFGYQLSDHTVGVLFNNGAHMSLLPDKKTVHYYAELGQCSVFPATDAPEQFISQVTVLKYFSHYMEENLMDGGDLPSVTDIRRPRLYLLQWLKSDKALMMLFNDGTFQVNFYHDHTKIIICNQNEEYLLTYINEDRISTTFRLTTLLMSGCSLELKHRMEYALNMLLQRCN | Function: Tumor suppressor serine/threonine-protein kinase involved in synaptic plasticity, centriole duplication and G1/S phase transition. Polo-like kinases act by binding and phosphorylating proteins are that already phosphorylated on a specific motif recognized by the POLO box domains. Phosphorylates CENPJ, NPM1, RAPGEF2, RASGRF1, SNCA, SIPA1L1 and SYNGAP1. Plays a key role in synaptic plasticity and memory by regulating the Ras and Rap protein signaling: required for overactivity-dependent spine remodeling by phosphorylating the Ras activator RASGRF1 and the Rap inhibitor SIPA1L1 leading to their degradation by the proteasome. Conversely, phosphorylates the Rap activator RAPGEF2 and the Ras inhibitor SYNGAP1, promoting their activity. Also regulates synaptic plasticity independently of kinase activity, via its interaction with NSF that disrupts the interaction between NSF and the GRIA2 subunit of AMPARs, leading to a rapid rundown of AMPAR-mediated current that occludes long term depression. Required for procentriole formation and centriole duplication by phosphorylating CENPJ and NPM1, respectively. Its induction by p53/TP53 suggests that it may participate in the mitotic checkpoint following stress.
PTM: Catalytic activity is enhanced by phosphorylation of Thr-236.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 77920
Sequence Length: 682
Domain: The POLO box domains act as phosphopeptide-binding module that recognize and bind serine-[phosphothreonine/phosphoserine]-(proline/X) motifs. PLK2 recognizes and binds docking proteins that are already phosphorylated on these motifs, and then phosphorylates them (By similarity).
Subcellular Location: Cytoplasm
EC: 2.7.11.21
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A0A6B9KZ66 | MKAGMKLVLVLVIASIALLALATEVAGDCIPQGASCNRLSTIPRRCCFPMVCGWDSSTCVPATINVKP | Function: Binds reversibly and blocks P/Q-type voltage-gated calcium channels (Cav).
Sequence Mass (Da): 7107
Sequence Length: 68
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
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Q20845 | MQHVLRTRGNSAQDKNKKHVPNVPPIIYDDMQVPYEKGAFLGEGGFAHCFEFRKLDCNDRLAVKVVPKVILLKSTAREKLTREVEIHRQLSHRNIVQFHHFFEDSQNVYFTLELCSKNSLMELNKQRGPLTEHEARFYTIQVAEGVKHLHNLQIIHRDLKLGNLFLNEHLQVKIGDFGLATFCEKNEKKMTRGGTPNYIAPEVLNETGHAFEVDIWAIGCILYVLLFGSPPFESRRVQETYVRIKNNDYVVPENASPTANRLIRSLLDPVPDRRPTAEAVLLDQFFKTTIEPTYPPVHQQLHKEQDVKYFAPINPVLPHVEEPISPIYQEVANEETSEIRRFVKTEQASSFGDELSQLQAQISHILQNVVASKNKSSTRFGLNHSPEATPIFWVSQWVHFPNHGIGYRLCENSSGMLFNDNTQMKVNSAGNQLTFVDENNTEQFYTMNDQVPMNLQTKINIFSNVQSYMNTHLEADTHLEAEDQCVNKVPPLRNFARLPTIQNWFETKSAVIFHLSNGTVQINFLDHVKMVLCPLLKSVTFIEENKRVSTFTFANILTNSCPKKYLSRIEYAQAKIKLLRPTNNQEHVVYVDSPCRPTTSNTAHGAPLASSRYLA | Function: May be required for cell division and may have a role during G1 or S phase.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 70436
Sequence Length: 615
Subcellular Location: Nucleus
EC: 2.7.11.21
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Q9H4B4 | MEPAAGFLSPRPFQRAAAAPAPPAGPGPPPSALRGPELEMLAGLPTSDPGRLITDPRSGRTYLKGRLLGKGGFARCYEATDTETGSAYAVKVIPQSRVAKPHQREKILNEIELHRDLQHRHIVRFSHHFEDADNIYIFLELCSRKSLAHIWKARHTLLEPEVRYYLRQILSGLKYLHQRGILHRDLKLGNFFITENMELKVGDFGLAARLEPPEQRKKTICGTPNYVAPEVLLRQGHGPEADVWSLGCVMYTLLCGSPPFETADLKETYRCIKQVHYTLPASLSLPARQLLAAILRASPRDRPSIDQILRHDFFTKGYTPDRLPISSCVTVPDLTPPNPARSLFAKVTKSLFGRKKKSKNHAQERDEVSGLVSGLMRTSVGHQDARPEAPAASGPAPVSLVETAPEDSSPRGTLASSGDGFEEGLTVATVVESALCALRNCIAFMPPAEQNPAPLAQPEPLVWVSKWVDYSNKFGFGYQLSSRRVAVLFNDGTHMALSANRKTVHYNPTSTKHFSFSVGAVPRALQPQLGILRYFASYMEQHLMKGGDLPSVEEVEVPAPPLLLQWVKTDQALLMLFSDGTVQVNFYGDHTKLILSGWEPLLVTFVARNRSACTYLASHLRQLGCSPDLRQRLRYALRLLRDRSPA | Function: Serine/threonine-protein kinase involved in cell cycle regulation, response to stress and Golgi disassembly. Polo-like kinases act by binding and phosphorylating proteins are that already phosphorylated on a specific motif recognized by the POLO box domains. Phosphorylates ATF2, BCL2L1, CDC25A, CDC25C, CHEK2, HIF1A, JUN, p53/TP53, p73/TP73, PTEN, TOP2A and VRK1. Involved in cell cycle regulation: required for entry into S phase and cytokinesis. Phosphorylates BCL2L1, leading to regulate the G2 checkpoint and progression to cytokinesis during mitosis. Plays a key role in response to stress: rapidly activated upon stress stimulation, such as ionizing radiation, reactive oxygen species (ROS), hyperosmotic stress, UV irradiation and hypoxia. Involved in DNA damage response and G1/S transition checkpoint by phosphorylating CDC25A, p53/TP53 and p73/TP73. Phosphorylates p53/TP53 in response to reactive oxygen species (ROS), thereby promoting p53/TP53-mediated apoptosis. Phosphorylates CHEK2 in response to DNA damage, promoting the G2/M transition checkpoint. Phosphorylates the transcription factor p73/TP73 in response to DNA damage, leading to inhibit p73/TP73-mediated transcriptional activation and pro-apoptotic functions. Phosphorylates HIF1A and JUN is response to hypoxia. Phosphorylates ATF2 following hyperosmotic stress in corneal epithelium. Also involved in Golgi disassembly during the cell cycle: part of a MEK1/MAP2K1-dependent pathway that induces Golgi fragmentation during mitosis by mediating phosphorylation of VRK1. May participate in endomitotic cell cycle, a form of mitosis in which both karyokinesis and cytokinesis are interrupted and is a hallmark of megakaryocyte differentiation, via its interaction with CIB1.
PTM: Phosphorylated in an ATM-dependent manner following DNA damage. Phosphorylated as cells enter mitosis and dephosphorylated as cells exit mitosis.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 71629
Sequence Length: 646
Domain: The POLO box domains act as phosphopeptide-binding module that recognize and bind serine-[phosphothreonine/phosphoserine]-(proline/X) motifs. PLK3 recognizes and binds docking proteins that are already phosphorylated on these motifs, and then phosphorylates them (By similarity). The POLO box domains mediates localization to the centrosome.
Subcellular Location: Cytoplasm
EC: 2.7.11.21
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P65735 | MTAREVGRIGLRKLLQRIGIVAESMTPLATDPVEVTQLLDARWYDERLRALADELGRDPDSVRAEAAGYLREMAASLDERAVQAWRGFSRWLMRAYDVLVDEDQITQLRKLDRKATLAFAFSHRSYLDGMLLPEAILANRLSPALTFGGANLNFFPMGAWAKRTGAIFIRRQTKDIPVYRFVLRAYAAQLVQNHVNLTWSIEGGRTRTGKLRPPVFGILRYITDAVDEIDGPEVYLVPTSIVYDQLHEVEAMTTEAYGAVKRPEDLRFLVRLARQQGERLGRAYLDFGEPLPLRKRLQEMRADKSGTGSEIERIALDVEHRINRATPVTPTAVVSLALLGADRSLSISEVLATVRPLASYIAARNWAVAGAADLTNRSTIRWTLHQMVASGVVSVYDAGTEAVWGIGEDQHLVAAFYRNTAIHILVDRAVAELALLAAAETTTNGSVSPATVRDEALSLRDLLKFEFLFSGRAQFEKDLANEVLLIGSVVDTSKPAAAADVWRLLESADVLLAHLVLRPFLDAYHIVADRLAAHEDDSFDEEGFLAECLQVGKQWELQRNIASAESRSMELFKTALRLARHRELVDGADATDIAKRRQQFADEIATATRRVNTIAELARRQ | Location Topology: Peripheral membrane protein
Sequence Mass (Da): 69224
Sequence Length: 621
Domain: The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.
Subcellular Location: Cell membrane
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Q88MQ0 | MTRSPLHRLIFGGLRRLLYLWVRSETINQSSMTLNLDRSRPVFYALPSPALTDLAVLDHECTKAGLPRPVLPVAVGPLQEPAAFFYLTPDPDWLGRQDKSGAPPTLERLVAAVSQHAEEDAQIIPVSVFWGQTPASESSPWKLLFADSWAVTGRLRRLLTVLILGRKTRVQFSAPIHLRELVQHNKGHERTVRMAQRLMRVHFRNLKTAVIGPDISHRRTLVKGLVHAPQVRQAIADEAQRENLPLAKAEAQALRYGNEIASDYTYTAIRFLEVVLSWFWNKIYDGIKVNHIEQVQGIAPGHEVIYVPCHRSHIDYLLLSYLLFRNGLTPPHVAAGINLNMPVVGNLLRRGGAFFMRRTFKGNPLYTAVFNEYLHTLYTKGFPVEYFVEGGRSRTGRMLQPRTGMLAITLRSFLRSSRTPIVFVPVYIGYERVLEGRTYLGELRGASKKKESVLDIFKVFGALKQRFGQVYVNFGEPIRLAGFLDQQQPGWREQDHGPQYRPEWLNATTARLGETVARHLNEAAAINPVNLVALALLSTSRLALDERALTRVLDLYLALLRQVPYSPHTTLPEGDGQALIEHVRSMNLVAEQKDALGRILYLDEGNAVLMTYYRNNVLHIFALPALLASFFLSSSRMSRQLLGQYVHALYPYLQAELFLRWTPEQLDEVIDQWLVALVEQGLLRQDNDLYVRPAPSSRQFVLLTLLARTITQTLQRFYMATSLLINSGQNSLSAEALEDLCVMMAQRLSILHGLNAPEFFDKTLFRHFIQTLLQQGVLHADAQGKLSYHDKLGELAEGVAKRVLSAELRLSIRQVALHRDDGLETSTL | Catalytic Activity: an acyl-CoA + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-phosphate + CoA
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 93693
Sequence Length: 828
Domain: The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.
Pathway: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 1/3.
Subcellular Location: Cell inner membrane
EC: 2.3.1.15
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Q886Q7 | MTRSPFRRLVFGTLRRLLYLWVRSETINQSSFTLNLDRSRPVFYALQSPSISDLAVIDTECRKAGLPRPVLSVAVGNLIEPSAYFYLTPAPDWLGRQDKRGAPPTLERLVAAVSQNPGEDAQIIPVSVFWGQSPDHESSAWKLLFADSWAVTGRLRRLVSILILGRKTRVQFSAPIHMRELVDQNKGHELTLRMSQRLLRTHFRNLKSAVIGPDVSHRRTVVKGLLDEPLVKQAIIEEAERENITQEKARERALSYGNEIASDYTYSVIRFMEVVLSWFWNKIYDGIKVSHIEGVQEIAPGHEVIYVPCHRSHIDYLLLSYLLFRNGLTPPHIAAGINLNMPVVGSLLRRGGAFFMRRTFKGSPLYTAVFTEYLHTLFTKGFPVEYFVEGGRSRTGRMLQPKTGMLAITLRSFLRNSRMPIVFIPVYIGYERVLEGRTYLGELRGATKKKESIFDIFKVIGALKQRFGQVSVNFGEPIRLAEFLDGEQPDWREQELAPQFRPDWLSETTHRLGERVAQHLNEAAAVNPMNLVAITLLSTQKLALDDQAMERVLDLYLTLLRAVPYSPHTTLPEGNGRSLIEHVKGMDLLAEQKDALGKILYLNEQNAVLMTYYRNNVLHIFALPSLLASFFQSSSRMSREQILRYTHALYPYLQSELFIRWPLSELDEVVDQWLAAFVEQGLLRFRNDAYVRPEPSSREFVLLTLLSRAIAQTLQRFYMAIALLLNSGPNTLNPEELEDLCTVMAQRLSILHGLNAPEFFDKSLFRHFIQTLLDLRVLRKDRAGKLSYHPMLGELAEGAAKRVLPAEIRLSIRQVALHSNEEEQNAGNESGAA | Catalytic Activity: an acyl-CoA + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-phosphate + CoA
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 94878
Sequence Length: 833
Domain: The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.
Pathway: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 1/3.
Subcellular Location: Cell inner membrane
EC: 2.3.1.15
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Q3IF27 | MRIVNYCLNVLSAGVSRLLVRSKVLPEKPTEQYELNSKNPTFYIVRLNSRFDLAALARVCKRHGLPDPREQQVLGTQRLDRFIGIENPPPLIGDIAKPTNALAQGKQIIDHLLSSGQKDVQVIPVTILWGRAPGKEKPGLSTLITHSLTPSWFRKLFVVLFSGRDNFIRFSQPLDLSLLVDEKADVNELPQKLLRVARVHFRRQKLAATGPKMPSREQLFNSLLASPTIKKAIQDEAKAKNISQAQARQNAVKLLNEIAANYSEAMIRVAERFLTWLWNKLYNGIDIKYTEQIHELTNKGHEIIYMPCHRSHMDYLLLTYAIYHQGLVPPHIAAGINLNFFPAGGIFRRSGAFFIRRSFAGNKLYSAVFKEYLSQLFIKGYSVKFYTEGGRSRTGRLLPPKTGMLAMTMQAMLRGIDRPISIVPVYIGYEHVMEINTYLKELAGNDKKGESIFGIFKAIKNLKNYGRGYLNFGDPISINQYLNDNQPNWRDDIHPTDVQKPQWLGPQVANLADQVMVKINNAAALNAVNLLAMILLVNDKHALSKPKLLAQLDFYLRLQRDASYSNKVTAPEETPEQLLTHALKLNKFDVISDEFGEIIAINDKEKTLFNYYRNNILHLFAVPSLIALHLFREKTTTVSKCQQLVAAFYPLFAKEWYLRELDEDYITRILANFVDQNLIELDGDNIHITNTNDCLAKLDMLGKALNFTLQRYAIVIGFIQTSNGIEKAELERESQVLAQRLGTLHGIKTPEFFDKKVLVSFIDNLRAQSLITDGDAGLIGSVQLCETYMHLKALLPARVWQSISDIVQGQCK | Catalytic Activity: an acyl-CoA + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-phosphate + CoA
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 92076
Sequence Length: 812
Domain: The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.
