ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q9NXI6 | MACTKTLQQSQPISAGATTTTTAVAPAGGHSGSTECDLECLVCREPYSCPRLPKLLACQHAFCAICLKLLLCVQDNTWSITCPLCRKVTAVPGGLICSLRDHEAVVGQLAQPCTEVSLCPQGLVDPADLAAGHPSLVGEDGQDEVSANHVAARRLAAHLLLLALLIILIGPFIYPGVLRWVLTFIIALALLMSTLFCCLPSTRGSCWPSSRTLFCREQKHSHISSIA | Function: E3 ubiquitin protein ligase that is part of an apoptotic signaling pathway activated by endoplasmic reticulum stress . Stimulates the expression of proteins specific of the unfolded protein response (UPR), ubiquitinates BNIP1 and regulates its localization to the mitochondrion and induces calcium release from... |
Q9D241 | MSCTEAPQPIPAGTTTTSTIIALGPTGRLSISVEGDLECLVCREPYNCARSPKLLSCQHTFCAVCLKLLLYVQEDTWSIPCPLCRKVTAVPGGLICSLRDQEAMVGRLALPCPEVRLCPQRLVGSAASATRPANWTGEEEQDTVSVNRVAARRLAVHLLLLALVIVLILPFIYPGVIRWVLAFVIALALLMSTLFCCHPQSQNSNWLCPRTLFCREQKQTQITSIA | Function: E3 ubiquitin protein ligase that is part of an apoptotic signaling pathway activated by endoplasmic reticulum stress. Stimulates the expression of proteins specific of the unfolded protein response (UPR), ubiquitinates BNIP1 and regulates its localization to the mitochondrion and induces calcium release from ... |
Q5TA31 | MALPAGPAEAACALCQRAPREPVRADCGHRFCRACVVRFWAEEDGPFPCPECADDCWQRAVEPGRPPLSRRLLALEEAAAAPARDGPASEAALQLLCRADAGPLCAACRMAAGPEPPEWEPRWRKALRGKENKGSVEIMRKDLNDARDLHGQAESAAAVWKGHVMDRRKKALTDYKKLRAFFVEEEEHFLQEAEKEEGLPEDELADPTERFRSLLQAVSELEKKHRNLGLSMLLQ | Function: E3 ubiquitin-protein ligase that acts as a coactivator of JUN-mediated gene activation in response to growth factor signaling via the MAP3K1 pathway, independently from MAPK8.
PTM: Ubiquitinated; undergoes 'Lys-48'-linked autoubiquitination in the absence of growth factors and MAP3K1-induced 'Lys-63'-linked p... |
Q8BFX1 | MALPAGPADAICALCQRAPREPVRADCGHRFCRACVVRFWAEEDGPFPCPECADDCWQRAVEPSRPPLSRRLLALEEAAAAPARDGPASEAALQLLCRADGDPLCSACRMAAGPEPPEWEPRWRKALRGKENKGSVEIMRKDLNDARDLHGQAESAAAVWKGHVMDRRKKALTDYKKLRAFFVEEEEHFLQEAEKDEGASEDDELADPADRFRSLLQAVSELEKKHRNLGLSMLLQ | Function: E3 ubiquitin-protein ligase that acts as a coactivator of JUN-mediated gene activation in response to growth factor signaling via the MAP3K1 pathway, independently from MAPK8.
PTM: Ubiquitinated; undergoes 'Lys-48'-linked autoubiquitination in the absence of growth factors and MAP3K1-induced 'Lys-63'-linked p... |
Q9NV58 | MQEQEIGFISKYNEGLCVNTDPVSILTSILDMSLHRQMGSDRDLQSSASSVSLPSVKKAPKKRRISIGSLFRRKKDNKRKSRELNGGVDGIASIESIHSEMCTDKNSIFSTNTSSDNGLTSISKQIGDFIECPLCLLRHSKDRFPDIMTCHHRSCVDCLRQYLRIEISESRVNISCPECTERFNPHDIRLILSDDVLMEKYEEFMLRRWLVADPDCRWCPAPDCGYAVIAFGCASCPKLTCGREGCGTEFCYHCKQIWHPNQTCDAARQERAQSLRLRTIRSSSISYSQESGAAADDIKPCPRCAAYIIKMNDGSCNHMT... | Function: E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates, such as SNCAIP or CASR. Specifically ubiquitinates pathogenic SOD1 variants, which leads to their proteasomal... |
P50636 | MQEQEISFIFKYNEGLCMNIDSDSILMSILDMSLHQQMGSDRDLQSSTSSVSLPSVKKAPKQRRISIGSLFRRKKDSKRKSRELNGGVDGIASIESIHSEMCADKNSIFSTNTSSDNGLTSISKQIGDFIECPLCLLRHSKDRFPDIMTCHHRSCVDCLRQYLRIEISESRVNISCPECTERFNPHDIRLILSDDVLMEKYEEFMLRRWLVADPDCRWCPAPDCGYAVIAFGCASCPKLTCGREGCGTEFCYHCKQIWHPNQTCDAARQERAQSLRLRTIRSSSISYSQESGAAADDIKPCPRCAAYIIKMNDGSCNHMT... | Function: E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates, such as SNCAIP or CASR.
Catalytic Activity: [E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acc... |
Q1L8L6 | MGSEKDSESPHSSVSGIPNPKCRGPGKKQGRISFHSLFHSKRGPRGSKANVGTPLAQQLHQQQQIQQQQLLQPPTPTNVSSDPSTADPAEPLSTSQASLGGQELLECPLCLVRQPAEQLPELQGCSHRSCLCCLRQYLRIEITESRVQLSCPECAERLAPWQVALILDDPNLMEKYEEFLLRRCLASDPDCRWCPAPDCGFAVIASGCASCPRLVCRREGCGAEFCYHCKQAWHPNQTCDSARQQRALSLRTHSNHSPSYTAEQGHTDDIKPCPRCGAYIIKMNDGSCNHMTCAVCGCEFCWLCMKEISDLHYLSPSGCT... | Function: E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates, such as UCKL1. Involved in the cytolytic activity of natural killer cells and cytotoxic T-cells. Protects aga... |
Q6ZMZ0 | MGSEKDSESPRSTSLHAAAPDPKCRSGGRRRRLTLHSVFSASARGRRARAKPQAEPPPPAAQPPPAPAPAAAQGPPPEALPAEPAAEAEAEAAAAAAEPGFDDEEAAEGGGPGAEEVECPLCLVRLPPERAPRLLSCPHRSCRDCLRHYLRLEISESRVPISCPECSERLNPHDIRLLLADPPLMHKYEEFMLRRYLASDPDCRWCPAPDCGYAVIAYGCASCPKLTCEREGCQTEFCYHCKQIWHPNQTCDMARQQRAQTLRVRTKHTSGLSYGQESGPADDIKPCPRCSAYIIKMNDGSCNHMTCAVCGCEFCWLCMK... | Function: E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates, such as UCKL1 . Involved in the cytolytic activity of natural killer cells and cytotoxic T-cells . Protects a... |
Q08B84 | MRLRNDCLVRLLTSWFGIFCLYEMTEGSAEPPPCPGARRRRLLLSLPNVFPGRTRAAPEPSVPSPPPSPPPPPPPPVSVPPPPSSPGGSESLIECPLCLVRQPPEEIPELLSCRHRSCLRCLRQYLRIEICESRVNLRCPECAERLSPQHVRAILRDPLLTRKYEEFLLRRCLAADPDCRWCPAPDCGYAVIAYGCASCPKLTCEREGCRTEFCYHCKHVWHPNQTCDMARQQRAPSLGVRRKHPSGISYGQESGSADDMKSCPRCSAYIIKMNDGSCNHMTCSVCGCEFCWLCMKEISDLHYLSPSGCTFWGKKPWSRK... | Function: E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates, such as UCKL1. Involved in the cytolytic activity of natural killer cells and cytotoxic T-cells. Protects aga... |
