ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q9MA98 | MANEDDDGEKSRSLHQQIARKPKTQIVIGVPSYQEVLESSQTKSTPPSLFKPSQSFSQAFAFVKSSDVYSPPPPSSAAASSSQPSGASQVPHSSSQTHQTDGASSSSTPVATGSVPSNTTQNRNAILVSHRQKGNPLLKHIRNVKWVFSDIIPDYVLGQNSCALYLSLRYHLLHPDYLYFRIRELQKNFKLSVVLCHVDVEDTVKPLLEVTKTALLHDCTLLCAWSMTECARYLETIKVYENKPADLIQGQMDTDYLSRLNHSLTSIRHVNKSDVVTLGSTFGSLAHIIDASMEDLARCPGIGERKVKRLYDTFHEPFKR... | Function: Seems to be involved in nucleotide excision repair (NER) of damaged DNA (dark repair mechanism). The UVH1/RAD1-ERCC1/RAD10 complex may act as an endonuclease making DNA incision 5' to the lesion site. In vitro, is implicated in double strand breaks (DSBs) repair and is required for homologous recombination in... |
Q1LZ75 | MDEEGVHKPAGPPTRKKFLIPTDEDVVPPPGAKPLFRSTRSLPTVETSPPPGPQTYAEYALSGPPGGAEATRPVGPEPLAEETPNQAPKPGAKSNSIIVSPRQRGNPVLRFVRNVPWEFGDVLPDYVLGQSTCALFLSLRYHNLHPDYIHQRLQSLGKSYALRVLLVQVDVKDPQQALKELAKMCILADCTLILAWSPEEAGRYLETYKAYEQKPADLLMEKLEQDFVSRVTECLTTVKSVNKTDSQTLLTTFGSLEQLIAASREDLSLCPGLGPQKARRLFDVFHEPFLKVPH | Function: Non-catalytic component of a structure-specific DNA repair endonuclease responsible for the 5'-incision during DNA repair. Responsible, in conjunction with SLX4, for the first step in the repair of interstrand cross-links (ICL). Participates in the processing of anaphase bridge-generating DNA structures, whic... |
P07992 | MDPGKDKEGVPQPSGPPARKKFVIPLDEDEVPPGVAKPLFRSTQSLPTVDTSAQAAPQTYAEYAISQPLEGAGATCPTGSEPLAGETPNQALKPGAKSNSIIVSPRQRGNPVLKFVRNVPWEFGDVIPDYVLGQSTCALFLSLRYHNLHPDYIHGRLQSLGKNFALRVLLVQVDVKDPQQALKELAKMCILADCTLILAWSPEEAGRYLETYKAYEQKPADLLMEKLEQDFVSRVTECLTTVKSVNKTDSQTLLTTFGSLEQLIAASREDLALCPGLGPQKARRLFDVLHEPFLKVP | Function: Non-catalytic component of a structure-specific DNA repair endonuclease responsible for the 5'-incision during DNA repair. Responsible, in conjunction with SLX4, for the first step in the repair of interstrand cross-links (ICL). Participates in the processing of anaphase bridge-generating DNA structures, whic... |
P07903 | MDPGKDEESRPQPSGPPTRRKFVIPLEEEEVPCAGVKPLFRSSRNPTIPATSAHVAPQTYAEYAITQPPGGAGATVPTGSEPAAGENPSQTLKTGAKSNSIIVSPRQRGNPVLKFVRNVPWEFGEVIPDYVLGQSTCALFLSLRYHNLHPDYIHERLQSLGKNFALRVLLVQVDVKDPQQALKELAKMCILADCTLVLAWSAEEAGRYLETYKAYEQKPADLLMEKLEQNFLSRATECLTTVKSVNKTDSQTLLATFGSLEQLFTASREDLALCPGLGPQKARRLFEVLHEPFLKVPR | Function: Non-catalytic component of a structure-specific DNA repair endonuclease responsible for the 5'-incision during DNA repair. Responsible, in conjunction with SLX4, for the first step in the repair of interstrand cross-links (ICL). Participates in the processing of anaphase bridge-generating DNA structures, whic... |
Q8W4M7 | MIFKIEDVTVYFPYDNIYPEQYEYMVELKRALDAKGHCLLEMPTGTGKTIALLSLITSYRLSRPDSPIKLVYCTRTVHEMEKTLGELKLLHDYQVRHLGTQAKILALGLSSRKNLCVNTKVLAAENRDSVDAACRKRTASWVRALSTENPNVELCDFFENYEKAAENALLPPGVYTLEDLRAFGKNRGWCPYFLARHMIQFANVIVYSYQYLLDPKVAGFISKELQKESVVVFDEAHNIDNVCIEALSVSVRRVTLEGANRNLNKIRQEIDRFKATDAGRLRAEYNRLVEGLALRGDLSGGDQWLANPALPHDILKEAVP... | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: ATP-dependent 5'-3' DNA helicase, component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to CAK, in RNA transcription b... |
Q55G81 | MKFYIEDLLVYFPYSYIYPEQYSYMVALKRSLDNGGPCILEMPSGTGKTVSLLSLISSYQVKNPSIKLIYCSRTVPEIEQATEEARRVLQYRNSEMGEESPKTLCMSMSSRRNLCIQPRVSEERDGKVVDALCRELTSSWNRESPTSEKCKFFENFESNGKEILLEGVYSLEDLKEYGLKHQMCPYFLSRHMLNFANIVIFSYQYLLDPKIASLISSSFPSNSIVVFDEAHNIDNVCINALSINIDNKLLDTSSKNIAKINKQIEDIKKVDEKRLKDEYQRLVNGLARSGSTRADETTSDPVLPNDVIQEAVPGNIRKAE... | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: ATP-dependent 5'-3' DNA helicase, component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to CAK, in RNA transcription b... |