Pathway: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 1/3.
Subcellular Location: Cell inner membrane
EC: 2.3.1.15
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Q49427 | MAFRFAVDCLGFENKPSEAIEAVLKYWSFHQDLNFILIGDEKAFDGLDILPKNITKKLANSFIEMTDTPLSARRKVNSSMQIAINLVREGNADVVISAGSSAVYASLTNDAFGKINKNTKSAFMSYVPTDNNNWFYFLDVGANKYFTGKELYFLGLMADIFVKKTTTKKTPKIGLLNIGTEENKGFDYHQEAFKLLKADKNLNFLGFVESRFLLDGICDILIADGYSGNLVLKAMEGTFKTIARILKRGYKRNPLAGLFSLGIIKSVAKKFDYKNNAGAVVMGLNKLALKTHGSADKQQFLSTIRLAHLSLKSDLINAIKTSLNNYEE | Function: Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
Catalytic Activity: a fatty acyl-[ACP] + phosphate = an acyl phosphate + holo-[ACP]
Sequence Mass (Da): 36502
Sequence Length: 328
Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Cytoplasm
EC: 2.3.1.274
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Q98R48 | MKTIAFDVMGNDFGPQAAVQASLEFVQKNPDFQIILVGDKKEIEKFTKETSQIKILESPNIASSKDGLRQVSKMENSMNSALDLVVEKKADAVLSSGDSGAYLTSALLKVKRLKGILRPAFMPIFPTIVKDKKILVLDVGANLETKVEYLIQWTKLASIFSNKILKVKNPKCALVNIGVEDYKGFDFHKQANEELKQSNANYIGFLEPRNILDGKVDVAVVDGYGGNLILKSMEGAVLALKKVIKESITKTFFRKILALFLKKAFKDAAERLDYRNVGAAWVLGLNGIVVKSHGSNDFKAYLGALEQVKQGINAKVIDVFRETLE | Function: Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
Catalytic Activity: a fatty acyl-[ACP] + phosphate = an acyl phosphate + holo-[ACP]
Sequence Mass (Da): 35918
Sequence Length: 325
Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Cytoplasm
EC: 2.3.1.274
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Q1D339 | MRLVLDAMGGDHAPAAPVEGGVLFARAHPGHEVLLVGDEAKVAPLLGKLRPPSNLQVHHASEVVEMDEHASTAFRRKRDSSLRVGFELVRDGRAEALVSAGNSGAVMAGGLLTLGRLPGVERPAIAALFPALKGGGRCLLLDAGANVDCKPTHLAQFAVMGEAYVRARMGVARPRVAVLSNGEESSKGTPLTREASGLLRRSDLDFVGYVEGKDLFSGEVQVVVTDGFTGNVVLKTSEGVGMGVIGMLRQAIERRGGLAEKVGAMLLQPALAGLRRVVDYAEYGGAPLLGIQGVGIVAHGRSTPRALFNALGAALAMAEGGVQAELTRCIGRAAAWLPTHPKGKRATDAGVSD | Function: Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
Catalytic Activity: a fatty acyl-[ACP] + phosphate = an acyl phosphate + holo-[ACP]
Sequence Mass (Da): 36631
Sequence Length: 353
Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Cytoplasm
EC: 2.3.1.274
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Q9JXR8 | MITLAVDAMGGDQGLAVTVPGATAFLQAHPDVRLIMTGDETQLRQALTAAGAPMERIDICHTTQVVGMDEAPQSALKNKKDSSMRVAINQVKEGKAQAAVSAGNTGALMATARFVLKTIPGIERPAIAKFLPSDTDHVTLALDLGANVDCTSEQLAQFAVIGSELVHALHPQKGQPRVGLVNVGTEDIKGTDTVKQTYKLLQNSKLNFIGNIESNGILYGEADVVVADGFVGNVMLKTIEGAVKFMSGAIRREFQSNLFNKLAAVAALPALKGLKNKLDPRKFNGAILLGLRGIVIKSHGGTDETGFRYALEEAYHEAKSAGLSKIEQGVAEQLAALETAKAVQNENVGGL | Function: Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
Catalytic Activity: a fatty acyl-[ACP] + phosphate = an acyl phosphate + holo-[ACP]
Sequence Mass (Da): 37006
Sequence Length: 351
Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Cytoplasm
EC: 2.3.1.274
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Q2GDD6 | MDQVGRKVVVALDTMGGDRAPDEILLGASVYLRQNPSSVFFRLFGNSSSIERCLSSKANVHLLESCEIIHAGDVVMSDDKLSSAVRKKGSSMYKAVQDVREKASQCVVSAGNTGAFMGISKILLGMLENIYRPAIVTTLPTKKGEVVVLDLGANLDCSSDVLYQFAFMGSAFAKAALGVKNPRVALLNVGVEENKGTDAVKEAFHLLNERTDEDFTFIGYAEPSDVLGGEVDVVVSDGFTGNVMLKTAESIFRLLRDDIVGATRTSLLSRLAGLVLAKSLKKSISRFNPDLRNGAMLIGVNGVAVKAHGGSDSVAFANAIGAAVKLVANNLNSKIIDSICTID | Function: Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
Catalytic Activity: a fatty acyl-[ACP] + phosphate = an acyl phosphate + holo-[ACP]
Sequence Mass (Da): 36395
Sequence Length: 343
Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Cytoplasm
EC: 2.3.1.274
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Q2YA47 | MTITVAVDCMGGDHGPHVTVPATVSYLQSNPAIDVVLVGLPDVIESELRALGYTQSPRLRIHAASEVVGMDESPATALRGKKNSSMRVALNLVKSGEAQACVSAGNTGALLATSRFVLKTLPGIDRPALAVVLPTMRGHTYVLDLGANVDCTAEHLLQFGVMGATLVSSIENKEKPSIGLLNIGEEEIKGNDVVKRAAELLRDSGLNFYGNIEGNDIYKGTTDVVVCDGFVGNVALKTSEGVAQMLSHYLREEFRRNLLTKLAGLIALPVISAFKRRVDHRRYNGASLLGLRGIVIKSHGSADRRAFGFAIARAVDEVRGGMLRHISERVAQLSHQSMQSSSYRRSLPEESPV | Function: Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
Catalytic Activity: a fatty acyl-[ACP] + phosphate = an acyl phosphate + holo-[ACP]
Sequence Mass (Da): 37879
Sequence Length: 353
Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Cytoplasm
EC: 2.3.1.274
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Q2JJA1 | MRIAVDAMGGDYAPEEIIKGALLAHRQLRVGIALVGRPDSLKPFLPQPLPAGITIVPAEEDVGMAEEPLMVRKKPKASINISMQQVRSNQADAVVAAGNTGAAMAAAYLNLGRLAGIDRPAIGALLPTLKGKPVLLLDVGANVDCRPRFLEQFARMGSLYCQCVLGIEKPRVGLLNIGEEPNKGNDLALATHQRLAQLPGIHFAGNAEGRDVLTGEFDVVVCDGFVGNALLKFAESVGQVITQVLREELPRGWRGKLGCWLLRPNLKQVKRRMDYVEYGGALLLGVNGICVITHGSSKAPMVYHAIRLAKEAAEQKILQRLQAEMVDPREPESNPRRRTRPLQVYSGSGPEVLPLGSLERTSSRCPEPVEDAQP | Function: Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
Catalytic Activity: a fatty acyl-[ACP] + phosphate = an acyl phosphate + holo-[ACP]
Sequence Mass (Da): 40412
Sequence Length: 374
Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Cytoplasm
EC: 2.3.1.274
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Q0AYW2 | MRIAVDAMGGDYAPLEIVAGAVKWVAEEEERQIFLVGQEELLKQELKSYSYDPSRLIVVNASEVITMEESPATAIRRKKDASIVVASRMVKEKKADAIISCGSTGAQMAAAIFILGRMEGIERPPIVASIPNMTGAYTLLIDVGANVDCKPRQLLQFALLGKTYASIIYGVEQPRVALLNNGEEESKGNTVTMETYALLRQQSGINFTGNVEGRDIFTGKSDVIVCDGFTGNVLLKTMEGMALFIAQGILGAGGPMPAFFQRLDYTQTGGAPLLGINGLSIVCHGSSKREAVYNGLRIAEDCYNKNIIEMQQLELSKISG | Function: Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
Catalytic Activity: a fatty acyl-[ACP] + phosphate = an acyl phosphate + holo-[ACP]
Sequence Mass (Da): 34553
Sequence Length: 320
Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Cytoplasm
EC: 2.3.1.274
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Q47TA8 | MSSPVTAQRPPAAPPLIAVDAMGGDHAPREIVAGAVRAVREHGLRLALVGRSSELAPLVAAEQAARELPIVHAEEALAMHEGALAAWRRARSSVAVGCKLVRQGTAAALVSAGSTGGVVSTATVRLRTLPGVLRPALALVLPTTPTPTILLDAGANADAKPEMLVQFAHLGAAYARVGHGIAEPRVGILTIGSEPGKGNKLARRAAELLSANATEDRLDFRGNIEGHDLLAGLVDVVVTDGFTGNVALKSVEGAVRFAFDEIRAALTSSPLARFGTLFQRRALRELRTRFDSETYGGAVLLGLNGTVVIAHGASRAEGIAHACLLAHNLVVGRITDQIRRGIAGVSRTPSWLHRLSAPEE | Function: Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
Catalytic Activity: a fatty acyl-[ACP] + phosphate = an acyl phosphate + holo-[ACP]
Sequence Mass (Da): 37479
Sequence Length: 360
Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Cytoplasm
EC: 2.3.1.274
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Q9WXZ6 | MKIAIDVMGGDRAPDEILKGALLASKEVEGEIVLIGPEEIVKNKGLPFVSASEIVKMDDPPLEVLRKKNSSMHMGLKLLSEGKVDAFVSAGATGPLFLGATSIVGKLEGIERPALGVAVPSLKGATVLIDAGANAKVRPEHLVDFAFMGIAYSKVLGAENPRVGLLNMGSEENKGPDDIKRAYQLLKEFLGDTFFGNVEGHDINLGTVDVVVADGFSGNVALKTMEGTAKLVTSVLKESIKDGGFLSLLGALLMKRSFDKMKEKLDPRSYGGTFILGVKGIVVKAHGSSDAKAIKHAIKVAEKGIRVNIVQEIERGISHVRNSGDGR | Function: Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
Catalytic Activity: a fatty acyl-[ACP] + phosphate = an acyl phosphate + holo-[ACP]
Sequence Mass (Da): 34609
Sequence Length: 327
Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Cytoplasm
EC: 2.3.1.274
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O65984 | MRIAVDAMGGDYAPLEITKGVYKALENFNIEIVLVGNKDQLDKYVKEEKGLTVVHTTETITNNEPPVAAIRKKKDSSMAVGIDMLKKGEVDAFLSAGNTGALMAGSLLKIGRIKGIDRPALAPILPTLNGATILLDAGSNTDCKPINLFQFAIMGNVYAQKMLNIDNPKIGLFNIGAEEEKGNELTKQVYDLIKNSHLNFIGNVEGRDIAYGVADVVTCDGFVGNAILKSMEGTASVISSLLKQELQRNLLTKLGAILIYNGLKNIVKKMDYTEYGGAPLLGIKKPVIKAHGSSKSKAIFNAIRQAKTIVEMDVISHIQREIELIGDDISAAK | Function: Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
Catalytic Activity: a fatty acyl-[ACP] + phosphate = an acyl phosphate + holo-[ACP]
Sequence Mass (Da): 35929
Sequence Length: 333
Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Cytoplasm
EC: 2.3.1.274
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B5YG77 | MLKIAVDAMGGDFAPEVNILGAYEVVQDIEVEIILVGDEKKIKSFLPEKKETKGIISVIPADDVIQMDENISSALRRKNTSMRKAVELVKAGKADAVISAGHSGAMMALSFLLLGKLPNVERPAIATVMPCLKGHFILLDAGANVDCKPEHLVQFAFMGEAYHKALFNSQSPKIALLSIGEEGSKGNELTKEAFKLLKSSRLNFVGNIEGKDIFFGQADVVVCDGFVGNIVLKVGEGLAEALMKMLKREIADIITGKLGYMMIKPAIKSFRKKVDYSEYGGALLLGINGTSIICHGRSSAKAIKNAIKVATEMVKKQIYTRISESLNQTEERDESQNSVNRLLCS | Function: Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
Catalytic Activity: a fatty acyl-[ACP] + phosphate = an acyl phosphate + holo-[ACP]
Sequence Mass (Da): 37451
Sequence Length: 345
Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Cytoplasm
EC: 2.3.1.274
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B1I461 | MSALAVILVIGLSYLVGSVPTGYLIARHVKGIDIRGHGSGNIGATNVWRTLGPGWGLASLVGDTAKGIVAVLLGRAVGVPGLELLTGAAALTGHGWSVFLRFQGGKIIATSLGVLIMLPPVALATAAAVWIAVLALTRYVSLASIIAASSVPLAFALGGVGWRHVLFGLFLALVAVYKHRANIDRLLKGKESRFSFRK | Function: Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
Catalytic Activity: an acyl phosphate + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-phosphate + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 20513
Sequence Length: 198
Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Cell membrane
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B8J229 | MLEILWIALAYVLGSAPWGLVIARTFCGIDPRESGSRNTGATNVARLCGFGWGVATLLCDVLKGAVPVWLAFRINASPVFVSMVALACVLGHVFSCFMKFRGGKAVATSIGIFLPLAFWQLLASSLLCMLVIWRSGFVSLGSLTLVTALPVALAVSGQWGWLPLSLAVWAVVVWKHRENIVRLRSGTEKSWLKSKNKGAAAGNAAEGDDTQNMNPQDAGRKDG | Function: Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
Catalytic Activity: an acyl phosphate + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-phosphate + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 23862
Sequence Length: 223
Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Cell inner membrane
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Q6AQV6 | MDFIFPLISYLLGAIPFGLLIGKLAGRDVRLEGSKNIGATNVSRILGKKLGFATLLCDSLKGFLPMVLAATLLPSSENRELIVCLSGVMGVLGHMFPVYLGFKGGKGVATGLGVFLFLSPAAIAISLGVFAASVFFSGFVSVGSLLASGLIPLWLYLLGASQLKIITAGFVALLIWIKHRKNIKRLMTGTEKSWKKK | Function: Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
Catalytic Activity: an acyl phosphate + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-phosphate + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 20959
Sequence Length: 197
Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Cell inner membrane
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A4J3P2 | MVHITTVMIIIGAYLIGSIPFGFLLAYFWKGIDIRKCGSGNIGATNVWRTLGKVPGMIVLILDMIKGISAVLLAKQLENTDIAVLGVALAVMAGHSWPLWLRFKGGKIIATGAGAILALSPMPLLLAFLVWLTTVVVSRYVSLGSILGAVSLPIWMALLNQNRHYLIFSVLVASFAVWKHSSNIGRLIKGTEFKIGQKKT | Function: Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
Catalytic Activity: an acyl phosphate + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-phosphate + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 21628
Sequence Length: 200
Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Cell membrane