Q93091 | MVLCFPLLLLLLVLWGPVCPLHAWPKRLTKAHWFEIQHIQPSPLQCNRAMSGINNYTQHCKHQNTFLHDSFQNVAAVCDLLSIVCKNRRHNCHQSSKPVNMTDCRLTSGKYPQCRYSAAAQYKFFIVACDPPQKSDPPYKLVPVHLDSIL | Function: Ribonuclease which shows a preference for the pyrimidines uridine and cytosine . Has potent antibacterial activity against a range of Gram-positive and Gram-negative bacteria, including P.aeruginosa, A.baumanii, M.luteus, S.aureus, E.faecalis, E.faecium, S.saprophyticus and E.coli . Causes loss of bacterial m... |
Q9D244 | MVVDLPRYLPLLLLLELWEPMYLLCSQPKGLSRAHWFEIQHIQTSRQPCNTAMRGVNNYTQHCKQINTFLHESFQNVAATCSLHNITCKNGRKNCHESAEPVKMTDCSHTGGAYPNCRYSSDKQYKFFIVACEHPKKEDPPYQLVPVHLDKIV | Function: Ribonuclease which shows a preference for the pyrimidines uridine and cytosine . Has potent antibacterial activity against a range of Gram-positive and Gram-negative bacteria, including P.aeruginosa, A.baumanii, M.luteus, S.aureus, E.faecalis, E.faecium, S.saprophyticus and E.coli . Causes loss of bacterial m... |
P81649 | MGPDLRCFPLLLLLLGLWWSVRPLCAIPKNLTRAQWFTIQHIQPSPLQCNKAMNSVNNYTWHCKPQNTFLHDSFQDVATACNLPNITCKNGQNNCHQSAKPVSLTQCSFTGGNYPNCRYKDAAQYKFFIVACDPPQKGDPPYPFVPVHLDKII | Function: Ribonuclease which shows a preference for the pyrimidines uridine and cytosine . Has potent antibacterial activity against a range of Gram-positive and Gram-negative bacteria, including P.aeruginosa, A.baumanii, M.luteus, S.aureus, E.faecalis, E.faecium, S.saprophyticus and E.coli (By similarity). Causes loss... |
Q9H1E1 | MAPARAGFCPLLLLLLLGLWVAEIPVSAKPKGMTSSQWFKIQHMQPSPQACNSAMKNINKHTKRCKDLNTFLHEPFSSVAATCQTPKIACKNGDKNCHQSHGAVSLTMCKLTSGKHPNCRYKEKRQNKSYVVACKPPQKKDSQQFHLVPVHLDRVL | Function: Exhibits a potent RNase activity . Has broad-spectrum antimicrobial activity against many pathogenic microorganisms including uropathogenic E.coli (UPEC), and remarkably potent activity (lethal dose of 90% < 30 nM) against a vancomycin resistant Enterococcus faecium . Causes loss of bacterial membrane integri... |
A1YLB9 | MAPARAGCCALLLLLLGLWVAEIPVSAKPKDMTSSQWLKTQHMQPSPQACNSAMNNINKYTEQCKDLNTFLHELFSSVATTCQTPNIACKNSRKNCHQSHGPMSLTMCELTSGKYPNCRYKEKHLNAPYIAACDPPQQGDPGYPLVPVHLDKVV | Function: Has a low ribonuclease activity.
Sequence Mass (Da): 16987
Sequence Length: 154
Subcellular Location: Secreted
EC: 3.1.27.-
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O69161 | MTKTPAKKKRARSSKAKGTDANAALEARIGHSFADPNLLMQGITHVSALKSGRKRGDSYQRLEFLGDHVLGLVVSDMLYHAFPNADEGELSKRLAELVRKESCADVAKSLGLLDDIKLGSVGPSADARLRKSVLGDICEAVIGAIFLDGGHAAAAEFVKRNWTERMHKPRRPLRDPKTVLQEWAQGKGLPTPVYREVERTGPHHDPQFRVAVDLPGLAPAEGIGGSKRAAEKVAASVMIEREGVGGGNDG | Function: Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the o... |
Q8R9W3 | MLTYLEQKINYEFKDKTLLLEALTHSSWAHEGKNEKVSNERLEFLGDSVLSLVISEYLYKNRKDLEEGSLSKYRAEIVCEPSLARCARKIELGSFLRMGKGEEISGGRDRDSILADAMEALLAAVYLDGGLEAVRRVILDLFKEIIDEVLKGIIYRDYKTRLQEVVQSMEVGKITYELVEEIGPDHNKTFVTQVKIGDVVLGIGQGKSKKESEQAAAMEALSKLGILK | Function: Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the o... |
Q5YS08 | MTASKDDAGASDDHASLLEALGVDVRPDLLRLALTHRSYAYENGGLPTNERLEFLGDSVLGLSITERLYHEHPDKSEGELAKLRASVVNMHALAEVARGLGEGGLGAHLLLGKGEELTGGRDKPSILADGMESLLGAVHLQHGIDVARGVVLRLFADLLERGPRMGAGLDWKTSLQELTAERGLGVPSYEISSTGPDHDKEFTATTVIGGRAYGQGVGRSKKEAEQKAAGAAYQALTAES | Function: Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the o... |
Q8ER05 | MDIRPLEEHLGISFQQKALLKEAFTHSSYVNEHRKQRLSDNERLEFLGDAVLELAVSQYLYRNNKDMPEGEMTKLRAAIVCEPSLKNFAEELEFGKFLRLGKGEQQTGGRERPAILADAFEAFLGALYLDQGFDNVLDFLNIHVFPKLTTGAFSHAMDYKSQLQEFVQQHKDQKIEYRIIEEKGPSHNKEFVAEVVIQEKAAGIGTGRTKKEAEQRAAKNALDSINNS | Function: Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the o... |
Q310Z1 | MFEKLQDVLCYRFADVRLLETALTHSSYANERGTEIEHNERLEYLGDAVLELTVSEQLFTRFPEAREGQLTRMRARLVSKPSLAELARELKLDTYLLLGKGEESQGGRTRSSVLSDAFEAILGAIFLDGGYAAAGKTVLHVFSSRWPQGAEAARTKDAKSTLQELTQRLFKERPVYTLLGSSGPEHEKIFKVRLLLPDGRALETEGQSVKRAEQKAAGLALELLEGESA | Function: Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the o... |
Q6YPW7 | MKNIQTLFQTLNITPQNLTLYKQALTHSSYSNEQNPPQEDNERLEFLGDAIVGLLMADYLYSQSKEDEGIMTKKRAQAVCERSLTIYAHNIELQNYLLLGKGEKNKDFNAKSIIADTFEALFGAIYLDLGYLTAKKVFHNIVLPHLAKTIYIIDFKTQLQEIVQSEKKTIQYKIVQEQGPAHSKNFVAEVYLEKNLLGTGEGSTKKAAEQKAAQQALSKVAKPKDLLNNKGGKEKELQ | Function: Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the o... |
Q6MEK1 | MLPRILYMNPIEHVIRQAPAIEAKLGYTFKDPQLLVLAFVHRSFINENREVNQHNERLEFLGDSVLGMLISDYLYCKLPKTPEGQLSYLRSRLVEASSCVHYIQSLDLSGYLLLGKGERMNDGRGRESILADLFEAIIGAIYLDGGLQAAKDFLFKNFHQHIEIILATPLRNWKALLQDYCQKNYQQTPLYQVLHESGPDHSKVFQISVWIQDRELGRGKGTSKKEAQQAAAADALSRVELP | Function: Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the o... |
P57805 | MTQNLERLQRQIGYQFNQPALLKQALTHRSAAVKHNERLEFLGDAILNFIIAEALYHQFPKCNEGELSRMRATLVREPTLASLARQFELGDYLSLGPGELKSGGFRRESILADCVEAIIGAISLDSDLATTTKIVQHWYQAQLKQIQPGDNQKDPKTRLQEYLQGKRLPLPTYNVVEIKGEAHCQTFTVECYVKNIDRTFMGSGASRRKAEQAAAEKILQLLEMK | Function: Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Also processes some mRNAs, and tRNAs when they are encoded in the rRNA operon (By similarity).
