ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q5A651 | MDLVIMNFVFLLYLTSVVKCSIKLDFNKVSTPSKYTKRDALPMPLINDKILYTTELEIGSNKDKVSVSIDTGSYDLWVMSNDAVCYKVSEFQTEGAPQLPDIFNDIDQDYSCTFNGTYNSKSSKTFKNTSEDFSIGYVDGSAAQGVWGYDSVQFGQYGVTGLKIGIANRSSVSDGILGIGIANGYDNFPVLLQKQGLINKIAYSVYLNSSNSTTGTILFGAIDHAKYKGALSTVPVDSKSQLSVNVTNLKTKNGNVASGGHSILLDTGSTFSIFPDEWIDALGHSLNATYDEDESVYEIECDGYDEHFFGFSIGDSDFSVPIQDLKTEKDGQCYLAIMSNSVIGGGGILFGDDILRQIYLVYDLQDMTISVAPVVYTEDEDIEEILNPNEDQNEVPTSTSFTQSASSSGSQPSSTISGENMDKNTTSSSSGNCQTRSWIAILSALFLVYIHII | Function: Secreted aspartic peptidases (SAPs) are a group of ten acidic hydrolases considered as key virulence factors. These enzymes supply the fungus with nutrient amino acids as well as are able to degrade the selected host's proteins involved in the immune defense. Required for cell surface integrity and cell separation during budding.
PTM: O-glycosylated.
Location Topology: Lipid-anchor
Catalytic Activity: Preferential cleavage at the carboxyl of hydrophobic amino acids, but fails to cleave 15-Leu-|-Tyr-16, 16-Tyr-|-Leu-17 and 24-Phe-|-Phe-25 of insulin B chain. Activates trypsinogen, and degrades keratin.
Sequence Mass (Da): 49333
Sequence Length: 453
Subcellular Location: Secreted
EC: 3.4.23.24
|
Q9BXL6 | MGELCRRDSALTALDEETLWEMMESHRHRIVRCICPSRLTPYLRQAKVLCQLDEEEVLHSPRLTNSAMRAGHLLDLLKTRGKNGAIAFLESLKFHNPDVYTLVTGLQPDVDFSNFSGLMETSKLTECLAGAIGSLQEELNQEKGQKEVLLRRCQQLQEHLGLAETRAEGLHQLEADHSRMKREVSAHFHEVLRLKDEMLSLSLHYSNALQEKELAASRCRSLQEELYLLKQELQRANMVSSCELELQEQSLRTASDQESGDEELNRLKEENEKLRSLTFSLAEKDILEQSLDEARGSRQELVERIHSLRERAVAAERQREQYWEEKEQTLLQFQKSKMACQLYREKVNALQAQVCELQKERDQAYSARDSAQREISQSLVEKDSLRRQVFELTDQVCELRTQLRQLQAEPPGVLKQEARTREPCPREKQRLVRMHAICPRDDSDCSLVSSTESQLLSDLSATSSRELVDSFRSSSPAPPSQQSLYKRVAEDFGEEPWSFSSCLEIPEGDPGALPGAKAGDPHLDYELLDTADLPQLESSLQPVSPGRLDVSESGVLMRRRPARRILSQVTMLAFQGDALLEQISVIGGNLTGIFIHRVTPGSAADQMALRPGTQIVMVDYEASEPLFKAVLEDTTLEEAVGLLRRVDGFCCLSVKVNTDGYKRLLQDLEAKVATSGDSFYIRVNLAMEGRAKGELQVHCNEVLHVTDTMFQGCGCWHAHRVNSYTMKDTAAHGTIPNYSRAQQQLIALIQDMTQQCTVTRKPSSGGPQKLVRIVSMDKAKASPLRLSFDRGQLDPSRMEGSSTCFWAESCLTLVPYTLVRPHRPARPRPVLLVPRAVGKILSEKLCLLQGFKKCLAEYLSQEEYEAWSQRGDIIQEGEVSGGRCWVTRHAVESLMEKNTHALLDVQLDSVCTLHRMDIFPIVIHVSVNEKMAKKLKKGLQRLGTSEEQLLEAARQEEGDLDRAPCLYSSLAPDGWSDLDGLLSCVRQAIADEQKKVVWTEQSPR | Function: Acts as a scaffolding protein that can activate the inflammatory transcription factor NF-kappa-B and p38/JNK MAP kinase signaling pathways. Forms a signaling complex with BCL10 and MALT1, and activates MALT1 proteolytic activity and inflammatory gene expression. MALT1 is indispensable for CARD14-induced activation of NF-kappa-B and p38/JNK MAP kinases . May play a role in signaling mediated by TRAF2, TRAF3 and TRAF6 and protects cells against apoptosis.
Sequence Mass (Da): 113270
Sequence Length: 1004
Domain: A linker region between the coiled-coil and PDZ region holds the protein in an inactive state .
Subcellular Location: Cytoplasm
|
Q9WVG6 | MAAAAATAVGPGAGSAGVAGPGGAGPCATVSVFPGARLLTIGDANGEIQRHAEQQALRLEVRAGPDAAGIALYSHEDVCVFKCSVSRETECSRVGRQSFIITLGCNSVLIQFATPHDFCSFYNILKTCRGHTLERSVFSERTEESSAVQYFQFYGYLSQQQNMMQDYVRTGTYQRAILQNHTDFKDKIVLDVGCGSGILSFFAAQAGARKIYAVEASTMAQHAEVLVKSNNLTDRIVVIPGKVEEVSLPEQVDIIISEPMGYMLFNERMLESYLHAKKYLKPSGNMFPTIGDVHLAPFTDEQLYMEQFTKANFWYQPSFHGVDLSALRGAAVDEYFRQPVVDTFDIRILMAKSVKYTVNFLEAKEGDLHRIEIPFKFHMLHSGLVHGLAFWFDVAFIGSIMTVWLSTAPTEPLTHWYQVRCLFQSPLFAKAGDTLSGTCLLIANKRQSYDISIVAQVDQTGSKSSNLLDLKNPFFRYTGTTPSPPPGSHYTSPSENMWNTGSTYNLSSGVAVAGMPTAYDLSSVIAGGSSVGHNNLIPLANTGIVNHTHSRMGSIMSTGIVQGSSGAQGGGGSSSAHYAVNNQFTMGGPAISMASPMSIPTNTMHYGS | Function: Methylates (mono- and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in several proteins involved in DNA packaging, transcription regulation, pre-mRNA splicing, and mRNA stability . Recruited to promoters upon gene activation together with histone acetyltransferases from EP300/P300 and p160 families, methylates histone H3 at 'Arg-17' (H3R17me), forming mainly asymmetric dimethylarginine (H3R17me2a), leading to activates transcription via chromatin remodeling . During nuclear hormone receptor activation and TCF7L2/TCF4 activation, acts synergically with EP300/P300 and either one of the p160 histone acetyltransferases NCOA1/SRC1, NCOA2/GRIP1 and NCOA3/ACTR or CTNNB1/beta-catenin to activate transcription . During myogenic transcriptional activation, acts together with NCOA3/ACTR as a coactivator for MEF2C . During monocyte inflammatory stimulation, acts together with EP300/P300 as a coactivator for NF-kappa-B . Acts as coactivator for PPARG, promotes adipocyte differentiation and the accumulation of brown fat tissue . Plays a role in the regulation of pre-mRNA alternative splicing by methylation of splicing factors . Also seems to be involved in p53/TP53 transcriptional activation . Methylates EP300/P300, both at 'Arg-2142', which may loosen its interaction with NCOA2/GRIP1, and at 'Arg-580' and 'Arg-604' in the KIX domain, which impairs its interaction with CREB and inhibits CREB-dependent transcriptional activation . Also methylates arginine residues in RNA-binding proteins PABPC1, ELAVL1 and ELAV4, which may affect their mRNA-stabilizing properties and the half-life of their target mRNAs . Acts as a transcriptional coactivator of ACACA/acetyl-CoA carboxylase by enriching H3R17 methylation at its promoter, thereby positively regulating fatty acid synthesis . Independently of its methyltransferase activity, involved in replication fork progression: promotes PARP1 recruitment to replication forks, leading to poly-ADP-ribosylation of chromatin at replication forks and reduced fork speed (By similarity).
PTM: Phosphorylation at Ser-217 is strongly increased during mitosis, and decreases rapidly to a very low, basal level after entry into the G1 phase of the cell cycle (By similarity). Phosphorylation at Ser-217 interferes with S-adenosyl-L-methionine binding and strongly reduces methyltransferase activity. Phosphorylation at Ser-217 may promote cytosolic location .
Catalytic Activity: L-arginyl-[protein] + 2 S-adenosyl-L-methionine = 2 H(+) + N(omega),N(omega)-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-homocysteine
Sequence Mass (Da): 65854
Sequence Length: 608
Subcellular Location: Nucleus
EC: 2.1.1.319
|
Q54ST2 | MTKNKSKNKSNNSNISNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNKNGESQLKNKNKNISENQHIYDKHNHDHSHDHNHDYDDNNEDDEEKEELEHYQLIVSTLLNYSQYSLHWVKDMQDFFHYKLSEDEKKLLPNYNAKMEALARAVLVNSQFLKKIGNEHCNIFSQSSDNSANSERIVDPTNLDHIKIDYFMMDQLKSTIRQLVREWSEEGKLERDQAFEPIKQQLLEIYGHIPFQERSKIRVYSPGAGLGRLCLEIASLGFSSQGIEYSFMMLIVSNFMLNKVEKINEFKIHPYIHQTVNVLRDIDQLRTVTIPDVLSSELLPKNNPALEFSMSAGDFTKNIEENSFDCICTCFFIDTAPNILEYVDCISKILKPGGTWINFGPLLYHHAKKKDSIELSYEQLRYLICKKQFQFKKEEIRDAEYCSNQKSLLRSIYKCQFFVVINNKPT | Function: N-methyltransferase that mediates the formation of anserine (beta-alanyl-N(Pi)-methyl-L-histidine) from carnosine.
Catalytic Activity: carnosine + S-adenosyl-L-methionine = anserine + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 54029
Sequence Length: 463
EC: 2.1.1.22
|
Q9I7X6 | MSSMDCATFPMHPKMDEQLARTFVINEEEEEKHIQKVQNAFLYYGPYACQRLKRSMDYLNSLSGEDQIMLAKYRGHLECVRTCIDRNQAVIREILRGRVLYPTDEATGDPSEFDEPPPNVRHGDMDQAQSTLKLIARDWSTEGALEREQSYKPIIDSIVAYFKHSDFELKDIKILVPGAGLGRLTYELACLGYSCEGNEFSYFMLIASNFVLNLCDNENKYVLYPWVHQYVNNLRREDQVAPVRFPDVCPLKNPPKGHFEIAAGDFLEVYKTPNAYNCVATCFFIDCANNVIDFIRTIYKILVPGGIWVNLGPLLYHFSDVSGQNSIEPAFEDLCIIMESVGFVIEKSRTGIRTKYAQNPSSMKQSEYQSLFWVCRKPDLFEEQRGKRKASREPHDLIVREDSEEEGEQQPERNETEEKQQLKPLATANCETEIKEQPS | Function: N-methyltransferase that mediates the formation of anserine (beta-alanyl-N(Pi)-methyl-L-histidine) from carnosine.
Catalytic Activity: carnosine + S-adenosyl-L-methionine = anserine + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 50504
Sequence Length: 439
EC: 2.1.1.22
|
Q8N4J0 | MQRRRRPPPPTSRLPEGCGGGGGGSEEVEVQFSAGRWGSAAAVSAAAAAATRSTEEEEERLEREHFWKIINAFRYYGTSMHERVNRTERQFRSLPANQQKLLPQFLLHLDKIRKCIDHNQEILLTIVNDCIHMFENKEYGEDGNGKIMPASTFDMDKLKSTLKQFVRDWSETGKAERDACYQPIIKEILKNFPKERWDPSKVNILVPGAGLGRLAWEIAMLGYACQGNEWSFFMLFSSNFVLNRCSEINKYKLYPWIHQFSNNRRSADQIRPIFFPDVDPHSLPPGSNFSMTAGDFQEIYSECNTWDCIATCFFIDTAHNVIDYIDTIWKILKPGGIWINLGPLLYHFENLANELSIELSYEDIKNVVLQYGFKVEVEKESVLSTYTVNDLSMMKYYYECVLFVVRKPQ | Function: N-methyltransferase that catalyzes the formation of anserine (beta-alanyl-N(Pi)-methyl-L-histidine) from carnosine. Anserine, a methylated derivative of carnosine (beta-alanyl-L-histidine), is an abundant constituent of vertebrate skeletal muscles. Also methylates other L-histidine-containing di- and tripeptides such as Gly-Gly-His, Gly-His and homocarnosine (GABA-His).
Catalytic Activity: carnosine + S-adenosyl-L-methionine = anserine + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 47186
Sequence Length: 409
Domain: The Gly-Xaa-Gly-Xaa-Gly (GXGXG) motif binds the adenosyl part of S-adenosyl-L-methionine.
Subcellular Location: Cytoplasm
EC: 2.1.1.22
|
Q5BJZ6 | MQRRRRAPPASQPAQDSGHSEEVEVQFSAGRLGSAAPAGPPVRGTAEDEERLEREHFWKVINAFRYYGTSMHERVNRTERQFRSLPDNQQKLLPQFPLHLDKIRKCVDHNQEILLTIVNDCIHMFENKEYGEDANGKIMPASTFDMDKLKSTLKQFVRDWSGTGKAERDACYKPIIKEIIKNFPKERWDPSKVNILVPGAGLGRLAWEIAMLGYACQGNEWSFFMLFSSNFVLNRCSEVDKYKLYPWIHQFSNNRRSADQIRPIFFPDVDPHSLPPGSNFSMTAGDFQEIYSECNTWDCIATCFFIDTAHNVIDYIDTIWRILKPGGIWINLGPLLYHFENLANELSIELSYEDIKNVVLQYGFQLEVEKESVLSTYTVNDLSMMKYYYECVLFVVRKPQ | Function: N-methyltransferase that catalyzes the formation of anserine (beta-alanyl-N(Pi)-methyl-L-histidine) from carnosine. Anserine, a methylated derivative of carnosine (beta-alanyl-L-histidine), is an abundant constituent of vertebrate skeletal muscles. Also methylates other L-histidine-containing di- and tripeptides such as Gly-Gly-His, Gly-His and homocarnosine (GABA-His).
Catalytic Activity: carnosine + S-adenosyl-L-methionine = anserine + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 46385
Sequence Length: 400
Domain: The Gly-Xaa-Gly-Xaa-Gly (GXGXG) motif binds the adenosyl part of S-adenosyl-L-methionine.
Subcellular Location: Cytoplasm
EC: 2.1.1.22
|
Q9Y7J3 | MEYDEEEVKVLKEVLSAFFLYRQYAHTITQQKRKSMSRLSFEHKDLLLQDSDNNFLKHLSRIDQCIEQNSVLAEAIANAAIPVFCSDFDQNELFHVNVDMMQKVSSTLKQIARDWSTECVEERRTTYAPFIEELNSLFPSDSIDRSKIRVLVPGSGLGRLAFDIAVEGFACQGNEFSYFMLLTSHFILNCVKQENQFLVYPYIHSFSNHVMRDDQVRSLNIPDAVPSQYLRNSQNFSMAAGDFLEVYGTEESRDSFQVVATCFFIDTTKNILDYLDTIKNCLVDGGYWINLGPLLYHFESEGTSNSNSDSQQQPFVELTLEQLFYVMDSMGFEVLKHNSVDTTYMGDKRSMLEWIYHPHYWVCRLQKSKLRFQ | Function: N-methyltransferase that mediates the formation of anserine (beta-alanyl-N(Pi)-methyl-L-histidine) from carnosine. Also methylates other L-histidine-containing di- and tripeptides such as Gly-Gly-His, Gly-His and homocarnosine (GABA-His).
Catalytic Activity: carnosine + S-adenosyl-L-methionine = anserine + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 43335
Sequence Length: 373
Subcellular Location: Cytoplasm
EC: 2.1.1.22
|
P53934 | MDENEFDNQRENKAVARVIISFLKYEEYALKEIYNLRVKKWASISDRQKDMVPNYTKYLANLKAAIIENGKFFRSVAEYALQSISFEPGEIVQPNDLDMSKTCSLLTQVYREWSAEAISERNCLNSRLVPFLKTLSPPKADILIPGCGTGRLLVDLSRMGYNCEGNEFSYHMLLVSQYMLNAGLLQNQIIIYPFIHCFSHWKKIEDQLSPIKVPDIEAWSSNKGMGSMSICAGSFVDCYGRNQGTKISSHYTFSRRMQLSRAKAENSKDVVVTNFFIDTGSNILDYLDTIGHVLKPGGIWCNFGPLLYHFENDHGVETTYEVNPYSGFQDKINDYTPLMGLELSSDDIISIATNHLDFELIRRESGILCGYGRYAGPESCAMPGYMCHYWILKSNPTNES | Function: N-methyltransferase that mediates the formation of anserine (beta-alanyl-N(Pi)-methyl-L-histidine) from carnosine. Also methylates other L-histidine-containing di- and tripeptides such as Gly-Gly-His, Gly-His and homocarnosine (GABA-His).