Q9UQW6 | MVNTEVYIVSAVRTPMGSFGGSFASLPATKLGSIAIKGALERVNIKPSDVDEVFMGNVVSANLGQNPARQCALGAGLPRSIVCTTVNKVCASGMKATILGAQTIMTGNAEIVVAGGTESMSNAPYYAPKNRFGAKYGNVELVDGLLRDGLSDAYDGLPMGNAAELCAEEHSIDRASQDAFAISSYKRAQNAQATKAFEQEIVPVEVPVGRGKPNKLVTEDEEPKNLNEDKLKSVRAVFKSNGTVTAANASTLNDGASALVLMSAAKVKELGLKPLAKIIGWGEAAQDPERFTTSPSLAIPKALKHAGIEASQVDYYEINE... | Function: Acetyl-CoA acetyltransferase; part of the first module of ergosterol biosynthesis pathway that includes the early steps of the pathway, conserved across all eukaryotes, and which results in the formation of mevalonate from acetyl-coenzyme A (acetyl-CoA) (By similarity). Erg10 catalyzes the formation of acetoa... |
P41338 | MSQNVYIVSTARTPIGSFQGSLSSKTAVELGAVALKGALAKVPELDASKDFDEIIFGNVLSANLGQAPARQVALAAGLSNHIVASTVNKVCASAMKAIILGAQSIKCGNADVVVAGGCESMTNAPYYMPAARAGAKFGQTVLVDGVERDGLNDAYDGLAMGVHAEKCARDWDITREQQDNFAIESYQKSQKSQKEGKFDNEIVPVTIKGFRGKPDTQVTKDEEPARLHVEKLRSARTVFQKENGTVTAANASPINDGAAAVILVSEKVLKEKNLKPLAIIKGWGEAAHQPADFTWAPSLAVPKALKHAGIEDINSVDYFE... | Function: Acetyl-CoA acetyltransferase; part of the first module of ergosterol biosynthesis pathway that includes the early steps of the pathway, conserved across all eukaryotes, and which results in the formation of mevalonate from acetyl-coenzyme A (acetyl-CoA) . ERG10 catalyzes the formation of acetoacetyl-CoA from ... |
O65404 | MAFTNVCLWTLLAFMLTWTVFYVTNRGKKATQLADAVVEEREDGATDVIIVGAGVGGSALAYALAKDGRRVHVIERDLREPERIMGEFMQPGGRLMLSKLGLEDCLEGIDAQKATGMTVYKDGKEAVASFPVDNNNFPFDPSARSFHNGRFVQRLRQKASSLPNVRLEEGTVKSLIEEKGVIKGVTYKNSAGEETTALAPLTVVCDGCYSNLRRSLNDNNAEVLSYQVGFISKNCQLEEPEKLKLIMSKPSFTMLYQISSTDVRCVFEVLPNNIPSISNGEMATFVKNTIAPQVPLKLRKIFLKGIDEGEHIKAMPTKKM... | Function: Catalyzes the stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, and is considered to be a rate-limiting enzyme in steroid biosynthesis.
Catalytic Activity: O2 + reduced [NADPH--hemoprotein reductase] + squalene = (S)-2,3-epoxysqualene + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]
Locatio... |
Q4WP25 | MGNPRGRRTNGSIKTSKGTQRGTVSNLLSDQPLAARPKVSIVSNDDSQDSSDGGAFTTPSTTESTLKTTINGTDSTERNMSRKPSSPMAPAFMVSAPGKVIVYGEHAVVHGKAAMAAAISLRSYLLVTTLSKSQRTITMNFRDIGLDHTWNIDELPWDVFHHPSKKKFYYDLVTSLDPELVAAIQPHADAVSPDKPEDVRKIHRRSASAFLYLFLSLGSSQNPGAIYTLRSTIPIGAGLGSSASVCVCLSAALLLQIRTLAGPHPDQPPDEAEVQIERINRWAFVGEMCTHGNPSGVDNTVSAGGKAVVFRREDYSKPPT... | Function: Mevalonate kinase; part of the second module of ergosterol biosynthesis pathway that includes the middle steps of the pathway (By similarity). Erg12 converts mevalonate into 5-phosphomevalonate (By similarity). The second module is carried out in the vacuole and involves the formation of farnesyl diphosphate,... |
A0A1D8PEL1 | MSQLPFIVGAPGKVIIFGEHAAVYGKPAIAAALSLRCYLLVSPSSDSNTIRLQFPDIKLDHSWNIKDLPWEEIKPYLTYDSANKPQIPSELVPEIVDKLSSFLNGFDNKMHYYACFCFLYLLMNLCDSKVSGMNFIVRSTLPIGAGLGSSASTSVCLSSALALMGGWINKPSLHENDKLDTADIPDLEFIDKWSLIGEKCFHGNPSGIDNAVATFGGAVMFQRTSTPEQPSIRTNMRNFPAIKLLLTNTKVPKSTADLVAGVGRLNAEFNSISTSILTAIEHLSQEAYKVMMNPMFGREETNVLRKLVNINHGLLVALGV... | Function: Mevalonate kinase; part of the second module of ergosterol biosynthesis pathway that includes the middle steps of the pathway (By similarity). ERG12 converts mevalonate into 5-phosphomevalonate (By similarity). The second module is carried out in the vacuole and involves the formation of farnesyl diphosphate,... |
Q09780 | MSKSLIVSSPGKTILFGEHAVVYGATALAAAVSLRSYCKLQTTNNNEIVIVMSDIGTERRWNLQSLPWQHVTVENVQHPASSPNLDLLQGLGELLKNEENGLIHSAMLCTLYLFTSLSSPSQGCTLTISSQVPLGAGLGSSATISVVVATSLLLAFGNIEPPSSNSLQNNKALALIEAWSFLGECCIHGTPSGIDNAVATNGGLIAFRKATAHQSAMKEFLKPKDTLSVMITDTKQPKSTKKLVQGVFELKERLPTVIDSIIDAIDGISKSAVLALTSESDKNSSAKKLGEFIVLNQKLLECLGVSHYSIDRVLQATKSI... | Function: Mevalonate kinase; part of the second module of ergosterol biosynthesis pathway that includes the middle steps of the pathway (By similarity). Erg12 converts mevalonate into 5-phosphomevalonate (By similarity). The second module is carried out in the vacuole and involves the formation of farnesyl diphosphate,... |