Catalytic Activity: Endonucleolytic cleavage to 5'-pho... |
Q03FX0 | MIKALEDDLSQTFDIHFNNHALLDEAFTQASYVNEHPHQELKFYERIEFLGDAVLQLIVSEYLFKRYPEMPQGKLTRLRAAMVCEASFSDFAKECHFDQYIRLGKGEEKSGARQRSSLLCDIFESFIGALYLDQGRAAVERFVRIVIFPKLDEGKFDHIIDHKSELQELLQKNGDVEIDYELVSEEGPENDLIFTVSVTADHKKLATGTGHSKKVAEQNAANQALQLLRRPK | Function: Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the o... |
Q4FLS9 | MKTNPIKLEKKLKLKFSDQKIFIKSLTHKSFDSINNNEKIEFLGDRVLGLIIAKKLLELYPDEKEGVLDKKFASLVNKKKCLEIAKKIELEKYILVLNPKNKKIEIEDKIVADCLEALIGAIYLDKGLNFTERFILNLWSEHITASVITQIDAKTKLQEYSLKIFKVLPIYKLISNTGPRHKPLFKVAVKLKNTKFFTAEGTSKKDAEQNAASLCLQDIFKK | Function: Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the o... |
G3XCR8 | MTKKDIVSIVSKERAEEIYGLLTQSNLHSSDIEVIKKNEDYCLKILNEALTHTSFNLSINHERLEFQGDAVLRLAASEYIQSHFPKLSVGDRSALRAQLVSDRWLAKVGYKIGIKTTMLIANKALKDEAATDTICAEGTEALIGALYECLRNIDAIQNWLEPYWNIESEEVLADPHKQNEKSALQEWSQGQGLNKPIYTIKEISKQHGDLKRFYCTVHIQNDFRGEGWGSSRKKAQKEAAKEALKKLTN | Function: Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the o... |
Q9PB98 | MISSKASDYQQRIGYVFTDPSLLLQALRHCSAGTPHNERLEFLGDSVVNLLIAEALFQRWPRADEGALTRARSELVRETSLASIARTMQLGEQLILGPGELKSGGHRRDSILADAVEAVIAAIYLDADLATCRTVVLPWFETALTALPVGKPEKDPKTRLQEWLQARQWSLPVYELIFESGDPHTKHFRVSCTLGELKLRTEGEGSSRRLAEQDAASHAIDQLDSNK | Function: Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the o... |
D5BDP9 | MSVIRNILNSRSSKGGNFFNTLHKLLGFRPKDLSVYERAFTHRSLNVKDPSGNPINYERLEFLGDAMLGSVIASHLYQEVPEGDEGYLTKMRSKIVSRKHLNELGKDLNLIRFVKSNIPNDQFGVNIHGNIFEALVGAIYLDRGYKYCNRFIYNRVIEPYVDIETLEGRVISYKSLLIEWCQKQKKEFNYQVYEDTGRDELKHFAVKLWIDKKVIAKARATSKKKAEEKASKRAYYALQNKMN | Function: Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the o... |
Q9Z5U2 | MADKRFFGTKTFPNQEKALKAKIMNNDAFISWIEKNLGHRPKDPALFLRAMTHPSHGNSDYQRLEFLGDRVLGLVIANWLYDLFPREPEGKLSRRLNSLVSGASCASIARIVGLPQWLRLGKQARDDGAAASDNVLGDVMEAMIGAIFLESGIEAAGKLIHKYWAPLVTGQESAPKHPKSALQEWAAAHNRRPPVYEIVSRTGPQHNPCFTIQVSIAGVGEASAEGSSKQEAQTAAAQALLDILAQ | Function: Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the o... |
Q92730 | MKERRAPQPVVARCKLVLVGDVQCGKTAMLQVLAKDCYPETYVPTVFENYTACLETEEQRVELSLWDTSGSPYYDNVRPLCYSDSDAVLLCFDISRPETVDSALKKWRTEILDYCPSTRVLLIGCKTDLRTDLSTLMELSHQKQAPISYEQGCAIAKQLGAEIYLEGSAFTSEKSIHSIFRTASMLCLNKPSPLPQKSPVRSLSKRLLHLPSRSELISSTFKKEKAKSCSIM | Function: Lacks intrinsic GTPase activity. Has a low affinity for GDP, and constitutively binds GTP. Controls rearrangements of the actin cytoskeleton. Induces the Rac-dependent neuritic process formation in part by disruption of the cortical actin filaments. Causes the formation of many neuritic processes from the cel... |
Q8BLR7 | MKERRAPQPVVVRCKLVLVGDVQCGKTAMLQVLAKDCYPETYVPTVFENYTACLETEEQRVELSLWDTSGSPYYDNVRPLCYSDSDAVLLCFDISRPETMDSALKKWRTEILDYCPSTRVLLIGCKTDLRTDLSTLMELSHQKQAPISYEQGCAIAKQLGAEIYLEGSAFTSETSIHSIFRTASMVCLNKSSPVPPKSPVRSLSKRLLHLPSRSELISTTFKKEKAKSCSIM | Function: Lacks intrinsic GTPase activity. Has a low affinity for GDP, and constitutively binds GTP. Controls rearrangements of the actin cytoskeleton. Induces the Rac-dependent neuritic process formation in part by disruption of the cortical actin filaments. Causes the formation of many neuritic processes from the cel... |
C4LEP7 | MLEYLLLLISTVLVNNFVLVKFLGLCPFMGVSKKIEPAVGMGLATTFVLTLTSAFAYLVQHYLLVPLAAESLSTLAFILVIAVVVQFTEMVIHKSAPDLYRILGIYLPLITTNCIVLGLALLNITMQHNFMQSVVYGFGGGLGFMLVLILFASLRERLAAADVPAPFQGIAIGMVTAGLMSLAFLGFTGLIKL | Function: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 20788
Sequence Length: 193
Subcellular Location: Cell inner membrane
EC: 7.-.-.-
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A0A0H3AKU6 | MLLLWQSRIMPGSEANIYITMTEYLLLLIGTVLVNNFVLVKFLGLCPFMGVSKKLETAIGMGLATTFVLTLASVCAYLVESYVLRPLGIEYLRTMSFILVIAVVVQFTEMVVHKTSPTLYRLLGIFLPLITTNCAVLGVALLNINENHNFIQSIIYGFGAAVGFSLVLILFASMRERIHVADVPAPFKGASIAMITAGLMSLAFMGFTGLVKL | Function: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 23263
Sequence Length: 213
Subcellular Location: Cell inner membrane
EC: 7.-.-.-
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Q3SHB7 | MFTAIWVMVGLAIAIGLILGWSAIRFKVEGNPLAEKIDAILPQTQCGQCGFPGCRPYAEAIAKGEADINQCPPGGEEGVKKLAELLGVEPKPLDEAHGTPKPKSVAFIDEQTCIGCTLCIQACPVDAISGAAKQMHTIIADECTGCELCLAPCPVDCISMVPIAEDLPHWKWKHPVVMMKQVGESTRV | Cofactor: Binds 3 [4Fe-4S] clusters.
Function: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
Sequence Mass (Da): 20053
Sequence Length: 188
Subcellular Location: Cell inner membrane
EC: 7.-.-.-
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C4LEP6 | MNHILLIILIFAALALIFGLLLGFAAIHFKVESDPIVDQLDALLPQTQCGQCGYPGCRPYAEAIANGDSINKCVPGGAQTIQNIADLMGVEPPSDDNELLMAPPKRVAFIHENLCIGCTKCIQACPVDAIIGAPKLMHTILRSECTGCDLCVDPCPTNCIEMIELPATPDRWKWDVETIPVRMVQ | Cofactor: Binds 3 [4Fe-4S] clusters.
Function: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
Sequence Mass (Da): 20055
Sequence Length: 185
Subcellular Location: Cell inner membrane
EC: 7.-.-.-
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A5F2R3 | MSTIVIAVIALAALAAVFGAILGFASIRFKVEADPIVDQIDAILPQTQCGQCGYPGCRPYAEAIANGDAINKCPPGGQATIEKLADLMGVEVQDSAHDLDNKVKMVAFIHEDMCIGCTKCIQACPVDAIVGGNKAVHTVIKNECTGCDLCVAPCPTDCIEMIPVQTTPESWKWQLNAIPVVNVTDSAPAAQKSAN | Cofactor: Binds 3 [4Fe-4S] clusters.