Catalytic Activity: carnosine + S-adenosyl-L-methionine = anserine + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 45497
Sequence Length: 400
EC: 2.1.1.22
|
D0C9N4 | MDMDNQNTKIYTDKFLAVTSLLFVFISVAGLAIYSQESIKIAATWMQWTTSVFTTPVLLFAFLAIIFTFGLAFSKYGKIKLGEGKPQYSTMSWIFMFILSGIGSSTLYWGFLDWAYYYQTPGLSLPPESAEALKYSVAYSFFHSGLSAWAIYALASISLCYSYHVRKNKGLSLASVIEAVTGFKSTGVVGRLVDLMFLLCMFGALTISLVLTAVTFTNILSQLTGIPNTFMTKVIIILAVSVLFALSSYVGMDKGMQRLSHMVCLGVVLFAIYVLCFGPTQFILNNSLMSFGLMATNFVDMSLFTDPMGDGKFTREWTVFYWLWWISYAPGVALFVTRVSKGRTIKEVIFAMVIGGSVGLWFIFGVFENYSVYSFIHGAVNVPQILSQQGGEVAIGQLLSLLPAGKLMMWIFLGIMVVFLAAHMDAVGYAVSATCTRGLSEGQDPSPNARLFWCVMLTLVPIAMIFSKAPLDTMKTATIVTALPFIVIILIQTYGLVKWLIQDYAKVPSHLIEQQGYDDQEIGLNQTQDEHAKRMQLELASSIKLDRKTS | Function: Catalyzes the energy-dependent uptake of carnitine and is essential for growth on carnitine. Can also mediate the uptake of choline. Is probably a proton:substrate symporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 60971
Sequence Length: 550
Subcellular Location: Cell inner membrane
|
S0ELR6 | MADHLYARKNDALNVNPDIVNGQRSDINITVRGSDWYWAVCAVMTVSTFAFLGLGMRKPRTDRIFHYITAGITMIASIAYFTMASNLGWTPIAVEFQRSNHRVAGIYREIFYARYIDWFLTTPLLLTDLLLTAGMPWPTVLWVILVDWVMIVTGLVGALVKSSYKWGYFAFGCAALAYIVYVLAWEARLHAKHVGPDVGRTFVMCGSLTAVVWILYPIAWGVCEGGNLIAPDSEAVFYGILDLIAKPVFGALLLWGHRNIDPARLGLRIRDIDERIFPDGPNNKVASGHGARNDTATASGSNVNPNA | Function: Opsin-like protein; part of the car gene cluster that mediates the biosynthesis of neurosporaxanthin, a carboxylic apocarotenoid acting as an essential protective pigments and leading to orange pigmentation . The exact role of carO in carotenoid biosynthesis is not known yet, but it could be involved in the regulation of the pathway by light or other stimuli (Probable).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34002
Sequence Length: 307
Subcellular Location: Membrane
|
F2XG53 | MKHINDYFWAKKTEENSRLLWLPLTQHLEDTKNIAGLLWEHWLSEGQKVLIENSINVKSNIENQGKRLAQFLGAVHDIGKATPAFQTQKGYANSVDLDIQLLEKLERAGFSGISSLQLASPKKSHHSIAGQYLLSHYGVDEDIATIIGGHHGRPVDDLDGLNSQKSYPSNYYQDEKKDSLVYQKWKSNQEAFLNWALTETGFNSVSQLPKIKQPAQVILSGLLIMSDWIASNEHFFPLLSLDETDVKNKSQRIETGFKKWKKSNLWQPETFVDLVTLYQERFGFSPRNFQLILSQTIEKTTNPGIVILEAPMGIGKTEAALAVSEQLSSKKGCSGLFFGLPTQATSNGIFKRIEQWTENIKGNNSDHFSIQLVHGKAALNTDFIELLKGNTINMDDSENGSIFVNEWFSGRKTSALDDFVVGTVDQFLMVALKQKHLALRHLGFSKKVIVIDEVHAYDAYMSQYLLEAIRWMGAYGVPVIILSATLPAQQREKLIKSYMAGMGVKWRDIENIDQIKIDAYPLITYNDGPDIHQVKMFEKQEQKNIYIHRLPEEQLFDIVKEGLDNGGVVGIIVNTVRKSQELARNFSDIFGDDMVDLLHSNFIATERIRKEKDLLQEIGKKAIRPPKKIIIGTQVLEQSLDIDFDVLISDLAPMDLLIQRIGRLHRHKIKRPQKHEVARFYVLGTFEEFDFDEGTRLVYGDYLLARTQYFLPDKIRLPDDISPLVQKVYNSDLTITFPKPELHKKYLDAKIEHDDKIKNKETKAKSYRIANPVLKKSRVRTNSLIGWLKNLHPNDSEEKAYAQVRDIEDTVEVIALKKISDGYGLFIENKDISQNITDPIIAKKVAQNTLRLPMSLSKAYNIDQTINELERYNNSHLSQWQNSSWLKGSLGIIFDKNNEFILNGFKLLYDEKYGVTIERLDKNESV | Cofactor: Mn(2+) or Mg(2+) or Ca(2+). ATPase and nuclease activities are dependent on divalent cations, for ATPase Mn(2+) is marginally preferred over Mg(2+) or Ca(2+).
Function: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Cas3 plus Cascade participate in CRISPR interference, the third stage of CRISPR immunity. Functions as a ssDNA-dependent ATPase; dsDNA, ssRNA do not stimulate ATPase activity, while other nucleotides (aside from dATP) are not hydrolyzed. Functions as a ssDNA nuclease; activity does not require ATP. Functions as an ATP-dependent helicase; helicase activity requires hydrolysable ATP. Unwinds both DNA/DNA hybrids and RNA/DNA hybrids, moving mostly in a 3' to 5' direction.
Sequence Mass (Da): 105760
Sequence Length: 926
Domain: Proteins of this family have an N-terminal nuclease domain and a C-terminal helicase/ATPase domain. In some CRISPR/Cas systems the domains are swapped, in others they are encoded separately.
EC: 3.1.-.-
|
Q53VY2 | MSVEEAALALWAKSGNPFHPLLAHMLDTAAVALAVLRMEPPRTRALYAEDWGLPEEGALAWAAALVGLHDLGKASPVFQAGWEEGKERVQRAGLPFGELLDWVAHGVFTELFLRRLLKEKGLPERAANDLAAALGAHHGFPANAEEKSRARRHLRTEDPLWKEARRWLLEEVFRRLGAPLPPSQGNGEARPEAVLRVMALASFADWVASDPSLFPYGRDPRRGDYLKEALRLAQEALNRLGWPAFAKAQRREFGELFPYIPKPNALQESVPALLEGACTPVLLLVEAPMGMGKTEAALYAHHLLQAGLGHRGLYVALPTQATANGLFPRVRGFLERLGEGSRLELQLQHGTALLNPHYAGLLERAAPRQVGEEEEGGAVASAWFSARKRAMLAPYGVGTLDQALLGVLRVKHHFVRLWGLMNRVVVLDEVHAYDVYTSGLLQALLRWLRALGSSAVVMTATLPPSRRRALLEAWAGEEVEGQDLGPYPRVVLVGEGVKARSLPPAREVEVALEVLREVDVEPLAQRLKGALPGAVGAIVNTVDRAQDLYRALGEGTPLTLEELARRLGGISGGQAWEEVRQALPERGGEVVGKVLTDGTLVFLLHARFPAEERALRGSVVLALFGKGGPRPPRAILVATQVAEQSLDLDFDLLYTDLAPIDLLFQRSGRLHRHERPRPEEHARPRLLLGVPEDLDFGKPLYWDKVYEDYVLLATWRALSGRDRLRVPGDLEALLEEIYEGENPESFPEGLRERAKKSLKALQERRDREANTARRLSLSELDRLLAYWDEGALVAQERLEDDEEKAETQRLLTRLGDPSVAVVPLFRVGEGLFLDREGRRRAPLKGEVSREEAEALFRRAVRLSRFPLPQELLKEEPPPAWRKSGLLRGLRPLEVGRVFRSGERAFQVELDPELGVVYLPV | Cofactor: The ssDNA endonuclease activity (residues 6-260) is stimulated by Mn(2+), Co(2+), Ni(2+), Cu(2+) and Zn(2+), but not by Mg(2+) or Ca(2+). A Ni(2+) ion is seen in crystals upon soaking.
Function: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Cas3 plus Cascade participate in CRISPR interference, the third stage of CRISPR immunity. The N-terminal domain (residues 6-260) acts as a ssDNA endonuclease, has no activity on dsDNA.
Sequence Mass (Da): 102127
Sequence Length: 920
Domain: Proteins of this family have an N-terminal nuclease domain and a C-terminal helicase/ATPase domain. In some CRISPR/Cas systems the domains are swapped, in others they are encoded separately.
EC: 3.1.-.-
|
Q9YCL9 | MRPVSMLKEYAYCPRVAYYMEVLRPSYRPTEPMNLSREIYSVDHVRGILRSSGFRIVKEEWAVPLRSKRLGLQGVADGVVVEGSLGIIVVEAKLSVRSNRWLHTRGRHVIFQAAAYALALEETRGYSVDYLAIVSLEDSKTYVVKMSPSLRRDVIRLADDMNKTLDDGLEPPPKPGRKCVACRFRRVCQPWVAERGSER | Cofactor: Mg(2+) or Mn(2+) required for ssDNA cleavage activity. Can also utilise Cu(2+).
Function: CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). This may be a 5' to 3' ssDNA exonuclease (By similarity).
Catalytic Activity: exonucleolytic cleavage in the 5'- to 3'-direction to yield nucleoside 3'-phosphates.
Sequence Mass (Da): 22699
Sequence Length: 199
EC: 3.1.12.1
|
A0Q5Y6 | MNMDIFDNDLSIPVNLIRQWCFCPRIVYYQELLAIKPNKPLWVAQGEEFHKKVEQLEKRRSFSRYGLENAIRHFNLSIKSQKYKLHGIVDWVIETDTNVYVVEYKTNPNPNSLGHKLQIAAYALLVQEYFAKPCKTTFLTSDKKSYEIKITDELINKLIKTISDILSTLDSGNKPDSSASDHQCIQCEYYNFCNDR | Cofactor: Mg(2+) or Mn(2+) required for ssDNA cleavage activity.
Function: CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). This may be a 5' to 3' ssDNA exonuclease (By similarity).
Catalytic Activity: exonucleolytic cleavage in the 5'- to 3'-direction to yield nucleoside 3'-phosphates.
Sequence Mass (Da): 22909
Sequence Length: 196
EC: 3.1.12.1
|
D4GQN9 | MSSTDVVEEYVQDERDPSRSPNVPITGLMVQYYHVCKRELWFMANGIDIDRETTNIQRGTHVDETSYGTSRRSFMIDNRIQLDILDSGDVMEVKVSSALEKPARMQLLFYLWYLREIHDIDKDGVLAYPTERKRESVVLDETTTAEVESTVRGVLDVVGRDSPPQLEKKPYCGTCLYQDLCWM | Cofactor: Mg(2+) or Mn(2+) required for ssDNA cleavage activity. Can also utilise Cu(2+).
Function: CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). This protein may be a 5' to 3' ssDNA exonuclease. Plasmid targeted by CRISPR locus P1 transform wild-type cells very poorly .
Catalytic Activity: exonucleolytic cleavage in the 5'- to 3'-direction to yield nucleoside 3'-phosphates.
Sequence Mass (Da): 21152
Sequence Length: 183
EC: 3.1.12.1
|
Q57822 | MENYLEEELIIGGIEINYLYVCKTKLWYFVRGITMEQESDFVDLGKFLHEKSYFGEEKEVQIGSIKIDFIKKRDVIEIHEVKRGKQMEKAHIMQVLYYIYYLNSLGIKSKAILHYPKLKEIKEIELKENNKEEIKRAIKEIEYIKSLKEPPEPIYQKICKNCAYYELCFI | Cofactor: Mg(2+) or Mn(2+) required for ssDNA cleavage activity. Can also utilise Cu(2+).
Function: CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). This protein may be a 5' to 3' ssDNA exonuclease.
Catalytic Activity: exonucleolytic cleavage in the 5'- to 3'-direction to yield nucleoside 3'-phosphates.
Sequence Mass (Da): 20420
Sequence Length: 170
EC: 3.1.12.1
|
A3MTK6 | MELLSPKPLCSVVNCEDLEKLDHVSALNELRREQEIFKLLPGIYAHRYDFRRVSPSIINDFEYCPRLLWVQHKLGLKLLSEKSVVSIIRGRILHERYERLLSQYENVVAEYKVEIGDLVGVVDLVIKRGGEYIPVEIKTGFSKEAHKTQLQIYISMLKARFGYLVYRNHVEVVHRNDAALDVLKKIREILSAREAPPAKCNSCIFKPICKNLL | Cofactor: Binds 1 [2Fe-2S] cluster per subunit. Not required for nuclease activity, since mutation of the Cys residues leads to a colorless but active protein.
Function: CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). A ssDNA exonuclease that has 5' to 3' activity, yielding 5'-OH and 3'-phosphate groups. Has Mn(2+)-dependent endonuclease activity on circular ssDNA. Can unwind dsDNA; unwinding does not require ATP.
Catalytic Activity: exonucleolytic cleavage in the 5'- to 3'-direction to yield nucleoside 3'-phosphates.
Sequence Mass (Da): 24673
Sequence Length: 213
EC: 3.1.12.1
|
Q2RRV2 | MAPSDTPPSAEDLPSQGELALFAPPATAEDALVPASMVNAWIYCPRLAVLEWGRGEKARSVDLIAGLRAHQATESGPTPALPDPMVLREDQSLKTRKLSLSSERLGLTAELDLLDVEEGVVIPVEIKVGKRPSVDEGAYLPERAQVCAQALLLREAGYTCLEGALWFAESRERVTVDLTEALVTATLVATSDLRLTVASGRLPPPLDHSAKCPRCSLLPICLPDEIAWFRKGSIARTPPPPASPALPLYGQTPGARIGKKDRGGSVCLDRMAAWLSSRPVPCYAAIGMLNTASGASHPSVARHADGGASARSFRLPTAFRRPVRRSLPCYAAR | Cofactor: Mg(2+) or Mn(2+) required for ssDNA cleavage activity. Can also utilise Cu(2+).
Function: CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). This may be a 5' to 3' ssDNA exonuclease (By similarity).
Catalytic Activity: exonucleolytic cleavage in the 5'- to 3'-direction to yield nucleoside 3'-phosphates.
Sequence Mass (Da): 35537
Sequence Length: 333
EC: 3.1.12.1
|
Q97TX9 | MITEFLLKKKLEEHLSHVKEENTIYVTDLVRCPRRVRYESEYKELAISQVYAPSAILGDILHLGLESVLKGNFNAETEVETLREINVGGKVYKIKGRADAIIRNDNGKSIVIEIKTSRSDKGLPLIHHKMQLQIYLWLFSAEKGILVYITPDRIAEYEINEPLDEATIVRLAEDTIMLQNSPRFNWECKYCIFSVICPAKLT | Cofactor: Mg(2+) or Mn(2+) required for ssDNA cleavage activity. Can also utilise Cu(2+).
Function: CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA) (By similarity). This protein is a 5' to 3' partially processive exonuclease that cleaves off single mononucleotides. Has a marked preference for ssDNA, although in vitro it also acts on dsDNA and ssRNA. Has low endonuclease activity with circular ssDNA. Binds ssDNA and can unwind dsDNA; unwinding does not require ATP.
Catalytic Activity: exonucleolytic cleavage in the 5'- to 3'-direction to yield nucleoside 3'-phosphates.
Sequence Mass (Da): 23239
Sequence Length: 202
EC: 3.1.12.1
|
G4RJY5 | MSLCINPSLIRQYLYCPMAAYYIAAGAPEPPTLRMQRGREIQQEAAQAAAKALGAERAEYSVHITAPPLCGTVDAVLWINGRPSPLEVKAAARPRRIPIHHKAQAAAYIAMVQRAYGRAVATAYIYYAESGQIAQIRMAKDLQELLNYAVSRLQQILQGKPPVLNPNPAKCQNCWYRKWCSHLPTTVEKI | Cofactor: Mg(2+) or Mn(2+) required for ssDNA cleavage activity. Can also utilise Cu(2+).
Function: CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). This may be a 5' to 3' ssDNA exonuclease (By similarity).
Catalytic Activity: exonucleolytic cleavage in the 5'- to 3'-direction to yield nucleoside 3'-phosphates.
Sequence Mass (Da): 21116
Sequence Length: 190
EC: 3.1.12.1
|
Q65TW5 | MANRIRLHIWGDYACFTRPEMKVERVSYDVITPSAARGILSAIHWKPAINWVIDKIYVLKPIRFESVRRNELGAKISESKVSGAMKRKSVADLYTVIEDDRQQRAATVLKDVAYVIEAHAVMTSKAGVDENTTKHIEMFKRRALKGQCFQQPCMGVREFPAHFALIDDNDPLPLSQLSESEFNRDLGWMLHDIDFEHGNTPHFFRAELKNGVIDVPPFYAEEVKR | Cofactor: Does not require a metal cofactor.
Function: CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). This protein is a sequence-specific endonuclease that cleaves pre-crRNA at G21 into mature crRNA. Does not cleave pre-crRNA associated with the T.thermophilus strain HB27 Cas5 protein (AC Q746C2) CRISPR locus . The reaction mechanism may proceed by an intramolecular attack of the 2'-hydroxyl group of G21 on the scissile phosphodiester, cutting the precursor 3' to G21 residue yielding 5'-hydroxyl and 2' and/or 3' ends lacking a hydroxyl group (perhaps a 2'/3' cyclic phosphodiester) (Ref.2).
Sequence Mass (Da): 25831
Sequence Length: 225
EC: 3.1.-.-
|
Q746C2 | MARLKVKVWGEYACFSRPEFKVERVSYPVPTPSAARGLLEAIFWKPEFRYEVRRIGVLRLGTPFALLRNEVGNRMGAKPFFVEDARQQRTSLVLKDVAYLVEADMVLRPHATDPLPKYLEQFERRLKKGQYHHTPYLGTREFPAYFSPPDGEVPDGGLNLDLGPMLFDLAFVEDPGRPELTFKRPGRGEVQGYALPLFFHARIREGWLEVPAEKYQELYRLEEGHAKGA | Cofactor: Does not require a metal cofactor.
Function: CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). This protein is a sequence-specific endonuclease that cleaves pre-crRNA into mature crRNA, possibly by an intramolecular attack of the 2'-hydroxyl group of G26 on the scissile phosphodiester, cutting the precursor 3' to G26 residue yielding 5'-hydroxyl and 2' and/or 3' ends lacking a hydroxyl group (perhaps a 2'/3' cyclic phosphodiester). Requires between 4 and 8 nt downstream of the cleavage site for both binding and cleavage of pre-crRNA. Substitution with dG at this position abolishes cleavage but not RNA binding. Does not cleave pre-crRNA associated with the M.succiniciproducens strain MBEL55E Cas5 protein (AC Q65TW5) CRISPR locus.
Sequence Mass (Da): 26367
Sequence Length: 229
EC: 3.1.-.-
|
P70677 | MENNKTSVDSKSINNFEVKTIHGSKSVDSGIYLDSSYKMDYPEMGICIIINNKNFHKSTGMSSRSGTDVDAANLRETFMGLKYQVRNKNDLTREDILELMDSVSKEDHSKRSSFVCVILSHGDEGVIYGTNGPVELKKLTSFFRGDYCRSLTGKPKLFIIQACRGTELDCGIETDSGTDEEMACQKIPVEADFLYAYSTAPGYYSWRNSKDGSWFIQSLCSMLKLYAHKLEFMHILTRVNRKVATEFESFSLDSTFHAKKQIPCIVSMLTKELYFYH | Function: Thiol protease that acts as a major effector caspase involved in the execution phase of apoptosis . Following cleavage and activation by initiator caspases (CASP8, CASP9 and/or CASP10), mediates execution of apoptosis by catalyzing cleavage of many proteins . At the onset of apoptosis, it proteolytically cleaves poly(ADP-ribose) polymerase PARP1 at a '216-Asp-|-Gly-217' bond. Cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop-helix leucine zipper domain and the membrane attachment domain. Cleaves and activates caspase-6, -7 and -9. Triggers cell adhesion in sympathetic neurons through RET cleavage (By similarity). Cleaves IL-1 beta between an Asp and an Ala, releasing the mature cytokine which is involved in a variety of inflammatory processes (By similarity). Cleaves and inhibits serine/threonine-protein kinase AKT1 in response to oxidative stress . Acts as an inhibitor of type I interferon production during virus-induced apoptosis by mediating cleavage of antiviral proteins CGAS, IRF3 and MAVS, thereby preventing cytokine overproduction . Also involved in pyroptosis by mediating cleavage and activation of gasdermin-E (GSDME) (By similarity). Cleaves XRCC4 and phospholipid scramblase proteins XKR4, XKR8 and XKR9, leading to promote phosphatidylserine exposure on apoptotic cell surface .