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Q726E5 | MGSLLWLAVAYVMGSIPFGLLFAKMFCGTDPRTGGSRNVGATNVARLCGTKVGVLTLVCDALKGAIPVAVALSISDSTVFHSLTALAALLGHLYSCFLSFKGGKAVATTVGVFLPLAFWPLVLSGIACLAVIWRSGFVSLGSLTLVTAMPAMLLLGGHWKLVPLALVVMVLVYWSHRENIGRLSRGEEKPWQKKHHDAAQGTDAGAAPEAAADAAHAGTVDCGCDCGCDAHKPSTEAAPSQETSDASAHGAEAPVAADEGDKRENEEHDNAPEASAAESKPEDKPAGKTVGKPASRSVAKPASKSAGKTGGKAADKSAGKSGKSSGQ | Function: Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
Catalytic Activity: an acyl phosphate + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-phosphate + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 33401
Sequence Length: 327
Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Cell inner membrane
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Q2RPF8 | MADLSTLMPALVLGVCALAGYLLGSVPFGLVLVRLAGLGDVRGIGSGNIGATNVLRTGRKDLALATLVLDSGKGAIAALVASALASRIAGFEDAVLAGLLAGGMAVVGHNFPIWLGFKGGKGVATTLGTLLATAWPVGLAACATWLVVAALFRYSSLAALVCLALAPAYALVLATPAHAAVFALLALLAWIRHRANIARLLKGEESRIGAKKKAAP | Function: Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
Catalytic Activity: an acyl phosphate + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-phosphate + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 21728
Sequence Length: 216
Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Cell inner membrane
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A5UZW0 | MMPTIASIALVLLAYLSGSIPFSLLVARAWGVDLRVSGSGNVGAANVWRTCGFSAFALAMGGDMLKGALPTIAAQALGLSPLAVVIVGTAAMLGHTRSIFLGFRGGKAVATGGGVVLTLAPLVALPGLAAWAVTFGITRISAVASLTAAAVCGIAAAVLLALGMLPPAYAIFVWGAVAAIVFLHRSNIHRLRTGTENRFEKLF | Function: Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
Catalytic Activity: an acyl phosphate + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-phosphate + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 20600
Sequence Length: 203
Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Cell membrane
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Q1AU71 | MLEVLLVLLGYVLGSVPTGILVGRAYGVDVRKVGSGNIGTANVMRAAGKGAAALTMLGDMLKGVAPVLLARALGAGPWVLAAVALAAVVGHCWPVFLRFRGGKGVATGAGTSIALAPPVGLGMFALWWVVALASRYTSLAAMVVTVVSPFAFLLSGQPLPYVLYTVVGGAAVLWRHRENARALLRGTERKFGGRSGGGG | Function: Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
Catalytic Activity: an acyl phosphate + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-phosphate + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 20294
Sequence Length: 199
Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Cell membrane
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Q5LX62 | MPAFDTPAMMLILWAVIGYGLGSIPFGLILTRAMGMGDLRQIGSGNIGTTNVLRTGNKGAAALTLLLDGGKGAVAVLLARAFAGEDAAQVAALAAFVGHCYPIWLGFKGGKGVATFLGLWLALAWPVGVACCLSWLAGAAVTRISSMGALVAAASSTFWLVLLDQGAGFVLGIVLTLMVFWRHRANIARLKARTEPKIGQKSA | Function: Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
Catalytic Activity: an acyl phosphate + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-phosphate + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 20999
Sequence Length: 203
Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Cell inner membrane
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A1AXL0 | MLPELLFIVLLLLSYLIGSISTAIIVCKMFNLPDSRTQGSNNPGATNVLRIGGKKAAAITLIGDGLKGAIPVLIAHYLAFNMLNVTWVILVTFLGHVYPIFFSFKGGKGVATFLGALLALSYLTGLSFIITWVFVAKVLKISSLSALISTVLTPVYFYLITNNLASTYVIILICLWIFYTHQSNIKRLLNSQENKIN | Function: Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
Catalytic Activity: an acyl phosphate + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-phosphate + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 21574
Sequence Length: 197
Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Cell inner membrane
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Q9LJ42 | MVIFSRSFLALSTTLIILALCINSSTMAQETEDLNSHSSSNSSTANKLPNDDGAWNEHAVKNPEEVAAMVDMKIKNSTERRRLGFFSCATGNPIDDCWRCDRNWHLRRKRLANCAIGFGRNAIGGRDGRYYVVTDPSDHDAVNPRPGTLRHAVIQDRPLWIVFKRDMVITLTQELIMNSFKTIDGRGVNVAIAGGACITIQYVTNIIIHGINVHDCRRTGNAMVRSSPSHYGWRTMADGDAISIFGSSHIWIDHNSLSNCADGLIDAIMGSTAITISNNYMTHHNEVMLMGHSDSYTRDKLMQVTIAYNHFGEGLIQRMPRCRHGYFHVVNNDYTHWVMYAIGGSANPTINSQGNRFLAPGNPFAKEVTKRVGSWQGEWKQWNWRSQGDLMLNGAYFTKSGAAAPASYARASSLGAKPASVVSMLTYSSGALKCRIGMRC | Cofactor: Binds 1 Ca(2+) ion. Required for its activity.
Catalytic Activity: Eliminative cleavage of (1->4)-alpha-D-galacturonan to give oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at their non-reducing ends.
Sequence Mass (Da): 48761
Sequence Length: 440
Pathway: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 2/5.
EC: 4.2.2.2
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Q9LTZ0 | MVSYSNNHFAYAFLLLLTIGNTLAFSSSLPDHVQDPNLVVDDVNRSVFNASRRSLAYLSCRTGNPIDDCWRCDPNWETNRQRLADCAIGFGKNAIGGRKGRIYVVTDPANDDPVNPRPGTLRYAVTQEEPLWIIFKRDMVIRLKKELIITSFKTIDGRGSSVHITDGPCLKIHYATNIIIHGINIHDCKPGSGGMIKDGPHHTGWWMQSDGDAVAIFGGKHVWIDHCSLSNCDDGLIDAIHGSTAITISNNHMTHHDKVMLLGHSDSYTQDKNMQVTIAFNHFGEGLVQRMPRCRHGYFHVVNNDYTHWEMYAIGGSASPTIYSQGNRFLAPNTRFNKEVTKHEDAPESKWRDWNWRSEGDMLLNGAYFRESGAEAPSTYARASSLSARPSSLVGSITTTAGTLSCRRGRRC | Cofactor: Binds 1 Ca(2+) ion. Required for its activity.
Catalytic Activity: Eliminative cleavage of (1->4)-alpha-D-galacturonan to give oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at their non-reducing ends.
Sequence Mass (Da): 45985
Sequence Length: 412
Pathway: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 2/5.
EC: 4.2.2.2
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Q9SCP2 | MMLQRSCIVLFFSLFLLVPQMVFSMLNRTLLLIPHPDPELVAYQVQWKVNASITRRQALDTTDQAGSTPCITGNPIDDCWKCDPNWPNNRQGLADCGIGFGQYALGGKGGQFYFVTDSSDDDAVNPKPGTLRYGVIQEEPLWIVFPSNMMIKLKQELIFNSYKTLDGRGANVHIVGGGCITLQYVSNIIIHNIHIHHCYQSGNTNVRSSPTHYGFRTKSDGDGISIFGSKDIWIDHCSLSRCKDGLIDAVMGSTGITISNNFFSHHNEVMLLGHSDHYEPDSGMQVTIAFNHFGEKLIQRMPRCRRGYIHVVNNDFTQWEMYAIGGSGNPTINSQGNRYTAPTNPFAKEVTKRVETPDGDWKGWNWRSEGDILVNGAFFVASGEGAEMRYEKAYSVEPKSASFITQITFHSGVLGVGGRNNNLGMWTTTGSEGTSGLDSYNDYTDEMSGAGSTNRLSFSVLVFLLSSISYLVVFTSSTQMFML | Cofactor: Binds 1 Ca(2+) ion. Required for its activity.
Catalytic Activity: Eliminative cleavage of (1->4)-alpha-D-galacturonan to give oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at their non-reducing ends.
Sequence Mass (Da): 53593
Sequence Length: 483
Pathway: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 2/5.
EC: 4.2.2.2
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Q93Z04 | MLLQNFSNTIFLLCLFFTLLSATKPLNLTLPHQHPSPDSVALHVIRSVNESLARRQLSSPSSSSSSSSSSSSSSCRTGNPIDDCWRCSDADWSTNRQRLADCSIGFGHGTLGGKNGKIYVVTDSSDNNPTNPTPGTLRYGVIQEEPLWIVFSSNMLIRLKQELIINSYKTLDGRGSAVHITGNGCLTLQYVQHIIIHNLHIYDCKPSAGFEKRGRSDGDGISIFGSQKIWVDHCSMSHCTDGLIDAVMGSTAITISNNYFTHHDEVMLLGHDDNYAPDTGMQVTIAFNHFGQGLVQRMPRCRRGYIHVVNNDFTEWKMYAIGGSGNPTINSQGNRYSAPSDPSAKEVTKRVDSKDDGEWSNWNWRTEGDLMENGAFFVASGEGMSSMYSKASSVDPKAASLVDQLTRNAGVFGGPRDDQGQSGNSYSPYGGDGGGGGSSGGSSGGGMDVMGGTTRGSSSSSGDDSNVFQMIFGSDAPSRPRLTLLFSLLMISVLSLSTLLL | Cofactor: Binds 1 Ca(2+) ion. Required for its activity.
Function: Susceptibility factor required for infection by most powdery mildews, but not by unrelated pathogens. Exact function not known, but clearly affects cell wall composition.
Catalytic Activity: Eliminative cleavage of (1->4)-alpha-D-galacturonan to give oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at their non-reducing ends.
Location Topology: Lipid-anchor
Sequence Mass (Da): 53929
Sequence Length: 501
Domain: The C-terminal domain not found in other pectate lyase-like protein is required for PMR6 function since the pmr6-2 mutation confers resistance by introducing a frameshift in the mature mRNA which eliminates the C-terminal domain.
Pathway: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 2/5.
Subcellular Location: Cell membrane
EC: 4.2.2.2
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Q9SVQ6 | MVVARTLFSISATLIIFLALFLHVNAVQETREPKHESSRNTSTVDNLSDGEWHEHAVKDPEEIAAMVDMSIRNSTYRRKLGFFSSCSTGNPIDDCWRCDKKWHRRRKRLADCAIGFGRNAVGGRDGRYYIVTDPSDHDPVTPKPGTLRYAVIQDEPLWIVFKRDMVITLSQELIMNSFKTIDGRGVNVHIAGGACLTVQYVTNIIIHGINIHDCKRTGNAMVRSSESHYGWRTMADGDGISIFGSSHIWIDHNSLSSCADGLIDAIMGSTAITISNNYLTHHNEAILLGHTDSYTRDKMMQVTIAYNHFGEGLIQRMPRCRHGYFHVVNNDYTHWEMYAIGGSANPTINSQGNRFLAPGNRFAKEVTKRVGAGKGEWNNWNWRSQGDLMLNGAYFTSSGAGASANYARASSLAAKSSSLVGMLTSSSGALKCRIGTLC | Cofactor: Binds 1 Ca(2+) ion. Required for its activity.
Catalytic Activity: Eliminative cleavage of (1->4)-alpha-D-galacturonan to give oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at their non-reducing ends.
Sequence Mass (Da): 48548
Sequence Length: 438
Pathway: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 2/5.
EC: 4.2.2.2
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Q944R1 | MASSSQKLISVCVAVLVVLALTAMIFRNSEISLSRKLKTEVIQSSNSSTMAAIRKLKTEEFQSLNSSTMAATRLDGEPQQQQHAVADDPDMVADEVAKLVQMSEQNRTARRKLGFFSCGTGNPIDDCWRCDRNWHKNRKRLADCGIGFGRNAIGGRDGRFYIVTDPTDEDVVNPKPGTLRHAVIQEEPLWIVFKRDMVIELKQELIMNSFKTIDARGSNVHIANGACITIQFITNVIIHGLHIHDCKPTGNAMVRSSPSHFGWRTMADGDAVSIFGSSHIWIDHNSLSHCADGLVDAVMGSTAITVSNNHFTHHNEVMLLGHSDSYTKDKLMQVTIAYNHFGEGLVQRMPRCRHGYFHVVNNDYTHWEMYAIGGSAEPTINSQGNRYAAPMDRFAKEVTKRVETDASEWKKWNWRSEGDLLLNGAFFRPSGAGASASYGRASSLAAKPSSMVDTITSTAGALGCRKGRPC | Cofactor: Binds 1 Ca(2+) ion. Required for its activity.
Catalytic Activity: Eliminative cleavage of (1->4)-alpha-D-galacturonan to give oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at their non-reducing ends.
Sequence Mass (Da): 51936
Sequence Length: 470
Pathway: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 2/5.
EC: 4.2.2.2
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O65456 | MTLFTVSCLLVVLFLCHSLVHAENNGYYGYTPTVANYLPEKPQNIMNPVDSCWRLKSDWAANRKDLADCVVGFGSSTLGGKKGNLYVVTNPYDNAQNPQPGSLRYGVIQAKPLWITFAKDMVITLENELMVNSYKTIDGRGAKVEIAYGPCITIQDVTNVIVHGISIHDCKPGKYGMVRSSPTHVGHRKGSDGDAIAIFGSSNIWIDHCYLASCTDGLIDVIHASTGITISNNYFTQHDKVMLLGHNDDFVQDVKMKVTVAFNHFGPGLVERMPRVRRGYAHVANNRYDKWIMYAIGGSADPTIFSEGNYFIASDKSNSKEVTKREVKGGWNNWRWRTSKDVFKNGAYFVPSGYGSISLPYSSAQRFTVAPGNLVPSLTADAGPLNCNRNGPCY | Cofactor: Binds 1 Ca(2+) ion. Required for its activity.
Catalytic Activity: Eliminative cleavage of (1->4)-alpha-D-galacturonan to give oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at their non-reducing ends.
Sequence Mass (Da): 43476
Sequence Length: 394
Pathway: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 2/5.
EC: 4.2.2.2
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Q9C5M8 | MKMQTKKLFITIVSFLLYAPLFLSSPVPDPESVVEEVHKSINASVAGRRKLGYLSCTTGNPIDDCWRCDPHWEQHRQRLADCAIGFGKNAIGGRDGRIYVVTDSGNDNPVSPKPGTLRHAVVQDEPLWIIFQRDMTIQLKEELIMNSFKTIDGRGASVHISGGPCITIQYVTNIIIHGIHIHDCKQGGNAMVRSSPRHFGWRTISDGDGVSIFGGSHVWVDHCSFSNCEDGLIDAIMGSTAITLSNNHMTHHDKVMLLGHSDTYSRDKNMQVTIAFNHFGEGLVQRMPRCRHGYFHVVNNDYTHWEMYAIGGSANPTINSQGNRFLAPNIRFSKEVTKHEDAPESEWKRWNWRSSGDLLLNGAFFTPSGGAASSSYAKASSLGAKPSSLVGPLTSTSGALNCRKGSRC | Cofactor: Binds 1 Ca(2+) ion. Required for its activity.
Catalytic Activity: Eliminative cleavage of (1->4)-alpha-D-galacturonan to give oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at their non-reducing ends.
Sequence Mass (Da): 45014
Sequence Length: 408
Pathway: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 2/5.