Function: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 20441
Sequence Length: 195
Subcellular Location: Cell inner membrane
EC: 7.-.-.-
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H6LC32 | MNVKHGTFKGGIHPPYRKESTAEVPLGFGKKPEMVIIPMSLHIGAPCTPIVKKGDTVFLGQRVGEPNGFVSVPVHASVSGKVIAVEERPHASGDRVMSVVIESDGLDTIDPSIKPYGTLEDMDADAIKKMVLNAGIVGLGGATFPTHVKLAIPPDKKVDCVVLNGAECEPYLTADHHLMTSQAEKVVMGLKLAMKSVGVEKGFIGVEDNKTDAIEALVKAIGNDSRLEVYSLHTKYPQGAEKQLIAAITGREVPSGALPADAGVVVMNVGTAAQIAESMITGLPLYKRYLTCTGDAIKNPQTIEIRIGVPFQSVIDQCGG... | Cofactor: Binds 2 [4Fe-4S] clusters per subunit.
Function: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane. Couples electron transfer from reduced ferredoxin to NAD(+) with electrogenic movement of Na(+) out of the cell. Involved in caffeate respiration.
Ca... |
P44291 | MGTVKITSRYGILLGFIALLCTIISAGIFFLTKDKIDAVIAAQQRELLLQVIPQDYFNNNLLESAVIPQDKNFVGIQKIYFAKKDGNVSAYAYETTAPDGYSGDIRLLVGLDPKGEVLGVRVIEHHETPGLGDKIERRISNWILGFTNQSINEHNLSEWAVKKDGGKFDQFSGATITPRAVVNQTKRSALIMLNNQALLQQLSTQVK | Function: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 22908
Sequence Length: 207
Subcellular Location: Cell inner membrane
EC: 7.-.-.-
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Q8TSY2 | MSDSKEITKVIVTMVVISAVAAALLALTYTPTQAQLKLLQAEQQKEAMKEILPQAADFEPVTGSEVDDDGNPVVLYYKGVDSSGNVVGYVVERNQVGAQGMIQLLAGISSDFSTITGFQVMKHSETPGLGALITTPEFQGQFVDLPVADTSLTKNGGQVDAISGATISSQAVVDALHSAVDYVSAQEG | Function: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane. Catalyzes Na(+) transport, most probably coupled to electron transfer from reduced ferredoxin to methanophenazine and heterodisulfide reductase. Involved in heterodisulfide reduction during methanog... |
Q9CNP4 | MKTVKISAYYAILLALIALICTALSTGIYLLTKSKIEDEINKQRQALLLEVVPQAYFDNPLSENCQRPNSEKLRAQRIDRLCIATKNNQKTAYAFETVAPDGYAGRIRLLVGITPTGTILGVRVLEHQETPGLGDKIETRISDWILSFSQQQLRSDNLADWAVKKDGGKFDQFAGATITPRAVVNQVKQSALSLLDELNQEN | Function: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 22450
Sequence Length: 202
Subcellular Location: Cell inner membrane
EC: 7.-.-.-
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Q15RL1 | MKQIIAKNGLILSLFAIITSGLIALTYFGTQEQIELQRQQTLLAILDELVPRGSYDNLMQHDCVLVTSQAYLGSNSPQHIYRATRAGEPVAAVIEATAPNGYSGRIELVVGLSGDATVSGVRVIDHKETPGLGDKIDLRISDWVLGFNNQQLTQDNASNWAVKKDGGQFDQFTGATITPRAVVSAVKNTALYYQANKEAIFSASNECRSQLASQG | Function: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 23244
Sequence Length: 215
Subcellular Location: Cell inner membrane
EC: 7.-.-.-
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B7UVW9 | MDAATRRSMLRNALLLGLFALVGVGLVALVQQFTEARIAEAQREARGRALLELLPPGSYDNHPLDSQVPTFAPKLLGLDAPRPAYVARLHGQASAVILQASAPDGYSGAIQLLVGVTAQGRLLGVRVVAHKETPGLGDRIELAKSPWVHGFDGKSLGDPADAGWAVKKDGGTFDQFAGATVTPRAVVRAVHKALRYFDANRERLLAPEEAAGHE | Function: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 22724
Sequence Length: 214
Subcellular Location: Cell inner membrane
EC: 7.-.-.-
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A4XS49 | MLPEISRSMLKNALVLGLFAIGTVGSVALLQQGTATRIAAAEREAQVRALAEILPAGSYDNHLLDNRIELNAPELGHRSPQSAYLALKGEQPSALILPVTAPDGYSGAIHLLVGIFADGRLAGVRVLGHRETPGLGDKIELAKSDWIRSFEGKSLSDPNEDGWAVKKDRGEFDQFAGATITPRAVVKAVHGALRYFDKHRAQLLGLAEDEQ | Function: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 22651
Sequence Length: 211
Subcellular Location: Cell inner membrane
EC: 7.-.-.-
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P97054 | MTDTPPPEKPKLPWFKASPLAHGIMLAMFALVTAVLLAVANDSTSAPIAARGAEDLAASLEQVIPHDLHDNDLAAAMRPVSDAEEGTIKVYVATKAGAVTGLAYELSGPGYSGQIRVLLGIAPDGTLLGVRVLSHTETPGLGDKIEVAKDDWILGFAGKSLADPEPGHWKVKRDGGVFDQFSGATITPRAVVKTIYRGLMFFDRNKAALTAPLPPKS | Function: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane (By similarity). Required for nitrogen fixation. Involved in electron transfer to nitrogenase .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 22847
Sequence Length: 217
Subcellu... |
Q8EE77 | MNNPMIKNGLLLALFALLCTGLVAVVNQQTFDKIKLQQQKELMGILHQLIPEEIHDNELTAQCTLLQNKEALGTEDAMPAYIATAAGKPVAIAMEAIAPDGYNGNIKLIVGINTQGEVLGVRTLAHQETPGLGDKIELRKSDWVTKFVGKVLKSEDDKQWQVQKDGGDFDQFTGATITPRAYVKAVKRAVWYFTQHQAEIFSQPLNCEAKHD | Function: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 23414
Sequence Length: 212
Subcellular Location: Cell inner membrane
EC: 7.-.-.-
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B9MQX2 | MRLSEDENYFEIEEKLLNEGYRFICGVDEAGRGPLAGPVFAAAVVMDRKRIIEGVRDSKKLTPKKREKLFEEIIKESIAYSVAMVDSKVIDEININNATFLAMKNAIENLKIEPDIVLVDGYKIPNLGFNQRAIIKGDRKSYSIACASILAKVSRDRYIVEISSKYPLYKFEKHKGYGTKEHIEILQKYGPCEIHRISFLKNILSL | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da)... |
A8MAH5 | MGTVNSLEAGIDEAGRGPVIGPMVIAIVGWSNSEAEGIGVKDSKQLTPSGRSRLYKLIVSKAPCVRHVIVEPSEIDYYVNRGLLNELEAIKMSELIKACSGVTRVYVDSPDPNPSRFRGFINVKDVELIVLNHADESIPLVSAASIVAKVIRDTIISRLKETYGDFGSGYPSDPRTISALRRWINNGTLPPIVRRSWRTIKRMTNSRLF | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da)... |
Q8R9X9 | MKKLNLRQLKEHLYHGSLQDLDFSNLTSSAKAWLEREIKRIEEMKFYEKKLYEEGLNFIAGVDEAGRGPLVGPVVAACVILPKEIFIPEINDSKKLPEEKREKLAEVIKKEAISYGIGIVDCREIDEINILNATLKAMKKAIFEVKEKIEYLLVDAISIPDMPIKQLPIVKGDSKSISIAAASILAKVERDRIMREYHKLYPQYNFAKNKGYGTKEHIEALKKYGPCPIHRRTYVEKILKG | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da)... |