PTM: Cleavage by granzyme B, caspase-6, caspase-8 and caspase-10 generates the two active subunits. Additional processing of the propeptides is likely due to the autocatalytic activity of the activated protease. Active heterodimers between the small subunit of caspase-7 protease and the large subunit of caspase-3 also occur and vice versa.
Catalytic Activity: Strict requirement for an Asp residue at positions P1 and P4. It has a preferred cleavage sequence of Asp-Xaa-Xaa-Asp-|- with a hydrophobic amino-acid residue at P2 and a hydrophilic amino-acid residue at P3, although Val or Ala are also accepted at this position.
Sequence Mass (Da): 31475
Sequence Length: 277
Subcellular Location: Cytoplasm
EC: 3.4.22.56
|
Q95ND5 | MENNKTSVDSKSIKTLETKILHGSKSMDSGISLDVSYKMDYPEMGLCIIINNKNFDKNTGMACRSGTDVDAANLRETFTNLKYEVRNKNDLTREEILELMHSVSKEDHSKRSSFICVLLSHGEEGKIFGTNGPVDLKKLTSFFRGDCCRTLTGKPKLFIIQACRGTELDCGIETDSGTEDDMACQKIPVEADFLYAYSTAPGYYSWRNSKDGSWFIQSLCAALKQYVHKLELMHILTRVNRKVAVEFESFSTDSTFHAKKQIPCIVSMLTKELYFYH | Function: Involved in the activation cascade of caspases responsible for apoptosis execution. At the onset of apoptosis, it proteolytically cleaves poly(ADP-ribose) polymerase PARP1 at a '216-Asp-|-Gly-217' bond. Cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop-helix leucine zipper domain and the membrane attachment domain. Cleaves and activates caspase-6, -7 and -9. Triggers cell adhesion in sympathetic neurons through RET cleavage (By similarity). Cleaves IL-1 beta between an Asp and an Ala, releasing the mature cytokine which is involved in a variety of inflammatory processes (By similarity). Cleaves and inhibits serine/threonine-protein kinase AKT1 in response to oxidative stress. Acts as an inhibitor of type I interferon production during virus-induced apoptosis by mediating cleavage of antiviral proteins CGAS, IRF3 and MAVS, thereby preventing cytokine overproduction. Also involved in pyroptosis by mediating cleavage and activation of gasdermin-E (GSDME) (By similarity). Cleaves XRCC4 and phospholipid scramblase proteins XKR4, XKR8 and XKR9, leading to promote phosphatidylserine exposure on apoptotic cell surface (By similarity).
PTM: Cleavage by granzyme B, caspase-6, caspase-8 and caspase-10 generates the two active subunits. Additional processing of the propeptides is likely due to the autocatalytic activity of the activated protease. Active heterodimers between the small subunit of caspase-7 protease and the large subunit of caspase-3 also occur and vice versa.
Catalytic Activity: Strict requirement for an Asp residue at positions P1 and P4. It has a preferred cleavage sequence of Asp-Xaa-Xaa-Asp-|- with a hydrophobic amino-acid residue at P2 and a hydrophilic amino-acid residue at P3, although Val or Ala are also accepted at this position.
Sequence Mass (Da): 31379
Sequence Length: 277
Subcellular Location: Cytoplasm
EC: 3.4.22.56
|
P55866 | MEESQNGVKYGGDATDAKEYFTIQPRSLQNCDLKDIERKTKFAHLQNYRTNYPEMGMCLIINNKNFHSSNMAVRNGTDVDALKLHETFTGLGYEVMVCNDQKSSDIIGRLKKISEEDHSKRSSFVCAILSHGEEDGSICGVDVPIHIKNLTDLFRGDRCKTLVGKPKIFFIQACRGTELDSGIETDSCSEPREEIQRIPVEADFLYAYSTVPGYCSWRDKMDGSWFIQSLCKMIKLYGSHLELIQILTCVNHMVALDFETFHAKKQIPCVVSMLTKSFYFFK | Function: Important mediator of apoptosis. At the onset of apoptosis, it proteolytically cleaves poly(ADP-ribose) polymerase PARP1 at a '216-Asp-|-Gly-217' bond (By similarity).
Catalytic Activity: Strict requirement for an Asp residue at positions P1 and P4. It has a preferred cleavage sequence of Asp-Xaa-Xaa-Asp-|- with a hydrophobic amino-acid residue at P2 and a hydrophilic amino-acid residue at P3, although Val or Ala are also accepted at this position.
Sequence Mass (Da): 32125
Sequence Length: 282
Subcellular Location: Cytoplasm
EC: 3.4.22.56
|
Q5E9C1 | MAEDKHNKNPLKMLESLGKELISGLLDDFVEKNVLKLEEEEKKKIYDAKLQDKARVLVDSIRQKNQEAGQVFVQTFLNIDKNSTSIKAPEETVAGPDESVGSAATLKLCPHEEFLKLCKERAGEIYPIKERKDRTRLALIICNTEFDHMPPRNGAALDILGMKQLLEGLGYTVEVEEKLTARDMESVLWKFAAREEHKSSDSTFLVFMSHGILDGICGTMHSEEEPDVLPYDTIFRTFNNRNCLSLKDKPKVIIVQACRGANRGELWVSDSPPALADSFSQSSENLEEDAVYKTHVEKDFIAFCSSTPHNVSWRDIKKGSLFITRLITCFQKYAWCCHLEEVFRKVQQSFEKPNVKAQMPTVERLSMTRYFYLFPGN | Function: Inflammatory caspase that acts as the effector of the non-canonical inflammasome by mediating lipopolysaccharide (LPS)-induced pyroptosis (By similarity). Also indirectly activates the NLRP3 and NLRP6 inflammasomes (By similarity). Acts as a thiol protease that cleaves a tetrapeptide after an Asp residue at position P1: catalyzes cleavage of CGAS, GSDMD and IL18 (By similarity). Effector of the non-canonical inflammasome independently of NLRP3 inflammasome and CASP1: the non-canonical inflammasome promotes pyroptosis through GSDMD cleavage without involving secretion of cytokine IL1B and IL18 (By similarity). In the non-canonical inflammasome, CASP4 is activated by direct binding to LPS without the need of an upstream sensor (By similarity). LPS-binding promotes CASP4 activation and CASP4-mediated cleavage of GSDMD, followed by pyroptosis of infected cells and their extrusion into the gut lumen (By similarity). Also indirectly promotes secretion of mature cytokines (IL1A, IL18 and HMGB1) downstream of GSDMD-mediated pyroptosis via activation of the NLRP3 and NLRP6 inflammasomes (By similarity). Involved in NLRP3-dependent CASP1 activation and IL1B and IL18 secretion in response to non-canonical activators, such as UVB radiation or cholera enterotoxin (By similarity). Involved in NLRP6 inflammasome-dependent activation in response to lipoteichoic acid (LTA), a cell-wall component of Gram-positive bacteria, which leads to CASP1 activation and IL1B and IL18 secretion (By similarity). Involved in LPS-induced IL6 secretion; this activity may not require caspase enzymatic activity (By similarity). The non-canonical inflammasome is required for innate immunity to cytosolic, but not vacuolar, bacteria (By similarity). Plays a crucial role in the restriction of S.typhimurium replication in colonic epithelial cells during infection (By similarity). Pyroptosis limits bacterial replication, while cytokine secretion promotes the recruitment and activation of immune cells and triggers mucosal inflammation (By similarity). Cleavage of GSDMD is not strictly dependent on the consensus cleavage site but depends on an exosite interface on CASP4 that recognizes and binds the Gasdermin-D, C-terminal (GSDMD-CT) part (By similarity). Catalyzes cleavage and maturation of IL18 (By similarity). Cleavage of GSDMD is not strictly dependent on the consensus cleavage site but depends on an exosite interface on CASP4/CASP11 that recognizes and binds the Gasdermin-D, C-terminal (GSDMD-CT) part (By similarity). Catalyzes cleavage and maturation of IL18 (By similarity). In contrast, it does not directly process IL1B (By similarity). During non-canonical inflammasome activation, cuts CGAS and may play a role in the regulation of antiviral innate immune activation (By similarity).
PTM: In response to activation signals, including cholera enterotoxin subunit B, infection by E.coli or S.typhimurium or endoplasmic reticulum stress, undergoes autoproteolytic cleavage.
Location Topology: Peripheral membrane protein
Catalytic Activity: Strict requirement for Asp at the P1 position. It has a preferred cleavage sequence of Tyr-Val-Ala-Asp-|- but also cleaves at Asp-Glu-Val-Asp-|-.
Sequence Mass (Da): 43012
Sequence Length: 377
Domain: The CARD domain mediates LPS recognition and homooligomerization.
Subcellular Location: Cytoplasm
EC: 3.4.22.57
|
P49662 | MAEGNHRKKPLKVLESLGKDFLTGVLDNLVEQNVLNWKEEEKKKYYDAKTEDKVRVMADSMQEKQRMAGQMLLQTFFNIDQISPNKKAHPNMEAGPPESGESTDALKLCPHEEFLRLCKERAEEIYPIKERNNRTRLALIICNTEFDHLPPRNGADFDITGMKELLEGLDYSVDVEENLTARDMESALRAFATRPEHKSSDSTFLVLMSHGILEGICGTVHDEKKPDVLLYDTIFQIFNNRNCLSLKDKPKVIIVQACRGANRGELWVRDSPASLEVASSQSSENLEEDAVYKTHVEKDFIAFCSSTPHNVSWRDSTMGSIFITQLITCFQKYSWCCHLEEVFRKVQQSFETPRAKAQMPTIERLSMTRYFYLFPGN | Function: Inflammatory caspase that acts as the effector of the non-canonical inflammasome by mediating lipopolysaccharide (LPS)-induced pyroptosis . Also indirectly activates the NLRP3 and NLRP6 inflammasomes . Acts as a thiol protease that cleaves a tetrapeptide after an Asp residue at position P1: catalyzes cleavage of CGAS, GSDMD and IL18 . Effector of the non-canonical inflammasome independently of NLRP3 inflammasome and CASP1: the non-canonical inflammasome promotes pyroptosis through GSDMD cleavage without involving secretion of cytokine IL1B and IL18 . In the non-canonical inflammasome, CASP4 is activated by direct binding to LPS without the need of an upstream sensor . LPS-binding promotes CASP4 activation and CASP4-mediated cleavage of GSDMD, followed by pyroptosis of infected cells and their extrusion into the gut lumen . Also indirectly promotes secretion of mature cytokines (IL1A, IL18 and HMGB1) downstream of GSDMD-mediated pyroptosis via activation of the NLRP3 and NLRP6 inflammasomes . Involved in NLRP3-dependent CASP1 activation and IL1B and IL18 secretion in response to non-canonical activators, such as UVB radiation or cholera enterotoxin . Involved in NLRP6 inflammasome-dependent activation in response to lipoteichoic acid (LTA), a cell-wall component of Gram-positive bacteria, which leads to CASP1 activation and IL1B and IL18 secretion . Involved in LPS-induced IL6 secretion; this activity may not require caspase enzymatic activity . The non-canonical inflammasome is required for innate immunity to cytosolic, but not vacuolar, bacteria (By similarity). Plays a crucial role in the restriction of S.typhimurium replication in colonic epithelial cells during infection . Pyroptosis limits bacterial replication, while cytokine secretion promotes the recruitment and activation of immune cells and triggers mucosal inflammation . May also act as an activator of adaptive immunity in dendritic cells, following activation by oxidized phospholipid 1-palmitoyl-2-arachidonoyl- sn-glycero-3-phosphorylcholine, an oxidized phospholipid (oxPAPC) (By similarity). Involved in cell death induced by endoplasmic reticulum stress and by treatment with cytotoxic APP peptides found in Alzheimer's patient brains . Cleavage of GSDMD is not strictly dependent on the consensus cleavage site but depends on an exosite interface on CASP4 that recognizes and binds the Gasdermin-D, C-terminal (GSDMD-CT) part . Catalyzes cleavage and maturation of IL18 . In contrast, it does not directly process IL1B . During non-canonical inflammasome activation, cuts CGAS and may play a role in the regulation of antiviral innate immune activation .
PTM: In response to activation signals, including endoplasmic reticulum stress or treatment with amyloid-beta A4 protein fragments (such as amyloid-beta protein 40), undergoes autoproteolytic cleavage.
Location Topology: Peripheral membrane protein
Catalytic Activity: Strict requirement for Asp at the P1 position. It has a preferred cleavage sequence of Tyr-Val-Ala-Asp-|- but also cleaves at Asp-Glu-Val-Asp-|-.
Sequence Mass (Da): 43262
Sequence Length: 377
Domain: The CARD domain mediates LPS recognition and homooligomerization.
Subcellular Location: Cytoplasm
EC: 3.4.22.57
|
Q59602 | MTTSKCPVTHLTMNNGAPVADNQNSLTAGTRGPLLTQDLWLNEKLADFVREVIPERRMHAKGSGAFGTFTVTRDITKYTRAKIFSEVGKKTEMFGRLATVAGERGADAYTRVRGFALKFYTEEGNWDVVGNNTPVFYPDLRKFPDLNKAVKRSAHQYSSATNNWDFWALLPEALHQVTIVMSDRGIPASYRHMHGFGSHTYSLWNEAGERFWVKFHFRSQQGIKNLTNEEAAKIIADDRESHQRDLYEAIERGEFPKWTMYIQVMPEADAAKVPYHPFDLTKVWPKKDYPLIEVAEFELNRNPENFFADVEQSAFAPSNLVPGIGASPDKMLQARLFNYADAQRYRLGVNFRQIPVNRPRCPVHSNQRDGQGRATELRQPAHYEPNSFGQWSQQPDFAEPPLKINGDAAHWDYRQDDDDYFSQPRALFNLMNDAQKQALFDNTAAAMGDAPDFIKYRHIRNCYRCDPAYGEGGSKALGLTVEEPQAARATDPALGQGGLL | Function: Decomposes hydrogen peroxide into water and oxygen; serves to protect cells from the toxic effects of hydrogen peroxide.
Catalytic Activity: 2 H2O2 = 2 H2O + O2
Sequence Mass (Da): 56671
Sequence Length: 500
EC: 1.11.1.6
|
P11934 | AAAQRRQNDSSVFLAIMVAAAVESESSLTDGDAGALLLQDISEWDEVFRFDRLEAVERAAHAAAAAAFGAFVARGDWTASAAAAFQAAGKQIAFMAAFSTVAGAKGSATVRDADAFAAKFASAAALQELVGNNSPISFFIFDLLFAAILFASKAKAANQAAFAAAAELAAESLFVRLPSLHQVSFFALAGFAAVAAHRHMNGYGSHTFKLVAKDGSVYCSKFWYKADQGQAAEVWKDAEEVAAEDVDYFRDLNFQAEAAGRYPLWELASQVMTFSDFEIDPFNENIPTKVVPRESVPLIVDAELLLNRNPLNMFAEVEQVFMDVAAASKGADEVEDPLIQRQFAYIDTHLSELTASYGIPVCRPYATVLNDQEDGARYDDVQDVLVIAPNAFSASAVEVQIPAAAAFNLAAARVAAAGDVRVNAVVEADQRKQSRQFWASDVNAQKKRLVDAFRMEVASAVSASIQVDVTVEFSFVAAAAAARIAAAVGSAAAGALANRRQIKVIASLAVLAKADAKVRQKNALESSSQAVAVDAKAAAQDIVDSSDAANVVTVAREFAVLPQTAAADAAEFVAAASAKAFSSFPAMEVISVAAAAGAVAEPARASLDLNMAMFFSRIVASRGAAANAIAALVKASRDGVFVAAVLAKAAANNRAAEAIFKFEVRQAVDA | Function: Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide.
Catalytic Activity: 2 H2O2 = 2 H2O + O2
Sequence Mass (Da): 70260
Sequence Length: 670
Subcellular Location: Peroxisome
EC: 1.11.1.6
|
P42321 | MEKKKLTTAAGAPVVDNNNVITAGPRGPMLLQDVWFLEKLAHFDREVIPERRMHAKGSGAFGTFTVTHDITKYTRAKIFSEVGKKTEMFARFSTVAGERGAADAERDIRGFALKFYTEEGNWDMVGNNTPVFYLRDPLKFPDLNHIVKRDPRTNMRNMAYKWDFFSHLPESLHQLTIDMSDRGLPLSYRFVHGFGSHTYSFINKDNERFWVKFHFRCQQGIKNLMDDEAEALVGKDRESSQRDLFEAIERGDYPRWKLQIQIMPEKEASTVPYNPFDLTKVWPHADYPLMDVGYFELNRNPDNYFSDVEQAAFSPANIVPGISFSPDKMLQGRLFSYGDAHRYRLGVNHHQIPVNAPKCPFHNYHRDGAMRVDGNSGNGITYEPNSGGVFQEQPDFKEPPLSIEGAADHWNHREDEDYFSQPRALYELLSDDEHQRMFARIAGELSQASKETQQRQIDLFTKVHPEYGAGVEKAIKVLEGKDAK | Function: Decomposes hydrogen peroxide into water and oxygen; serves to protect cells from the toxic effects of hydrogen peroxide.
Catalytic Activity: 2 H2O2 = 2 H2O + O2
Sequence Mass (Da): 55614
Sequence Length: 484
Subcellular Location: Cytoplasm
EC: 1.11.1.6
|
P04762 | MADSRDPASDQMKQWKEQRAPQKPDVLTTGGGNPIGDKLNIMTAGPRGPLLVQDVVFTDEMAHFDRERIPERVVHAKGAGAFGYFEVTHDITRYSKAKVFEHIGKRTPIAVRFSTVAGESGSADTVRDPRGFAVKFYTEDGNWDLVGNNTPIFFIRDAMLFPSFIHSQKRNPQTHLKDPDMVWDFWSLCPESLHQVTFLFSDRGIPDGHRHMNGYGSHTFKLVNANGEAVYCKFHYKTDQGIKNLPVEEAGRLAQEDPDYGLRDLFNAIASGNYPSWTFYIQVMTFKEAETFPFNPFDLTKVWPHKDYPLIPVGKLVLNRNPANYFAEVEQMAFDPSNMPPGIEPSPDKMLQGRLFAYPDTHRHRLGPNYLQIPVNCPYRARVANYQRDGPMCMHDNQGGAPNYYPNSFSAPEQQGSALEHHSQCSADVKRFNSANEDNVTQVRTFYTKVLNEEERKRLCENIANHLKDAQLFIQRKAVKNFTDVHPDYGARVQALLDQYNSQKPKNAIHTYVQAGSHIAAKGKANL | Function: Catalyzes the degradation of hydrogen peroxide (H(2)O(2)) generated by peroxisomal oxidases to water and oxygen, thereby protecting cells from the toxic effects of hydrogen peroxide. Promotes growth of cells including T-cells, B-cells, myeloid leukemia cells, melanoma cells, mastocytoma cells and normal and transformed fibroblast cells.