EC: 4.2.2.2
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P24396 | MSTLFFTFSLLLLAPLLVISSIQDPELVVQDVHRSINASLTRRNLGYLSCGSGNPIDRLLAMQPQLGKKSPAFSYCAIGFGKNAIGGKNGRIYVVTDSGNDDPVNPKPGTLRHAVIQDEPLWIIFKRDMVIQLKQELVMNSYKTIDGRGASVHISGGPCITIHHTSNIIIHGINIHDCKQSGNGNIRDSPNHSGWWDVSDGDGISIFGGKNIWVDHCSLSNCHDGLIDAIHGSTAITISNNYFTHHDKVMLLGHSDSFTQDKGMQVTVAFNHFGEGLVQRMPRCRHGYFHVVNNDYTHWEMYAIGGSAAPTINSQGNRFLAPNEKYRKEVTKHEDAPESQWRSWNWRSEGDLMLNGAYFRQTGAGASSSSTYARASSLSARPSSLVGSITTNAGPVNCKKGSRC | Cofactor: Binds 1 Ca(2+) ion. Required for its activity.
Function: May have a role in the development of the transmitting tissue of the style and/or in the events related to pollination such as some aspect in the facilitation of compatible pollen tube growth.
Catalytic Activity: Eliminative cleavage of (1->4)-alpha-D-galacturonan to give oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at their non-reducing ends.
Sequence Mass (Da): 44298
Sequence Length: 404
Pathway: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 2/5.
Subcellular Location: Secreted
EC: 4.2.2.2
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P17872 | MVKSILASVLFAATALAASRMTAPSGAIVVAKSGGDYDTISAAVDALSTTSTETQTIFIEEGSYDEQVYIPALSGKLIVYGQTEDTTTYTSNLVNITHAIALADVDNDDETATLRNYAEGSAIYNLNIANTCGQACHQALAVSAYASEQGYYACQFTGYQDTLLAETGYQVYAGTYIEGAVDFIFGQHARAWFHECDIRVLEGPSSASITANGRSSESDDSYYVIHKSTVAAADGNDVSSGTYYLGRPWSQYARVCFQKTSMTDVINHLGWTEWSTSTPNTENVTFVEYGNTGTGAEGPRANFSSELTEPITISWLLGSDWEDWVDTSYIN | Function: Involved in maceration and soft-rotting of plant tissue.
Catalytic Activity: [(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O = [(1->4)-alpha-D-galacturonosyl](n) + n H(+) + n methanol
Sequence Mass (Da): 35715
Sequence Length: 331
Pathway: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5.
Subcellular Location: Secreted
EC: 3.1.1.11
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P86085 | IDAFQDTLYTHTLRTYLGRPWK | Catalytic Activity: [(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O = [(1->4)-alpha-D-galacturonosyl](n) + n H(+) + n methanol
Sequence Mass (Da): 2696
Sequence Length: 22
Pathway: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5.
Subcellular Location: Secreted
EC: 3.1.1.11
|
Q42920 | MEICNEVLDYAVDGIHKSVGTLDQFDFHKLSEYAFDLKVWLTGTLSHQQTCLDGFANTTTKAGETMTKVLKTSMELSSNAIDMMDAVSRILKGFDTSQYSVSRRLLSDDGIPSWVNDGHRRLLAGGNVQPNAVVAQDGSGQFKTLTDALKTVPPKNAVPFVIHVKAGVYKETVNVAKEMNYVTVIGDGPTKTKFTGSLNYADGINTYNTATFGVNGANFMAKDIGFENTAGTGKHQAVALRVTADQAIFYNCQMDGFQDTLYVQSQRQFYRDCSISGTIDFVFGERFGVFQNCKLVCRLPAKGQQCLVTAGGREKQNSASALVFQSSHFTGEPALTSVTPKVSYLGRPWKQYSKVVIMDSTIDAIFVPEGYMPWMGSAFKETCTYYEYNNKGPGADTNLRVKWHGVKVLTSNVAAEYYPGKFFEIVNATARDTWIVKSGVPYSLGPM | Function: Acts in the modification of cell walls via demethylesterification of cell wall pectin.
Catalytic Activity: [(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O = [(1->4)-alpha-D-galacturonosyl](n) + n H(+) + n methanol
Sequence Mass (Da): 49133
Sequence Length: 447
Pathway: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5.
Subcellular Location: Secreted
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Q43043 | MVKLLNSTRELSINALSMLNSFGDMVAQATGLNRKLLTTDSSDATARRLLQISNAKPNATVALDGSGQYKTIKEALDAVPKKNTEPFIIFIKAGVYKEYIDIPKSMTNVVLIGEGPTKTKITGNKSVKDGPSTFHTTTVGVNGANFVAKNIGFENTAGPEKEQAVALRVSADKAIIYNCQIDGYQDTLYVHTYRQFYRDCTITGTVDFIFGNGEAVLQNCKVIVRKPAQNQSCMVTAQGRTEPIQKGAIVLQNCEIKPDTDYFSLSPPSKTYLGRPWKEYSRTIIMQSYIDKFIEPEGWAPWNITNFGRDTSYYAEYQNRGPGAALDKRITWKGFQKGFTGEAAQKFTAGVYINNDENWLQKANVPYEAGMMKV | Function: May play a role in pollen germination and/or tube growth.
Catalytic Activity: [(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O = [(1->4)-alpha-D-galacturonosyl](n) + n H(+) + n methanol
Sequence Mass (Da): 41467
Sequence Length: 374
Pathway: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5.
Subcellular Location: Secreted
EC: 3.1.1.11
|
Q43062 | MPYLLMASHNPLPAGKQLLLLVLLCAFFSSSFIPFASCSITDDLQTQCLKVSATEFAGSLKDTIDAVQQVASILSQFANAFGDFRLANAISDCLDLLDFSADELNWSLSASQNQKGKNNSTGKLSSDLRTWLSAALVNQDTCSNGFEGTNSIVQGLISAGLGQVTSLVQELLTQVHPNSNQQGPNGQIPSWVKTKDRKLLQADGVSVDAIVAQDGTGNFTNVTDAVLAAPDYSMRRYVIYIKRGTYKENVEIKKKKWNLMMIGDGMDATIISGNRSFVDGWTTFRSATFAVSGRGFIARDITFENTAGPEKHQAVALRSDSDLSVFYRCNIRGYQDTLYTHTMRQFYRDCKISGTVDFIFGDATVVFQNCQILAKKGLPNQKNSITAQGRKDPNEPTGISIQFCNITADSDLEAASVNSTPTYLGRPWKLYSRTVIMQSFLSNVIRPEGWLEWNGDFALNSLFYGEYMNYGPGAGLGSRVKWPGYQVFNESTQAKNYTVAQFIEGNLWLPSTGVKYTAEFGV | Function: May have roles in the deposition of pectin in developing tissues and in the wall loosening and cell separation that occurs in cell expansion, fruit ripening and abscission.
Catalytic Activity: [(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O = [(1->4)-alpha-D-galacturonosyl](n) + n H(+) + n methanol
Sequence Mass (Da): 57397
Sequence Length: 522
Pathway: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5.
Subcellular Location: Secreted
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P24791 | MQSTTLYLKTAAFLGGCSLFAATALAATSTATRPQLSNADARAYTIASYMASFGTIGSLTTDNWDPTGGVGAVSGFRANYAVAADGSAQYKTVQAAIDAAVADGGVARKYISVKAGTYNELVCVPESAPPITLYSLDANANNTVIVYNNANPTPASGAKTNPCMGTSSNATVGTVRSATAMVRASNFNARNLTFKNSYVEGTFADNNQSAVALAVRGDKAILENVSVIGNQDTLYLGATNNTMVIRAYFKNSFIQGDTDFIFGAGTAVFHGCTIQYTAARLGARATSYVFAPSTAPDNPHGFLAINSTFNATGNASNNSTHLGRAWDQGVSGTSAYINGSSPNGQVVIRDSSLGAHIRLADPWGPSTAGRPYCSSKCAYSANRFFEYNNTGAGSGN | Function: Involved in maceration and soft-rotting of plant tissue.
Catalytic Activity: [(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O = [(1->4)-alpha-D-galacturonosyl](n) + n H(+) + n methanol
Sequence Mass (Da): 41016
Sequence Length: 396
Pathway: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5.
Subcellular Location: Secreted
EC: 3.1.1.11
|
E7CIP7 | MKIIVLLLLAVVLASADQTAPGTASRPILTASESNYFTTATYLQGWSPPSISTSKADYTVGNGYNTIQAAVNAAINTGGTTRKYIKINAGTYQEVVYIPNTKVPLTIYGGGSSPSDTLITLNMPAQTTPSAYKSLVGSLFNSADPAYSMYNSCASKSGTIGTSCSTVFWVKAPAVQIVNLSIENSAKNTGDQQAVALQTNSDQIQIHNARLLGHQDTLYAGSGSSSVERSYYTNTYIEGDIDFVFGGGSAIFESCTFYVKADRRSDTAVVFAPDTDPHKMYGYFVYKSTITGDSAWSSSKKAYLGRAWDSGVSSSSAYVPGTSPNGQLIIKESTIDGIINTSGPWTTATSGRTYSGNNANSRDLNNDNYNRFWEYNNSGNGA | Function: Pectinesterase which probably plays an important role in the digestion of plant cell walls.
Catalytic Activity: [(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O = [(1->4)-alpha-D-galacturonosyl](n) + n H(+) + n methanol
Sequence Mass (Da): 40697
Sequence Length: 382
Pathway: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5.
Subcellular Location: Secreted
EC: 3.1.1.11
|
P53514 | MLIPYSPHTIWKTICATLLLSLAFFSQAEQDDSVEFNIHMLDAEDRDNVDLSRFSTSNYIIPGMYYLDIRLNGRDFPRQNINYIEVADNHSVACIDPTLLKKLTINQENQKYIKQISPDCFDISQLPGISIKNDGGVLDITLPRSLMKYEESDWTPPELWDSGVSGLIFDYTLTGTSTRPNKGNNNNTLTGYGQAGLNLGEWRLRAEYQGNYSSEYSSNNRFDWNQIYAYKPLPDLAAKLTVGETYLNSQIFDSFRFTGANLQSDERMLPPSLQGYAPEIHGIANTNAKVTVTQNGRLIYETTVPAGPFVINHLQNTVQGQLDVRVEEQNGKINEFQVQTANLPYMTRPGSVRFNTSLGQSSVNNHKMQGPLFYQGDFSWGMNNTWSLYGGTLLTAKDYNAWSLGIGHDMGRFGTLSGDITQSYSKTYDNEKINGMSFKLNYAKTFDEYHSTITFAGYRFSEKTFRSFSQYIDERYNGINNNGYEKEMYTITGNKTFWADDAEKSTTLYLSYRHQNYWDKNTQEQYGVTVSRNFSIMGIEQINTNLSAFRTQYKGNTDDTLSFNISLPLGSGRNIGYNLQDNNGKVTQMASYADNRDYNNLWRIRAGLSSDKKANTDGYYQHRSQYAEINANASYQQDNYLAVGATIKGGFTATRYGAALHSSSMTSSTARIMVDTDGVAGVPFNGQSTTTNRFGIGVLTDLTSYNNVDARIDVDKMDQDIETRKAIASTTLTEGAIGYYQFPVRQGERLMAVLQTTDNKYPPFGAEVTNQKGESIGMVMEEGLVYIAGVNLNESLNVIWNGKTQCSITIPAEITDPLKHQSLVCQDR | Function: Involved in the export and assembly of PMF fimbrial subunits across the outer membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 93108
Sequence Length: 828
Subcellular Location: Cell outer membrane
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O74837 | MSNVTLSDFLLIVLSFFVPFIVVGIRRGFCTADFLINICLCALGIPGIIHAIYIVIKYPRTVRLDIENSPNDPLVRYTPNPEHAVSPHSGPAPPSYSSLASNDNKHQSP | Function: Has a role in meiosis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 11962
Sequence Length: 109
Subcellular Location: Vacuole membrane
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Q9P824 | MNSEKIIEVIIAIFLPPVAVFMKCGATTPLWINLVLCIFIWFPAILHALYVVLKD | Function: Plays a role in the regulation of membrane potential.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 6230
Sequence Length: 55
Subcellular Location: Membrane
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Q2HAR0 | MPFTASDICKIIFAVILPPLGVFLERGCNSDLLINILLTILGVGSILASMNPA | Function: Plays a role in the regulation of membrane potential. Could mediate a proton leak (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 5587
Sequence Length: 53
Subcellular Location: Cell membrane
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P0CS19 | MAFTCSDIFKIILAIILPPLGVFLERGCGADLLINILLTILGYIPGIIHALYIILKY | Function: Plays a role in the regulation of membrane potential. Could mediate a proton leak (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 6275
Sequence Length: 57
Subcellular Location: Cell membrane
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Q6BVN0 | MAFTCSDIFKIIIAIILPPLGVFLERGCASSFWINIVLTILGYIPGIIHALYVILKY | Function: Plays a role in the regulation of membrane potential. Could mediate a proton leak (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 6356
Sequence Length: 57
Subcellular Location: Cell membrane
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Q9C1W4 | MALTGSDIFKVIFAIILPPLGVFLERGCGADVIINILLCCLGYVPGIIHALYIILKY | Function: Plays a role in the regulation of membrane potential. Could mediate a proton leak. Regulated by the spc1-atf1 pathway and so expression is stress-induced.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 6179
Sequence Length: 57
Subcellular Location: Cell membrane
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P87284 | MDSAKIINIILSLFLPPVAVFLARGWGTDCIVDIILTILAWFPGMLYALYIVLQD | Function: Plays a role in the regulation of membrane potential. Could mediate a proton leak.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 6138
Sequence Length: 55
Subcellular Location: Cell membrane
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Q89SS3 | MTVTDIASRTYNHSWRLDPIIRSLLDTDFYKLLMLQMIREDYSNQQVTFSVINRSRHVRLAEIIDEGELRAQLDHARTIRFTKKELIWLAGNTFYGKTHMFSADFIRWLAEFRLPEYELRKVEGQYELHFHGPWTHTTMWEIPALAILNELRSRAAIKGRGRFELDVLYARAKAKLWTKVERLRKLENLRLSDFGTRRRHGFLWQRWCVEAVKEGLGPSFIGTSNVLLAMDNDLEAIGTNAHELPMVAAGLAKDDEELRWAPYRILDQWRQTYGGNLLIALPDAFGTKAFLRDAPEWVADWTGFRPDSAPPIQAGEEIIAWWEKKGRNPRDKLLVFSDAMDVGSIEETYHHFTGRVRLSFGWGTNLTNDFVGCAPDGSFNLDPISLVCKVSSVDGHPAVKLSDNPEKATGLPSEIERYLRVFGDVGRVRKPVLV | Function: Catalyzes the synthesis of beta-nicotinate D-ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate at the expense of ATP.
PTM: Transiently phosphorylated on a His residue during the reaction cycle. Phosphorylation strongly increases the affinity for substrates and increases the rate of nicotinate D-ribonucleotide production. Dephosphorylation regenerates the low-affinity form of the enzyme, leading to product release.
Catalytic Activity: 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O + nicotinate = ADP + diphosphate + nicotinate beta-D-ribonucleotide + phosphate
Sequence Mass (Da): 49902
Sequence Length: 434
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-ribonucleotide from nicotinate: step 1/1.