Q9PJA1 | MKTLFDTKELLNEFDINLIGIDEAGRGALAGPMMMAACKLNKQLDGLCDSKKLSEKKREELYEIIIKNSNYLILAFSSEQIDALGLSTCLKKGLKLIKKHFKTENNFLYDGNTNLGINGIKTQIKADTSILQVSAASILAKVSKDRVMNFLAKDFPCYEFEKNKAYGTKAHKEFIAKFGICKLHRKSFKLL | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da)... |
Q3AC76 | MQGKFDKIANITLVMKTLDNNLPFNLQIENQLFSSGYELVAGGDEAGRGPVAGPVVAAIVVIKPGIYIPEVDDSKKLSSKKREKLFEEIINLVTDWSVAVVGPDLIDRLNIYQATKFAFKAALDSLSIKPEALILDALKLTGFSGKQVSMVKADEISFAVACASILAKVIRDKIMEQYDKDFPGYGFKKNKGYLTREHREALELLGPSPIHRKSFEPIKSFYGQLKLFEKV | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da)... |
P0CAW4 | MPPGPDMTLELACGQAPVCGVDEAGRGPWAGPVSAGAVILDPDRIPKGLNDSKKLSAKARAALEEEIKDVAISWCVGLASIEEIAQLNILHAAGLAMRRAVEGLAVTPAFALVDGNYAFKLPCPVKTVIKGDSLSCSIAAASILAKEARDRIMIEADALYPGYGFAGHKGYHAKVHVEGLRRLGPSPIHRLGWAPVKAALAAAAVNGELDL | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da)... |
A0RV25 | MLVCGVDEAGRGSLVGPLVIAGVAIKRNRMRELKSMGVRDSKKLTRKARESLYPEIVNMADSYHISRVPPGVVDRSVGRHMLNDLEARYMARVITRLGHGTTYVDSCDVNPRRFGGRVSEMSGRTVRSYHRADDRFVIVSAASILAKVARDRSIERLRKSHDVGSGYPSDRRTVGFVRGYYNKNGAMPPFVRRSWRPARLIEAGG | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da)... |
Q3J6H3 | MEITCPDWTHETAALAEGFTCVVGVDEVGRGPLAGPVTAAAVRLFPGRIPEGLNDSKKLTAPRREMLAAEIHTVAEVSIAHASVEEIDRLNILQASHLAMGRALAGLPSRPDFALIDGHMVPKGLGHRCRAIVKGDALCLSIAAASIVAKVARDRIMVDLEQQHPGYGWRTNAGYGTKDHLQALLNLGPTPHHRRSFKPVHNILYQEASISP | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da)... |
Q5ZVR7 | MNTVLKILMAGVDEVGRGPLAGAVVTAAVILKKPIDGLTDSKKLSPKQRNLLAIRIKEEALAFAYGRAEVEEIDQLNIHHATLLAMRRAVEALPIQPDNVFVDGAFTPQLNIPCKAIVQGDSLIPEISAASILAKVLRDEEMVALDKIYPGYGFAEHKGYATPVHKEALMRLGPCKIHRRSYSPVADLISK | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da)... |
B1MZ17 | MTETIATIKEKLASLADPHDARLLTWRQDKRCGVQKAIALWEKRLALARKKQADFNQRFNFERDYWLKGVELVAGVDEVGRGPLAGPVVAAAVILPHDFNIVDVIDSKQVAQHKREQLYEIILDQAVSIGIGSVDAKTIDEINIYEAARQAMTEAINNLAPQPQALLIDAMQVYLDITQQSLIKGDARSNSIGAASIVAKVIRDKMMTDYDKVYPGYDFAQNAGYGTKKHLAGIDKLGVTPIHRRSFQPVHDAIVNKKNC | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da)... |
Q1WU07 | MEKLTIAQIKKMLTEEISSEQLAELKLDERKGVQLAIKSYEKRLKKIENEKLEFQNRLKIERDLWDKGIEYIAGVDEVGRGPLAGPVVTAAVILPHDFDVFEVNDSKQLSEKKREELYKKILEKAVAVSVGLSDNNLIDEVNIYEATRLAMKQAIESLNITPQKIIVDAMTIDTKIPQLRLIKGDAKSASVAAASIVAKVTRDHLMQFYARIYPGYGFEKNDGYGTKQHLEGLENKGVTPIHRQSFEPVKKILLK | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da)... |
Q8Y7K4 | MSDSISVIKEKLSEVTSENDPFFQKCIQDERKGVEKLVQSVRRKWEKEAKLLVKLKEMTQYETDLFQQGYKYIAGVDEVGRGPLAGPVVAAAVILPADFSVVGINDSKQLSEAKRDALFEKIKKEAIAIGVGIIEHDVIDQVNIYEATKLAMCEALNQLTPEPDFVLIDAMPLRYTEAELSLIKGDTKSISIAAASIIAKVTRDRLMQMYDEKYPGYDFANNMGYGTKKHLLGLDTIGICPIHRMSFSPVKESKLHFDSLN | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da)... |
B9EBC6 | MKSNDYTIASLKEKVREMNQAELIDFFEEESRSGALKVKQARVKQIAQETQAIHEYEQMLEYERRYNGKVVCGIDEVGRGPLAGPVIACAVILNDGHHYIGLNDSKQLSKHKRASLYDALTQSVTYAIGAASVEEIDKFNIYEATKLAMHRAIDKLPVKPDVLLIDAMNLNTGLIEESIIKGDAKSVSIAAASVIAKVYRDHLMEEIHEEFPYYDFNRNAGYGTKRHLDGLMQYGITAHHRKSFEPIKSMIKTEENAKTITKPS | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da)... |
A0L4Z0 | MRHKAHPGPDLELECALLRSNRAIKTLCGVDEAGRGPLCGPVVAAAVVLDLDNLPVGLNDSKQLSAKKREQLFEQIYVTSQVGVGEASVAEIDALNILHASMLAMVRAVTALQGRLVVDHALIDGNRVPATLPVPGQAVVKGDAKSLSIAAASIIAKVTRDRIMAELDRDYPHYGWAKSQGYPTQAHLQALALHGVTPHHRRSFKPVKQLLPH | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da)... |
Q50412 | MPDLALEFEIGGIVCGIDEVGRGPLAGPVVAAAVILDPARLPKTLLERLDDSKKLSKRNREELAELVPATAILGFGEASVEEIDRINILQATFLAMRRAYDALGRECAHALVDGNRPPGLPCPVRCVVGGDGISLSIAAASVVAKVRRDAMMADLARAHPEFGWERNAGYGTAEHLDALKRLGPTPHHRRSFAPVAQYMLF | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da)... |
Q0AMK3 | MSVTIPQKDNQSLNKAGMGNTVRIAGVDEAGRGPLSGPVVAAAVILDPTRPITGLGDSKALSERRRRELFRLIRANAWVGIGIAEPAEIDRLNILHATMAAMRRAVARLPVRPTLVLVDGNRLPPGLPCPAEAIIKGDAKEACIGAASIIAKTVRDDLMEQAARRFPGYGFEGHKGYPSAAHKAALETSGACPIHRRSYAPVRAALESRFSTNANRCG | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da)... |
P94541 | MSHSVIKVSLSAIDQMKMTYSGSLTASVPQGAVFQAKPPGCTITAYQSGKVLFQGKNAAAESARWGTAEPQEKKKTAKKPADPRYAPPADIAGMSVIGSDEVGTGDYFGPMTVVCAYVDKTMLPLMKELGVKDSKDLKDPQIIEIARNLIKTIPYSLLVLKNEKYNSMQEKGMSQGKMKALLHNQAITHLLRKLDGVKPEAILIDQFAEPGVYFNHLKGRDIVKERTYFSTKAEGIHLAVAAASIIARYSFLMEMDKLSRAAGMTLPKGAGPHVDEAAAKLILKKGASALRTFTKLHFANTQKAQRLADKKRS | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da)... |
Q9Z6J1 | MPPPFVVTLTTSAQNNLRDQLKEKNFIFSQPQNTVFQARSNTVTCTLYPSGKLVIQGKGSEEFIEFFLEPEILHTFTHARVEQDLRPRLGVDESGKGDFFGPLCIAAVYASNAEILKKLYENKVQDSKNLKDTKIASLARIIRSLCVCDVIILYPEKYNELYGKFQNLNTLLAWAHATVINNLAPKPAGDVFAISDQFAASEYTLLKALQKKETDITLIQKPRAEQDVVVAAASILARDAFVQSIQKLEEQYQVQLPKGAGFNVKAAGREIAKQRGKELLAKISKTHFKTFDEICSGK | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da)... |
Q31H49 | MQEVELFTDGGCRGNPGPGGWGALLRFGGVEKELKGAELDTTNNRMELTAAIEGLKALKRPCKVTLTTDSQYVKNGITQWMTNWKKNNWKTAAKKPVKNKDLWQALDEALQPHDVTWAWVKGHSGHDENERVDELANQAMDELTG | Cofactor: Binds 1 Mg(2+) ion per subunit. May bind a second metal ion at a regulatory site, or after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da): 16177
Sequence Length: 145
Subcel... |