P07277 | MSLPFLTSAPGKVIIFGEHSAVYNKPAVAASVSALRTYLLISESSAPDTIELDFPDISFNHKWSINDFNAITEDQVNSQKLAKAQQATDGLSQELVSLLDPLLAQLSESFHYHAAFCFLYMFVCLCPHAKNIKFSLKSTLPIGAGLGSSASISVSLALAMAYLGGLIGSNDLEKLSENDKHIVNQWAFIGEKCIHGTPSGIDNAVATYGNALLFEKDSHNGTINTNNFKFLDDFPAIPMILTYTRIPRSTKDLVARVRVLVTEKFPEVMKPILDAMGECALQGLEIMTKLSKCKGTDDEAVETNNELYEQLLELIRINHG... | Function: Mevalonate kinase; part of the second module of ergosterol biosynthesis pathway that includes the middle steps of the pathway . ERG12 converts mevalonate into 5-phosphomevalonate . The second module is carried out in the vacuole and involves the formation of farnesyl diphosphate, which is also an important in... |
A0A1D8PTW6 | MVMTNSPQNIGIKGIEVYIPGQAVNQSDLEKFDGIPQGKYTIGLGQTNMAFVNDREDIYSISLTVLSRLIKNYSIDTNKIGRLEVGTETLLDKSKSVKSVLMQLFPGNNDIEGIDTVNACYGGTSSVINAINWIESSSWDGRDAIVVAGDIAIYDKGAARPTGGVGAIALLIGPDAPIVFDSIRGSFMEHAYDFYKPDFTSEYPVVDGHFSLSCYVKAVDNCYKNYSKKITGDANKTVGVYDHFDFSAFHVPTCKLVTKSYARLLYNDYVSNPSKFADLIDETTRKHIDGLTYDESLTDKILEKTFVGLAKDETKKRVQP... | Function: Hydroxymethylglutaryl-CoA synthase; part of the first module of ergosterol biosynthesis pathway that includes the early steps of the pathway, conserved across all eukaryotes, and which results in the formation of mevalonate from acetyl-coenzyme A (acetyl-CoA) (By similarity). ERG13 condenses acetyl-CoA with a... |
I1RY35 | MSSRPQNIGIKAIELYFPSQYVDQVELEKFDGVSAGKYTIGLGQTKMSFCDDREDIYSFALTATSKLLKNYNIDPNSIGFLEVGTETLLDKSKSVKSVLMQLFGDNTNIEGVDTINACYGGTNAVFNAINWVESSAWDGRDAIVVAGDIALYAKGNARPTGGAGAVALLIGPNAPIVAEPGLRGTYMQHAYDFYKPDLTSEYPYVDGHYSVNCYSKALDAAYRAYCKREAKQANGTNGVTNGDASTKTGLDRFDYMAFHSPTCKLVQKSYARLLYHDYLANADSPVFAEVAPELRDMDYEKSLTDKVVEKTFMTLTKKRF... | Function: Hydroxymethylglutaryl-CoA synthase; part of the first module of ergosterol biosynthesis pathway that includes the early steps of the pathway, conserved across all eukaryotes, and which results in the formation of mevalonate from acetyl-coenzyme A (acetyl-CoA) (By similarity). ERG13 condenses acetyl-CoA with a... |
P54874 | MSFDRKDIGIKGLVLYTPNQYVEQAALEAHDGVSTGKYTIGLGLTKMAFVDDREDIYSFGLTALSQLIKRYQIDISKIGRLEVGTETIIDKSKSVKSVLMQLFGDNHNVEGIDCVNACYGGVNALFNTIDWIESSAWDGRDGIVVAGDIALYAKGNARPTGGAGCVALLVGPNAPIVFEPGLRGTYMQHAYDFYKPDLTSEYPYVDGHFSLECYVKALDGAYANYNVRDVAKNGKSQGLGLDRFDYCIFHAPTCKQVQKAYARLLYTDSAAEPSNPELEGVRELLSTLDAKKSLTDKALEKGLMAITKERFNKRVSPSVY... | Function: Hydroxymethylglutaryl-CoA synthase; part of the first module of ergosterol biosynthesis pathway that includes the early steps of the pathway, conserved across all eukaryotes, and which results in the formation of mevalonate from acetyl-coenzyme A (acetyl-CoA) . Hcs1 condenses acetyl-CoA with acetoacetyl-CoA t... |
P54839 | MKLSTKLCWCGIKGRLRPQKQQQLHNTNLQMTELKKQKTAEQKTRPQNVGIKGIQIYIPTQCVNQSELEKFDGVSQGKYTIGLGQTNMSFVNDREDIYSMSLTVLSKLIKSYNIDTNKIGRLEVGTETLIDKSKSVKSVLMQLFGENTDVEGIDTLNACYGGTNALFNSLNWIESNAWDGRDAIVVCGDIAIYDKGAARPTGGAGTVAMWIGPDAPIVFDSVRASYMEHAYDFYKPDFTSEYPYVDGHFSLTCYVKALDQVYKSYSKKAISKGLVSDPAGSDALNVLKYFDYNVFHVPTCKLVTKSYGRLLYNDFRANPQ... | Function: Hydroxymethylglutaryl-CoA synthase; part of the first module of ergosterol biosynthesis pathway that includes the early steps of the pathway, conserved across all eukaryotes, and which results in the formation of mevalonate from acetyl-coenzyme A (acetyl-CoA) . ERG13 condenses acetyl-CoA with acetoacetyl-CoA ... |
Q4V8Y6 | MSFDVRRFDIYRKVPKDLTQPTYTGAFISICCCVFMLFLFLSELTGFIATEIVNELYVDDPDKDSGGKIDVSLNISLPNLHCDLVGLDIQDEMGRHEVGHIENSMKVPLNNGHGCRFEGEFSINKVPGNFHVSTHSATAQPQSPDMTHIIHKLAFGAKLQVQHVQGAFNALGGADRLQSNALASHDYILKIVPTVYEELGGKQRFSYQYTVANKEYVAYSHTGRIIPAIWFRYDLSPITVKYTERRRPFYRFITTICAIIGGTFTVAGIIDSCIFTASEAWKKIQIGKMS | Function: Possible role in transport between endoplasmic reticulum and Golgi.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32529
Sequence Length: 290
Subcellular Location: Endoplasmic reticulum membrane
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Q969X5 | MPFDFRRFDIYRKVPKDLTQPTYTGAIISICCCLFILFLFLSELTGFITTEVVNELYVDDPDKDSGGKIDVSLNISLPNLHCELVGLDIQDEMGRHEVGHIDNSMKIPLNNGAGCRFEGQFSINKVPGNFHVSTHSATAQPQNPDMTHVIHKLSFGDTLQVQNIHGAFNALGGADRLTSNPLASHDYILKIVPTVYEDKSGKQRYSYQYTVANKEYVAYSHTGRIIPAIWFRYDLSPITVKYTERRQPLYRFITTICAIIGGTFTVAGILDSCIFTASEAWKKIQLGKMH | Function: Possible role in transport between endoplasmic reticulum and Golgi.