Catalytic Activity: 2 H2O2 = 2 H2O + O2
Sequence Mass (Da): 59757
Sequence Length: 527
Subcellular Location: Peroxisome
EC: 1.11.1.6
|
P95607 | GSGSAATDKFKAERATADTSPERLAAIAKDALGALNDVILKHGVTYPEYRVFKQWLIDVGEGGEWPLFLDVFIEHSVEEVLARSRKGTMGSIEGPYYIENSPELPSKCTLPMREEDEKITPLVFSGQVTDLDGNGLAGAKVELWHADNDGYYSQFAPHLPEWNLRGTIIADEEGRYEITTIQPAPYQIPTDGPTGQFIEAQNGHPWRPAHLHLIVSAPGKESVTTQLYFKGGEWIDSDVASATKPELILDPKTGDDGKNYVTYNFVLDPA | Cofactor: Binds 1 Fe(3+) ion per subunit.
Catalytic Activity: catechol + O2 = cis,cis-muconate + 2 H(+)
Sequence Mass (Da): 29704
Sequence Length: 270
EC: 1.13.11.1
|
P55306 | MNSKDSNTVPVYTTNTGCPIFNPMAAARVGKGGPVLLQDSHLIDVFQHFDRERIPERVVHAKGSGAFGEFECTDDITKYTKHTMFSKVGKKTPMVARFSTVGGERGTPDTARDPRGFALKFYTDEGIFDMVGNNTPVFFLRDPAKFPLFIHTQKRNPQNDMKDATMFWDYLSQNAESIHQVMILFSDLGGTPYSYRFMDGFSSHTYKFVNDKGEFYYCKWHFITNQGTKGLTNEEAAALDGSNPDHARQDLFEAIERGDYPSWTLYVQVMTPQEAEKYRYNIFDLTKVWPHKDVPMQRVGRFTLNQNPTNFFADIEQAGFSPSHMVPGIEVSADPVLQVRTFSYPDTHRHRLGANFEQIPVNSPKCPVFNYSRDGPMNVNGNQGNWPNYPSSIRPLAKVQYEPDEGHEKWVGQVTYHMDEITDVDFEQPRAFWQNVLGKKPGQQDNFVKNVAGHLSGAISPVRERQYGVFTRVDSELGRRIREATEAEVKKMEEKAPKPINKGEPHMFQGSS | Function: Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide.
Catalytic Activity: 2 H2O2 = 2 H2O + O2
Sequence Mass (Da): 58279
Sequence Length: 512
EC: 1.11.1.6
|
P07711 | MNPTLILAAFCLGIASATLTFDHSLEAQWTKWKAMHNRLYGMNEEGWRRAVWEKNMKMIELHNQEYREGKHSFTMAMNAFGDMTSEEFRQVMNGFQNRKPRKGKVFQEPLFYEAPRSVDWREKGYVTPVKNQGQCGSCWAFSATGALEGQMFRKTGRLISLSEQNLVDCSGPQGNEGCNGGLMDYAFQYVQDNGGLDSEESYPYEATEESCKYNPKYSVANDTGFVDIPKQEKALMKAVATVGPISVAIDAGHESFLFYKEGIYFEPDCSSEDMDHGVLVVGYGFESTESDNNKYWLVKNSWGEEWGMGGYVKMAKDRRNHCGIASAASYPTV | Function: Thiol protease important for the overall degradation of proteins in lysosomes (Probable). Plays a critical for normal cellular functions such as general protein turnover, antigen processing and bone remodeling. Involved in the solubilization of cross-linked TG/thyroglobulin and in the subsequent release of thyroid hormone thyroxine (T4) by limited proteolysis of TG/thyroglobulin in the thyroid follicle lumen (By similarity). In neuroendocrine chromaffin cells secretory vesicles, catalyzes the prohormone proenkephalin processing to the active enkephalin peptide neurotransmitter (By similarity). In thymus, regulates CD4(+) T cell positive selection by generating the major histocompatibility complex class II (MHCII) bound peptide ligands presented by cortical thymic epithelial cells. Also mediates invariant chain processing in cortical thymic epithelial cells (By similarity). Major elastin-degrading enzyme at neutral pH. Accumulates as a mature and active enzyme in the extracellular space of antigen presenting cells (APCs) to regulate degradation of the extracellular matrix in the course of inflammation (By similarity). Secreted form generates endostatin from COL18A1 . Critical for cardiac morphology and function. Plays an important role in hair follicle morphogenesis and cycling, as well as epidermal differentiation (By similarity). Required for maximal stimulation of steroidogenesis by TIMP1 (By similarity).
PTM: During export along the endocytic pathway, pro-CTSL undergoes several proteolytic cleavages to generate the CTSL single-chain and two-chain mature forms, composed of a heavy chain linked to a light chain by disulfide bonds (By similarity). Autocleavage; produces the single-chain CTSL after cleavage of the propeptide. The cleavage can be intermolecular .
Location Topology: Peripheral membrane protein
Catalytic Activity: Specificity close to that of papain. As compared to cathepsin B, cathepsin L exhibits higher activity toward protein substrates, but has little activity on Z-Arg-Arg-NHMec, and no peptidyl-dipeptidase activity.
Sequence Mass (Da): 37564
Sequence Length: 333
Subcellular Location: Lysosome
EC: 3.4.22.15
|
P06797 | MNLLLLLAVLCLGTALATPKFDQTFSAEWHQWKSTHRRLYGTNEEEWRRAIWEKNMRMIQLHNGEYSNGQHGFSMEMNAFGDMTNEEFRQVVNGYRHQKHKKGRLFQEPLMLKIPKSVDWREKGCVTPVKNQGQCGSCWAFSASGCLEGQMFLKTGKLISLSEQNLVDCSHAQGNQGCNGGLMDFAFQYIKENGGLDSEESYPYEAKDGSCKYRAEFAVANDTGFVDIPQQEKALMKAVATVGPISVAMDASHPSLQFYSSGIYYEPNCSSKNLDHGVLLVGYGYEGTDSNKNKYWLVKNSWGSEWGMEGYIKIAKDRDNHCGLATAASYPVVN | Function: Thiol protease important for the overall degradation of proteins in lysosomes (Probable). Involved in the solubilization of cross-linked TG/thyroglobulin and in the subsequent release of thyroid hormone thyroxine (T4) by limited proteolysis of TG/thyroglobulin in the thyroid follicle lumen . In neuroendocrine chromaffin cells secretory vesicles, catalyzes the prohormone proenkephalin processing to the active enkephalin peptide neurotransmitter . In thymus, regulates CD4(+) T cell positive selection by generating the major histocompatibility complex class II (MHCII) bound peptide ligands presented by cortical thymic epithelial cells . Also mediates invariant chain processing in cortical thymic epithelial cells . Major elastin-degrading enzyme at neutral pH. Accumulates as a mature and active enzyme in the extracellular space of antigen presenting cells (APCs) to regulate degradation of the extracellular matrix in the course of inflammation . Secreted form generates endostatin from COL18A1 . Critical for cardiac morphology and function . Plays an important role in hair follicle morphogenesis and cycling, as well as epidermal differentiation . Required for maximal stimulation of steroidogenesis by TIMP1 (By similarity).
PTM: During export along the endocytic pathway, pro-CTSL undergoes several proteolytic cleavages to generate the CTSL single-chain and two-chain mature forms, composed of a heavy chain linked to a light chain by disulfide bonds . Autocleavage; produces the single-chain CTSL after cleavage of the propeptide. The cleavage can be intermolecular (By similarity).
Location Topology: Peripheral membrane protein
Catalytic Activity: Specificity close to that of papain. As compared to cathepsin B, cathepsin L exhibits higher activity toward protein substrates, but has little activity on Z-Arg-Arg-NHMec, and no peptidyl-dipeptidase activity.
Sequence Mass (Da): 37547
Sequence Length: 334
Subcellular Location: Lysosome
EC: 3.4.22.15
|
Q94714 | MMLLGASLYLNNTQEVSDEIDTANLYANWKMKYNRRYTNQRDEMYRYKVFTDNLNYIRAFYESPEEATFTLELNQFADMSQQEFAQTYLSLKVPRTAKLNAANSNFQYKGAEVDWTDNKKVKYPAVKNQGSCGSCWAFSAVGALEINTDIELNRKYELSEQDLVDCSGPYDNDGCNGGWMDSAFEYVADNGLAEAKDYPYTAKDGTCKTSVKRPYTHVQGFKDIDSCDELAQTIQERTVAVAVDANPWQFYRSGVLSKCTKNLNHGVVLVGVQADGAWKIRNSWGSSWGEAGHIRLAGGDTCGICAAPSFPILG | Function: May be involved in extracellular digestion.
Catalytic Activity: Specificity close to that of papain. As compared to cathepsin B, cathepsin L exhibits higher activity toward protein substrates, but has little activity on Z-Arg-Arg-NHMec, and no peptidyl-dipeptidase activity.
Sequence Mass (Da): 35159
Sequence Length: 314
Subcellular Location: Secreted
EC: 3.4.22.15
|
Q28944 | MKPSLFLTALCLGIASAAPKLDQNLDADWYKWKATHGRLYGMNEEGWRRAVWEKNMKMIELHNQEYSQGKHGFSMAMNAFGDMTNEEFRQVMNGFQNQKHKKGKVFHESLVLEVPKSVDWREKGYVTAVKNQGQCGSCWAFSATGALEGQMFRKTGKLVSLSEQNLVDCSRPQGNQGCNGGLMDNAFQYVKDNGGLDTEESYPYLGRETNSCTYKPECSAANDTGFVDIPQREKALMKAVATVGPISVAIDAGHSSFQFYKSGIYYDPDCSSKDLDHGVLVVGYGFEGTDSNSSKFWIVKNSWGPEWGWNGYVKMAKDQNNHCGISTAASYPTV | Function: Thiol protease important for the overall degradation of proteins in lysosomes (By similarity). Plays a critical for normal cellular functions such as general protein turnover, antigen processing and bone remodeling. Involved in the solubilization of cross-linked TG/thyroglobulin and in the subsequent release of thyroid hormone thyroxine (T4) by limited proteolysis of TG/thyroglobulin in the thyroid follicle lumen (By similarity). In neuroendocrine chromaffin cells secretory vesicles, catalyzes the prohormone proenkephalin processing to the active enkephalin peptide neurotransmitter (By similarity). In thymus, regulates CD4(+) T cell positive selection by generating the major histocompatibility complex class II (MHCII) bound peptide ligands presented by cortical thymic epithelial cells. Also mediates invariant chain processing in cortical thymic epithelial cells. Major elastin-degrading enzyme at neutral pH. Accumulates as a mature and active enzyme in the extracellular space of antigen presenting cells (APCs) to regulate degradation of the extracellular matrix in the course of inflammation (By similarity). Secreted form generates endostatin from COL18A1 (By similarity). Critical for cardiac morphology and function. Plays an important role in hair follicle morphogenesis and cycling, as well as epidermal differentiation (By similarity). Required for maximal stimulation of steroidogenesis by TIMP1 (By similarity).
PTM: During export along the endocytic pathway, pro-CTSL undergoes several proteolytic cleavages to generate the CTSL single-chain and two-chain mature forms, composed of a heavy chain linked to a light chain by disulfide bonds (By similarity). Autocleavage; produces the single-chain CTSL after cleavage of the propeptide. The cleavage can be intermolecular (By similarity).
Location Topology: Peripheral membrane protein
Catalytic Activity: Specificity close to that of papain. As compared to cathepsin B, cathepsin L exhibits higher activity toward protein substrates, but has little activity on Z-Arg-Arg-NHMec, and no peptidyl-dipeptidase activity.
Sequence Mass (Da): 37178
Sequence Length: 334
Subcellular Location: Lysosome
EC: 3.4.22.15
|
Q10991 | VPKSVDWTKKGYVTPVKNQGQCGSCWAFSATGALEGQMFRKTGKLVSLSEQNLVDSSRPQGNQGCNGGLMDNAFQYIKENGGLDSEESYPYEATDTSCNYKPEYSAAKDTGFVDIPQREKALMKAVATVGPISVAIDAGHSSFQFYKSGIYYDPDCSSKDLDHGVLVVGYGFEGTNNKFWIVKNSWGPEWGNKGYVKMAKDQNNHCGIATAASYPTV | Function: Thiol protease important for the overall degradation of proteins in lysosomes (By similarity). Plays a critical for normal cellular functions such as general protein turnover, antigen processing and bone remodeling. Involved in the solubilization of cross-linked TG/thyroglobulin and in the subsequent release of thyroid hormone thyroxine (T4) by limited proteolysis of TG/thyroglobulin in the thyroid follicle lumen (By similarity). In neuroendocrine chromaffin cells secretory vesicles, catalyzes the prohormone proenkephalin processing to the active enkephalin peptide neurotransmitter (By similarity). In thymus, regulates CD4(+) T cell positive selection by generating the major histocompatibility complex class II (MHCII) bound peptide ligands presented by cortical thymic epithelial cells. Also mediates invariant chain processing in cortical thymic epithelial cells. Major elastin-degrading enzyme at neutral pH. Accumulates as a mature and active enzyme in the extracellular space of antigen presenting cells (APCs) to regulate degradation of the extracellular matrix in the course of inflammation (By similarity). Secreted form generates endostatin from COL18A1 (By similarity). Critical for cardiac morphology and function. Plays an important role in hair follicle morphogenesis and cycling, as well as epidermal differentiation (By similarity). Required for maximal stimulation of steroidogenesis by TIMP1 (By similarity).
PTM: During export along the endocytic pathway, pro-CTSL undergoes several proteolytic cleavages to generate the CTSL single-chain and two-chain mature forms, composed of a heavy chain linked to a light chain by disulfide bonds (By similarity). Autocleavage; produces the single-chain CTSL after cleavage of the propeptide. The cleavage can be intermolecular (By similarity).
Location Topology: Peripheral membrane protein
Catalytic Activity: Specificity close to that of papain. As compared to cathepsin B, cathepsin L exhibits higher activity toward protein substrates, but has little activity on Z-Arg-Arg-NHMec, and no peptidyl-dipeptidase activity.
Sequence Mass (Da): 23608
Sequence Length: 217
Subcellular Location: Lysosome
EC: 3.4.22.15
|
P80342 | AVPDKIDRRESGYV | Function: Thiol protease that assists the parasite in burrowing through the gut wall and liver of its mammalian host.
Catalytic Activity: Specificity close to that of papain. As compared to cathepsin B, cathepsin L exhibits higher activity toward protein substrates, but has little activity on Z-Arg-Arg-NHMec, and no peptidyl-dipeptidase activity.
Sequence Mass (Da): 1605
Sequence Length: 14
Subcellular Location: Lysosome
EC: 3.4.22.15
|
O60911 | MNLSLVLAAFCLGIASAVPKFDQNLDTKWYQWKATHRRLYGANEEGWRRAVWEKNMKMIELHNGEYSQGKHGFTMAMNAFGDMTNEEFRQMMGCFRNQKFRKGKVFREPLFLDLPKSVDWRKKGYVTPVKNQKQCGSCWAFSATGALEGQMFRKTGKLVSLSEQNLVDCSRPQGNQGCNGGFMARAFQYVKENGGLDSEESYPYVAVDEICKYRPENSVANDTGFTVVAPGKEKALMKAVATVGPISVAMDAGHSSFQFYKSGIYFEPDCSSKNLDHGVLVVGYGFEGANSNNSKYWLVKNSWGPEWGSNGYVKIAKDKNNHCGIATAASYPNV | Function: Cysteine protease. May have an important role in corneal physiology.
Catalytic Activity: The recombinant enzyme hydrolyzes proteins (serum albumin, collagen) and synthetic substrates (Z-Phe-Arg-NHMec > Z-Leu-Arg-NHMec > Z-Val-Arg-NHMec).
Sequence Mass (Da): 37329
Sequence Length: 334
Subcellular Location: Lysosome
EC: 3.4.22.43
|
P80532 | DVPASIDWREYGYVTEVKD | Function: Thiol protease.
Catalytic Activity: Specificity close to that of papain. As compared to cathepsin B, cathepsin L exhibits higher activity toward protein substrates, but has little activity on Z-Arg-Arg-NHMec, and no peptidyl-dipeptidase activity.
Sequence Mass (Da): 2242
Sequence Length: 19
Subcellular Location: Lysosome
EC: 3.4.22.15
|
Q94715 | MKQFLTAAIVTLLMTAGYYHLQEDDTNDFERWALKNNKFYTESEKLYRMEIYNSNKRMIEEHNQREDVTYQMGENQFMTLSHEEFVDLYLQKSDSSVNIMGASLPEVQLEGLGAVDWRNYTTVKEQGQCASGWAFSVSNSLEAWYAIRGFQKINASTQQIVDCDYNNTGCSGGYNAYAMEYVLRVGLVSSTNYPYVAKNQTCKQSRNGTYFINGYSFVGGSQSNLQYYLNNYPISVGVEASNWQFYRSGLFSNCSSNGTNHYALAVGFDSANNWIVQNSWGTQWGESGNIRLYPQNTCGILNYPYQVY | Function: May be involved in extracellular digestion.
Catalytic Activity: Specificity close to that of papain. As compared to cathepsin B, cathepsin L exhibits higher activity toward protein substrates, but has little activity on Z-Arg-Arg-NHMec, and no peptidyl-dipeptidase activity.
Sequence Mass (Da): 35189
Sequence Length: 308
Subcellular Location: Secreted
EC: 3.4.22.15
|
Q24940 | MRLFILAVLTVGVLGSNDDLWHQWKRMYNKEYNGADDQHRRNIWEKNVKHIQEHNLRHDLGLVTYTLGLNQFTDMTFEEFKAKYLTEMSRASDILSHGVPYEANNRAVPDKIDWRESGYVTEVKDQGNCGSCWAFSTTGTMEGQYMKNERTSISFSEQQLVDCSGPWGNNGCSGGLMENAYQYLKQFGLETESSYPYTAVEGQCRYNKQLGVAKVTGYYTVHSGSEVELKNLVGARRPAAVAVDVESDFMMYRSGIYQSQTCSPLRVNHAVLAVGYGTQGGTDYWIVKNSWGTYWGERGYIRMARNRGNMCGIASLASLPMVARFP | Function: Thiol protease. Probably involved in interaction with host tissues. Displays a similar activity to that of papain. Has high activity on Z-Phe-Arg-NHMec, but no activity on Z-Arg-NHMec.
PTM: Contains cysteine residues involved in intramolecular disulfide bonding.
Sequence Mass (Da): 36896
Sequence Length: 326
Subcellular Location: Secreted
EC: 3.4.22.-
|
Q95029 | MNHLGVFETRFRPRTRHKSQRAQLIPEQITMRTAVLLPLLALLAVAQAVSFADVVMEEWHTFKLEHRKNYQDETEERFRLKIFNENKHKIAKHNQRFAEGKVSFKLAVNKYADLLHHEFRQLMNGFNYTLHKQLRAADESFKGVTFISPAHVTLPKSVDWRTKGAVTAVKDQGHCGSCWAFSSTGALEGQHFRKSGVLVSLSEQNLVDCSTKYGNNGCNGGLMDNAFRYIKDNGGIDTEKSYPYEAIDDSCHFNKGTVGATDRGFTDIPQGDEKKMAEAVATVGPVSVAIDASHESFQFYSEGVYNEPQCDAQNLDHGVLVVGFGTDESGEDYWLVKNSWGTTWGDKGFIKMLRNKENQCGIASASSYPLV | Function: Important for the overall degradation of proteins in lysosomes. Essential for adult male and female fertility. May play a role in digestion.