Q0C3M1 | MTDKDMIEIWTDGACSGNPGPGGWGALIRWNGHEKELYGGDPATTNNRMEMTAVIEALNALNRPSKITLNVDSTYVKDGLTKWIKGWKRNGWKTADKKPVKNQELWMAMEEACKRHEITWVWVKGHAGDEGNERADGLARKGTDEVRGRK | Cofactor: Binds 1 Mg(2+) ion per subunit. May bind a second metal ion at a regulatory site, or after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da): 16853
Sequence Length: 150
Subcel... |
A9KLJ9 | MKVTIYTDGAARGNPDGPGGYGTILSYIDSTGVEHIREYSGGYKKTTNNRMELMAAIVGLEALTKPCVVTLYSDSQYVVKAFNEHWLDGWIKKGWKRGKNEPVKNVDLWKRLLAAKNQHDVTFCWVKGHDGHPQNERCDVLATTAADGGNLADDNVVE | Cofactor: Binds 1 Mg(2+) ion per subunit. May bind a second metal ion at a regulatory site, or after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da): 17485
Sequence Length: 158
Subcel... |
Q0AMI4 | MSTITIHTDGACSGNPGPGGWGAILEWNGHRKELKGGEADTTNNRMEMMAAIQALEALRKADRSVILITDSVYLRDGITKWIHGWKKRGWKTADKKPVKNVDLWQRLDELTRSHTIDWRWVKGHAGDPGNERADELAREGLAEARGRQP | Cofactor: Binds 1 Mg(2+) ion per subunit. May bind a second metal ion at a regulatory site, or after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da): 16707
Sequence Length: 149
Subcel... |
A9W185 | MGPMRTIVYADGGCDPNPGPGGWAAVIQAPTGTIELYGGELATTNNRMELTAAIRALEHFPEGAAIEMRCDSQYVVKSVTEWMRGWKARGWRTATGPVKNIDLMQRLDALAAARDVRWTWVRGHAGEAGNERADRLATLGRREALSGKTSGEAMPLPADAAPALAPAQPVQSKTVQVALSADLANALSRAAGRAGITPQAYLEDAVRLALELKPPGVARVRAELQKAS | Cofactor: Binds 1 Mg(2+) ion per subunit. May bind a second metal ion at a regulatory site, or after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da): 24205
Sequence Length: 228
Subcel... |
Q5UPY1 | MLSLIVLLEKETLRFSQMVLAWGNGRVGASGGIGIHFPNGELQDISLEFDKGCCTNQRTELYAILYAIQYIDDNFDLNKCKVMIKTDSTYSVNSITKWAEGHSRNDWCKRTGEPIANREFIQEIYEYYQNFNIDFEWVEAHTGQTDSESIANAQADFLANSAAKRAARDKKICRPSSSGSKRNSREFYCEKSSKQVYNTPYRSKSRASINGFPIDDDFEIELVKRRSDN | Cofactor: Binds 1 divalent metal ion per subunit. May bind a second metal ion at a regulatory site, or after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Mass (Da): 26195
Sequence Length: 22... |
O31760 | MKKKNTENVRIIALGGVGEIGKNLYVIEIDSDIFVVDAGLMHPENEMLGIDVVIPDISYLIERADRVKAIFLTHGHDENIGGVFYLLNKLSVPVYGTKLTLALLREKLKQYGHNRKTDLREIHSKSVITFESTKVSFFRTIHSIPDSVGVSFKTSLGSIVCTGDFKFDQTPALNQTCDIGEIAKIGNSGVLALLSDSANAERPGYTPSEAAVSGEISDALYNSQNRVIIAVFASNINRIQQVIHAAAQNGRKIAVAGKNLQSVLQLARKLGYIEADDELFISVQDVKKYPKREVAIITAGSQGEPLAALTRMANKAHKQL... | Cofactor: Binds 1 zinc ion per subunit. The inability to bind a second zinc ion may explain its very poor exonuclease activity .
Function: Endonucleolytically cleaves the 5'-leader sequence of certain mRNAs. Endonuclease digestion by the RNase J1/J2 complex occurs at a different site and in some cases more efficiently ... |
Q8TYB5 | MRVSENFALRVHVDEVDPLRMALAAERLDYEIAVLCLELEAERLNIDDLRWLIEEIRDIREHVESVLVLPGCKLEAESAGALRRAIRRTRPLVYLLAVGGGDPKINRAAVSDTRVDLLSHPERGNPHAGLGKYEIELAREKWTYVEIDLSRLFRREGERLAWQVSRIRDLLRLRRRKRFPTTVALGARDPLELIRPKQVEDLLKLMGFEDSEVKEMCVEAPREILRWNAACKHVFTVPGVVSLG | Function: Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 28043
Sequence Length: 244
Subcellular Location: Cytoplasm
EC: 3.1.26.5
|
P60781 | MLEGIFDINHVFDEEGIKTLKRFGWDGSVAVQNHNEYSEEKINTAVEYGENCEFKVYSGVKISTKNQNEMEKAVKKYRNKVDILLVEGGDVKINRRVLEMNDVDILSTPELNRMDNGLDHILARLGSTNRVAVELNFGNLLKSKNYDRSKILWAFQRNLKLSKKYDTPVVISSGANDIYGIKAPGDLRGFLNTVADPLYSKKIIETTSKIIDYRLYLKNKNVLMPGLEIVEE | Function: Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 26452
Sequence Length: 232
Subcellular Location: Cytoplasm
EC: 3.1.26.5
|
O26784 | MIPQRILMKFFDFHIQGRDHDSSLRLLLEASRLGYQGGVLVYPSERYPDLKSDLESLRENPELQDFEIARGVMINASDPRDMRRSVNKFRKKADVIYVSGGNLKVNRAACESRRVDVLSAPYTSRRDPGINHVLAREAARNNVAVELPLADVIGSWLKVRARVLEQFREILKLHRKFGFPLLLTSRASSIYDLRTPGDIMNLAECFGMESSEAEESLTSTPASILEDSGNRHLLIAEGVRLLPES | Function: Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 27680
Sequence Length: 245
Subcellular Location: Cytoplasm
EC: 3.1.26.5
|
Q3IPJ7 | MYEGVHAHPDGNATVARFAETAASRGYDGIVVRNHGDAQTDYDADAVAAEYGVEVVSGIEIRTDDTAQASGLVGNYRSKRDIVCVHGGELNRFAVEEPKVDVLAHPMRDGDVNHVLAKAAAENGVHFEFNFGRVLRADGGKRVQAIQGLRKLRELVDQYDAPYVVSADPESHLELRSSRDLAAVGETVGFDREAITDGLAAWADIVERNRRRRSAAVVEPGVRIERADGETDDSRE | Function: Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 25695
Sequence Length: 236
Subcellular Location: Cytoplasm
EC: 3.1.26.5
|
O59543 | MVGGGGVKFIEMDIRDKEAYELAKEWFDEVVVSIKFNEEVDKEKLREARKEYGKVAILLSNPKPSLVRDTVQKFKSYLIYVESNDLRVIRYSIEKGVDAIISPWVNRKDPGIDHVLAKLMVKKNVALGFSLRPLLYSNPYERANLLRFMMKAWKLVEKYKVRRFLTSSAQEKWDVRYPRDLISLGVVIGMEIPQAKASISMYPEIILKRLKY | Function: Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Not absolutely essential for activity in vitro, however it strongly stimulates activity. Binds RNase P RNA.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA prec... |
P87120 | MFIDLNVVWPTLGVKDLNLVKTVKTLERLGYTAIALNYQYDGKLQNVIKNPIVKELYPEQKIKIYSRITLTIESMPQNKVLSNVTKEFDILAIRPIGDRLLQQTCSDLEFDILSIDFTQRLPFYLKHTFMGLAVSRDIGIEISYSSGLRDVSNRRNLITNATSLVRATRGRGIIVTSETRTPLECRAGFDVINLATFWDLKQDQARKSVGESCRSVLLHAETRRDTYRSILNGCH | Function: Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 26799
Sequence Length: 235
Subcellular Location: Nucleus
EC: 3.1.26.5
|
Q9YD20 | MKSRRSRCRRSFTTLVRREEERLARWALELARRGLTGEARRVAEQLFQLAASTRVRPPRRVKRLFCKNCRTPLIPGLTARVRLRSQGGMSYTVVTCLSCGWIHRYPYRKGPRGGAPISPPAAEYGSGGRDSGEREDKGPQGPPRQGGRDNRQGGGHQGGPKGD | Cofactor: Binds 1 zinc ion per subunit.