PTM: N-glycosylated.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32592
Sequence Length: 290
Subcellular Location: Endoplasmic reticulum membrane
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Q9DC16 | MPFDFRRFDIYRKVPKDLTQPTYTGAIISICCCLFILFLFLSELTGFITTEVVNELYVDDPDKDSGGKIDVSLNISLPNLHCELVGLDIQDEMGRHEVGHIDNSMKIPLNNGAGCRFEGQFSINKVPGNFHVSTHSATAQPQNPDMTHTIHKLSFGDTLQVQNVHGAFNALGGADRLTSNPLASHDYILKIVPTVYEDKSGKQRYSYQYTVANKEYVAYSHTGRIIPAIWFRYDLSPITVKYTERRQPLYRFITTICAIIGGTFTVAGILDSCIFTASEAWKKIQLGKIH | Function: Possible role in transport between endoplasmic reticulum and Golgi.
PTM: N-glycosylated.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32562
Sequence Length: 290
Subcellular Location: Endoplasmic reticulum membrane
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Q6NS19 | MPFDFRRFDIYRKVPKDLTQPTYTGAIISICCCLFITFLFLSELTGFIANEIVNELYVDDPDKDSGGKIDVTLNVTLPNLPCEVVGLDIQDEMGRHEVGHIDNSMKIPINNAYGCRFEGLFSINKVPGNFHVSTHSAIAQPANPDMRHIIHKLSFGNTLQVDNIHGAFNALGGADKLASKALESHDYVLKIVPTVYEDLNGKQQFSYQYTVANKAYVAYSHTGRVVPAIWFRYDLSPITVKYTERRQPMYRFITTVCAIIGGTFTVAGILDSFIFTASEAWKKIQLGKMQ | Function: Possible role in transport between endoplasmic reticulum and Golgi.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32533
Sequence Length: 290
Subcellular Location: Endoplasmic reticulum membrane
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Q7T2D4 | MRRLNKKKALNFVRELDAFPKVPESYVETTASGGTVSLLAFTAMALLAFFEFFVYRDTWMKYEYEVDKDFTSKLRINIDITVAMRCQFVGADVLDLAETMVASDGLVYEPVVFDLSPQQRLWHRTLLLIQGRLREEHSLQDVLFKNVMKGSPTALPPREDDPNQPLNACRIHGHLYVNKVAGNFHITVGKAIPHPRGHAHLAALVSHETYNFSHRIDHLSFGEEIPGILNPLDGTEKVSADHNQMFQYFITIVPTKLQTYKVYADTHQYSVTERERVINHAAGSHGVSGIFMKYDISSLMVKVTEQHMPFWQFLVRLCGI... | Function: Possible role in transport between endoplasmic reticulum and Golgi.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 42590
Sequence Length: 376
Subcellular Location: Endoplasmic reticulum-Golgi intermediate compartment membrane
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Q96RQ1 | MRRLNRKKTLSLVKELDAFPKVPESYVETSASGGTVSLIAFTTMALLTIMEFSVYQDTWMKYEYEVDKDFSSKLRINIDITVAMKCQYVGADVLDLAETMVASADGLVYEPTVFDLSPQQKEWQRMLQLIQSRLQEEHSLQDVIFKSAFKSTSTALPPREDDSSQSPNACRIHGHLYVNKVAGNFHITVGKAIPHPRGHAHLAALVNHESYNFSHRIDHLSFGELVPAIINPLDGTEKIAIDHNQMFQYFITVVPTKLHTYKISADTHQFSVTERERIINHAAGSHGVSGIFMKYDLSSLMVTVTEEHMPFWQFFVRLCG... | Function: Possible role in transport between endoplasmic reticulum and Golgi.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 42549
Sequence Length: 377
Subcellular Location: Endoplasmic reticulum-Golgi intermediate compartment membrane
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Q803I2 | MDALNKLKQFDAYPKTLEDFRIKTCGGATVTIISGLIMLILFFSELQYYLTKEVHPELFVDTSRGDKLRINIDVIFPHMPCAYLSIDAMDVAGEQQLDVEHNLFKQRLDKDGQPVTTEAEKHDLGKEEEGVFDPSTLDPDRCESCYGAETDDLKCCNTCDDVREAYRRRGWAFKTPDTIEQCKREGFSQKMQEQKNEGCQVYGFLEVNKVAGNFHFAPGKSFQQSHVHVHDLQSFGLDNINMTHFIKHLSFGKDYPGIVNPLDDTNVAAPQASMMYQYFVKIVPTIYVKGDGEVVKTNQFSVTRHEKIANGLIGDQGLPG... | Function: Possible role in transport between endoplasmic reticulum and Golgi.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43139
Sequence Length: 383
Subcellular Location: Endoplasmic reticulum-Golgi intermediate compartment membrane
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Q54DW2 | MLISQLKKFDAYPKTVDDFRVKTYTGAIVSIIGGVFILWLFFSQVTLYFSTDIHHELFVDTTRGEKLKINMDITFHHLPCAYLSLDAMDVSGEHQFDVAHNIFKKRLSPTGQPIIEAPPIREEEINKKESVKDNNDVVGCGSCYGAEDPSKGIGCCNTCEEVRVAYSKKGWGLDPSGIPQCIREGFTKNLVEQNGEGCQVYGFILVNKVAGNFHFAPGKSFQQHHMHVHDLQPFKDGSFNVSHTINRLSFGNDFPGIKNPLDDVTKTEMVGVGMFQYFVKVVPTIYEGLNGNRIATNQYSVTEHYRLLAKKGEEPSGLPG... | Function: Possible role in transport between endoplasmic reticulum and Golgi.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 42921
Sequence Length: 383
Subcellular Location: Endoplasmic reticulum-Golgi intermediate compartment membrane
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Q9Y282 | MEALGKLKQFDAYPKTLEDFRVKTCGGATVTIVSGLLMLLLFLSELQYYLTTEVHPELYVDKSRGDKLKINIDVLFPHMPCAYLSIDAMDVAGEQQLDVEHNLFKQRLDKDGIPVSSEAERHELGKVEVTVFDPDSLDPDRCESCYGAEAEDIKCCNTCEDVREAYRRRGWAFKNPDTIEQCRREGFSQKMQEQKNEGCQVYGFLEVNKVAGNFHFAPGKSFQQSHVHVHDLQSFGLDNINMTHYIQHLSFGEDYPGIVNPLDHTNVTAPQASMMFQYFVKVVPTVYMKVDGEVLRTNQFSVTRHEKVANGLLGDQGLPG... | Function: Possible role in transport between endoplasmic reticulum and Golgi. Positively regulates trafficking of the secretory proteins SERPINA1/alpha1-antitrypsin and HP/haptoglobin .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43222