EC: 6.3.4.21
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Q55G10 | MSQSNTPLKRKKTENGYSENGSTTGATSNQIRELKRATTVDYVYRDQESKDKIKPLNGFVTPLLTDLYQITMAYSLWKNNRHEIPAVFDLYFRKSPFGGEFTVFAGLEEVIRFVSDFHYTKEEVGFIKEMIPDCEQEFLDYLSKLDSSSVTLYAMKEGSVVFPRVPLLRVEGPMILCQLFETTLLCLVNFASLVATNAARHRLAVGKEKVMLEFGLRRAQGPDGAMSASRYSYLGGADGTSNVLAHCFFGIPIRGTHAHSFITNYSGPDELLDASIKDTNGNVHNLLEMSQKYRDELGYTATNLSELVAFVAYARTFPNGLVALVDTYDTLASGVPNFICVALALHQLGYKAVGIRLDSGDLSYLSKASRKLFKQIGEQFKIDYFEKFSIVASNDLNEPTIIALNRQGHEIDVFAIGTNLVTCQAQPALGCVYKLVEINGSPRIKLSQEANKITLPGRKTAYRLFGSEGHPLVDLLVDDNDMIKDGSKQIPQVGKKVLCLHPFEEQKRVIVTPVQIEKLHHIVFEKGQLTMPLPALNDIREYCFQQISKVREDHLRNSNPTPYKVSVTKELFDTLHNLWLDSVPIKEMK | Cofactor: Activity is highest with Mn(2+).
Function: Catalyzes the first step in the biosynthesis of NAD from nicotinic acid, the ATP-dependent synthesis of beta-nicotinate D-ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate. Helps prevent cellular oxidative stress via its role in NAD biosynthesis.
PTM: Transiently phosphorylated on a His residue during the reaction cycle. Phosphorylation strongly increases the affinity for substrates and increases the rate of nicotinate D-ribonucleotide production. Dephosphorylation regenerates the low-affinity form of the enzyme, leading to product release.
Catalytic Activity: 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O + nicotinate = ADP + diphosphate + nicotinate beta-D-ribonucleotide + phosphate
Sequence Mass (Da): 66085
Sequence Length: 589
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-ribonucleotide from nicotinate: step 1/1.
EC: 6.3.4.21
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Q9VQX4 | MNDRELGCAGGQFMDRGRMNQNGVVQPLLTDLYQITMAYAYWKSDKTDDTAVFDLFFRNNPFHGEFTIFAGLEECLKFLDSFHYSQSDIEYLKQTLPEGIEHEFFEYLGNLTARDVTLYAIDEGTVAFPRVPIIKIEGPLIIVQLLETTLLTLVNYASLMATNAARYRMVAGKHVKLLEFGLRRAQGPDGGLSASKYSYTGGFDGTSNVLAGKLFNIPVKGTHAHAYITSFSSIGELKTRLIKHKQTGILEDLLEHAVRHRALLSHLLDVSTEESSEGELAAMVSYAIAFPDGFMALVDTYDVKRSGLLNFSAVALALNDLGYHALGIRIDSGDLAYLSCLARETFEKVAERFKVPWFNKLTIVASNDINEDTILSLNEQGHKIDCFGIGTHLVTCQRQPALGCVYKLVEINGQPRIKLSQDVEKVTMPGNKNAYRLYSADGHALIDLLQKVSEPPPAVGQKVLCRHPFQESKRAYVIPSHVESLYKVYWKSGKICQQLPTLEQVREKVQISLKTLRNDHKRTLNPTPYKVAVSDNLYNFIHDLWLQNAPIGELS | Cofactor: Activity is highest with Mn(2+).
Function: Catalyzes the first step in the biosynthesis of NAD from nicotinic acid, the ATP-dependent synthesis of beta-nicotinate D-ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate. Helps prevent cellular oxidative stress via its role in NAD biosynthesis.
PTM: Transiently phosphorylated on a His residue during the reaction cycle. Phosphorylation strongly increases the affinity for substrates and increases the rate of nicotinate D-ribonucleotide production. Dephosphorylation regenerates the low-affinity form of the enzyme, leading to product release.
Catalytic Activity: 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O + nicotinate = ADP + diphosphate + nicotinate beta-D-ribonucleotide + phosphate
Sequence Mass (Da): 62165
Sequence Length: 555
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-ribonucleotide from nicotinate: step 1/1.
EC: 6.3.4.21
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P10938 | MSGTDRSQAAGAVPDSDPGLAAVSSAYQRFEPRAYLRNNYAPPRGDLSCPDGVGPWKLRCLAQTFATGEVSGRTLIDIGSGPTIYQLLSACAHFEDITMTDFLEVNRQELRLWLREEPGAFDWSVYSQHVCLIEGKGESWQEKECQLRARVKRILPIDVHRPQPLGAGGLAPLPADALVSAFCLEAVSPDLASFQRALDHITTLLRPGGHLLLIGALEESWYLAGEARLAVVPVREEEVREALVRTATRCGICARTPMPAHLQTGVDDVKGIFFTRAQKKVGV | Function: Catalyzes the transmethylation of nonepinephrine (noradrenaline) to form epinephrine (adrenaline), using S-adenosyl-L-methionine as the methyl donor . Other substrates include phenylethanolamine and octopamine (By similarity). Also methylates normetanephrine .
PTM: The N-terminus is blocked.
Catalytic Activity: phenylethanolamine + S-adenosyl-L-methionine = H(+) + N-methylphenylethanolamine + S-adenosyl-L-homocysteine
Sequence Mass (Da): 30918
Sequence Length: 283
Pathway: Catecholamine biosynthesis; (R)-adrenaline biosynthesis; (R)-adrenaline from (R)-noradrenaline: step 1/1.
EC: 2.1.1.28
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P10937 | MDRGSDPKHTAGMDSDSDPGQAEVALAYQRFEPRAYLRNNYAPPRGDLSNPDGVGPWKLRCMAQVFATGEVSGQVLIDIGSGPTIYQLLSACAHFEDITMTDFLEVNRQELGLWLREEPGAFDWSVYSQHVCLIEDKGESWQEKERQLRARVKRVLPIDVHKPQPLGASGLAPLPADALVSAFCLEAVSPDLPSFRQALYHITTLLRPGGNLLFIGALEESWYLAGEARLSVVPVSEEEVREALVCSGYEVRDLRTYIMPAHLRTGVDDVKGIFFAWAQKIEVQV | Function: Catalyzes the transmethylation of nonepinephrine (noradrenaline) to form epinephrine (adrenaline), using S-adenosyl-L-methionine as the methyl donor (By similarity). Other substrates include phenylethanolamine, octopamine and normetanephrine .
Catalytic Activity: phenylethanolamine + S-adenosyl-L-methionine = H(+) + N-methylphenylethanolamine + S-adenosyl-L-homocysteine
Sequence Mass (Da): 31670
Sequence Length: 285
Pathway: Catecholamine biosynthesis; (R)-adrenaline biosynthesis; (R)-adrenaline from (R)-noradrenaline: step 1/1.
EC: 2.1.1.28
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A1R0N0 | MRKILKLKVGREDLILETGLLAKQANGAVLATYGGSTVLATVCCSDSARENLDFVPLSVEYNEKYYAAGKIPGGFIKREGKPKDKEVLVSRLIDRPMRPLFDKRFGREIQVVPTTLSTDQMNPPDIVGMNAAFAAVFLSDIPFNGPIAAVRIAYLNSEFIVNPSFDEIQDSILDIVVAGSLDGITMVEGGANEVSEEVLLAAIDQAYEYIKQICNLQKEFILIVGEREKLPLAYEERVFEFKAELKDFIYSELKDACFVKGKLNRDKAIKLVKQKAYEHFSSVSQVDEENETLFYKALDDFEQEIVRRSILENNLRTDGRNPTQIRDIVAEVDLLRRTHGSALFTRGETQALAVTTLGTSIDEQIMDDIDGDKRLNFMLHYNFPPFSVGETGRLMTGRREIGHGHLAQRSLEAMLPKKDDFPYTIRVVSEILESNGSSSMATVCSGSMSLMAAGVPVKEQVAGIAMGLVSEGDKYVILSDILGEEDHLGDMDFKVAGTKNGITGFQMDIKISNVTKQLMKDALAQARIGRMHILSIMDSVISRSRDDISVNAPKIIQLQIDIDKISLVIGSTGKTVKAITDEFEVRVQIEQDGRITLFGTDSLKMQKAKARIESIVREPKIGEIYEGVVKKINSFGAFIELTPTKEGFLSNRPKSRDDRYGDMRHSRYGSGRHSRYGRDSRNTFAMRPPRLEEGQMVKVRISDIDKFGKIELELVRD | Function: Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Catalytic Activity: phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n)
Sequence Mass (Da): 80046
Sequence Length: 717
Subcellular Location: Cytoplasm
EC: 2.7.7.8
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C0R0E0 | MVTVKSVFCGEELILETGLLAKQAHGSVTLRLGNTTILATVVAAKEPNLESDFFPLTVNYNEKYYAGGKIPGGFFKREAKPRDKEILISRIIDRPLRPLFPEGFRNEVQIIPTVLSVDTDMPTDALALIASSAALTISWIPFGGPVAAVRIGYKNGEYIINPKNSELSTSELDIIVAGSKDAILMIEGEAKEVSEEVFIGAIELAHKEMQKYIDMQNEMASLCGTQKIEQELFEFDADLVKMVTEYGRDKIESANYNPDKTKRNESMDNAFNEIEEYIKTKVEDEKLISQVKGICHSIEEEIVREAIVEKCMRPDGRALDEIRPITTMTNLIPRVHGSALFTRGQTQCLSIVTLGSEKDAQLMDDIYGKENKTFMLHYNFPPFSVGEVGRYGAPGRREIGHGNLAERSFNAVLPPKDKFPYTIRVVAEILESNGSSSMATICASTMSLLSAGVPLNASVAGIAMGLATYKDGYKILTDIQGVEDHLGDMDFKVAGTRKGITAFQLDIKLTGISAQILKEALEQAKKARYFILDKIDATIANAGEISDFAPKYKTMDVNPEKIRVLIGPGGKNIKAIIEETGSDVEIQDSGVVNIFAPDTPTLDKTIKLINSYVKDPEVGEVYDGIVKDIKDFGAFVEILPGVEGLCHISELAYKHVMNVEEVLKIGDEVKVKILDVKGGKYSLSRKALLEKPADYVEEEYNKKEKKHGKKRF | Function: Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Catalytic Activity: phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n)
Sequence Mass (Da): 78604
Sequence Length: 712
Subcellular Location: Cytoplasm
EC: 2.7.7.8
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C4L6J6 | MLGTKQVFSTEWGGRPLSVEVGQLAKQANGSALVRYGDTVVLATVTASKAPKDLDFFPLTVNYEEKLYSVGKIPGGFLRREGRPGENAILTSRLIDRPIRPLFPDGFRHDIQVMIYVMSNDPDCSAEMAGMLGTSIALSISDVPFDGPIAGVTVGRVDGEFVINPTTAQLEKTDLELQVAGTSTAINMVEAGANEVPEDVMLESILFGHEEIKRLIAFQQEIVEAVGKPKFEYTVSKYDEALTAELEAARPEIVEAVQVEEKHARDEAINEVIAKYVAMYEARLADEPSKLGEVSGILNKFVKDEVRRLITVEKVRPDGRRPDVIRPLASEVGLLPRAHGVGLFTRGQTQVMSVATLGVIGDAQIIDGIGLEENKRFMHHYNFPPFSVGEARPVRAPGRREIGHGALGERALLPIIPKEADFPYTIRLVSEVLESNGSSSQASICGSTLALMDAGVPIKAPVAGIAMGLIMEGEHYTVLTDIQGLEDHLGDMDFKVAGTKDGITALQMDIKIAGITREILEEALEQARVGRLHILDHMLETLETPRTQLSKYAPKIVTMTINPDKIRDVIGPGGKMINSIIDQTGVKIDIEQDGTVFIASTDQEGIDLAMSMIGDIVREVVVGEVYDATVRRIEKFGAFVELFKGKDALVHVSEFSLERVANVEDVVKLGDSIQVKVTEIDDKGRVNASRKALILEGLSPEEREAYEAKRKAARESRPPRDSRPPRRDGDRRPPRSTN | Function: Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Catalytic Activity: phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n)
Sequence Mass (Da): 80709
Sequence Length: 738
Subcellular Location: Cytoplasm
EC: 2.7.7.8
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B0S1D9 | MIKKYEYDLCGKKIEVTIGKVAEQANGACLIQSGETVLLVTAVGSKEPREGVDFFPLTCDFEEKLYSVGKIPGGFIKREGRPSEKATLTARLIDRPLRPLFPEGYHNDVQVIATALSVDQDNTPDILAMIGSSIALSISDIPFLGPTGSVAVGMIDGEFIINPTKEQREKSDLELTVAGTKDAIMMVEAGCNNITEQQVLKAILRAHEEIKKICEFIESIQKECGKPKQEFIQPEKNIELDEEVKSFCIEDLKKITVNEDKLDREDHINTLKRSVVDYFVEKYDESIASKVSTIYDDLEKSEVRRLILEDYIRPDNRKLDQIREITCDVDILPRPHGSGLFKRGQTQVLSVTTLGTPSDAQVLDGLIEQEDKRYMHQYNFPPYSVGDARPLRSPGRREIGHGALAERALLPVIPSEEEFPYTIRVVSEVLSSNGSSSQASVCGSTLSLLDAGVPIKEPVAGIAMGLIKEDDNVVILSDIQGLEDHLGDMDFKVAGTKDGITALQMDIKITGISEEILTEALERARVGRLHILSLMNECISEPNKEISKYAPRIMVINIAPEKVREVIGPGGKVINKIIDETGVKIDTEDDGKITVAGENTESAQRAIDMIKEIVREPEIGEKYLGRVTKIMNFGAFVEILPGKEGLLHISNIAHERTNKVEDVLKENDEIMVKLMDIDDQGKMTLSRKALLPKPERKEKKNFDKKSEDQNSEDK | Function: Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Catalytic Activity: phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n)
Sequence Mass (Da): 79341
Sequence Length: 714
Subcellular Location: Cytoplasm
EC: 2.7.7.8
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A6H185 | MIPQLFVESIDLGDGRNITIETGRLAKQADGSVVVRIGKTVILGTVVSSRKATPGIDFLPLTVDYREKFAAAGRFPGGFFKREARPSDSEVLTMRLVDRVLRPLFPSDYHAEVQVMIQLMSHDEEVMPDALAGLAASAALALSDIPFETLISEARVGRIDGKFIINPSRAQLELSDIDMMIGASTDSIAMVEGEMKEISEAEMLEAIKFAHEHIKVQIAAQERLAAAFGKKEVRTYEKEKSDDAIYAKVKEAAYDKIYNIAKVGSAKQERTAAFDAVKEEVKALFTEEELAENGDLVSKYFYKTNKEAVRNVTLDLGTRLDGRKTTEIRPIWCEVDYLPSVHGSALFTRGETQALATATLGTSREANQIDSPSQQGEEKFYLHYNFPPFSTGEARPLRGTSRREVGHGNLAQRALKNMIPADCPYTIRVVSEVLESNGSSSMATVCAGTLSLMDAGIQMIRPVSGIAMGLITDGERFAVLSDILGDEDHLGDMDFKVTGTSEGITACQMDIKIDGLKYEIMEAALAQARDGRLHILNILTETLATPKVDVKAYAPKIIMRTIPGNFIGALIGPGGKVIQELQKATGTTIVINEVDEMGVVEILGTDPAGIEAVLAKIESITFKPQIGEAYEVKVIKMLDFGAVVEYTAVPGNEVLLHVSELAWERTENVTDVVNMGDVFMVKYLGLDPKTRKEKVSRKALLPRPPREEKKE | Function: Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Catalytic Activity: phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n)
Sequence Mass (Da): 77852
Sequence Length: 711
Subcellular Location: Cytoplasm
EC: 2.7.7.8
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Q8RIA1 | MKELMFDEKIMELELAGRTLKVSTGKISRQSSGAIVIQYGDTVLLSTANRSKEARKGADFFPLTVDYIEKFYSSGKFPGGFNKREGRPSTNATLVARLIDRPIRPMFPDGFNYDVHIVNTVLSYDEINIPDYLGVIGSSLALMISDIPFLGPVASVIVGYKNGEFILNPSPKELEESELDLIVAGTKEAVNMVEAGAKELDEETMLKAIMFAHENIKKICEFQEEFSKLYGKENIEFEKPEVLTLVKDFIDTNGYERLQQAVLTTGKKNREDAVDSLEEELMEKFIQENYPDVPEEELPEDIILEFKTYYHDLMKKLVREAILYHKHRVDGRTTTEIRPLDAQINVLPIPHGSALFTRGETQSLAITTLGTKEDEQLIDDLEKEYYKKFYLHYNFPPYSVGEVGRMGSPGRRELGHGSLAERALSYVIPTEEEFPYTIRVVSEITESNGSSSQASICGGSLSLMSAGVPIKEHVAGIAMGLIKEGEEFTVLTDIMGLEDHLGDMDFKVAGTKSGITALQMDIKITGITEEIMRIALNQAHQARIQILELMNNTISKPAELKSNVPRIQQITIPKDKIAALIGPGGKNIKGIIEQTGATVDITDDGLVSVFAKDADTLEKTLKLVDSFVREVEYNEVYEGRVVSIMKFGAFMEILPGKEGLLHISEISPERVEKVEDVLSVGDVFKVRVISMEGGKISLSKKKV | Function: Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Catalytic Activity: phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n)