Catalytic Activity: Specificity close to that of papain. As compared to cathepsin B, cathepsin L exhibits higher activity toward protein substrates, but has little activity on Z-Arg-Arg-NHMec, and no peptidyl-dipeptidase activity.
Sequence Mass (Da): 41601
Sequence Length: 371
Subcellular Location: Lysosome
EC: 3.4.22.15
|
P12360 | MASNTLMSCGIPAVCPSFLSSTKSKFAAAMPVYVGATNFMSRFSMSADWMPGQPRPSYLDGSAPGDFGFDSLGLGEVPANLERYKESELIHCRWAMLAVPGIIVPEALGLGNWVKAQEWAAIPGGQATYLGQPVPWGTLPTILAIEFLAIAFVEHQRSMEKDSEKKKYPGGAFDPLGYSKDPAKFEELKVKEIKNGRLALLAIVGFCVQQSAYLGTGPLENLATHLADPWHNNIGDVIIPKGIFPN | Cofactor: Binds at least 14 chlorophylls (8 Chl-a and 6 Chl-b) and carotenoids such as lutein and neoxanthin.
Function: The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated.
PTM: Photoregulated by reversible phosphorylation of its threonine residues.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26575
Sequence Length: 246
Domain: The N-terminus of the protein extends into the stroma where it is involved with adhesion of granal membranes and post-translational modifications; both are believed to mediate the distribution of excitation energy between photosystems I and II.
Subcellular Location: Plastid
|
Q36718 | RIQAYRFRTRVPPSPAASGSPRSTRRDVAVQAKGSWLPGLQSPAYLDGSLEGDNGFDPLALAEDPEDLRWFVQADVVNGRWAMLGVAGMLIPEVLTKAGLMNAPEWLRLPGKETYFASSSTALRVHMSSTYVEIRRWQDIKNPGSVNQDPIFKSYSLPPHECGYPGRVFNPLNFAPLENKEKELANGRLAMLAFLGFLVQHNVHGKGPFENLQQHLADPWHNTIIQTISGQ | Cofactor: Binds at least 14 chlorophylls (8 Chl-a and 6 Chl-b) and carotenoids such as lutein and neoxanthin.
Function: The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated.
PTM: Photoregulated by reversible phosphorylation of its threonine residues.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 25674
Sequence Length: 231
Subcellular Location: Plastid
|
Q9SDM1 | MASSSGLRSCSAVGVPSLLAPSSRSGRSGLPFCAYATTSGRVTMSAEWFPGQPRPAHLDGSSPGDFGFDPLGLATVPENFERFKESEIYHCRWAMLCVPGVLVPEALGLGNWVKAQEWAALPDGQATYLGNPVPWGNLPTILAIEFLAIAFAEQQRTMEKDPEKKKYPGGAFDPLGFSKDPAKFEELKLKEIKNGRLAMLAFVGFCVQQSAYPGTGPLENLATHLADPWHNNIGDIVIPRNIYGP | Cofactor: Binds at least 14 chlorophylls (8 Chl-a and 6 Chl-b) and carotenoids such as lutein and neoxanthin.
Function: The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated.
PTM: Photoregulated by reversible phosphorylation of its threonine residues.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26464
Sequence Length: 245
Subcellular Location: Plastid
|
P10708 | MASACASSTIAAVAFSSPSSRRNGSIVGTTKASFLGGRRLRVSKYSTTPTARSATTVCVAADPDRPLWFPGSTPPPWLDGSLPGDFGFDPLGLASDPESLRWNQQAELVHCRWAMLGAAGIFIPELLTKIGILNTPSWYTAGEQEYFTDTTTLFIVELVLIGWAEGRRWADIIKPGCVNTDPIFPNNKLTGTDVGYPGGLWFDPLGWGSGSPAKIKELRTKEIKNGRLAMLAVMGAWFQHIYTGTGPIDNLFAHLADPGHATIFAAFSPK | Cofactor: Binds at least 14 chlorophylls (8 Chl-a and 6 Chl-b) and carotenoids such as lutein and neoxanthin.
Function: The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated.
PTM: Photoregulated by reversible phosphorylation of its threonine residues.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 29046
Sequence Length: 270
Domain: The N-terminus of the protein extends into the stroma where it is involved with adhesion of granal membranes and post-translational modifications; both are believed to mediate the distribution of excitation energy between photosystems I and II.
Subcellular Location: Plastid
|
P27522 | MATQALISSSSISTSAEAARQIIGSRISQSVTRKASFVVRAASTPPVKQGANRQLWFASKQSLSYLDGRLPGDFGFDPLGLSDPEGTGGFIEPKWLAYGEVINGRFAMLGAAGAIAPEILGKAGLIPQETALAWFQTGVIPPAGTYNYWADNYTLFVLEMALMGFAEHRRFQDWAKPGSMGKQYFLGLEKGLGGSGDPAYPGGPLFNPLGFGKDEKSMKELKLKEIKNGRLAMLAILGYFIQALVTGVGPYQNLLDHLADPVNNNVLTSLKFH | Cofactor: Binds at least 14 chlorophylls (8 Chl-a and 6 Chl-b) and carotenoids such as lutein and neoxanthin.
Function: The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated.
PTM: Photoregulated by reversible phosphorylation of its threonine residues.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 29363
Sequence Length: 273
Domain: The N-terminus of the protein extends into the stroma where it is involved with adhesion of granal membranes and post-translational modifications; both are believed to mediate the distribution of excitation energy between photosystems I and II.
Subcellular Location: Plastid
|
P76364 | MSDTLPGTTLPDDNHDRPWWGLPCTVTPCFGARLVQEGNRLHYLADRAGIRGLFSDADAYHLDQAFPLLMKQLELMLTSGELNPRHQHTVTLYAKGLTCKADTLSSCDYVYLAVYPTPEMKN | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Antitoxin component of a type IV toxin-antitoxin (TA) system . Antitoxin that counteracts the effect of its cognate toxin CbtA (YeeV) . It does not bind to the toxin but instead binds to MreB and FtsZ (the toxin targets), enhancing their polymerization by forming higher-order bundles; it is probably retained in the MreB and FtsZ filament bundles . The mechanism has been proposed to require intergenic DNA, in cis, between the cbeA (yeeU) and cbta (yeeV) genes . The intergenic region was not found to be necessary in another study . Also counteracts the morphological defects caused by overexpression of SulA and DicB on cell shape . Also counteracts the effect of non-cognate toxins YfkI and YpjF .
Sequence Mass (Da): 13684
Sequence Length: 122
Subcellular Location: Cytoplasm
|
Q9LD90 | MAEVDISHSKKKKQDKTENDAADTGDYMIKPQSFTPAIDTSQWPILLKNYDRLNVRTGHYTPISAGHSPLKRPLQEYIRYGVINLDKPANPSSHEVVAWIKRILRVEKTGHSGTLDPKVTGNLIVCIDRATRLVKSQQGAGKEYVCVARLHSAVPDVAKVARALESLTGAVFQRPPLISAVKRQLRIRTIYESKLLEYDADRHLVVFWVSCEAGTYIRTMCVHLGLLLGVGGHMQELRRVRSGILGENNNMVTMHDVMDAQFVYDNSRDESYLRRVIMPLEMILTSYKRLVVKDSAVNAICYGAKLMIPGLLRFENDIDVGTEVVLMTTKGEAIAVGIAEMTTSVMATCDHGVVAKIKRVVMDRDTYPRKWGLGPRASMKKKLIADGKLDKHGKPNEKTPVEWSRNVVLPTGGDAIIAGAAAAPEEIKADAENGEAGEARKRKHDDSSDSPAPVTTKKSKTKEVEGEEAEEKVKSSKKKKKKDKEEEKEEEAGSEKKEKKKKKDKKEEVIEEVASPKSEKKKKKKSKDTEAAVDAEDESAAEKSEKKKKKKDKKKKNKDSEDDEE | Function: Plays a central role in ribosomal RNA processing. Probable catalytic subunit of H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Pseudouridine ('psi') residues may serve to stabilize the conformation of rRNAs (By similarity).
Catalytic Activity: a uridine in RNA = a pseudouridine in RNA
Sequence Mass (Da): 63026
Sequence Length: 565
Subcellular Location: Nucleus
EC: 5.4.99.-
|
G0SGK0 | MSGSAAIMKAPAKSEFIIKPENTKAEVDTSNWPGLLKNYDKMLIRTSHFTPIPDHGSAPWSRDIKSYVSSGVINLDKPSNPSSHEVVAWIKRILRVDKTGHSGTLDPKVTGCLIVCIDRATRLVKAQQGAGKEYVCCIRFHDTVPGGEPAFAKALETLTGALFQRPPLISAVKRQLRIRTIHKSRLLEFDNERHLGVFWVSCEAGTYIRTLCVHLGLLLGVGAHMQELRRVRSGVMSEDDGSLVTLHDVLDAQWQYDNNGDEALLRKVIQPLETLLCTYKRLVVKDTAVNAVCYGAKLMIPGLLRYDQGIEQGEEVVLMTTKGEAIAIAIAQMGAVELATCDHGCVAKVKRCIMERDLYPRRWGMGPVASEKKKLKASGLLDKYGRPNEKTPASWLQSYKDYNVSSSEAPALPAPAGADAAAAPSTPALPAPEEKNESEEKSADASDSKKRKKDETAEEKAERKRLKKEKKEKKEKKKSDKDE | Function: Catalytic subunit of H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Pseudouridine ('psi') residues may serve to stabilize the conformation of rRNAs and play a central role in ribosomal RNA processing. The H/ACA snoRNP complex also mediates pseudouridylation of other types of RNAs. Catalyzes pseudouridylation at position 93 in U2 snRNA. Also catalyzes pseudouridylation of mRNAs; H/ACA-type snoRNAs probably guide pseudouridylation of mRNAs.
Catalytic Activity: uridine in 5S rRNA = pseudouridine in 5S rRNA
Sequence Mass (Da): 53313
Sequence Length: 483
Subcellular Location: Nucleus
EC: 5.4.99.-
|
O43100 | MAKEVDYTIKPEATASNINTEDWPLLLKNYDKLMVRTGHFTPIPAGSSPLKRDLKSYINSGVINLDKPSNPSSHEVVAWMKRILRAEKTGHSGTLDPKVTGCLIVCIDRATRLVKSQQGAGKEYVCVIRLHDKIPGGEAQFKRALETLTGALFQRPPLISAVKRQLRIRTIHESKLYEFDNERHLGVFWVSCEAGTYIRTLCVHLGLLLGVGAHMQELRRVRSGAMSENEGMVTLHDVLDAQWLYDNQRDESYLRKVIKPLESLLTTYKRIVVKDSAVNAVCYGAKLMIPGLLRFEAGIELGEEVVLMTTKGEAIAIGIAQMSTVELSTCDHGVVAKVKRCIMERDLYPRRWGLGPVALEKKKLKSSGKLDKYGRANEATPAKWKSEYKDYSAPDGDSSQQAVDVVAKEEASPKEEPSLEANESKMDIDDAQDDEDKKKRKRHEGETPEERAERKRKKKEKKEKKERRKSKQEKDDSDDSD | Function: Catalytic subunit of H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Pseudouridine ('psi') residues may serve to stabilize the conformation of rRNAs and play a central role in ribosomal RNA processing. The H/ACA snoRNP complex also mediates pseudouridylation of other types of RNAs. Catalyzes pseudouridylation at position 93 in U2 snRNA. Also catalyzes pseudouridylation of mRNAs; H/ACA-type snoRNAs probably guide pseudouridylation of mRNAs.
Catalytic Activity: uridine in 5S rRNA = pseudouridine in 5S rRNA
Sequence Mass (Da): 54204
Sequence Length: 481
Subcellular Location: Nucleus
EC: 5.4.99.-
|
O14007 | MTDTHPGVDFMIKPEATSASKIDTAEWPLLLKNFDKLLVRTGHYTPIPCGNNPLKRPIAEYVSSGVINLDKPANPSSHEVVAWVKKILRVEKTGHSGTLDPKVTGCLIICNDRATRLVKSQQSAGKEYVCVLRLHDSVEGERNVASAIETLTGALFQRPPLISAVKRQLRIRSIYESKLIEFDNERNLAVFWASCEAGTYMRTLCVHLGLLLGVGGHMQELRRVRSGCLSENDDIVTMHDVLDAQWIYDNTRDESYLRRVIRPLESLLVGYKRIVVKDSAVNAICYGAKLMIPGLLRYEAGIEVNEEIVLITTKGEAIAVGIAQMSTVELSTCDHGVVAKVKRCIMERDVYPRRWGLGPQSMKKKTLKKEGKLDKYGRPNENTPADWSKSYIDYSDPNAEVAKPAPVVAPAAPTVEAEVNGVEDSKKRKSVESSEKDEDEAAKKEEKRRKKEAKKEKKEKKEKKEKKEKKKKSE | Function: Catalytic subunit of H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Pseudouridine ('psi') residues may serve to stabilize the conformation of rRNAs and play a central role in ribosomal RNA processing. The H/ACA snoRNP complex also mediates pseudouridylation of other types of RNAs. Catalyzes pseudouridylation at position 93 in U2 snRNA. Also catalyzes pseudouridylation of mRNAs; H/ACA-type snoRNAs probably guide pseudouridylation of mRNAs.
Catalytic Activity: uridine in 5S rRNA = pseudouridine in 5S rRNA
Sequence Mass (Da): 53110
Sequence Length: 474
Subcellular Location: Nucleus
EC: 5.4.99.-
|
P33322 | MSKEDFVIKPEAAGASTDTSEWPLLLKNFDKLLVRSGHYTPIPAGSSPLKRDLKSYISSGVINLDKPSNPSSHEVVAWIKRILRCEKTGHSGTLDPKVTGCLIVCIDRATRLVKSQQGAGKEYVCIVRLHDALKDEKDLGRSLENLTGALFQRPPLISAVKRQLRVRTIYESNLIEFDNKRNLGVFWASCEAGTYMRTLCVHLGMLLGVGGHMQELRRVRSGALSENDNMVTLHDVMDAQWVYDNTRDESYLRSIIQPLETLLVGYKRIVVKDSAVNAVCYGAKLMIPGLLRYEEGIELYDEIVLITTKGEAIAVAIAQMSTVDLASCDHGVVASVKRCIMERDLYPRRWGLGPVAQKKKQMKADGKLDKYGRVNENTPEQWKKEYVPLDNAEQSTSSSQETKETEEEPKKAKEDSLIKEVETEKEEVKEDDSKKEKKEKKDKKEKKEKKEKKDKKEKKEKKEKKRKSEDGDSEEKKSKKSKK | Function: Catalytic subunit of H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA . This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1 . Pseudouridine ('psi') residues may serve to stabilize the conformation of rRNAs and play a central role in ribosomal RNA processing . The H/ACA snoRNP complex also mediates pseudouridylation of other types of RNAs . Catalyzes pseudouridylation at position 93 in U2 snRNA . Also catalyzes pseudouridylation of mRNAs; H/ACA-type snoRNAs probably guide pseudouridylation of mRNAs . It is a centromeric DNA-CBF3-binding factor which is involved in mitotic chromosome segregation . Essential for cell growth .
Catalytic Activity: uridine in 5S rRNA = pseudouridine in 5S rRNA
Sequence Mass (Da): 54705
Sequence Length: 483
Subcellular Location: Nucleus
EC: 5.4.99.-
|
Q05590 | MLSVIGIGPGSQAMMTMEAIEALQAAEIVVGYKTYTHLVKAFTGDKQVIKTGMCREIERCQAAIELAQAGHNVALISSGDAGIYGMAGLVLELVSKQKLDVEVRLIPGMTASIAAASLLGAPLMHDFCHISLSDLLTPWPVIEKRIVAAGEADFVICFYNPRSRGREGHLARAFDLLAASKSAQTPVGVVKSAGRKKEEKWLTTLGDMDFEPVDMTSLVIVGNKTTYVQDGLMITPRGYTL | Function: Methyltransferase that likely catalyzes the ring contraction and methylation of C-17 in cobalt-factor III to form cobalt-factor IV. May also convert cobalt-precorrin-3 to cobalt-precorrin-4.
Catalytic Activity: Co(II)-factor III + H(+) + S-adenosyl-L-methionine = Co(II)-factor IV + S-adenosyl-L-homocysteine
Sequence Mass (Da): 25869
Sequence Length: 241
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 3/10.
EC: 2.1.1.-
|
Q977V1 | MNIWIRGGTSDANNISKEIKRNFKDSFLILTTTTDFGGKIAENFADLVISEKMTYDNLKKTLLDKKIDVFIDATHPFATHASETGIKISKELNIPYIRYERPSEKFKNAFYVENYEEAAKLALKISKKNIFYMSGIKNLKNVSEIIPIEKLIVRILPTSVPEALKILPSKNIVAMQGVFSENLNKELIIDYNCDVIITKDSGKSGGLYEKVSGATLAGAKPIIIKRPEINYPLKFEKIVEIVNYLKNV | Function: Catalyzes the reduction of the macrocycle of cobalt-precorrin-6A to cobalt-precorrin-6B.
Catalytic Activity: Co-precorrin-6B + NAD(+) = Co-precorrin-6A + H(+) + NADH
Sequence Mass (Da): 27999
Sequence Length: 248
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 7/10.
EC: 1.3.1.106
|
O27083 | MQTPEIKEGTEQYLWRRKTMNPGDKGVKRKGSDRQREKMSVIVMAGTEDARRIISRLSGMPWVEVTATATTEHGSDLAEKSGASRTVTGALDSDGLRELMADLDACILIDATHPFAAQATENALRACRETGTIYVRFERPEVIPDGVIRVGSFREAGEVASSLIGDGEVVMHLAGVSTLGDVLRSLEPERVAVRVLPSTSSIEKCLQLGVPPSHIIAMQGRFSAEMNLALLREYRAGAVITKESGETGGLPEKVEAASELGIPVILVERPEVNLEGEAVFGNINDLMDHVLKILRDMGQPGD | Function: Catalyzes the reduction of the macrocycle of cobalt-precorrin-6A to cobalt-precorrin-6B.
Catalytic Activity: Co-precorrin-6B + NAD(+) = Co-precorrin-6A + H(+) + NADH
Sequence Mass (Da): 32673
Sequence Length: 302
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 7/10.
EC: 1.3.1.106
|
O87691 | MILLLAGTSDARALAVQVKKAGYDVTATVVTDNAAIELQRAEVKVKIGRLTKEDMTDFINEHGVKAIVDASHPFAEEASKNAIGAAAETAIPYIRYERASQAFTYDNMTMVSTYEEAAEVAAEKKGVIMLTTGSKTLQVFTEKLLPLSDVRLVARMLPRLDNMEKCQQLGLPQKNIIAIQGPFTKEFDRALYKQYGVTVMVTKESGKVGSVDKKVEAAKELGLDIIMIGRPKIEYGTVYSTFEEVVHALVNQTRS | Function: Catalyzes the reduction of the macrocycle of cobalt-precorrin-6A to cobalt-precorrin-6B.