Sequence Length: 383
Subcellular Location: Endoplasmic reticu... |
Q4R8X1 | MEALGKLKQFDAYPKTLEDFRVKTCGGATVTIVSGLLMLLLFLSELQYYLTTEVHPELYVDKSRGDKLKINIDVLFPHMPCAYLSIDAMDVAGEQQLDVEHNLFKQRLDKDGTPVSSEAERHELGKVEVTVFGPDSLDPDRCESCYGAEAEDIKCCNTCEDVREAYRRRGAFKNPDTIEQCRREGFSQKMQEQKNEGCQVYGFLEVNKVAGNFHFAPGKSFQQSHVHVHDLQSFGLDNINMTHYIQHLSFGEDYPGIVNPLDHTNVTAPQASMMFQYFVKVVPTVYMKVDGEVLRTNQFSVTRHEKVANGLLGDQGLPGV... | Function: Possible role in transport between endoplasmic reticulum and Golgi. Positively regulates trafficking of the secretory proteins alpha1-antitrypsin/SERPINA1 and HP/haptoglobin (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 42966
Sequence Length: 382
Subcellular Location: End... |
Q9CQE7 | MEALGKLKQFDAYPKTLEDFRVKTCGGATVTIVSGLLMLLLFLSELQYYLTTEVHPELYVDKSRGDKLKINIDVLFPHMPCAYLSIDAMDVAGEQQLDVEHNLFKKRLDKDGVPVSSEAERHELGKVEVTVFDPNSLDPNRCESCYGAESEDIKCCNSCEDVREAYRRRGWAFKNPDTIEQCRREGFSQKMQEQKNEGCQVYGFLEVNKVAGNFHFAPGKSFQQSHVHVHDLQSFGLDNINMTHYIKHLSFGEDYPGIVNPLDHTNVTAPQASMMFQYFVKVVPTVYMKVDGEVLRTNQFSVTRHEKVANGLLGDQGLPG... | Function: Possible role in transport between endoplasmic reticulum and Golgi. Positively regulates trafficking of the secretory proteins alpha1-antitrypsin/SERPINA1 and HP/haptoglobin (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43208
Sequence Length: 383
Subcellular Location: End... |
Q6NVS2 | MESLHRLRQFDAYPKTLEDFRVKTCGGALVTVISGLIMLILFFSELQYYLTKEIYPELFVDKSRGDKLKINIDVIFPHMPCAYLSIDAMDVAGEQQLDVEHNLFKQRLDKDKKPVTSEADRHELGKSEEHVVFDPKSLDPNRCESCYGAETDDFSCCNTCDDVREAYRRRGWAFKTPDSIEQCKREGFSQKMQEQKNEGCQVYGFLEVNKVAGNFHFAPGKSFQQSHVHVHDLQSFGLDNINMTHEIRHLSFGRDYPGLVNPLDGSSVAAMQSSMMFQYFVKIVPTVYVKVDGEVLRTNQFSVTRHEKMTNGLIGDQGLP... | Function: Possible role in transport between endoplasmic reticulum and Golgi.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43621
Sequence Length: 384
Subcellular Location: Endoplasmic reticulum-Golgi intermediate compartment membrane
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Q9P6K6 | MMSFGSFVYIACLLLNGANMLLQIFCVIMFSDLEMDYINPIDLCNKLNDLVMPEIISHTLVTLLLLLGKKWLLFLANLPLLVFHANQVIHKTHILDATEIFRQLGRHKRDNFIKVTFYLIMFFTLLYCMVMSLIQEE | Function: Regulates export of the secretory proteins from the endoplasmic reticulum in COPII-coated vesicles.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 15990
Sequence Length: 137
Subcellular Location: Endoplasmic reticulum
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P53173 | MGAWLFILAVVVNCINLFGQVHFTILYADLEADYINPIELCSKVNKLITPEAALHGALSLLFLLNGYWFVFLLNLPVLAYNLNKIYNKVQLLDATEIFRTLGKHKRESFLKLGFHLLMFFFYLYRMIMALIAESGDDF | Function: Could regulate export of the bud site and axial growth sites selection protein AXL2 and possibly other secretory proteins from the endoplasmic reticulum in COPII-coated vesicles. Seems to be required for axial budding pattern in haploid cells.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da):... |
Q8GXX0 | MGEKPWQPLLQSFEKLSNCVQTHLSNFIGIKNTPPSSQSTIQNPIISLDSSPPIATNSSSLQKLPLKDKSTGPVTKEDLGRATWTFLHTLAAQYPEKPTRQQKKDVKELMTILSRMYPCRECADHFKEILRSNPAQAGSQEEFSQWLCHVHNTVNRSLGKLVFPCERVDARWGKLECEQKSCDLHGTSMDF | Function: FAD-dependent sulfhydryl oxidase that catalyzes disulfide bond formation . Oxidizes thioredoxin in vitro . Required for the import and folding of small cysteine-containing proteins in the mitochondrial intermembrane space. Forms a redox cycle with MIA40 that involves a disulfide relay system. Important for ma... |
Q10Q80 | MPPPAWGWGSNPLEPVVHTVAAFSRRLLIAPDAAPDEARLRPLLSLSLSPPPTPPSPPPPPPEVLKKDSKAAPLTKEEVGRATWMLLHTIAAQFPDEPTRQQRRDARELMAIISRLYPCKECAEHFKEVLKANPVQAGSQAEFSQWLCYVHNVVNRSLGKPIFPCQRVNARWGKLDCPERSCDLEGSNDIIPNR | Function: FAD-dependent sulfhydryl oxidase that catalyzes disulfide bond formation (By similarity). Required for the import and folding of small cysteine-containing proteins in the mitochondrial intermembrane space. Forms a redox cycle with MIA40 that involves a disulfide relay system. Important for maintaining the cys... |
O14144 | MVFGKRYRDKETGIIYDENGRPCKTCNIFSSFRNVAQQPNSSTVPEVKSNTQLESKQSSIDCNTNAIPDSVSFPRLPDVAELGRSTWTFLHAMAANFPKNPTPTQQNDMSSFLYNFSKFYPCWSCAEDLRIWMAKYGNSPRVDSRESLCEWICEAHNDVNERLGKPLFNCQVWSKKASELAD | Function: FAD-dependent sulfhydryl oxidase that catalyzes disulfide bond formation. Required for the import and folding of small cysteine-containing proteins in the mitochondrial intermembrane space (IMS) (By similarity).