Sequence Mass (Da): 78262
Sequence Length: 703
Subcellular Location: Cytoplasm
EC: 2.7.7.8
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B3CTX1 | MFNEILKKVDWHGNMLSLSTGKIARNADGAVLASMGNTSVLCTVVFDKNTKKDIDFFPLGVYYREMAYAAGKIPGGFIKKEGKFSEYEVLVSRLIDRSIRPLFDSNFRNDTQVICTVMSYDPRYSPDILAIIGSSAALAISGIPIVKPIGAARVGIVNDEFILNPVIHDNTGVNELDLVVAATFDSVTMIEAQACEIDEEKMLAAIEFGYKSLKPVINAIEEIKSSIRKDIFEVTARPHLRYNDEILKHFSSDIKSALLLQTKNERNQQLQLIQQKVVDYFSSEANDDDAILNIEKALDDVKSKIFRDLVLQDKTRIGNRAIDEIRPIICEAGLFNTVHGSALFTRGDTQSLATITLGSSTDEQIVEQLNKCERQNFLLDYIFLPYSVGEISPLRAASRREIGHGWLAKKAIQLVIPSKDVFPYTIRIVSEITQSDGSSSMATVCSASLSLMEAGVPIKTHVAGIAMGLVLGEGNKFEILSDISGCEDHLGDMDFKVASTKNGITALQLDIKVQGINLSMIESTFRQAKIGINHILNVMNNTISCPKSELSTYAPMVQTLEIQKEKIRDVIGLGGKVIKELCKTFDVEIDISENGEVKVWGNVGENVKKAVQSIENIVFVPQIGDIFDGEVVKVIESGAFIKYVTGRDGFVHISEINDTHIKDINAHVKLGDKVKVKIIGIDHKNRVKLTLRTDKEHCKNKNEQYNDITTTTGSVKKKIKIAPKEAAVISNRKYFD | Function: Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Catalytic Activity: phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n)
Sequence Mass (Da): 81456
Sequence Length: 736
Subcellular Location: Cytoplasm
EC: 2.7.7.8
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A6LFK9 | MLNPINKTIELGDGRTITIETGKLAKQADGAVTVRMNNTVLLATVCAAKDANPGVDFMPLQVEYKEKYSAFGRFPGGFTKREGKASDYEILTSRLVDRALRPLFPDNYHAEVYVNIILFSADGEDLPDALAGLAASAALAVSDIPFNGPISEVRVARTDGKYIVNPTSAELEKADIDIMVAATIDNIMMVEGEMNEVQESEMLEAIKVAHEAIKVQCKAQLELSEACGKLVKREYCHEVNDDELRKDVHDKCYAKAYAVATSGSGKHERSEAFEKIVEEYKAQFSEEELTDEKLEMIGRYYHDVEKEAMRRAILDEGKRLDGRKTTEIRPIWIETDCLPGPHGSAIFTRGETQSLSTVTLGTKSDEKMIDDVLNHGYERFLLHYNFPPFSTGEAKATRGVGRREIGHGNLAHRALKRMIPDNYPYVVRVISDILESNGSSSMATVCAGTLALRDAGVPMKKPVSGIAMGLISENKGTNYAILSDILGDEDHLGDMDFKVTGTKDGITATQMDIKVDGLSYEILENALAQAKEGRMHILGKILEAQPEAREDLKPHAPRIETMIIGKEFIGAVIGPGGKIIQGIQEKTGATVSIDEVDGVGKIEISGTNKATIDAAVKAIKAIVAVPEIGEVYEGKISSIMPYGAFVEFMPGKDGLLHISEIDWKRLETVEQAGLKEGDTVSVKLVDIDPKTGKFKLSRKVLLPKPEGYEERPPRPERGERGPRQDRGDRGPRQDRGDRGPRREYRD | Function: Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Catalytic Activity: phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n)
Sequence Mass (Da): 82019
Sequence Length: 746
Subcellular Location: Cytoplasm
EC: 2.7.7.8
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Q6MDI2 | MQRETISVPVGAQEIIFETGKIARQAGGAVVVRCGETVVFTTACAAPNADSTTDFLPLRVDYQEKFSSAGKTLGGFIKREGRPTEKEVLVSRLIDRPIRPMFEEGYYNEVQLLSFVWSYDGINSPEPLAICGASAALVISDIPLIKPVGAVRIGFIDAQFIVNPTIEQQKQSKLDLLIAGTEEAVLMIEGFCDFLTEDQVLEAIEIGHRSIKTICQTLEQWRAKVGKPKNRETLRQLPKELYADVESIANPLLEKALRICEKQKREEALAEVTKAVNDRLMPENEEPKYPAKHIAYVIKDVSSKMMRQMILNENVRSDGRTSTDIRFIDIEQSLLPRAHGSSLFTRGETQALAVCTLGGASMAQRFEDLEGEGNNRFYLQYSFPPYSVGEVGRVGAPGRREIGHGKLAERALMAVIPTKEQFPYTIRLESNITESNGSSSMATVCGGCLALMDAGVAIKRPVAGIAMGLILENERFIILSDILGIEDALGDMDFKVTGDQNGITAFQMDIKVEGITIEIMRVALKQAKEGRVHILNKMLAVCPTYKGEMSRYAPRIETIQIKPSKIAVVIGPGGKQIRAIIEQTGVQIDIDDTGLVNIAAIDLVSIEKAKAIIHGLTAEIEIGRIYSGKAISIAPFGVFVEILPGKEGLCHISEFDVNRINSLDEFVKQGDMLMVKVLDINERGQIKLSRKATLQSQ | Function: Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Catalytic Activity: phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n)
Sequence Mass (Da): 76628
Sequence Length: 697
Subcellular Location: Cytoplasm
EC: 2.7.7.8
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B4SDX4 | MIINKEIDLGQGKIISIETGKMAKQADGAVVVRQGDTMVIATVVSSKKTPPPNQDYFPLQVEYREKYSAAGKFPGGFFKRESRPSEKEILSARLIDRALRPLFPDGYLYETQIIVTVISSDQINDADVLGGLAASCAIMVSDIPFQNPMSEVRVGRINGLFVVNPDINELVNSDLDICIGGTENTICMLEGEMKEISEAEMLDAIKFGHAAIRKLCALQSEIAAEVAKPIRPFTPTVIPAELTETVRVLCETRLKELAYTPLKKEERADQTAAIYHEIIESTIEHFKATCSSEEFSTDPAKALCINPHIIDEQIHMVEKRVMRHMILDDAKRLDGRALDQVRPISIELGIIPRAHGSALFTRGETQALVTITLGTKKDAQSVDNLTSSADKKFYLHYNFPPFCVGETGRLGSIGRREIGHGNLAERSIKMVAPTEEEFPYTIRIVSDILESNGSSSMASVCGGTLALMDGGVPIKKPVSGIAMGLIKEGASYAVLSDILGNEDHLGDMDFKVSGTRDGITACQMDIKIDGLDYHILETALEQARRGRLHILGEMEKAIPSTRQELANFAPKLTSIKVPVDCIGMIIGKGGETIRSITEETGAEINIDDDGTITIACSTSEGTNAALATIKNLTAKPEVGNIYIGKVRDIRDELGAFVEFLPKTDGLVHISEISSERVTKVSDHLKIGEKVRVKLVDVRKDSRTGKTRFALSIKAAEQDAPKENGAENK | Function: Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Catalytic Activity: phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n)
Sequence Mass (Da): 79422
Sequence Length: 728
Subcellular Location: Cytoplasm
EC: 2.7.7.8
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A5D2S6 | MADRSILTREIIVGGRPMILETGRLANQASGAVFVRYGDTAVLVTATVAPTVRAGIDFFPLTVDYEERFYAVGKIPGGFIKRESRPSEKAILSGRLIDRPIRPLFPKEMRNEVQVIATILSVDQDNAPEIAAMVGASAALHISEIPLKFPIGGVIVGRVDGRFVINPVLAQAEKSDMHLVVAGTKDAVMMVEAGAKEVPEEVILEAISFGHETVKEIVAFIERYREEALEMGLAKEKMVIEVAEPDPVLVEAVTGPATEKLDGVLRRCVNERLSKQERDSLLNNIKDELMQKFLADYPEQESLIKDLLDSIEKKLVRRMITEEGLRIDGRALNEVRPISVEVGVLPRPHGSGLFTRGQTQILSVVTLGTVSEEQILDGLGVEESKRFMHHYNFPPYSTGETRPLRSPGRREIGHGALAERALAAVIPGEEEFPYTIRIVSEALESNGSTSMGSVCGSTLALMDAGVPISAPVAGVAMGLIKEGDNFTVLTDIQGFEDHLGDMDFKVAGTAKGITALQMDIKIPGITREVFEKALAQAYEGRMHILNKMLEVLPAPRPELSPHAPRIIHITIDPDKIRDVIGPGGKVIKKIVEETGAEIDIEDDGRVFIAAVDQEKGRKAQEIIETLTKEVQTGEIYTGRVTRITDFGCFVEIIPGVLGMQGKEGLVHISQLAHHRVNRVEDVVKEGDVILVKVTGYDSQGRLKLSKKEATPPPESTAMKEGRAHRPSRRRESAR | Function: Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Catalytic Activity: phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n)
Sequence Mass (Da): 80315
Sequence Length: 734
Subcellular Location: Cytoplasm
EC: 2.7.7.8
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Q67P77 | MPPGAPDGPGHRRRTNVTASFSMELGGRTMTLETGRLAKQASGSVLVNYGDSVVLCTAVGSATPREGVDFFPLTVDYEERMYSVGRIPGNWFRREGRPTSKAILWARLTDRPIRPLFPEGFRNDVQVVCTVLSVDPDHPVEIMGMIGASAALTISDIPFEGPIGGVIVGLVDGQFVINPTAEQQERSEMHLVVAGTEHAVLMVEAGAKEVPEQTMLDAILFGHEVIKNTIIPTIKQMQAEVGKPKREVVLFNPPPELEQAVREAATVRLREAVRNPDKLAREEAVAAVGEAVQAELAEQFPESEKHIAYLLKKVLKEEVRRAIIEEGIRPDGRSLTEIRPIECAVDLLPRPHGSGLFQRGQTQVLSICTLGTLGDMQKLDDLTLEETKRFMHHYNFPPYSVGETRPLRGPGRREIGHGALAERALEPVIPPEEEFPYTIRVVSEVLESNGSSSMASVCGSTLALMAAGVPIKAPVAGVAMGLVEDPETGRYAVLTDIQGIEDALGDMDFKVAGTKKGVTALQMDMKISGTSREILEKALMQAREGRMFIMEKMLACISEPRKELSPWAPRIITMKISPEKIRDVIGKGGSTINKIIEETKVGHTKVEIDIQDDGTIYIAAVNLEAGERARQMIEALVKDPEPGMIYTGRVTRLMQFGAFVEILPGKEGLVHISELSDKRVARVEDVVNIGDEVTVKVTEIDRLGRINLSIKDAMPKQAASQPSGRPEARQPQPKPGQGKPGPAKAGAGRPGPGKPGPGRHGR | Function: Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Catalytic Activity: phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n)
Sequence Mass (Da): 82820
Sequence Length: 762
Subcellular Location: Cytoplasm
EC: 2.7.7.8
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Q2LWT4 | MSTIFSAEFAGRNISIKTGYVAGQADGAVMVIYGDTVVMVTAVSLKTAREGVDFLPLTVDYQEMTYAAGKIPGGFFKREGRPNEREILTSRVIDRSIRPLFPKGYCYETQLVATVLSVDSENDSDVAALLAASAALEISDIPFKGPIVGVRVGRVDGQFICNPSKLEQEKGDLNLYLVGRKVVPGTEGRPYDVNLVMLEGEAQQVEEEHVIAGIDFGLECMRPVIELQDQLRSALGKPKREFEAVEIDDALLAEVSEKAAVRMREAYRMSRKLDRHAALDEIRNSVLKAVTADEAGLRLRTAAALEALEKRIVRDVILKEKQRIDGRSYAEIRAISAEVGILPRAHGSALFNRGETQSLAALALGTSSDEQRLDYVAGEETRSFILHYNFPPYCVGEARPLRSPGRREIGHGNLARKALMPVIPSPEEFPYTIRIVSEILSSNGSSSMATVCGGLLCLMDGGVPVKGVVAGIAMGLLKEGEQVVILSDILGDEDHAGDMDFKVCGTSKGITAMQMDIKIDGINEDILRKALAQAREGRLFIIDKILATISEPRKELSIYAPRITTVKVKPEKVRAVIGTGGKNIRQIVSETGVTIDVEDDGTVTIASSDMEASARAIAMVRWLTEDAEVGKIYRGTVKKVVDFGAFVEILPGTEGLLHISQLAKERVNKVTDIVNEGDEVIVKVLEVDKQGKIRLSRKEALGSDI | Function: Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Catalytic Activity: phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n)
Sequence Mass (Da): 76711
Sequence Length: 705
Subcellular Location: Cytoplasm
EC: 2.7.7.8
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A0LHM4 | MKHSVQVEVGGRPMVFEAGEIARQAGGSVLMRYGDTVVLIAATKEDRIREGIDFVPLMVDYQEMSYAAGRIPGGFFRREIGRPSEKETLTSRLIDRPIRPLFPKKYCYETQVVATVLSVDMENEPDVVALTGASTALHISPVPFQGPVAAVRVGRINGSFAINPSAKELLESDLNVVVAGSRDAVVMVEGGADFVSEDDLVDAIDFGHKAILPILDAQDELQRRIAPVKEAPPEVVRNESLVQAVRDAAAAEMRAVMTTPEKHPRRDRKKALKERIQAELVSDDPDRPKQIDNILEDLEKEVVRRMMVEEGRRIDGRRFDEIRPINIQAGVLPRTHGSAVFTRGETQVLAVVTLGSSSDEQKIEALAGETFKSFMLHYNFPAFSVGEVRPLRGPGRREIGHGALAERSVKAVLPRDGEFPYTIRVVSEVLESNGSSSMATVCGSSLALMDAGVPITEPVGGIAMGLVKEGDKIIVLSDILGDEDHLGDMDFKVTGSERGITAIQMDVKIAGIDRGIMQRALEQARAGRIFILGKMKEVLSAPRPELSPYAPRVITIMINPEKIRDVIGPGGKVIRSIVAETGAKIDIEDSGKVVIMSPDGAACDKAVERIRGLTQEPEVGQLYMSRIVRVTDFGAFAEILPNIEGLIHISQLEHRRVRKVTDVVQEGDEVLVKVIEIDKDGRIRLSRKAALEKPEGGGQ | Function: Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Catalytic Activity: phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n)
Sequence Mass (Da): 76332
Sequence Length: 699
Subcellular Location: Cytoplasm
EC: 2.7.7.8
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P27954 | RNLGKVIDTLTCGFADLMGYIPLVGAPLGGAARALAHGVRVLEDGVNYATGNLPGCSFSIFLLALLSCLTVPASAYQVRNSSGLYHVTNDCPNSSIVYEAADAILHTPGCVPCVHEGNVSRCWVAMTPTVATRDGKLPTTQLRRHIDLLVGSATLCSALYVGDLCGSVFLVGQLFTFSPRRHWTTQGCNCSI | Function: Packages viral RNA to form a viral nucleocapsid, and promotes virion budding (Probable). Participates in the viral particle production as a result of its interaction with the non-structural protein 5A (By similarity). Binds RNA and may function as a RNA chaperone to induce the RNA structural rearrangements taking place during virus replication (By similarity). Modulates viral translation initiation by interacting with viral IRES and 40S ribosomal subunit (By similarity). Affects various cell signaling pathways, host immunity and lipid metabolism (Probable). Prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) and IFN-gamma signaling pathways and by blocking the formation of phosphorylated STAT1 and promoting ubiquitin-mediated proteasome-dependent degradation of STAT1 (By similarity). Activates STAT3 leading to cellular transformation (By similarity). Regulates the activity of cellular genes, including c-myc and c-fos (By similarity). May repress the promoter of p53, and sequester CREB3 and SP110 isoform 3/Sp110b in the cytoplasm (By similarity). Represses cell cycle negative regulating factor CDKN1A, thereby interrupting an important check point of normal cell cycle regulation (By similarity). Targets transcription factors involved in the regulation of inflammatory responses and in the immune response: suppresses TNF-induced NF-kappa-B activation, and activates AP-1 (By similarity). Binds to dendritic cells (DCs) via C1QR1, resulting in down-regulation of T-lymphocytes proliferation (By similarity). Alters lipid metabolism by interacting with hepatocellular proteins involved in lipid accumulation and storage (By similarity). Induces up-regulation of FAS promoter activity, and thereby contributes to the increased triglyceride accumulation in hepatocytes (steatosis) (By similarity).