Function: Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 18167
Sequence Length: 163
Subcellular Lo... |
O30127 | MLRRDKKRESRIARERVFYLIKRAEEWKNIDYELARRYVELARKIAMRYRVRIPRELKATYCKKCLYPYKAGKFRVRVRKSRVIITCLNCGFERRIPIRPKRVNRKV | Cofactor: Binds 1 zinc ion per subunit.
Function: Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 13307
Sequence Length: 107
Subcellular Lo... |
B0R3R4 | MASIAAERIDRLHTLARAAARTGDDDRAREYVRLARRLAERNRLTLPPAFRRFTCDDCDAVLVPGRNARVRTRSGHVVVTCDCGTHARYPYTG | Cofactor: Binds 1 zinc ion per subunit.
Function: Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Mass (Da): 10469
Sequence Length: 93
Subcellular Loc... |
Q98R57 | MKKIYHIRKNWEFQAIINSKRQVISKNLIFYYQRNNTFKIGVSIPKKFAGAVKRNFYKRQIMAILRDIQDLTNLEYKIVMIVRKNFMALDFLEKKKEIQKMLERFKNEKRK | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of... |
Q4A5G4 | MKKQYRLRKNWEFDLVLKNKKFIANKYVIVYYKKASAFKVGITVPKKFANSVGRNYHKRQMKAIVHKMNLYNYPYEMVIIIRKNFINCNFLTKVIEIEKIFTQFKQQNEKIK | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of... |
A1TI29 | MLPAQHRMTRSTEFGATVSKGTRAAQPDVVVYRLRSDQTADPGPRVGLIVSKAVGNAVQRHRVSRRLRHAALAVLEDLDPSDRVVIRALPRSRDAVTPRLEQELRTALERIRQRTGAPS | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of... |
B2A474 | MSQIVTLKKNYQFRRVFRYGQSYATKYIVLFVLENSLNINRVGFSVGKKVGNSVTRNRVKRLLREVYRLNNPNMMQGYDLILLARFRADELDYHKCQREFIRLTKKSKLLQKNVI | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of... |
Q9JXS6 | MDYRFGRQYRLLKTDDFSSVFAFRNRRSRDLLQVSRSNGNGLGHPRIGLVVGKKTAKRANERNYMKRVIRDWFRLNKNRLPPQDFVVRVHRKFDRATAKQARAELAQLMFGNPATGCRKQA | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of... |
Q82X99 | MTTRQICTLPRQCKLRKADEFRAVLRNRIVFESLSLRLYVKPIDVDYARIGLIVAKRVERKAVRRNRIKRLIREAFRRHRQMLMGLDCVMQLRHPVELLDSTRIYQEAVMLFNKAARQL | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of... |
Q3J6L7 | MKQFGFTRLMRLVDPGDFKQIFAAGERVSSKAFTVLYHSNSLEYPRLGMAIPRKHFSRAVDRNRIKRLVRESFRQRQQVLGGRDLVVLSKPGINRHPNSDLLRCLERQWIGLVKQCSDS | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of... |
A6Q3D2 | MKGVQTLKTKREFDYVYKRGIAFHSPYFVLFYIPDKDMRIGFVASKKVGKAVQRNRAKRVLKALFIQYFDQLPIGRYVFVAKPKLLGADFKRIDQEMTKILERIKRRKW | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of... |
Q6FFX5 | MRLDQRALDQLRDVKITRNYTRYAEGSVLVEFGHTKVLCTASIDNSVPRFLKGQGQGWVTAEYGMLPRSTHTRSDREAARGKQTGRTQEIQRLIGRSLRAMVDLKKLGENTITIDCDVIQADGGTRTAAITGAAVALIDAMNVLLEKKKIKQDPLKGLVAAISVGIYQDEVLLDLCYEEDSNCQTDLNVVMTQAGEFIEIQGTAEEKPFTRTQANAMLEVAEKGIQELIKKQQQALGW | Function: Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. ... |
A0AHX9 | MRVDGREKNALRKIEVTPDYLMHPEGSVLIASGNTKVICSASVETKVPPFMRGEGRGWISAEYSMLPRATNTRNIRESSKGKVTGRTMEIQRLIGRALRAVVDLDALGERTIWLDCDVIQADGGTRTASITGAFIAMVMAIAKLDEQVPFTKFPVKDFLAATSVGVLEEGGTVLDLNYIEDSAAQVDMNIIMTGSGAFVELQGTGEEATFSETELAELIALGKKGISELIEIQKEILGDKITARIKGE | Function: Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. ... |
Q9HAU8 | MAAQCCCRQAPGAEAAPVRPPPEPPPALDVASASSAQLFRLRHLQLGLELRPEARELAGCLVLELCALRPAPRALVLDAHPALRLHSAAFRRAPAAAAETPCAFAFSAPGPGPAPPPPLPAFPEAPGSEPACCPLAFRVDPFTDYGSSLTVTLPPELQAHQPFQVILRYTSTDAPAIWWLDPELTYGCAKPFVFTQGHSVCNRSFFPCFDTPAVKCTYSAVVKAPSGVQVLMSATRSAYMEEEGVFHFHMEHPVPAYLVALVAGDLKPADIGPRSRVWAEPCLLPTATSKLSGAVEQWLSAAERLYGPYMWGRYDIVFLP... | Cofactor: Binds 1 zinc ion per subunit.
Function: Broad specificity aminopeptidase which preferentially hydrolyzes an N-terminal methionine, citrulline or glutamine.
Catalytic Activity: Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.
Sequence Mass (Da): 80000
Sequence Length:... |
A6QR16 | MDLSGVKKKSLLGVKENNKKSSTRAPSPTKRKDRSDEKSKDRSKDKGATKESSEKDRGRDKTRKRRSASSGSSSTRSRSSSTSSSGSSTSTGSSSGSSSSSASSRSGSSSTSRSSSSSSSSGSPSPSRRRHDNRRRSRSKSKPPKRDEKERKRRSPSPKPTKVHIGRLTRNVTKDHIMEIFSTYGKIKMIDMPVERMHPHLSKGYAYVEFENPDEAEKALKHMDGGQIDGQEITATAVLAPWPRPPPRRFSPPRRMLPPLPMWRRSPPRMRRRSRSPRRRSPARRRSRSPGRRRHRSRSSSNSSR | Function: Part of pre- and post-splicing multiprotein mRNP complexes. Auxiliary component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors... |
Q15287 | MDLSGVKKKSLLGVKENNKKSSTRAPSPTKRKDRSDEKSKDRSKDKGATKESSEKDRGRDKTRKRRSASSGSSSTRSRSSSTSSSGSSTSTGSSSGSSSSSASSRSGSSSTSRSSSSSSSSGSPSPSRRRHDNRRRSRSKSKPPKRDEKERKRRSPSPKPTKVHIGRLTRNVTKDHIMEIFSTYGKIKMIDMPVERMHPHLSKGYAYVEFENPDEAEKALKHMDGGQIDGQEITATAVLAPWPRPPPRRFSPPRRMLPPPPMWRRSPPRMRRRSRSPRRRSPVRRRSRSPGRRRHRSRSSSNSSR | Function: Part of pre- and post-splicing multiprotein mRNP complexes. Auxiliary component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors... |
O67622 | MDVLSILLILVAVGVGIFVGRQFLGQKQAPAPTYQPVPSPQILEEAKSKAEEIIKEAKEKAEVILKEAKESAEKIVREAEEKAEKLIREAKEEVERIKEEVERRKKELKEREENVLAKERHLDRRWEALEKREEELLHRERELKDFERSLERWRDEIRHKEEELKHMKEEVEELKKKELEELQRIAKLTLEEARQEIIKKVEEEAKKDAVKLMKVIEEDAKRRAEFEAKKIIATATQRLAPQIAVNYTTTTVELPSNEFKGRIIGREGRNIRTFEILTGVDLIIDDTPDIVTISSFDPLRREIAKEALQRLIADGRIHPA... | Function: Endoribonuclease that initiates mRNA decay.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 64329
Sequence Length: 558
Subcellular Location: Cell membrane
EC: 3.1.-.-
|
Q81A17 | MTSTVWILISILLATVGAVVGFFVRKSIAEAKINGAANEARRILDGANRDAEALKKEALLEAKDEIHTLRTEAELEIRDRRSELQKQENRLMQKEENLDRKDETLDKREQQLEKKEESLVARQQQIEELESKVGELVQKQQTELERISNLTREQAKAIILGKVESEVSHEIAVMVKESEVRAKEEADKKAKEILSLAMQRCAADHVAETTVSVVNLPNDEMKGRIIGREGRNIRTLETLTGIDLIIDDTPEAVILSGFDPIRRETARIALDKLVQDGRIHPARIEEMVEKSRREVDEYIREVGEQTTFEVGVHGLHPDLI... | Function: Endoribonuclease that initiates mRNA decay.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 58588
Sequence Length: 520
Subcellular Location: Cell membrane
EC: 3.1.-.-
|
O31774 | MTPIMMVLISILLILLGLVVGYFVRKTIAEAKIAGARGAAEQILEDAKRDAEALKKEALLEAKDEIHKLRIDAEQEVRERRNELQKQENRLLQKEENLDRKHEGIDKREAMLEKKDHSLNERQQHIEEMESKVDEMIRMQQSELERISSLTRDEAKQIILERVENELSHDIAIMTKETENRAKEEADKKAKNILSLALQRCAADHVAETTVSVVNLPNDEMKGRIIGREGRNIRTLETLTGIDLIIDDTPEAVILSGFDPIRRETARIALDKLVQDGRIHPARIEEMVEKSRREVDDYIREMGEQTTFEVGVHGLHPDLI... | Cofactor: Magnesium. Can also use manganese or zinc.