Catalytic Activity: O2 + 2 R'C(R)SH = H2O2 + R'C(R)S-S(R)CR'
Sequence Mass (Da): 20769
Sequence Le... |
P27882 | MKAIDKMTDNPPQEGLSGRKIIYDEDGKPCRSCNTLLDFQYVTGKISNGLKNLSSNGKLAGTGALTGEASELMPGSRTYRKVDPPDVEQLGRSSWTLLHSVAASYPAQPTDQQKGEMKQFLNIFSHIYPCNWCAKDFEKYIRENAPQVESREELGRWMCEAHNKVNKKLRKPKFDCNFWEKRWKDGWDE | Function: FAD-dependent sulfhydryl oxidase that catalyzes disulfide bond formation. Required for the import and folding of small cysteine-containing proteins in the mitochondrial intermembrane space (IMS). Forms a redox cycle with MIA40 that involves a disulfide relay system. Important for maintaining the cysteine resi... |
Q9LJG3 | MADNLNLVSVLGVLLVLTIFHNPIIVYAGEGVPNVALFTFGDSYYDAGNKVFLSQRKDLPQTYWPYGKSRDYPNGKFSDGHIVPDFIADFISIPNGVLPPVLKPGVDISRGVSFAVADASILGAPVESMTLNQQVVKFKNMKSNWNDSYIEKSLFMIYIGTEDYLNFTKANPNADASAQQAFVTNVINRLKNDIKLLYSLGASKFVVQLLAPLGCLPIVRQEYKTGNECYELLNDLAKQHNGKIGPMLNEFAKISTSPYGFQFTVFDFYNAVLRRIATGRSLNYRFFVTNTSCCGVGTHNAYGCGKGNVHSKLCEYQRSY... | Function: Represses or inhibits nitriles production from methionine-derived and from indol-3-ylmethyl glucosinolates. Favors isothiocyanate production.
Sequence Mass (Da): 44060
Sequence Length: 392
Subcellular Location: Secreted
EC: 3.1.1.-
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Q9NQ30 | MKSVLLLTTLLVPAHLVAAWSNNYAVDCPQHCDSSECKSSPRCKRTVLDDCGCCRVCAAGRGETCYRTVSGMDGMKCGPGLRCQPSNGEDPFGEEFGICKDCPYGTFGMDCRETCNCQSGICDRGTGKCLKFPFFQYSVTKSSNRFVSLTEHDMASGDGNIVREEVVKENAAGSPVMRKWLNPR | Function: Involved in angiogenesis; promotes angiogenic sprouting. May have potent implications in lung endothelial cell-leukocyte interactions.
PTM: May contain intrachain disulfide bonds.
Sequence Mass (Da): 20095
Sequence Length: 184
Subcellular Location: Secreted
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Q9QYY7 | MKSLLLLTTLLVPLHLGMAWSAKYAVDCPEHCDKTECRSSLRCKRTVLDDCGCCQVCAAGPGETCYRTVSGMDGVKCGPGLKCHFYSEEDDFGDEFGICKDCPYGTFGMECKETCNCQSGICDRVTGRCLDFPFFQYAAAKSPSRTSASHTERDSASGDGNAVREEIGEGNAARPSVMKWLNPR | Function: Involved in angiogenesis; promotes angiogenic sprouting. May have potent implications in lung endothelial cell-leukocyte interactions (By similarity).
PTM: O-glycosylated; contains chondroitin sulfate and dermatan sulfate.
Sequence Mass (Da): 20043
Sequence Length: 184
Subcellular Location: Secreted
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P97682 | MKSLLLLTTLLIPLHLGMAWSAKYAVDCPEHCDNTECRSSLRCKRTVLDDCGCCQVCAAGPGETCYRTVSGMDGVKCGPGLKCHFYSEEDDFGDEFGVCKDCPYGTFGMDCKETCNCQSGICDRVTGRCLDFPFFQYAAAKSPSRTSASQTERDAASGDGNAVREEIGDRNAARPSVMKWLNPR | Function: Involved in angiogenesis; promotes angiogenic sprouting. May have potent implications in lung endothelial cell-leukocyte interactions (By similarity).
PTM: O-glycosylated; contains chondroitin sulfate and dermatan sulfate.
Sequence Mass (Da): 20075
Sequence Length: 184
Subcellular Location: Secreted
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Q01068 | MVMEMSKTYQYRKVMKPLLERKRRARINKCLDDLKDLMVECLQQEGEHVTRLEKADILELTVDHMRKLKQRGGLSLQGVVAGVGSPPTSTSTAHVESFRSGYVHAADQITQVLLQTQQTDEIGRKIMKFLSTRLIELQTQLLQQQQQQQQHQQQQIPQSSGRLAFPLLGGYGPAAAAAAISYSSFLTSKDELIDVTSVDGNALSETASVSSQESGASEPVWRPW | Function: Transcriptional repressor of genes that require a bHLH protein for their transcription. May serve as a transcriptional regulator of the Achaete-scute complex (AS-C) genes. Belongs to notch signaling pathway and depends on Su(H) for transcriptional activation.
Sequence Mass (Da): 24983
Sequence Length: 224
Dom... |
P13097 | MATKYEMSKTYQYRKVMKPLLERKRRARINKCLDELKDLMAECVAQTGDAKFEKADILEVTVQHLRKLKESKKHVPANPEQSFRAGYIRAANEVSRALASLPRVDVAFGTTLMTHLGMRLNQLEQPMEQPQAVNTPLSIVCGSSSSSSTYSSASSCSSISPVSSGYASDNESLLQISSPGQVWRPW | Function: Participates in the control of cell fate choice by uncommitted neuroectodermal cells in the embryo. Transcriptional repressor. Binds DNA on N-box motifs: 5'-CACNAG-3'.
Sequence Mass (Da): 20687
Sequence Length: 186
Domain: The orange domain and the basic helix-loop-helix motif mediate repression of specific t... |
P13098 | MEYTTKTQIYQKVKKPMLERQRRARMNKCLDNLKTLVAELRGDDGILRMDKAEMLESAVIFMRQQKTPKKVAQEEQSLPLDSFKNGYMNAVNEVSRVMASTPGMSVDLGKSVMTHLGRVYKNLQQFHEAQSAADFIQNSMDCSSMDKAPLSPASSGYHSDCDSPAPSPQPMQQPLWRPW | Function: Participates in the control of cell fate choice by uncommitted neuroectodermal cells in the embryo . Transcriptional repressor . Binds DNA on N-box motifs: 5'-CACNAG-3' . Part of the Notch signaling pathway .