PTM: Specific enzymatic cleavages in vivo yield mature proteins (By similarity). The structural proteins, core, E1, E2 and p7 are produced by proteolytic processing by host signal peptidases (By similarity). The core protein precursor is synthesized as a 23 kDa, which is retained in the ER membrane through the hydrophobic signal peptide (By similarity). Cleavage by the signal peptidase releases the 21 kDa mature core protein (By similarity). The cleavage of the core protein precursor occurs between aminoacids 176 and 188 but the exact cleavage site is not known (By similarity). Some degraded forms of the core protein appear as well during the course of infection (By similarity). The other proteins (p7, NS2, NS3, NS4A, NS4B, NS5A and NS5B) are cleaved by the viral proteases (By similarity). Autoprocessing between NS2 and NS3 is mediated by the NS2 cysteine protease catalytic domain and regulated by the NS3 N-terminal domain (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 20315
Sequence Length: 192
Domain: The transmembrane regions of envelope E1 and E2 glycoproteins are involved in heterodimer formation, ER localization, and assembly of these proteins.
Subcellular Location: Host endoplasmic reticulum membrane
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Q5EG65 | MSTNPKPQRKTKRNTNRRPQDVKFPGGGQIVGGVYLLPRRGPRLGVRATRKTSERSQPRGRRQPIPKARRPKGRNWAQPGYPWPLYGNEGCGWAGWLPSPRGSRPSWGPNDPRRRSRNLGKVIDTLTCGFVDLMGYIPLVGAPLRGAARALAHGVRVLEDGVNYATGNLPGCSFSIFLLALLSCLTVPASAYQVRNSTGLYHVTNDCPNSSIVYEAVDAILHTPGCVPCVREGNASRCWVAMTPTVATRDGRLPTTQLRRHIDLLVGSATLCSALYVGDLCGSVFLVGQLFTFSPRRHWTTQGCNCSIYPGHITGHRMAWDMMMNWSPTTALVVAQLLRIPQAILDMIAGAHWGVLAGMAYFSMVGNWAKVLAVLLLFAGVDAETHVTGGAAARSTLQLAGLFQPGAKQNVQLINTNGSWHVNRTALNCNDSLNTGWIAGLFYYHGFNSSGCSERLASCRSLTDFDQGWGPISYAGGGGPDHRPYCWHYPPKPCGIVPAKSVCGPVYCFTPSPVVVGTTDRSGAPTYSWGADDTDVFVLNNTRPPLGNWFGCTWMNSTGFTKVCGAPPCVIGGVGNNTLHCPTDCFRKHPEATYSRCGSGPWLTPRCLVDYPYRLWHYPCTINHSIFKVRMYVGGVEHRLDAACNWTRGERCDLEDRDRSELSPLLLSTTQWQVLPCSFTTLPALSTGLIHLHQNIVDVQYLYGVGSSIASWAIKWEYVVLLFLLLADARVCSCLWMMLLISQAEAALENLVVLNAASLAGTHGLVSFLVFFCFAWFLRGKWVPGAVYALYGMWPLLLLLLALPQRAYALDTEVAASCGGVVLVGLMAL | Cofactor: Activity of protease NS2 is dependent on zinc ions and completely inhibited by EDTA. This is probably due to the fact that NS2 protease activity needs NS3 N-terminus that binds a zinc atom (active region NS2-3).
Function: Packages viral RNA to form a viral nucleocapsid, and promotes virion budding (Probable). Participates in the viral particle production as a result of its interaction with the non-structural protein 5A (By similarity). Binds RNA and may function as a RNA chaperone to induce the RNA structural rearrangements taking place during virus replication (By similarity). Modulates viral translation initiation by interacting with viral IRES and 40S ribosomal subunit (By similarity). Affects various cell signaling pathways, host immunity and lipid metabolism (Probable). Prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) and IFN-gamma signaling pathways and by blocking the formation of phosphorylated STAT1 and promoting ubiquitin-mediated proteasome-dependent degradation of STAT1 (By similarity). Activates STAT3 leading to cellular transformation (By similarity). Regulates the activity of cellular genes, including c-myc and c-fos (By similarity). May repress the promoter of p53, and sequester CREB3 and SP110 isoform 3/Sp110b in the cytoplasm (By similarity). Represses cell cycle negative regulating factor CDKN1A, thereby interrupting an important check point of normal cell cycle regulation (By similarity). Targets transcription factors involved in the regulation of inflammatory responses and in the immune response: suppresses TNF-induced NF-kappa-B activation, and activates AP-1 (By similarity). Binds to dendritic cells (DCs) via C1QR1, resulting in down-regulation of T-lymphocytes proliferation (By similarity). Alters lipid metabolism by interacting with hepatocellular proteins involved in lipid accumulation and storage (By similarity). Induces up-regulation of FAS promoter activity, and thereby contributes to the increased triglyceride accumulation in hepatocytes (steatosis) (By similarity).
PTM: Specific enzymatic cleavages in vivo yield mature proteins (By similarity). The structural proteins, core, E1, E2 and p7 are produced by proteolytic processing by host signal peptidases (By similarity). The core protein precursor is synthesized as a 23 kDa, which is retained in the ER membrane through the hydrophobic signal peptide (By similarity). Cleavage by the signal peptidase releases the 21 kDa mature core protein (By similarity). The cleavage of the core protein precursor occurs between aminoacids 176 and 188 but the exact cleavage site is not known (By similarity). Some degraded forms of the core protein appear as well during the course of infection (By similarity). The other proteins (p7, NS2, NS3, NS4A, NS4B, NS5A and NS5B) are cleaved by the viral proteases (By similarity). Autoprocessing between NS2 and NS3 is mediated by the NS2 cysteine protease catalytic domain and regulated by the NS3 N-terminal domain (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 90587
Sequence Length: 829
Domain: The transmembrane regions of envelope E1 and E2 glycoproteins are involved in heterodimer formation, ER localization, and assembly of these proteins.
Subcellular Location: Host endoplasmic reticulum membrane
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Q01403 | MSTNPKPQRKTKRNTNRRPQDVKFPGGGQIVGGVYLLTRRGPRLGVRATRKTSERSQPRGRRQPIPKARRPEGRAWAQPGYPWPLYGNEGLGWAGWLLSPRGSRPSWGPTDPRRRSRNLGKVIDTLTCGFADLMGYIPLVGAPLGGASRALAHGVRVLEDGVNYATGNLPGCSFSIFLSALMSCLTTPASAYEVRNVSGIYHVTNDCSNSSIAYEAAGMIMHTPGCVPCVRENNSSRCWVALTPTLAARNASVPTTTIRRHVDLLVGAATLCSAMYVGDLCGSVFLVSQLFTFSPRRYETVQDCNCSIYPGHVSGHRMAWDMMMNWSPTAALVVSQLLRIPQAVVDMVAGAHWGVLAGLAYYSMVGNWAKVLIVMLLFAGVDGANTHTVGGTEGFATQRLTSLFALGPSQKIQLINTNGSWHINRTALNCNDSFKTGFLAALFYVHKFNASGCPEHMASCRPIDKFDQGWGPVTYAEPSISEQRPYCWHYAPRPCGTIPASEVCGPVYCFTPSPVVVGTT | Function: Packages viral RNA to form a viral nucleocapsid, and promotes virion budding (Probable). Participates in the viral particle production as a result of its interaction with the non-structural protein 5A (By similarity). Binds RNA and may function as a RNA chaperone to induce the RNA structural rearrangements taking place during virus replication (By similarity). Modulates viral translation initiation by interacting with viral IRES and 40S ribosomal subunit (By similarity). Affects various cell signaling pathways, host immunity and lipid metabolism (Probable). Prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) and IFN-gamma signaling pathways and by blocking the formation of phosphorylated STAT1 and promoting ubiquitin-mediated proteasome-dependent degradation of STAT1 (By similarity). Activates STAT3 leading to cellular transformation (By similarity). Regulates the activity of cellular genes, including c-myc and c-fos (By similarity). May repress the promoter of p53, and sequester CREB3 and SP110 isoform 3/Sp110b in the cytoplasm (By similarity). Represses cell cycle negative regulating factor CDKN1A, thereby interrupting an important check point of normal cell cycle regulation (By similarity). Targets transcription factors involved in the regulation of inflammatory responses and in the immune response: suppresses TNF-induced NF-kappa-B activation, and activates AP-1 (By similarity). Binds to dendritic cells (DCs) via C1QR1, resulting in down-regulation of T-lymphocytes proliferation (By similarity). Alters lipid metabolism by interacting with hepatocellular proteins involved in lipid accumulation and storage (By similarity). Induces up-regulation of FAS promoter activity, and thereby contributes to the increased triglyceride accumulation in hepatocytes (steatosis) (By similarity).
PTM: Specific enzymatic cleavages in vivo yield mature proteins (By similarity). The structural proteins, core, E1, E2 and p7 are produced by proteolytic processing by host signal peptidases (By similarity). The core protein precursor is synthesized as a 23 kDa, which is retained in the ER membrane through the hydrophobic signal peptide (By similarity). Cleavage by the signal peptidase releases the 21 kDa mature core protein (By similarity). The cleavage of the core protein precursor occurs between aminoacids 176 and 188 but the exact cleavage site is not known (By similarity). Some degraded forms of the core protein appear as well during the course of infection (By similarity). The other proteins (p7, NS2, NS3, NS4A, NS4B, NS5A and NS5B) are cleaved by the viral proteases (By similarity). Autoprocessing between NS2 and NS3 is mediated by the NS2 cysteine protease catalytic domain and regulated by the NS3 N-terminal domain (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 56477
Sequence Length: 520
Domain: The transmembrane regions of envelope E1 and E2 glycoproteins are involved in heterodimer formation, ER localization, and assembly of these proteins.
Subcellular Location: Host endoplasmic reticulum membrane
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P27960 | MSTNPKPQRKTKRNTNRRPQDVKFPGGGQIVGGVYLLPRRGPRLGVRATRKTSERSQPRGRRQPIPKDRRSTGKSWGKPGYPWPLYGNEGLGWAGWLLSPRGSRPSWGPNDPRHRSRNVGKVIDTLTCGFADLMGYIPVVGAPLGGVARALAHGVRVLEDGVNYATGNLPGCSFSIFLLALLSCITVPVSAVQVKNTSNSYMVTNDCSNDSITWQLQGAVLHVPGCVPCEKVGNMSRCWIPVSPNVAVRQPGALTQGLRTHIDMVVVSATLCSALYVGDLCGGVMLAAQMFIVSPQHHWFVQECNCSIYPGAITGHRMAWDMMMNWSPTATMILAYAMRVPEVIIDIISGAHWGVMFGLAYFSMQGAWAKVVVILLLAAGVDANTRTVAGSAAATTRGFTSMFSSGSKQNLQLINTNGSWHINRTALNCNDSLNTGFIASLFYVNRFNSSGCPHRLSVCRSIEAFRIGWGTLQYEDNVTNPEDMRPYCWHYPPKPCGIVPARSVCGPVYCFTPSPVVVGTTDARGVPTYTWGENETDVFLLNSTRPPRGSWFGCTWMNSTGFTKTCGAPPCRIRADFNASTDLLCPTDCFRKHSDATYIKCGSGPWLTPKCMVDYPYRLWHYPCTVNYSIFKIRMYVGGVEHRLTAACNFTRGDPCNLEDRDRSQLSPLLHSTTEWAILPCTYSDLPALSTGLLHLHQNIVDVQYMYGLSPALTKYVVRWEWVVLLFLLLADARVCA | Function: Packages viral RNA to form a viral nucleocapsid, and promotes virion budding (Probable). Participates in the viral particle production as a result of its interaction with the non-structural protein 5A (By similarity). Binds RNA and may function as a RNA chaperone to induce the RNA structural rearrangements taking place during virus replication (By similarity). Modulates viral translation initiation by interacting with viral IRES and 40S ribosomal subunit (By similarity). Affects various cell signaling pathways, host immunity and lipid metabolism (Probable). Prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) and IFN-gamma signaling pathways and by blocking the formation of phosphorylated STAT1 and promoting ubiquitin-mediated proteasome-dependent degradation of STAT1 (By similarity). Activates STAT3 leading to cellular transformation (By similarity). Regulates the activity of cellular genes, including c-myc and c-fos (By similarity). May repress the promoter of p53, and sequester CREB3 and SP110 isoform 3/Sp110b in the cytoplasm (By similarity). Represses cell cycle negative regulating factor CDKN1A, thereby interrupting an important check point of normal cell cycle regulation (By similarity). Targets transcription factors involved in the regulation of inflammatory responses and in the immune response: suppresses TNF-induced NF-kappa-B activation, and activates AP-1 (By similarity). Binds to dendritic cells (DCs) via C1QR1, resulting in down-regulation of T-lymphocytes proliferation (By similarity). Alters lipid metabolism by interacting with hepatocellular proteins involved in lipid accumulation and storage (By similarity). Induces up-regulation of FAS promoter activity, and thereby contributes to the increased triglyceride accumulation in hepatocytes (steatosis) (By similarity).