Catalytic Activity: Co-precorrin-6B + NAD(+) = Co-precorrin-6A + H(+) + NADH
Sequence Mass (Da): 27994
Sequence Length: 255
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 7/10.
EC: 1.3.1.106
|
Q05591 | MNEGDVLVVGGTSDARALCRQLDAANVAYTLSVATPAGKALAGDIKGQVRCGRLEYGQMVAWLKENRTRWVIDASHPYAEMVSHNLLRACETAGVLLSRYQRPEQLSNLTHPLLYTARSIADACEIARRFGPRVLLTTGSKDLAVWRAGLAEKTLLARVLPVAEVIQRCSELGFGVGEIFALCGPFSADFNAAFYHQCRADVVITKASGAEGGYQEKVQPCLDAGIPCIVIARPTPLVTGDELLESQAAFAQRLSRWLAAAKE | Function: Catalyzes the reduction of the macrocycle of cobalt-precorrin-6A to cobalt-precorrin-6B.
Catalytic Activity: Co-precorrin-6B + NAD(+) = Co-precorrin-6A + H(+) + NADH
Sequence Mass (Da): 28403
Sequence Length: 263
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 7/10.
EC: 1.3.1.106
|
P72711 | MVDSLATVWLIGGTVDSRAVAEGLIAQGINCLVTVTTSEAKHLYPIHQCLTVHVGALTPQEIPKFLKRHSIAVIVDASHPFAAQITTTVTAIAKEQQIPYIRFERPPLALGKNTLEVPDIQSLTRGKYQPYLRGKRVLLTVGARWLSHFSLLQDEAVLFARILPYPQALAQAIAAGFTSDRIIALRPPVAEPLEKALWQQWQIQGVVTKASGAQGGELVKQKVAEALGVNLIRIARPQTIPGQITDDLSQINQFCQRHLPS | Function: Catalyzes the reduction of the macrocycle of cobalt-precorrin-6A to cobalt-precorrin-6B.
Catalytic Activity: Co-precorrin-6B + NAD(+) = Co-precorrin-6A + H(+) + NADH
Sequence Mass (Da): 28565
Sequence Length: 261
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 7/10.
EC: 1.3.1.106
|
Q72CB8 | MVPPRWGSLDSLKPQQHLPMTKKGILLAAFGSGNRQGESTLRLFDERVRERFPGVPVRWAFTSVIMRRRLAAARKKTDSVLKALQKMWFEKYTHVAVQSLHIIPGAEYGDLVADVEAMRRDDGFTAATVGAPLLAGSGDMERSAAALLAHLPAGRKPDEAVVFMGHGTRHPAESSYEALAALVRRVDPHVHIGTMGGSRTLDHILPELQQGGVKGVWLMPLLSVVGRHATEDMAGTDPESWKSRLEASGLRCIPVLRGTAEYEGFVDIWLDHLTAAVSALDD | Function: Catalyzes the insertion of Co(2+) into sirohydrochlorin as part of the anaerobic pathway to cobalamin biosynthesis. To a lesser extent, is also able to insert Fe(2+) into sirohydrochlorin, yielding siroheme.
Catalytic Activity: Co-sirohydrochlorin + 2 H(+) = Co(2+) + sirohydrochlorin
Sequence Mass (Da): 30825
Sequence Length: 282
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 1/10.
Subcellular Location: Cytoplasm
EC: 4.99.1.3
|
Q72EC8 | MSRHPMVTRLLCLVFSCLIILACSPAFAGHGAPKAQKTGILLVAFGTSVEEARPALDKMGDRVRAAHPDIPVRWAYTAKMIRAKLRAEGIAAPSPAEALAGMAEEGFTHVAVQSLHTIPGEEFHGLLETAHAFQGLPKGLTRVSVGLPLIGTTADAEAVAEALVASLPADRKPGEPVVFMGHGTPHPADICYPGLQYYLWRLDPDLLVGTVEGSPSFDNVMAELDVRKAKRVWLMPLMAVAGDHARNDMAGDEDDSWTSQLARRGIEAKPVLHGTAESDAVAAIWLRHLDDALARLN | Function: Catalyzes the insertion of Co(2+) into sirohydrochlorin. To a lesser extent, is also able to insert Fe(2+) into sirohydrochlorin, yielding siroheme. Its periplasmic location means that it cannot participate in cobalamin biosynthesis and its genomic environment suggests it is likely to be associated with a heme or metal transport system.
Catalytic Activity: Co-sirohydrochlorin + 2 H(+) = Co(2+) + sirohydrochlorin
Sequence Mass (Da): 31807
Sequence Length: 297
Subcellular Location: Periplasm
EC: 4.99.1.3
|
Q05592 | MKKALLVVSFGTSYHDTCEKNIVACERDLAASCPDRDLFRAFTSGMIIRKLRQRDGIDIDTPLQALQKLAAQGYQDVAIQSLHIINGDEYEKIVREVQLLRPLFTRLTLGVPLLSSHNDYVQLMQALRQQMPSLRQTEKVVFMGHGASHHAFAAYACLDHMMTAQRFPARVGAVESYPEVDILIDSLRDEGVTGVHLMPLMLVAGDHAINDMASDDGDSWKMRFNAAGIPATPWLSGLGENPAIRAMFVAHLHQALNMAVEEAA | Function: Catalyzes the insertion of Co(2+) into sirohydrochlorin as part of the anaerobic pathway to cobalamin biosynthesis.
Catalytic Activity: Co-sirohydrochlorin + 2 H(+) = Co(2+) + sirohydrochlorin
Sequence Mass (Da): 29239
Sequence Length: 264
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 1/10.
EC: 4.99.1.3
|
Q58181 | MNKLVKKVYGVGVGVGDKKLLTLKALEVLKKVDKIFVPVSKKGKKSIAYEIIKDYVDGKNIEELLFPMIKDKERLKKYWENALEKVLKEDGEVAIITIGDPTLYSTFSYVWKLLKERGVEVEIVNGISSIFASAAALNIPLVEGDEKLCILPQGKDLEKYIDEFDTIIIMKTKNLNEKLSVIKNRDDYIIGLVKRATFEDEKVVIGKLDEINFDEFNDYLSLAIIKRFKR | Function: Methylates cobalt-precorrin-2 at the C-20 position to produce cobalt-precorrin-3A in the anaerobic cobalamin biosynthesis pathway.
Catalytic Activity: Co-precorrin-2 + S-adenosyl-L-methionine = Co-precorrin-3 + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 26267
Sequence Length: 230
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 2/10.
EC: 2.1.1.151
|
Q05593 | MNGKLYALSTGPGAPDLITVRAARILGSLDILYAPAGRKGGDSLALSIVRDYLGEQTEVRCCHFPMSADGAEKEAVWNEVAAALTAEVEAGKQVGFITLGDAMLFSTWIFLLQRIGCPEWLEIVPGVTSFAAIAARAKMPLAIERQSLAVISCTAPEAEIAQALQQHDSLVLMKVYGRFARIKALLAQAGLLECALMMSEATLPGEQCWRHLHEVNDDRPLPYFSTILVNKQWEYAE | Function: Methylates cobalt-precorrin-2 at the C-20 position to produce cobalt-precorrin-3A in the anaerobic cobalamin biosynthesis pathway.
Catalytic Activity: Co-precorrin-2 + S-adenosyl-L-methionine = Co-precorrin-3 + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 25806
Sequence Length: 237
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 2/10.
EC: 2.1.1.151
|
A2SQF0 | MHFMDGFLPIGWCVFWAVLAAPFLIYGMWKITKMINNDRHVLPLMAVCGAFIFVVSLVDIPSPTGSCSHPTGTGLSASFFGPAVTSVLGLIILVFQALLLGHGGFTTLGATAFSMAVMGPLAAWLVFKGLRKTGRVPLGPAVFCAAVVANCVTYLITSLQIALAYPVEGSVLTAFLAAAAVFAVVQIPISIIEGIISGLVATYIARIKPEILQKLGVISGEEVKKVLSEQA | Function: Part of the energy-coupling factor (ECF) transporter complex CbiMNOQ involved in cobalt import.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 24296
Sequence Length: 231
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
Subcellular Location: Cell membrane
|
Q46AL8 | MHIMEGYLPAIWCIVWFVVSIPVVAYGVYKLNKLVKEERGILPVLAVAGAFIFVLSSLKMPSVTGSCSHPTGTGIGAIIFGPAITAVLSTIVLIYQALFLAHGGLTTLGANVFSMGIVGPIVAYLIYKTGMKAKLNFYLIVFLAATLGDWATYIVTSTELALAFPAGDILTFGGFFSSFSKFVAIFAITQVPLAIVEGAVSALLFKYIIQAKSDLLVEMKVIGEPLVRKLRGLPA | Function: Part of the energy-coupling factor (ECF) transporter complex CbiMNOQ involved in cobalt import.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 25069
Sequence Length: 235
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
Subcellular Location: Cell membrane
|
A1ANE2 | MHIMEGFLPVEHAIGWSVASAPVVAYGLYSINKKIKKNPEQRMLLGVAAAFTFVLSALKMPSVTGSCSHPTGTGLGAILFGPSAVAPIGAVVLLFQALLLAHGGLTTLGANIFSMAIVGPFAAAAVFRLARAARFPFGVGVFLAASLGDLLTYVTTACQLAFAFPDPVGGFTASLAKFAGVFALTQIPLAISEGLLTVVVMNALLRFNREELGSLNIEGNGQEVQA | Function: Part of the energy-coupling factor (ECF) transporter complex CbiMNOQ involved in cobalt import.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 23364
Sequence Length: 226
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
Subcellular Location: Cell inner membrane
|
Q8U3L0 | MEEVFQNETIKQILAKYRRIWAIGHAQSVLGWDLEVNMPKEGILERSVAQGELSVLSHELLLHPEFVNLVEKAKGLENLNEYERGIVRVLDRSIRIARAFPPEFIREVSETTSLATKAWEEAKAKDDFSKFEPWLDKIISLAKRAAEYLGYEEEPYDALLDLYEEGLRTRDVEKMFEVLEKKLKPLLDKILEEGKVPREHPLEKEKYEREWMERVNLWILQKFGFPLGTRARLDVSAHPFTTEFGIRDVRITTRYEGYDFRRTILSTVHEFGHALYELQQDERFMFTPIAGGVSLGIHESQSRFWENIIGRSKEFVELIYPVLKENLPFMSNYTPEDVYLYFNIVRPDFIRTEADVVTYNFHILLRFKLERLMVSEEIKAKDLPEMWNDEMERLLGIRPRKYSEGILQDIHWAHGSIGYFPTYTIGTLLSAQLYYHIKKDIPDFEEKVAKAEFDPIKAWLREKIHRWGSIYPPKELLKKAIGEDMDAEYFVRWVKEKYL | Cofactor: Binds 1 cobalt ion per subunit. Can also utilize Mn(2+) (in vitro). Is not active with zinc ions.
Function: Broad specificity carboxypetidase that releases amino acids sequentially from the C-terminus, including neutral, aromatic, polar and basic residues, but not Pro, Gly, Asp and Glu.
Catalytic Activity: Release of a C-terminal amino acid with broad specificity, except for -Pro.
Sequence Mass (Da): 59043
Sequence Length: 499
EC: 3.4.17.19
|
P86516 | AFDLNDFNTLEDTYDQMNVFQLSEAGLTHEGRDMKSWIDSLTHCRSHLDEDVFMFKRNEPDSGSACVGTDLNRSSNNPCSDTYGGSGPASALETRHSYSQQYEDELNQRQRYEPSGTTVNNLLNKDAGSIYSYTPELR | Cofactor: Binds 1 zinc ion per subunit.
Function: Carboxypeptidase that catalyzes the release of hydrophobic and acidic C-terminal amino acids.
Sequence Mass (Da): 15590
Sequence Length: 138
Subcellular Location: Secreted
EC: 3.4.17.-
|
P42663 | MTPEAAYQNLLEFQRETAYLGSLGALAAWDQRTMIPRKGHGHRARQMAALARLLHERATDPRIGEWLEKVEGSSLVEDPLSDAAVNVRAWRRAYERARAIPERLAVELAQARSEGETAWEALRPRDDWQGFLPYLKRLFALAKEEAEILMAVGPDPLDPPYGELYDALLDGYEPGARARDLEPLFRELSSGLKGLLDRILGSGRRPDVGVLHRHYPKEAQRAFALELLQACGYDLEAGRLDPTAHPFEIAIGPGDVRITTRYYEDFFNAGIFGTLHEMGHALYEQGLPEAHWGTPRGEAASLGVHESQSRTWENLVGRSLGFWERFFPRAKEVFSSLADVRLEDFHFAVNAVEPSLIRVEADEVTYNLHILVRLELELALFRGELFLEDLPEAWREKYRAYLGVAPRDYKDGVMQDVHWSGGMFGYFPTYTLGNLYAAQFFAKAQEELGPLEPLFARGEFTPFLDWTRRKIHAEGSRFRPRALVERVTGSPPGAQAFLRYLEAKYGALYGF | Cofactor: Binds 1 zinc ion per subunit. Can also utilize cobalt ions, but contains bound zinc when purified after heterologous expression in E.coli.
Function: Broad specificity carboxypetidase that releases amino acids sequentially from the C-terminus, including neutral, aromatic, polar and basic residues, but not Pro.
Catalytic Activity: Release of a C-terminal amino acid with broad specificity, except for -Pro.
Sequence Mass (Da): 57954
Sequence Length: 511
EC: 3.4.17.19
|
P55747 | GSDLLTPGDNKTAHDSYAFLVNWLERFPQYKYRDFYIAGESYAGHYVPQLSQLVHRNNKGVRKPILNFKGFMVGNAVIDDYHDFVGTFEYWWTHGLISDDTYQKLQLACEFDSAEHESEACNKINNVAEAEEGLIDAYSIYTPTCKKTSLHRRRLIKGRRPWLPRGYDPCTEQYSTKYYNLPEVQKAFRANVTGIPYSWTACSDVLSDHWKDSPRSMLPIYRELIAAGIRIWVFSGDADSVVPLTATRYSIDALYLPTVTNWYPWYDEEEVAGWCQVYKGLTLVTIRGAGHEVPLHRPQQALKLFEHFLQDKPMPRPAHSIQSF | PTM: The linker peptide is endoproteolytically excised during enzyme maturation.
Catalytic Activity: Preferential release of a C-terminal arginine or lysine residue.
Sequence Mass (Da): 37408
Sequence Length: 324
EC: 3.4.16.6
|
P55748 | VPRVPGQAFDASFAHYAGYVTVSEDRGAALFYWFFEAAHDPASKPLLLWLNGGPGCSSIAFGVGEEVGPFHVNADGKGVHMNPYSWNQVANILFLDSPVGVGYSYSNTSADILSNGDERTAKDSLVFLTKWLERFPQYKEREFYLTGESYAGHYVPQLAQAIKRHHEATGDKSINLKGYMVGNALTDDFHDHYGIFQYMWTTGLISDQTYKLLNIFCDFESFVHTSPQCDKILDIASTEAGNIDSYSIFTPTCHSSFASSRNKVVKRLRSVGKMGEQYDPCTEKHSIVYFNLHEVQKALHVNPVIGKSKWETCSEVINTNWKDCERSVLHIYHELIQYGLRIWMFSGDTDAVIPVTSTRYSIDALKLPTVTPWHAWYDDDGEVGGWTQGYKGLNFVTVRGAGHEVPLHRPKQALTLIKSFLAGRPMPVLSDLRSDM | PTM: The linker peptide is endoproteolytically excised during enzyme maturation.
Catalytic Activity: Preferential release of a C-terminal arginine or lysine residue.
Sequence Mass (Da): 48952
Sequence Length: 436
EC: 3.4.16.6
|
P52711 | MKCTVVALVLLVAVQCLVLGAGPAAAAKARRTRQGDYLNRLRGSPSSRASWESLAAVEEQTTTKAAGRPAPVAAAVEAGRKEADRVEALPGHPRGVDFAQYAGYVTVDAAAGRALFYYLAEAVGGNGDKTKPLLLWLNGGPGCSSLGYGAMEELGPFRVMSDGKTLYSNPYSWNHAANVLFLESPAGVGYSYSNTTADYGRSGDNGTAEDAYQFLDNWLERFPEYKGREFYITGESYAGHYVPQLAHAILRHASPDINLKGIMIGNAVINDWTDSKGMYDFFWTHALISDETADGISKNCNFTAYGAGVASNALCDAASDEVGESLADIDIYNIYAPNCQSEKLVTPPIAPSIDNFDPCTDYYVEAYLNRPDVQKALHANVTRLDHPWSACSDVLTRWVDSAKTVLPIIQELMKNSIRVWVYSGDTDGRVPVTSSRLSVNQLQLPVAAKWRPWFSSTKGAGEVGGYIVQYKGDLSLVTVRGAGHEVPSYQPRRALVLVQNFLAGKALPDCKECEQD | PTM: The linker peptide is endoproteolytically excised during enzyme maturation.
Catalytic Activity: Preferential release of a C-terminal arginine or lysine residue.
Sequence Mass (Da): 55914
Sequence Length: 516
EC: 3.4.16.6
|
P08818 | MRTTTRRLPPAPAAAAVLLAALTCLLLRPAAVAAAGGHAADRIVRLPGQPEVDFDMYSGYITVDEAAGRSLFYLLQEAPEEAQPAPLVLWLNGGPGCSSVAYGASEELGAFRVMPRGAGLVLNEYRWNKVANVLFLDSPAGVGFSYTNTSSDIYTSGDNRTAHDSYAFLAAWFERFPHYKYREFYVAGESYAGHYVPELSQLVHRSGNPVINLKGFMVGNGLIDDYHDYVGTFEFWWNHGIVSDDTYRRLKDACLHDSFIHPSPACDAATDVATAEQGNIDMYSLYTPVCNISSSSSSSSLSRRRTRGRYPWLTGSYDPCTERYSTAYYNRRDVQTALHANVTGAMNYTWTNCSDTINTHWHDAPRSMLPIYRELIAAGLRIWVFSGDTDAVVPLTATRYSIGALGLATTTSWYPWYDDLQEVGGWSQVYKGLTLVSVRGAGHEVPLHRPRQALILFQQFLQGKPMPGRTTNVTVA | Function: May be involved in the degradation of small peptides (2-5 residues) or in the degradation of storage proteins in the embryo.
Catalytic Activity: Preferential release of a C-terminal arginine or lysine residue.