Sequence Mass (Da): 20303
Sequence Length: 179
Domain: The orange domain and the basic helix-loop-hel... |
Q8BK48 | MPLYKLLGWLNAVACGVLLLVLHVQGQDSASPIRNTHTGQVRGSLVHVKDTDIAVHTFLGIPFAKPPVGPLRFAPPEAPEPWSGVRDGTSHPNMCLQNDNLMGSEDLKMMNLILPPISMSEDCLYLNIYVPAHAHEGSNLPVMVWIHGGALTVGMASMYDGSMLAATEDVVVVAIQYRLGVLGFFSTGDQHAKGNWGYLDQVAALRWVQQNIVHFGGNPDRVTIFGESAGGTSVSSHVVSPMSQGLFHGAIMESGVAVLPDLISSSSEMVHRIVANLSGCAAVNSETLMCCLRGKNEAEMLAINKVFKIIPGVVDGEFLP... | Function: Carboxylesterase that catalyzes the hydrolysis of pyrethroids pesticides. Hydrolyzes trans-permethrin at a rate about 22-fold higher than cis-permethrin. Also hydrolyzes trans-cypermethrin. Hydrolyzes retinyl esters (By similarity).
PTM: Glycosylated.
Catalytic Activity: (-)-trans-permethrin + H2O = (1S,3R)-3... |
G3V7J5 | MAQTRAWKSIMPLESLPGWLNAVVWGLLLLFCQVQGQDSASPIRNTHTGQVRGSFVHVKDTKSGVHTFLGIPFAKPPIGPLRFAPPEPPEPWSGVRDGTSHPAMCLQNIDGLNLENLKIKMSRSPVSMSEDCLYLSIYTPAHTHKDSNLPVMVWIHGGGLCWGMASTYDGSMLAAIEDVVVVTIQYRLGILGFFSTGDEHARGNWGYLDQVAALRWVQQNIVHFGGNPDRVTIFGESAGGISVSSHVVSPMSQGLFHGAIMESGVALLPNLISNTSEVIYTMVANLSGCEPVDSEALMSCLREKSEEEMLAINNIVRTIS... | Function: Carboxylesterase that catalyzes the hydrolysis of pyrethroids pesticides. Hydrolyzes trans-permethrin at a rate about 22-fold higher than cis-permethrin. Also hydrolyzes trans-cypermethrin (By similarity). Hydrolyzes retinyl esters .
Catalytic Activity: all-trans-retinyl hexadecanoate + H2O = all-trans-retino... |
Q07085 | MGGFLSHLTPEQNVEALKASCGPVRGNIYKHDDVIVDGYLGIPYAKPPVGELRFKKPVTVDVWTEIKDCYKYGPACVQTGGFEQIAGPRTPTPEEAGCLTLNVFTPRNASSEFKNGRPVMVYIHGGGYELCASSDFCAYSLSGTLPLKDVVVVSINYRLGVFGFLTTGDNVCPGNFGLWDQTLALKWVQKHISSFGGDPNCVTVFGQSAGGASTDLLSLSPHSRDLFQRFIPISGTAHCDFAIRASENQAKIFREFAEFHGFSGRDSSALFKWYQEQSPETLSNVKGYKKSISGFLTFIPNLDGDFFPKPLDELRKEAPK... | Catalytic Activity: a carboxylic ester + H2O = a carboxylate + an alcohol + H(+)
Location Topology: Lipid-anchor
Sequence Mass (Da): 61825
Sequence Length: 554
Subcellular Location: Cytoplasm
EC: 3.1.1.1
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P21370 | KLLTDQDMQDDIFTPFGPTVEPYLTEQCMIPKEPFEMARTAWGDRIDIMIGGTSEEGLLLLQKIKLHPELLSHPHLFLGNVPPNLKISMEKRIEFAAKLKQRYYPDSSPSMENNLGYVHMMSDRVFWHGLHRTILARGARSRARTFVYRICLDSEFYNHYRIMMIDPKLRGTAHADELSYLFSNFTQQVPGKETFEYRGLQTLVDVFTAFVINGD | Function: Overproduction of nonspecific esterases is a common mechanism of resistance to organophosphate insecticides.
Catalytic Activity: a carboxylic ester + H2O = a carboxylate + an alcohol + H(+)
Sequence Mass (Da): 24937
Sequence Length: 215
EC: 3.1.1.1
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O00748 | MRLHRLRARLSAVACGLLLLLVRGQGQDSASPIRTTHTGQVLGSLVHVKGANAGVQTFLGIPFAKPPLGPLRFAPPEPPESWSGVRDGTTHPAMCLQDLTAVESEFLSQFNMTFPSDSMSEDCLYLSIYTPAHSHEGSNLPVMVWIHGGALVFGMASLYDGSMLAALENVVVVIIQYRLGVLGFFSTGDKHATGNWGYLDQVAALRWVQQNIAHFGGNPDRVTIFGESAGGTSVSSLVVSPISQGLFHGAIMESGVALLPGLIASSADVISTVVANLSACDQVDSEALVGCLRGKSKEEILAINKPFKMIPGVVDGVFLP... | Function: Involved in the detoxification of xenobiotics and in the activation of ester and amide prodrugs . Shows high catalytic efficiency for hydrolysis of cocaine, 4-methylumbelliferyl acetate, heroin and 6-monoacetylmorphine . Hydrolyzes aspirin, substrates with large alcohol group and small acyl group and endogeno... |
Q53547 | MTEPLILQPAKPADACVIWLHGLGADRYDFMPVAEALQESLLTTRFVLPQAPTRPVTINGGYEMPSWYDIKAMSPARSISLEELEVSAKMVTDLIEAQKRTGIDASRIFLAGFSQGGAVVFHTAFINWQGPLGGVIALSTYAPTFGDELELSASQQRIPALCLHGQYDDVVQNAMGRSAFEHLKSRGVTVTWQEYPMGHEVLPQEIHDIGAWLAARLG | Function: Hydrolyzes carboxylic ester bonds with relatively broad substrate specificity.