PTM: Specific enzymatic cleavages in vivo yield mature proteins (By similarity). The structural proteins, core, E1, E2 and p7 are produced by proteolytic processing by host signal peptidases (By similarity). The core protein precursor is synthesized as a 23 kDa, which is retained in the ER membrane through the hydrophobic signal peptide (By similarity). Cleavage by the signal peptidase releases the 21 kDa mature core protein (By similarity). The cleavage of the core protein precursor occurs between aminoacids 176 and 188 but the exact cleavage site is not known (By similarity). Some degraded forms of the core protein appear as well during the course of infection (By similarity). The other proteins (p7, NS2, NS3, NS4A, NS4B, NS5A and NS5B) are cleaved by the viral proteases (By similarity). Autoprocessing between NS2 and NS3 is mediated by the NS2 cysteine protease catalytic domain and regulated by the NS3 N-terminal domain (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 81208
Sequence Length: 737
Domain: The transmembrane regions of envelope E1 and E2 glycoproteins are involved in heterodimer formation, ER localization, and assembly of these proteins.
Subcellular Location: Host endoplasmic reticulum membrane
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P03318 | DADLAAVYRAVASLADETVRTMAIPLLSTGTFAGGKDRVLQSLNHLFTALDTTDVDVTIYCRDKSWEKKIQEAIDMRTATELLDDDTTVMKELTRVHPDSCLVGRSGFSTVDGRLHSYLEGTRFHQTAVDVAERPTLWPRREEANEQITHYVLGESMEAIRTKCPVDDTDSSAPPCTVPCLCRYAMTPERVHRLRAAQVKQFTVCSSFPLPKYKIPGVQRVACSAVMLFNHDVPALVSPRKYREPSISSESSSSGLSVFDLDIGSDSEYEPMEPVQPEPLIDLAVVEETAPVRLERVAPVAAPRRARATPFTLEQRVVAPVPAPRTMPVRPPRRKKAATRTPERISFGDLDAECMAIINDDLTFGDFGAGEFERLTSAXLDRAGAYIFSSDTGPGHLQQRSVRQTRLADCVAEDVHEERVFAPKCDKEKERLLLLQMQMAPTEANKSRYQSRKVENMKAEVIDRLLGGAKLFVTPTTDCRYVTHKHPKPMYSTSVAFYLSSAKTAVAACNEFLSRNYPTVTSYQITDEYDAYLDMVDGSESCLDRAAFCPSKLRSFPKKHSYHRAEIRSAVPSPFQNTLQNVLAAATKRNCNVTQMRELPTLDSAVFNVECFKKYACNNDYWDEFAQKPIRLTTENITSYVTRLKGPKAAALFAKTYDLKPLQEVPMDRFVVDMKRDVKVTPGTKHTEERPKVQVIQAAEPLATAYLCGIHRELVRRLNAVLLPNVHTLFDMSAEDFDAIISEHFRPGDAVLETDIASFDKSQDDSLAYTGLMLLEDLGVDQPLLELIEASFGEITSTHLPTGTRFKFGAMMKSGMFLTLFVNTMLNMTIASRVLEERLTNSKCAAFIGDDNIVHGVKSDKLLAERCAAWMNMEVKIIDAVMCERPPYFCGGFIVFDQVTGTCCRVADPLKRLFKLGKPLPAEDKQDEDRRRALADEAQRWNRVGIQADLEAAMNSRYEVEGIRNVITALTTLSRNYHNFRHLRGPVIDLYGGPK | Cofactor: For nsP4 adenylyltransferase activity; Mn(2+) supports catalysis at 60% of the levels observed with Mg(2+).
Function: Polyprotein P1234: Inactive precursor of the viral replicase, which is activated by cleavages carried out by the viral protease nsP2.
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
PTM: Polyprotein P1234: Specific enzymatic cleavages in vivo yield mature proteins (By similarity). The processing of the polyprotein is temporally regulated (By similarity). In early stages (1.7 hpi), P1234 is first cleaved in trans through its nsP2 protease activity, releasing P123' and nsP4, which associate to form the early replication complex (By similarity). At the same time, P1234 is also cut at the nsP1/nsP2 site early in infection but with lower efficiency (By similarity). After replication of the viral minus-strand RNAs (4 hpi), the polyproteins are cut at the nsP1/nsP2 and nsP2/nsP3 sites very efficiently, preventing accumulation of P123' and P1234 and allowing the formation of the late replication complex (By similarity). NsP3'/nsP4 site is not cleaved anymore and P34 is produced rather than nsP4 (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 111393
Sequence Length: 995
Domain: In the N-terminus, the macro domain displays a mono-ADP-ribosylhydrolase activity (By similarity). The central part has a zinc-binding function (By similarity). The C-terminus contains two FGDF motifs necessary and sufficient for formation of the nsP3/G3BP1 complex (By similarity).
Subcellular Location: Host cytoplasmic vesicle membrane
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P09523 | MTSSSLFREGELGHFCLNKQEMLHLNVTNPNSIYIEGKLSFEGYKSFNIHCYVDTGASLCIASRYIIPEELWENSPKDIQVKIANQELIKITKVCKNLKVKFAGKSFEIPTVYQQETGIDFLIGNNFCRLYNPFIQWEDRIAFHLKNEMVLIKKVTKAFSVSNPSFLENMKKDSKTEQIPGTNISKNIINPEERYFLITEKYQKIEQLLDKVCSENPIDPIKSKQWMKASIKLIDPLKVIRVKPMSYSPQDREGFAKQIKELLDLGLIIPSKSQHMSPAFLVENEAERRRGKKRMVVNYKAINQATIGDSHNLPNMQELLTLLRGKSIFSSFDCKSGFWQVVLDEESQKLTAFTCPQGHFQWKVVPFGLKQAPSIFQRHMQTALNGADKFCMVYVDDIIVFSNSELDHYNHVYAVLKIVEKYGIILSKKKANLFKEKINFLGLEIDKGTHCPQNHILENIHKFPDRLEDKKHLQRFLGVLTYAETYIPKLAEIRKPLQVKLKKDVTWNWTQSDSDYVKKIKKNLGSFPKLYLPKPEDHLIIETDASDSFWGGVLKARALDGVELICRYSSGSFKQAEKNYHSNDKELLAVKQVITKFSAYLTPVRFTVRTDNKNFTYFLRINLKGDSKQGRLVRWQNWFSKYQFDVEHLEGVKNVLADCLTRDFNA | Function: Encodes for at least two polypeptides: protease (PR) and reverse transcriptase (RT). The protease processes the polyprotein in cis. Reverse transcriptase is multifunctional enzyme that converts the viral RNA genome into dsDNA in viral cytoplasmic capsids. This enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes in a partially processive 3'- to 5'-endonucleasic mode. Neo-synthesized pregenomic RNA (pgRNA) are encapsidated, and reverse-transcribed inside the nucleocapsid. Partial (+)DNA is synthesized from the (-)DNA template and generates the relaxed circular DNA (RC-DNA) genome. After budding and infection, the RC-DNA migrates in the nucleus, and is converted into a plasmid-like covalently closed circular DNA (cccDNA) (By similarity).
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (Da): 77081
Sequence Length: 666
Domain: The polymerase/reverse transcriptase (RT) and ribonuclease H (RH) domains are structured in five subdomains: finger, palm, thumb, connection and RNase H. Within the palm subdomain, the 'primer grip' region is thought to be involved in the positioning of the primer terminus for accommodating the incoming nucleotide. The RH domain stabilizes the association of RT with primer-template (By similarity).
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Q9CGD4 | MSKTIIEFKNVSKTYADTDTTVLKDISFELEEGKFYTLLGASGSGKSTILNIIAGLLDATDGDVILDNKRINDLPANKRNVHTIFQSYALFPNMNVFDNVAFALKIKGVDKKEIAKRVSESLKLVRLDGFEKRSITKLSGGQKQRVAIARAIIDRPKVLLLDESLSALDMKLRKDMQYELRELQQSLGITFIFVTHDQEEALAMSDWVFIMNEGEIVQSGTPTDIYDEPINHFVADFIGESNILNGRMIEDYLVEFNGQKFEAVDGGMRKNEPIEVVIRPEDIWFTLPDEGKFNVKVDTQLFRGVHYEIVAYDEFNNEWLIHSTHKAIVGETVGLDFDPEAIHIMRLNETEEEFDARIEEYVEEEETVGLANAVEEENAEEEAAIQEAVKEALENTMELTELAETVNEILQKQENEPESENKESGANK | Function: Part of the ABC transporter complex PotABCD involved in spermidine/putrescine import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + polyamine-[polyamine-binding protein]Side 1 = ADP + phosphate + polyamineSide 2 + [polyamine-binding protein]Side 1.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 48486
Sequence Length: 428
Subcellular Location: Cell membrane
EC: 7.6.2.11
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Q5ZWE4 | MTTPLIEIRQIYKSYGNTPILNNVSLNVNHGEFLTLLGPSGCGKTTLLRLISGFEQPTQGEIFINGQCVNQLPPQKRDVHTVFQSYALFPHLSVFENVAFALRCKKTPNQEIRKRVFDALKLVQLESLAERNVKQLSGGQQQRVAIARAIINRPQVLLLDEPLSSLDYRLRKAMQSELKQLQKTLNMTFIFVTHDQEEALSMSDRIVVFNHGHIEQIGTPKAVYETPANLHVAMFIGEANIFDIQVHTVKDQDIITNIEGIQLSCKNTGNYQVNDRLHLIVRPEDIRVWSLSEVEKTEGMLPGRIVDIIYKGSTVDLKVELSSGKIINASEFFDEDDDKLEYTLHETVWVQWLPGWEVLLPYEG | Function: Part of the ABC transporter complex PotABCD involved in spermidine/putrescine import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + polyamine-[polyamine-binding protein]Side 1 = ADP + phosphate + polyamineSide 2 + [polyamine-binding protein]Side 1.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 41379
Sequence Length: 364
Subcellular Location: Cell inner membrane
EC: 7.6.2.11
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Q8Y8T6 | MIVTETIIRFENVTKQFDNDPPVLDNVSFEIEKGKFYTLLGPSGCGKTTILRLIAGFLEASKGQIYLGDKVINQIPANKRPVNTVFQDYALFPHLNVYENVAFGLRIKKLKKEAIDEKVKEALRFVNLKGYEKREISEMSGGQRQRVAIARAIVNEPEVILLDEPLSALDLKLRTEMQYELRDLQKRLGITFIFVTHDQEEALAMSDEIFVLNKGEIQQSGTPIDIYDEPINKFVADFIGESNIVNGKMIQDFEVEFVERRFECVDQGFRPNEVVEVVIRPEDLEITSAEKGQLQVTVDWMLFRGVHYEVGCIDIDGNEWLVHTTRKVRVGDKIGLAFEPEAIHVMRLGETEEEFDKRLDSYDEVQ | Function: Part of the ABC transporter complex PotABCD involved in spermidine/putrescine import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + polyamine-[polyamine-binding protein]Side 1 = ADP + phosphate + polyamineSide 2 + [polyamine-binding protein]Side 1.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 41953
Sequence Length: 366
Subcellular Location: Cell membrane
EC: 7.6.2.11
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P44768 | MSAKSNKIGVVQLTILTMVNMMGSGIIMLPTKLAEIGTISIVSWLVTAVGSTALAYAFAQCGMFSKKSGGMGGYAEYSFGKAGNFMANYTYGVSLVIANTAIAISAVGYGSELFGTILSPLSIALWTIFTLWLATVLNFGGARITGNISSFTIWGVIIPVVGISIIGWKWFDGSMYVNSWNPHNVPTFEAIGVSISMTLWAFLGLESACANADAVENPEKNVPIAVLGGTLGAAVIYIVSTNVIAGIVPNLELANSTAPFGLAFAHMFDETVGKVIMGLMVMSCFGSLLGWQFTIAQVFKSSAEEGYFPAFFKKITSKDAPVVGMITITALQTLLSLMTISPSLNKQFNVLVDLAVVTNVIPYLLSMAALAVLLKAENVAPQKYKTTVFVAFIGSLYSIYALYAAGEQAMLYGSIVTFIGWTLYGFVSYKFDLKK | Function: Catalyzes both the uptake and excretion of putrescine. The uptake of putrescine is dependent on the membrane potential and the excretion involves putrescine-ornithine antiporter activity.
Catalytic Activity: H(+)(in) + putrescine(in) = H(+)(out) + putrescine(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46349
Sequence Length: 435
Subcellular Location: Cell inner membrane
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P31134 | MNDAIPRPQAKTRKALTPLLEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPYLRPINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNVFEGVLKERQEDGLVLDSPGLVHPLKVDADASVVDNVPVHVALRPEKIMLCEEPPANGCNFAVGEVIHIAYLGDLSVYHVRLKSGQMISAQLQNAHRHRKGLPTWGDEVRLCWEVDSCVVLTV | Function: Part of the ABC transporter complex PotFGHI involved in putrescine uptake . Responsible for energy coupling to the transport system . Imports putrescine for maintenance of the optimal concentration of polyamines necessary for cell growth in the presence of glucose .
Catalytic Activity: ATP + H2O + putrescine(out) = ADP + H(+) + phosphate + putrescine(in)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 41931
Sequence Length: 377
Subcellular Location: Cell inner membrane
EC: 7.6.2.16
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P31135 | MSTLEPAAQSKPPGGFKLWLSQLQMKHGRKLVIALPYIWLILLFLLPFLIVFKISLAEMARAIPPYTELMEWADGQLSITLNLGNFLQLTDDPLYFDAYLQSLQVAAISTFCCLLIGYPLAWAVAHSKPSTRNILLLLVILPSWTSFLIRVYAWMGILKNNGVLNNFLLWLGVIDQPLTILHTNLAVYIGIVYAYVPFMVLPIYTALIRIDYSLVEAALDLGARPLKTFFTVIVPLTKGGIIAGSMLVFIPAVGEFVIPELLGGPDSIMIGRVLWQEFFNNRDWPVASAVAIIMLLLLIVPIMWFHKHQQKSVGEHG | Function: Part of the ABC transporter complex PotFGHI involved in putrescine uptake . Responsible for the translocation of the substrate across the membrane (Probable). Imports putrescine for maintenance of the optimal concentration of polyamines necessary for cell growth in the presence of glucose .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35490
Sequence Length: 317
Subcellular Location: Cell inner membrane
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P0AFL2 | MNNLPVVRSPWRIVILLLGFTFLYAPMLMLVIYSFNSSKLVTVWAGWSTRWYGELLRDDAMMSAVGLSLTIAACAATAAAILGTIAAVVLVRFGRFRGSNGFAFMITAPLVMPDVITGLSLLLLFVALAHAIGWPADRGMLTIWLAHVTFCTAYVAVVISSRLRELDRSIEEAAMDLGATPLKVFFVITLPMIMPAIISGWLLAFTLSLDDLVIASFVSGPGATTLPMLVFSSVRMGVNPEINALATLILGAVGIVGFIAWYLMARAEKQRIRDIQRARRG | Function: Part of the ABC transporter complex PotFGHI involved in putrescine uptake. Responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30541
Sequence Length: 281
Subcellular Location: Cell inner membrane
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