Function: Endoribonuclease that initiates mRNA decay. Initiates the decay of all SAM-dependent riboswitches, such as yitJ riboswitch. Involved in processing of the gapA operon mRNA, it cleaves between cggR and gapA . Is also the decay-initiating endonuclease for rpsO... |
Q89ZG0 | MIAIIATAIACFVVGGILSYVLFRYVLKSKYDSVLKDAETEAEVIKKNKLLEVKEKFLNKKADLEKEVALRNQKIQQAENKLKQREMVLSQRQEEIQRKKLEAEAVKENLEAQLVIVDKKKEELDKLQHQEIEKLEAISGLSADEAKERLVESLKEEAKTQAQSFINDIMDDAKLTASKEAKRIVIQSIQRVATETAIENSVTVFHIESDEIKGRIIGREGRNIRALEAATGVEIVVDDTPEAIVLSAFDPVRREIARLALHQLVTDGRIHPARIEEVVSKVRKQVEEEIIETGKRTTIDLGIHGLHPELIRIIGKMKYR... | Function: Endoribonuclease that initiates mRNA decay.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 57199
Sequence Length: 511
Subcellular Location: Cell membrane
EC: 3.1.-.-
|
Q73R54 | MNWILYVILPAVCIILGWTIRWLYARFQLSASEQRAERILQEAIKDAEAQKKEFLLEAKEQLIREQKQQERENRERRSDLQRFERRLAQKEEVLDKRVETVEKQEKELIKREAALDERTEILSGEEERYREELERISGLTQQQAKDLIIRDLEAEAKHDAVTIINKIEQEAQLTAEKKAQDILITTIQRLATETASDITVSTVSLPSDEMKGRIIGREGRNIRALETLTGVDIIIDDTPEAVVVSCFDPVRKEIARVALERLILDGRIHPARIEEIVQKVTREISQKVYEEGEKVLFDLGIHNMNQEGVRALGRLYFRTS... | Function: Endoribonuclease that initiates mRNA decay.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 58024
Sequence Length: 509
Subcellular Location: Cell membrane
EC: 3.1.-.-
|
B1AI70 | MGYLIAFIILLILFVLLITIVPVVMVVYLKKKQLKLTFVPKSQTSFKKIVQKTKDLEEECEDLNNKNNELKKAISDQNLQIDLLKKNNENFLLNATSLTAEQAKKELFNLLKIKFKKELAQEYAKIKHEFNEAQEIYAQNILVETMEQIAEPLIVERSLFNIDIIDENLKGKIIGRDGRNKAVFENEGGVDLIVDRQQPIVGISTPNPIRREIARIVMQKLIDSKNIDINRIELLFKEEREKFEKKVFEIGKNVVEQTLGFFDLPEGIYSYIGRMKFRNSYGQNILSHSLEVAEYAERIAKLINIDPIKAKKAAFFHDIG... | Function: Endoribonuclease that initiates mRNA decay.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 54323
Sequence Length: 473
Subcellular Location: Cell membrane
EC: 3.1.-.-
|
Q8LGU7 | MEKKKAMQIEGYPIEGLSIGGHETCIIFPSLRIAFDIGRCPHRAISQDFLFISHSHMDHIGGLPMYVATRGLYKMKPPTIIVPASIKETVESLFEVHRKLDSSELKHNLVGLDIGEEFIIRKDLKVKAFKTFHVIQSQGYVVYSTKYKLKKEYIGLSGNEIKNLKVSGVEITDSIITPEVAFTGDTTSDFVVDETNADALKAKVLVMESTFLDDSVSVEHARDYGHIHISEIVNHAEKFENKAILLIHFSARYTVKEIEDAVSALPPPLEGRVFALTQGF | Cofactor: Besides the tightly bound Zn(2+) ion, TRZ1 requires additional Ca(2+), Mn(2+) or Mg(2+) for pre-tRNA processing, while bpNPP hydrolysis occurs without addition of metal ions but is stimulated 2- to 3-fold when free Mn(2+) or Zn(2+) ions are added.
Function: Zinc phosphodiesterase, which displays tRNA 3'-proce... |
Q9H777 | MSMDVTFLGTGAAYPSPTRGASAVVLRCEGECWLFDCGEGTQTQLMKSQLKAGRITKIFITHLHGDHFFGLPGLLCTISLQSGSMVSKQPIEIYGPVGLRDFIWRTMELSHTELVFHYVVHELVPTADQCPAEELKEFAHVNRADSPPKEEQGRTILLDSEENSYLLFDDEQFVVKAFRLFHRIPSFGFSVVEKKRPGKLNAQKLKDLGVPPGPAYGKLKNGISVVLENGVTISPQDVLKKPIVGRKICILGDCSGVVGDGGVKLCFEADLLIHEATLDDAQMDKAKEHGHSTPQMAATFAKLCRAKRLVLTHFSQRYKP... | Cofactor: Binds 2 Zn(2+) ions.
Function: Zinc phosphodiesterase, which displays some tRNA 3'-processing endonuclease activity . Specifically involved in tRNA repair: acts downstream of the ribosome-associated quality control (RQC) pathway by removing a 2',3'-cyclic phosphate from tRNAs following cleavage by ANKZF1 . tR... |
Q10155 | MSKTVNFRATKNFYLQFVSVSSRDTSCIPCIHLFFDSKRYVFGSVGEGCQRAILSQQLRLSKIKDVFLMQGSSISSPDTYDSSSSSSTTSVSDMLQLDDRDKVIVSERNSMCSTVNYPTWWDSCGGFPGFLLSLNDISEPGETGEASPFVLHGPSEVHQFLSSMRHFTYHTNVNLTVQGYTSAEAPVFVDENICVTPVVVSLVKNSFKKRKHENINRGTNARPLKEDRANTSPHWYSHVSNDTSFVVENAMYNTPAPLEPDKPELFISYIVQSHPTPGKFDAAKAKSLGITKGLDCGRLARGEPVTLENGKTVYPKEVIG... | Function: Zinc phosphodiesterase, which displays some tRNA 3'-processing endonuclease activity. May be involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing extra 3' nucleotides from tRNA precursor, generating 3' termini of tRNAs. A 3'-h... |
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