Sequence Mass (Da): 52625
Sequence Length: 476
Subcellular Location: Secreted
EC: 3.4.16.6
|
P21529 | MVTTPRLVSLLLLLALCAAAAGALRLPPDASFPGAQAERLIRALNLLPKDSSSSSGRHGARVGEGNEDVAPGQLLERRVTLPGLPEGVADLGHHAGYYRLPNTHDARMFYFFFESRGKKEDPVVIWLTGGPGCSSELAVFYENGPFTIANNMSLVWNKFGWDKISNIIFVDQPTGTGFSYSSDDRDTRHDETGVSNDLYDFLQVFFKKHPEFIKNDFFITGESYAGHYIPAFASRVHQGNKKNEGTHINLKGFAIGNGLTDPAIQYKAYTDYALEMNLIQKADYERINKFIPPCEFAIKLCGTNGKASCMAAYMVCNTIFNSIMKLVGTKNYYDVRKECEGKLCYDFSNLEKFFGDKAVRQAIGVGDIEFVSCSTSVYQAMLTDWMRNLEVGIPALLEDGINVLIYAGEYDLICNWLGNSRWVHSMEWSGQKDFAKTAESSFLVDDAQAGVLKSHGALSFLKVHNAGHMVPMDQPKAALEMLRRFTQGKLKEAVPEEESSTTSFYAAM | Catalytic Activity: Release of a C-terminal amino acid with broad specificity.
Sequence Mass (Da): 56362
Sequence Length: 508
Subcellular Location: Secreted
EC: 3.4.16.5
|
Q96VC4 | MRVLPATLLVGAATAATPAQQVLGGLQDFGNAVQDAMHENLPKINKPLEAFQEQLKSLYEAREFWEEVANAFPQNLDHNPVFSLPKKHTRRPDSHWDHIVRGADVQSVWVTGENGEKEREIEGKLEAYDLRIKKTDPSSLGIDPDVKQYTGYLDDNENDKHLFYWFFESRNDPKNDPVVLWLNGGPGCSSLTGLFMELGPSSIDENIKPVYNPYAWNSNASVIFLDQPVNVGYSYSGSTVSDTVAAGKDVYALLTLFFKQFPEYAEQDFHIAGESYAGHYIPVFTSEILSHQKRNINLKSVLIGNGLTDGLTQYEYYRPMACGEGGYPAVLDESSCRSMDNALGRCQSMIESCYNSESAWVCVPASIYCNNALLAPYQRTGQNVYDVRGKCEDESNLCYKGMGYVSEYLNKPEVRAAVGAEVDGYDSCNFDINRNFLFHGDWMKPYHRLVPGILEQIPVLIYAGDADFICNWLGNKAWTEALEWPGHKEFAAAPMEDLKIVDNEHTGKKIGQIKTHGNFTFMRLYGGGHMVPMDQPEASLEFFNRWLGGEWF | Function: Vacuolar carboxypeptidase involved in degradation of small peptides. Digests preferentially peptides containing an aliphatic or hydrophobic residue in P1' position, as well as methionine, leucine or phenylalanine in P1 position of ester substrate (By similarity).
Catalytic Activity: Release of a C-terminal amino acid with broad specificity.
Sequence Mass (Da): 62066
Sequence Length: 552
Subcellular Location: Vacuole
EC: 3.4.16.5
|
D4ANB6 | MELYLNMLSFWYILLATSFFGPSQAVYQAPLSVDESQKVTIEEGFQIFTSKHSPQHSIRIKKQDGSICDAHSAQYTGWLDIGPKHLFFWYFESQNDPENDPLTLWMTGGPGYSSMLGMLEEVGPCLVNEYGNGTKYNPWGWSKKSSMLFVDQPVGVGFSYGDEGHDIPNDSYLAAVDMHRFLQLFISEVFPNKLNSPFHISGESYGGHYIPYLGAQIVRQNKLYPNEPQVQLKSCLIGNGCMSHMHTTFGYWETLCTTNPGVEKPIFNETRCDIMAKNMPRCMKVAEVCRRNPDPAICLSAQSVCDEGITGLYNKESDVKGGRNRFDITTPCQADDICYVQGLHLQNYLNTKLVWDALSPPKEVKEYKFASKNVEHAFGLTSDSMVPSTEEVEFLLSNQIHIMSYQGNLDLACNTAGNLKWMHDIPWKGQAELSSKALVPWKSVLASTGKNETVGRMKEVKIRVTDSATFATRYAFVTVDNAGHMVPQDRPDVAFDLMNRWISGETFV | Function: Involved in degradation of small peptides.
Catalytic Activity: Release of a C-terminal amino acid with broad specificity.
Sequence Mass (Da): 57171
Sequence Length: 508
Subcellular Location: Secreted
EC: 3.4.16.5
|
P52710 | MILHTYIILSLLTIFPKAIGLSLQMPMALEASYASLVEKATLAVGQEIDAIQKGIQQGWLEVETRFPTIVSQLSYSTGPKFAIKKKDATFWDFYVESQELPNYRLRVKRNNPEVLKVDFTKQYSGYLDVEADDKHFFYWFFESRNDPQNDPIILWLNGGPGCSSLTGLFFELGSSRINENLKPIFNPYSWNGNASIIYLDQPVNVGFSYSSSSVSNTVVAGEDVYAFLQLFFQHFPEYQTNDFHIAGESYAGHYIPVFADEILSQKNRNFNLTSVLIGNGLTDPLTQYRYYEPMACGEGGAPSVLPADECENMLVTQDKCLSLIQACYDSQSAFTCAPAAIYCNNAQMGPYQRTGKNVYDIRKECDGGSLCYKDLEFIDTYLNQKFVQDALGAEVDTYESCNFEINRNFLFAGDWMKPYHEHVSSLLNKGLPVLIYAGDKDFICNWLGNRAWTDVLPWVDADGFEKAEVQDWLVNGRKAGEFKNYSNFTYLRVYDAGHMAPYDQPENSHEMVNRWISGDFSFH | Function: Involved in degradation of small peptides.
Catalytic Activity: Release of a C-terminal amino acid with broad specificity.
Sequence Mass (Da): 59448
Sequence Length: 523
Subcellular Location: Vacuole
EC: 3.4.16.5
|
O13849 | MLMKQTFLYFLLTCVVSAQFNGYVPPEQNGGDIVVPKDFYEKFGEDFIREQEESSAPLMNPVPERDEAEAPHHPKGHHEFNDDFEDDTALEHPGFKDKLDSFLQPARDFLHTVSDRLDNIFDDDEDEHVREKRPHDSADEDAPRRKHGKCKGKGKHHKGKHAKGKGKKSHPKPEDDSVFFDDERPKHHEFDDEDREFPAHHEPGEHMPPPPMHHKPGEHMPPPPMHHEPGEHMPPPPMHHEPGEHMPPPPMHHEPGEHMPPPPMHHEPGEHMPPPPMHHEPGEHMPPPPMHHEPGEHMPPPPMHHEPGEHMPPPPMHHEPGEHMPPPPMHHEPGEHMPPPPFKHHELEEHEGPEHHRGPEDKEHHKGPKDKEHHKGPKDKEHHKGPKDKEHHKGPKDKEHHKGPKDKEHHKGPKDKEHHQGPKEKHNERPEQNMQSSHELLVIEAFADLINSVPVEEIAEEFSRFLDTLGIEYYGNIPVHIQENAPKDSSIPPLFEFDDDLELSDLTPEQFAYLEMLKAEGIDPMTAFRDQSHPAKPSNAQPADSSRPYAVFSQEENGEHVNLKAFPDHTLRVKDSKPESLGIDTVKQYTGYLDVEDDRHLFFWFFESRNDPENDPVVLWLNGGPGCSSLTGLFMELGPSSINIETLKPEYNPHSWNSNASVIFLDQPINTGFSNGDDSVLDTVTAGKDVYAFLNLFFAKFPQYAHLDFHIAGESYAGHYIPQFAKEIMEHNQGANFFVASGYEMEKQYINLKSVLIGNGLTDPLVQYYFYGKMACESPYGPIMSQEECDRITGAYDTCAKLITGCYQTGFTPVCIGASLYCNNAMIGPFTKTGLNIYDIREECRDQEHLCYPETGAIESYLNQEFVQEALGVEYDYKGCNTEVNIGFLFKGDWMRKTFRDDVTAILEAGLPVLIYAGDADYICNYMGNEAWTDALEWAGQREFYEAELKPWSPNGKEAGRGKSFKNFGYLRLYEAGHMVPFNQPEASLEMLNSWIDGSLFA | Function: Involved in degradation of small peptides. Digests preferentially peptides containing an aliphatic or hydrophobic residue in P1' position, as well as methionine, leucine or phenylalanine in P1 position of ester substrate.
Catalytic Activity: Release of a C-terminal amino acid with broad specificity.
Sequence Mass (Da): 114237
Sequence Length: 1002
Subcellular Location: Vacuole
EC: 3.4.16.5
|
P00729 | MKAFTSLLCGLGLSTTLAKAISLQRPLGLDKDVLLQAAEKFGLDLDLDHLLKELDSNVLDAWAQIEHLYPNQVMSLETSTKPKFPEAIKTKKDWDFVVKNDAIENYQLRVNKIKDPKILGIDPNVTQYTGYLDVEDEDKHFFFWTFESRNDPAKDPVILWLNGGPGCSSLTGLFFELGPSSIGPDLKPIGNPYSWNSNATVIFLDQPVNVGFSYSGSSGVSNTVAAGKDVYNFLELFFDQFPEYVNKGQDFHIAGESYAGHYIPVFASEILSHKDRNFNLTSVLIGNGLTDPLTQYNYYEPMACGEGGEPSVLPSEECSAMEDSLERCLGLIESCYDSQSVWSCVPATIYCNNAQLAPYQRTGRNVYDIRKDCEGGNLCYPTLQDIDDYLNQDYVKEAVGAEVDHYESCNFDINRNFLFAGDWMKPYHTAVTDLLNQDLPILVYAGDKDFICNWLGNKAWTDVLPWKYDEEFASQKVRNWTASITDEVAGEVKSYKHFTYLRVFNGGHMVPFDVPENALSMVNEWIHGGFSL | Function: Vacuolar serine-type carboxypeptidase involved in degradation of small peptides . Digests preferentially peptides containing an aliphatic or hydrophobic residue in P1' position, as well as methionine, leucine or phenylalanine in P1 position of ester substrate . Also plays a role in breakdown of the autophagic body and the autophagosome-dependent protein synthesis . Plays a key role in phytochelatin (PC) synthesis from glutathione (GSH) by cleaving the Gly from GSH and form the PC-peptides of the structure (gamma-Glu-Cys)2-Gly . Also involved in resistance to xenobiotics via the degradation of glutathione-S-conjugates .
PTM: Enters the endoplasmic reticulum as an inactive zymogen and is modified by four N-linked core oligosaccharides, giving rise to a precursor known as P1 (67 kDa). As P1 transits through the Golgi, extension of its core oligosaccharides leads to the Golgi-modified P2 precursor (69 kDa). P2 is sorted away from secretory proteins at or beyond a late Golgi compartment and is subsequently delivered to the vacuole via a prevacuolar endosome-like compartment. Upon arrival in the vacuole, the N-terminal prosegment of P2 is cleaved by vacuolar proteases to yield the enzymatically active mature vacuolar form of CPY (61 kDa).
Catalytic Activity: Release of a C-terminal amino acid with broad specificity.
Sequence Mass (Da): 59802
Sequence Length: 532
Subcellular Location: Vacuole lumen
EC: 3.4.16.5
|
Q66K79 | MPPPLPLLLLTVLVVAAARPGCEFERNPAGECHRPPAADSATCVDLQLRTCSDAAYNHTTFPNLLQHRSWEVVEASSEYILLSVLHQLLEGQCNPDLRLLGCAVLAPRCEGGWVRRPCRHICEGLREVCQPAFDAIDMAWPYFLDCHRYFTREDEGCYDPLEKLRGGLEADEALPSGLPPTFIRFSHHSYAQMVRVLRRTASRCAHVARTYSIGRSFDGRELLVIEFSSRPGQHELMEPEVKLIGNIHGNEVAGREMLIYLAQYLCSEYLLGNPRIQRLLNTTRIHLLPSMNPDGYEVAAAEGAGYNGWTSGRQNAQNLDLNRNFPDLTSEYYRLAETRGARSDHIPIPQHYWWGKVAPETKAIMKWMQTIPFVLSASLHGGDLVVSYPFDFSKHPQEEKMFSPTPDEKMFKLLSRAYADVHPMMMDRSENRCGGNFLKRGSIINGADWYSFTGGMSDFNYLHTNCFEITVELGCVKFPPEEALYILWQHNKESLLNFVETVHRGIKGVVTDKFGKPVKNARISVKGIRHDITTAPDGDYWRLLPPGIHIVIAQAPGYAKVIKKVIIPARMKRAGRVDFILQPLGMGPKNFIHGLRRTGPHDPLGGASSLGEATEPDPLRARRQPSADGSKPWWWSYFTSLSTHRPRWLLKY | Function: Cleaves substrates with C-terminal arginine residues. Probably modulates the Wnt signaling pathway, by cleaving some undefined protein. May play a role in cleavage during prohormone processing.
Sequence Mass (Da): 73655
Sequence Length: 652
Subcellular Location: Secreted
EC: 3.4.17.-
|
P42788 | QYHTLPEIYSWLDRLVQEHPEHVEPVVGGKSYEGREIRGVKVSYKKGNPVVMVESNIHAREWITAATTTYLLNELLTSKNSTIREMAENYDWYIFPVTNPDGYVYTHTTDRMWRKTRSPNPDSLCAGTDPNRNWNFHWMEQGTSSRPCTETYGGKKAFSEVETRSFSDFLKTLKGQIKVYLAFHSYSQLLLFPYGHTCQHTYNHDDLQAIGDAAARSLAQRYGTDYTVGNIYDAIYPASGGSMDWAYDTLDIPIAYTYELRPRDGWNGFQLPANQIIPTGEETVDSVVTILKESRRLGYFNTSD | Cofactor: Binds 1 zinc ion per subunit.
Function: Involved in the digestion of the blood meal.
Sequence Mass (Da): 34849
Sequence Length: 304
Subcellular Location: Secreted
EC: 3.4.17.-
|
Q5F362 | MAVNYSAKEEADGHPAGGGPGGGATAGGGGAVKTRKPDNTAFKQQRLPAWQPILTAGTVLPAFFIIGLIFIPIGIGIFVTSNNIREYEIDYTGVEPSSPCNKCLNVSWDSTPPCTCTINFTLEHSFESNVFMYYGLSNFYQNHRRYVKSRDDSQLNGDNSSLLNPSKECEPYRTNEDKPIAPCGAIANSMFNDTLELYHIENDTRTAITLIKKGIAWWTDKNVKFRNPKGDGNLTALFQGTTKPVNWPKPVYMLDSEPDNNGFINEDFIVWMRTAALPTFRKLYRLIERKSNLQPTLQAGKYSLNITYNYPVHSFDGRKRMILSTISWMGGKNPFLGIAYITVGSICFFLGVVLLIIHHKYGNRNTSADIPN | Function: Accessory component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules. The beta subunit may assist in binding of the phospholipid substrate. Required for the proper folding, assembly and ER to Golgi exit of the ATP8A2:TMEM30A flippase complex. Required for the formation of the ATP8A2, ATP8B1 and ATP8B2 P-type ATPAse intermediate phosphoenzymes (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 41448
Sequence Length: 372
Domain: The N-terminal domain seems to play a role in the reaction cycle of the catalytic subunit such as ATP8A2.
Subcellular Location: Membrane
|
Q9NV96 | MAMNYNAKDEVDGGPPCAPGGTAKTRRPDNTAFKQQRLPAWQPILTAGTVLPIFFIIGLIFIPIGIGIFVTSNNIREIEIDYTGTEPSSPCNKCLSPDVTPCFCTINFTLEKSFEGNVFMYYGLSNFYQNHRRYVKSRDDSQLNGDSSALLNPSKECEPYRRNEDKPIAPCGAIANSMFNDTLELFLIGNDSYPIPIALKKKGIAWWTDKNVKFRNPPGGDNLEERFKGTTKPVNWLKPVYMLDSDPDNNGFINEDFIVWMRTAALPTFRKLYRLIERKSDLHPTLPAGRYSLNVTYNYPVHYFDGRKRMILSTISWMGGKNPFLGIAYIAVGSISFLLGVVLLVINHKYRNSSNTADITI | Function: Accessory component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules. The beta subunit may assist in binding of the phospholipid substrate. Required for the proper folding, assembly and ER to Golgi exit of the ATP8A2:TMEM30A flippase complex. ATP8A2:TMEM30A may be involved in regulation of neurite outgrowth, and, reconstituted to liposomes, predomiminantly transports phosphatidylserine (PS) and to a lesser extent phosphatidylethanolamine (PE). The ATP8A1:TMEM30A flippase complex seems to play a role in regulation of cell migration probably involving flippase-mediated translocation of phosphatidylethanolamine (PE) at the plasma membrane. Required for the formation of the ATP8A2, ATP8B1 and ATP8B2 P-type ATPAse intermediate phosphoenzymes. Involved in uptake of platelet-activating factor (PAF), synthetic drug alkylphospholipid edelfosine, and, probably in association with ATP8B1, of perifosine. Also mediates the export of alpha subunits ATP8A1, ATP8B1, ATP8B2, ATP8B4, ATP10A, ATP10B, ATP10D, ATP11A, ATP11B and ATP11C from the ER to other membrane localizations.
PTM: N-glycosylated. Contains high mannose-type oligosaccharides (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 40684
Sequence Length: 361
Domain: The N-terminal domain seems to play a role in the reaction cycle of the catalytic subunit such as ATP8A2.
Subcellular Location: Membrane
|
Q8VEK0 | MAMNYSAKDEVDGGPAGPPGGAAKTRRPDNTAFKQQRLPAWQPILTAGTVLPTFFIIGLIFIPIGIGIFVTSNNIREIEIDYTGTEPSSPCNKCLSPNVTSCACTINFTLKQSFEGNVFMYYGLSNFYQNHRRYVKSRDDSQLNGDPSALLNPSKECEPYRRNEDRPIAPCGAIANSMFNDTLELYLVANESDPKPIPIPLKKKGIAWWTDKNVKFRNPPGKESLEEKFKDTIKPVNWHKAVYELDPEDESNNGFINEDFIVWMRTAALPTFRKLYRLIERRDDLHPTLPAGQYFLNITYNYPVHSFDGRKRMILSTISWMGGKNPFLGIAYITIGSISFLLGVVLLVINHKYRNSSNTADITI | Function: Accessory component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules. The beta subunit may assist in binding of the phospholipid substrate. Required for the proper folding, assembly and ER to Golgi exit of the ATP8A2:TMEM30A flippase complex. ATP8A2:TMEM30A may be involved in regulation of neurite outgrowth, and, reconstituted to liposomes, predomiminantly transports phosphatidylserine (PS) and to a lesser extent phosphatidylethanolamine (PE). The ATP8A1:TMEM30A flippase complex seems to play a role in regulation of cell migration probably involving flippase-mediated translocation of phosphatidylethanolamine (PE) at the plasma membrane. Required for the formation of the ATP8A2, ATP8B1 and ATP8B2 P-type ATPAse intermediate phosphoenzymes. Involved in uptake of platelet-activating factor (PAF). Can also mediate the export of alpha subunits ATP8A1, ATP8B1, ATP8B2, ATP8B4, ATP10A, ATP10B, ATP10D, ATP11A, ATP11B and ATP11C from the ER to other membrane localizations.
PTM: N-glycosylated. Contains high mannose-type oligosaccharides.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 41061
Sequence Length: 364
Domain: The N-terminal domain seems to play a role in the reaction cycle of thr catalytic subunit such as ATP8A2.
Subcellular Location: Membrane
|
Q6AY41 | MAMNYSAKDEVDGGPTGPPGGAAKTRRPDNTAFKQQRLPAWQPILTAGTVLPTFFIIGLIFIPIGIGIFVTSNNIREIEGNVFMYYGLSNFYQNHRRYVKSRDDSQLNGDPSALLNPSKECEPYRRNEDKPIAPCGAIANSMFNDTLELFLVANESDPKPVPILLKKKGIAWWTDKNVKFRNPPGKDSLQEKFKDTTKPVNWHKPVYELDPDDESNNGFINEDFIVWMRTAALPTFRKLYRLIERTDDLHPTLPAGQYYLNITYNYPVHFFDGRKRMILSTISWMGGKNPFLGIAYITIGSISFLLGVVLLVINHKYRNSSNTADITI | Function: Accessory component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules. The beta subunit may assist in binding of the phospholipid substrate. Required for the proper folding, assembly and ER to Golgi exit of the ATP8A2:TMEM30A flippase complex. ATP8A2:TMEM30A may be involved in regulation of neurite outgrowth, and, reconstituted to liposomes, predomiminantly transports phosphatidylserine (PS) and to a lesser extent phosphatidylethanolamine (PE). The ATP8A1:TMEM30A flippase complex seems to play a role in regulation of cell migration probably involving flippase-mediated translocation of phosphatidylethanolamine (PE) at the plasma membrane. Required for the formation of the ATP8A2, ATP8B1 and ATP8B2 P-type ATPAse intermediate phosphoenzymes. Involved in uptake of platelet-activating factor (PAF). Can also mediate the export of alpha subunits ATP8A1, ATP8B1, ATP8B2, ATP8B4, ATP10A, ATP10B, ATP10D, ATP11A, ATP11B and ATP11C from ER to other membrane localizations (By similarity).
PTM: N-glycosylated. Contains high mannose-type oligosaccharides (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 37173
Sequence Length: 328
Domain: The N-terminal domain seems to play a role in the reaction cycle of the catalytic subunit such as ATP8A2.
Subcellular Location: Membrane
|
Q3MIR4 | MTWSATARGAHQPDNTAFTQQRLPAWQPLLSASIALPLFFCAGLAFIGLGLGLYYSSNGIKELEYDYTGDPGTGNCSVCAAAGQGRALPPPCSCAWYFSLPELFQGPVYLYYELTNFYQNNRRYGVSRDDAQLSGLPSALRHPVNECAPYQRSAAGLPIAPCGAIANSLFNDSFSLWHQRQPGGPYVEVPLDRSGIAWWTDYHVKFRNPPLVNGSLALAFQGTAPPPNWRRPVYELSPDPNNTGFINQDFVVWMRTAALPTFRKLYARIRQGNYSAGLPRGAYRVNITYNYPVRAFGGHKLLIFSSISWMGGKNPFLGIAYLVVGSLCILTGFVMLVVYIRYQDQDDDDEE | Function: Accessory component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules. The beta subunit may assist in binding of the phospholipid substrate (Probable). Can mediate the export of alpha subunits ATP8A1, ATP8B1, ATP8B2 and ATP8B4 from the ER to the plasma membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 38941
Sequence Length: 351
Subcellular Location: Cell membrane
|
A7GN74 | MKRFKRAGAIIETLKEHGHEAYFVGGSVRDFIIDRPIGDIDIATSALPEEVMKLFPKHVPVGLEHGTVIVLQDGEPYEVTTFRTESDYEDFRRPSSVQFVRSLEEDLKRRDFTMNAIAMNEDGEIIDLFGGQEAIQKREIVTVGNAAERFQEDALRMMRGIRFVSTLGFSLEEKTECAIKRYGHLLEHIAIERITVEFEKLLTGPYCVKGLQKLVETKLFMHLPYLQMSEEKILKAAEYNWESFETEIEAWAFFLSCIGEEHPSVFLRQWKFSNKKIKEIVAVLLAIRTRKTKEWDAVFLYQTGVQIALMAERVYQVMIEEYNMSTVSEVQRLFDSLPIQKRQEMNVSGNDLLSWTDKTPGPWVAEVLQKIEEEILQKRLENEKEAIRGWIEECNLL | Function: Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. tRNA 3'-terminal CCA addition is required both for tRNA processing and repair. Also involved in tRNA surveillance by mediating tandem CCA addition to generate a CCACCA at the 3' terminus of unstable tRNAs. While stable tRNAs receive only 3'-terminal CCA, unstable tRNAs are marked with CCACCA and rapidly degraded.
Catalytic Activity: a tRNA precursor + ATP + 2 CTP = a tRNA with a 3' CCA end + 3 diphosphate
Sequence Mass (Da): 46056
Sequence Length: 397
EC: 2.7.7.72
|
A9VME7 | MERFKKASSIIEMLKQHGHEAYFVGGSVRDLIIDRPIGDIDIATSALPEEVMAIFPRHVPVGLEHGTVIVVENGEPYEVTTFRTESEYEDFRRPSSVQFVRSLEEDLKRRDFTMNAIAMTEEGEMVDLFAGKEAIRLKEITTVGDAADRFQEDALRMMRGIRFVSTLGFSLEIKTKQAIETYGHLLEHIAIERITVEFEKLLTGTYCVNGLQELVETKLFSHLPYLQMSEERLLKATQYKWDSFETDVEAWAFFLYCIGEEHPSVFLRQWKFSNKKIKDIVAVLLAIRSRKEKEWDTILLYKTGIRIAEMAERVYEAIIESYNSASVKQVQSLFHALPIKNRQEMNVTGNDLLSWTDKKPGPWVAEMLQNIEEAIVQGDLVNKKEDIREWLQRCNLL | Function: Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. tRNA 3'-terminal CCA addition is required both for tRNA processing and repair. Also involved in tRNA surveillance by mediating tandem CCA addition to generate a CCACCA at the 3' terminus of unstable tRNAs. While stable tRNAs receive only 3'-terminal CCA, unstable tRNAs are marked with CCACCA and rapidly degraded.
Catalytic Activity: a tRNA precursor + ATP + 2 CTP = a tRNA with a 3' CCA end + 3 diphosphate
Sequence Mass (Da): 45896
Sequence Length: 397
EC: 2.7.7.72
|
P42977 | MEKVFIKALPVLRILIEAGHQAYFVGGAVRDSYMKRTIGDVDIATDAAPDQVERLFQRTVDVGKEHGTIIVLWEDETYEVTTFRTESDYVDFRRPSEVQFISSLEEDLKRRDLTINAMAMTADGKVLDYFGGKKDIDQKVIRTVGKPEDRFQEDALRMLRAVRFMSQLGFTLSPETEEAIAKEKSLLSHVSVERKTIEFEKLLQGRASRQALQTLIQTRLYEELPGFYHKRENLISTSEFPFFSLTSREELWAALLINLGIVLKDAPLFLKAWKLPGKVIKEAIHIADTFGQSLDAMTMYRAGKKALLSAAKISQLRQNEKLDEKKLKDIQYAYQNLPIKSLKDLDITGKDLLALRNRPAGKWVSEELQWIEQAVVTGKLSNQKKHIEEWLKTCGQH | Function: Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. Has no poly(A) polymerase activity.
Catalytic Activity: a tRNA precursor + ATP + 2 CTP = a tRNA with a 3' CCA end + 3 diphosphate
Sequence Mass (Da): 45452
Sequence Length: 397
EC: 2.7.7.72
|
Q493X4 | MEKYLVGGAVRDALLKLPVQEKDWVVVGSSPQEMLNIGYEQVGKDFPVFLHPESHEEYALARTERKSGQGYTGFICHTAPSITIEEDLYRRDLTINAMAYDSHGNLIDPYHGQRDIKLRLLRHVSHTFHEDPLRVLRVARFAARFAHMNFAIAPETLILMKQMIHELLSLSPERIWTETKKALITDNPQVYFTVLRHCGALKILFPELDALFDIPTPTQYCTKINTGYYTMTTLSKAAYLTDDISVRFSVLCRDLGKGIPLNKINKNTKHHDHRKLGITLIHNLCNRFKIPHEIRNFSKITSEYHDYLYNVKILKPEMLMTLFHVFDCWRRPNRIDQIILVSQSDPIRWKNYNNYSLNQENLLRTAFTVTKKISTVDIIKDGFTGSNISRELYARRLHALNSWKNKQI | Function: Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. tRNA 3'-terminal CCA addition is required both for tRNA processing and repair. Also involved in tRNA surveillance by mediating tandem CCA addition to generate a CCACCA at the 3' terminus of unstable tRNAs. While stable tRNAs receive only 3'-terminal CCA, unstable tRNAs are marked with CCACCA and rapidly degraded.
Catalytic Activity: a tRNA precursor + ATP + 2 CTP = a tRNA with a 3' CCA end + 3 diphosphate
Sequence Mass (Da): 47442
Sequence Length: 408
EC: 2.7.7.72
|
Q7U358 | MSRTDDPGVAGLRVYIVGGAVRDDLLGLPAGDRDWVVVGATPEDMARRGFIPVGGDFPVFLHPRTKEEYALARTERKSGRGYKGFTFYTGADVTLEQDLQRRDLTVNAIARTPQGELVDPLDGVADVRARVLRHVGEAFAEDPVRILRLGRFAARFGDFSIAPETMQLCRRMVEAGEADALVPERVWKEVSRGLMAQAPSRMLDVLARAGALARVMPELHDDTAVRAEIDRAAAAGLPLAGRYALLCRHTPERDALGRRLRAPVECMDQARLLPLAVDALAASATPAAQLDLIERCDALRKPERFDALLQAAAIVAPVDLSAWRARVQAVRAIDAGAIARQCAGDPARIKPALRQARLQALGGA | Function: Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. tRNA 3'-terminal CCA addition is required both for tRNA processing and repair. Also involved in tRNA surveillance by mediating tandem CCA addition to generate a CCACCA at the 3' terminus of unstable tRNAs. While stable tRNAs receive only 3'-terminal CCA, unstable tRNAs are marked with CCACCA and rapidly degraded.
Catalytic Activity: a tRNA precursor + ATP + 2 CTP = a tRNA with a 3' CCA end + 3 diphosphate
Sequence Mass (Da): 39427
Sequence Length: 364
EC: 2.7.7.72
|
Q9HI95 | MIDYQEVLSRYRPTQEEENKLKIISDDIIRKINSICRSRGLRAEAVIVGSYAKGTNLRDGDLDIFIAFDRDYPEEIINTEGLHIGHAVIPNGREKYAEHPYVSGEIGGVKIDVVPCYKMSFGDKKISAVDRTLLHTEYVNGHLDEKGRDEVRLLKIFTKSIGVYGAEARTFGFSGYLCELLVIRFGSFENVIRYFSKAKGRVLIDLDERFRDPMVLIDPVDPDRNVASPVSLESLSRMKIASKMFLSSPDEGFFQIEHNGKNVQYHDRGTCIMIYSLPKPDLTDDVIYPQVYRFRSVLQKIMESHEIRVISSEIDVSDRIYVLIETPACAEERIRVHTGPPVDTDNAVDFVNSWKARDRSRGPYIVADRLYVDVFTGQRSIEDIVRQEIFNYSIGKNLDRFKKSMEIMKFNVGMKSLPVLDKFFGADVFRK | Function: Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. tRNA 3'-terminal CCA addition is required both for tRNA processing and repair. Also involved in tRNA surveillance by mediating tandem CCA addition to generate a CCACCA at the 3' terminus of unstable tRNAs. While stable tRNAs receive only 3'-terminal CCA, unstable tRNAs are marked with CCACCA and rapidly degraded.
Catalytic Activity: a tRNA precursor + ATP + 2 CTP = a tRNA with a 3' CCA end + 3 diphosphate
Sequence Mass (Da): 49400
Sequence Length: 431
EC: 2.7.7.72
|
Q9V302 | MIDYQEVLSRYRPTQEEENRLRIISDDIIRKINSICRSRRLRAEAVIVGSYAKGTNLRDGDLDIFIAFDRDYPEEIINTEGLHIGHAVIPNGREKYAEHPYVSGEIGGVKIDVVPCYKMSFGDRKISAVDRTLLHTEYVNGHLDEKGRDEVRLLKIFTKSIGVYGAEARTFGFSGYLCELLVIRFRSFENVIRYFSKAKGRVLIDPDERFRDPMLLIDPVDP | Function: Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. tRNA 3'-terminal CCA addition is required both for tRNA processing and repair. Also involved in tRNA surveillance by mediating tandem CCA addition to generate a CCACCA at the 3' terminus of unstable tRNAs. While stable tRNAs receive only 3'-terminal CCA, unstable tRNAs are marked with CCACCA and rapidly degraded.
Catalytic Activity: a tRNA precursor + ATP + 2 CTP = a tRNA with a 3' CCA end + 3 diphosphate
Sequence Mass (Da): 25546
Sequence Length: 222
EC: 2.7.7.72
|
A1WHX2 | MQIYMVGGAVRDRLLGRPVHDRDWVVVGATPEQMRAQGYLPVGRDFPVFLHPATREEYALARTERKSGRGYRGFVVHSAPEVTLQEDLSRRDLTINAIATSADASGAGCLIDPHHGARDIAARVLRHVSTAFREDPVRILRVARFAARLPDFTVAPETLQLMREMVAHGETDHLVAERVWQELARGLMAEKPSRMFEVLRACGALERLLPEVERLWGVPQSAEHHPEIDTGAHLLLVLDMAARLQAPLAVRFACLAHDLGKGSTPADMLPRHIGHETRGAELLKHLAERLRVPADCRATADKVAREHGHIHCSNALSAAALVRLLERCDALRLPQRFADILLACECDARGRLGFAESAYPQRPRLTAALAAAQSVHSSAIAAQAAARGLAGPQVGALIRQARVAAVAQWLASQ | Cofactor: Magnesium is required for nucleotidyltransferase activity.
Function: Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. tRNA 3'-terminal CCA addition is required both for tRNA processing and repair. Also involved in tRNA surveillance by mediating tandem CCA addition to generate a CCACCA at the 3' terminus of unstable tRNAs. While stable tRNAs receive only 3'-terminal CCA, unstable tRNAs are marked with CCACCA and rapidly degraded.
Catalytic Activity: a tRNA precursor + ATP + 2 CTP = a tRNA with a 3' CCA end + 3 diphosphate
Sequence Mass (Da): 45163
Sequence Length: 413
Domain: Comprises two domains: an N-terminal domain containing the nucleotidyltransferase activity and a C-terminal HD domain associated with both phosphodiesterase and phosphatase activities.
|
Q9KPC6 | MQIYLVGGAVRDQLLQLPVYDRDWVVVGSSPQAMLAAGFQAVGKDFPVFLHPNSKEEHALARTERKTSVGYTGFACHYAPDVTLEEDLLRRDLTINAMAQDNSGQLIDPYGGQRDLAAKVLRHVSPAFVEDPLRVLRVARFAAKLHHLGFTVAEETMQLMAKIAQSGELQHLTAERVWQEWHKSLSAHHPEMFLQVLRDCGALAVVLPEIDRLFGVPQPEKWHPEIDTGIHTLMVAKQAAQLSDSLLVRFAAQVHDLGKGVTPPSEWPRHKLHCHTGLNIIESLCERIRVPNEFRDLALAVCAQHSNIHRADELKPTTKLKVLGLLDVWRKPERLEQVLLCCEADHRGRLGLESEPYPQREIFLRAYQAALGVAVQAVIADGFQGKHIKEELDKRRVSAIEAL | Cofactor: Magnesium is required for nucleotidyltransferase activity.
Function: Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. tRNA 3'-terminal CCA addition is required both for tRNA processing and repair. Also involved in tRNA surveillance by mediating tandem CCA addition to generate a CCACCA at the 3' terminus of unstable tRNAs. While stable tRNAs receive only 3'-terminal CCA, unstable tRNAs are marked with CCACCA and rapidly degraded.
Catalytic Activity: a tRNA precursor + ATP + 2 CTP = a tRNA with a 3' CCA end + 3 diphosphate
Sequence Mass (Da): 45204
Sequence Length: 403
Domain: Comprises two domains: an N-terminal domain containing the nucleotidyltransferase activity and a C-terminal HD domain associated with both phosphodiesterase and phosphatase activities.
|
Q6Z0E2 | MENGEIEGAADDGVPVPAPPNGRRYRPVGSSDRAVIQMTSMEPGSSSSTAVAAVSGITPQPPRNLTVDPSMQEDHTVSQGDSKLELFGFDSLVNILGLKSMTGEQIQAPSSPRDGEDVAITIGRPKETGPKFGTMMGVFVPCLQNILGIIYYIRFTWIVGMAGVWQSLVLVSFCGACTFLTGISLSAIATNGAMKGGGPYYLIGRALGPEVGVSIGLCFFLGNAVAGSMYVLGAVETFLDAVPSAGFFKESVTVVNNTLVNGTATASTATISTPSLHDLQVYGVIVTILLCFIVFGGVKIINKVAPAFLIPVLFSLLCIYLGVFIAPRHNAPKGITGLSITTFKDNWGSEYQRTNNAGVPDPNGSIYWDFNALVGLFFPAVTGIMAGSNRSASLKDTQRSIPIGTLSATLTTTAMYLFSVLLFGALATREELLTDRLLTATVAWPAPAVIYIGIILSTLGAALQSLTGAPRLLAAIANDDILPVLNYFKVSEGAEPHSATLFTAFICICCVVIGNLDLITPTITMFFLLCYAGVNLSCFLLDLLDAPSWRPRWKFHHWSLSLVGALLCVVIMFLISWSFTVVSLALASLIYYYVSLKGKAGDWGDGFKSAYFQLALRSLRSLGANQVHPKNWYPIPLIFCRPWGKLPENVPCHPKLADFANCMKKKGRGMSIFVSIIDGDYHELAEDAKTACRQLDTYIEYKRCEGVAEIIVAPSMSEGFRSIVQTMGLGNLKPNIIVMRYPEIWRRENLIQIPSTFVSIINDCIIANKAVVIVKGLDEWPNEYQRQYGTIDLYWIVRDGGLMLLLSQLLLTKETFESCKIQVFCIAEEDTDAEELKADVKKFLYDLRMHAEVIVVTMKSWEPHMESSSSGAPQDDSQEAYTSAQRRISTYLSEMKETAQREGHPLMEDGKQVVVNEQKIEKFLYTMFKLNSTILRYSRMAAVVLVSLPPPPLNHPAYFYMEYMDLLVENVPRMLIVRGYRRDVVTFFT | Function: Probable cation/chloride cotransporter that may mediate potassium-chloride cotransport. Involved in plant development and K(+) and Cl(-) homeostasis. May not be involved in sodium-chloride cotransport.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 108454
Sequence Length: 989
Subcellular Location: Membrane
|
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.