Catalytic Activity: a carboxylic ester + H2O = a carboxylate + an alcohol + H(+)
Sequence Mass (Da): 23880
Sequence Length: 218
EC: 3.1.1.1
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P14943 | QDSASPIRNTHTGQVRGSLVHVEGTDAGVHTFLGIPFAKPPLGPLRFAPPEPAEAWSGVRDGTSLPAMCLQNLAIMDQDVLLLHFTPPSIPMSEDCLYLNIYSPAHAREGSDLPVMVWIHGGGLTMGMASMYDGSALAAFEDVVVVTIQYRLGVLGFFSTGDQHATGNHGYLDQVAALRWVQKNIAHFGGNPGRVTIFGESAGGTSVSSHVLSPMSQGLFHGAIMESLVALLPGLITSSSEVVSTVVANLSRCGQVDSETLVRCLRAKSEEEMLAITQVFMLIPGVVDGVFLPRHPEELLALADFQPVPSIIGINNDEYG... | Function: Involved in the detoxification of xenobiotics and in the activation of ester and amide prodrugs. Converts monoacylglycerides to free fatty acids and glycerol. Hydrolyzes of 2-arachidonoylglycerol and prostaglandins (By similarity).
Catalytic Activity: a carboxylic ester + H2O = a carboxylate + an alcohol + H(... |
Q6UWW8 | MERAVRVESGVLVGVVCLLLACPATATGPEVAQPEVDTTLGRVRGRQVGVKGTDRLVNVFLGIPFAQPPLGPDRFSAPHPAQPWEGVRDASTAPPMCLQDVESMNSSRFVLNGKQQIFSVSEDCLVLNVYSPAEVPAGSGRPVMVWVHGGALITGAATSYDGSALAAYGDVVVVTVQYRLGVLGFFSTGDEHAPGNQGFLDVVAALRWVQENIAPFGGDLNCVTVFGGSAGGSIISGLVLSPVAAGLFHRAITQSGVITTPGIIDSHPWPLAQKIANTLACSSSSPAEMVQCLQQKEGEELVLSKKLKNTIYPLTVDGTV... | Function: Involved in the detoxification of xenobiotics and in the activation of ester and amide prodrugs. Shows low catalytic efficiency for hydrolysis of CPT-11 (7-ethyl-10-[4-(1-piperidino)-1-piperidino]-carbonyloxycamptothecin), a prodrug for camptothecin used in cancer therapeutics.
PTM: N-glycosylated.
Catalytic ... |
P94132 | MITIEREAMEFDVVIVGAGPAGLSAAIKIRQLAIENNLPDLSVCVVEKGSEVGAHILSGAVLEPRAINELFPNWKEEGAPLNVPVTEDKTYFLMSDEKSQEAPHWMVPKTMHNDGNYVISLGNVVRWLGQKAEELEVSIFPGFAAAEILYHADGTVKGIQTGDMGIGKDGEPTHNFAPGYELHAKYTLFAEGCRGHLGKRLINKFNLDQDADPQHYGIGIKELWEIDPAKHKPGLVMHGSGWPLSETGSSGGWWLYHAENNQVTLGMIVDLSYENPHMFPFMEMQRWKTHPLIKQYLEGGKRISYGARAVVKGGLNSLPK... | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Accepts electrons from ETF and reduces ubiquinone.
Catalytic Activity: a ubiquinone + reduced [electron-transfer flavoprotein] = a ubiquinol + H(+) + oxidized [electron-transfer flavoprotein]
Sequence Mass (Da): 62996
Sequence Length: 570
EC: 1.5.5.1
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Q2KIG0 | MQVLLARLACPVYQCFHAIKIKKNYLPLCATRWSSTSVVPRITTHYTVYPRDQDKRWEGVNMERFAEEADVVIVGAGPAGLSAAARLKQLAAQHEKDIRVCLVEKAAQIGAHTLSGACLDPRALQELFPDWKEKGAPLNTPVTEDRFGILTEKYRIPVPILPGLPMNNHGNYIVRLGHLVSWMGEQAEALGVEVYPGYAAAEVLFHEDGSVKGIATNDVGIQKDGAPKTTFERGLELHAKVTIFAEGCHGHLAKQLYRKFDLRANCEPQTYGIGLKELWVIDEKKWKPGRVDHTVGWPLDRHTYGGSFLYHLNEGEPLVA... | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Accepts electrons from ETF and reduces ubiquinone.
Catalytic Activity: a ubiquinone + reduced [electron-transfer flavoprotein] = a ubiquinol + H(+) + oxidized [electron-transfer flavoprotein]
Sequence Mass (Da): 68612
Sequence Length: 617
Subcellular Location: Mitochondrion... |
Q11190 | MRISGVTLFRVSSQLRNVVNGQWTTTHYTVKDRSTDPRWKDVDLARESDVYDVVIVGGGPSGLSAAIRLRQLAEKAQKELRVCVVEKASVIGGHTLSGAVIETRALDELIPNWKELGAPVYQQVTSESIAILTESGRIPVPVLPGVPLANHGNYIVRLGKVVQWLGEQAEAAGVEVWPEIAASEVLYNEDGSVKGIATSDVGIGKDGAPKDGFARGMEFHAKCTIFAEGCRGHLSKQVLDKFDLRTHAMTYGIGLKELWEIDPAKHRPGYVEHTMGWPLNVDQYGGSFLYHIEDQGQPLVSVGFVVALDYANPNLNPYKE... | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Accepts electrons from ETF and reduces ubiquinone.
Catalytic Activity: a ubiquinone + reduced [electron-transfer flavoprotein] = a ubiquinol + H(+) + oxidized [electron-transfer flavoprotein]
Sequence Mass (Da): 65335
Sequence Length: 597
Subcellular Location: Mitochondrion... |
Q54XM6 | MLKSFSLIGKNITKNVSLSSSNKFLFGKNHQNMKSIYSSIRFFSSEQELPPRDSDQFDVVIVGAGPSGLSTAIRLKQLSEKAGKDLRVCVVEKGSEVGSHILSGAVMDPKALNELIPDWKEKGAPLITEVKQDKFYFLTENRSLRLPTPRLMHNEGNYIISLGNVVRWLGEQAESMGVEVYPSFAASEVLYHDNGAVRGIATNDMGIAKDGSLTSNFTRGMELNARLTIFAEGCRGSLTKGLFEKFNLRDECEPQTFGLGIKETWEIKPEKHQQGLVIHTLGYPLSDELLGGSFIYHAENNTVNLGLVVGLDYSNPYLNP... | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Accepts electrons from ETF and reduces ubiquinone.
Catalytic Activity: a ubiquinone + reduced [electron-transfer flavoprotein] = a ubiquinol + H(+) + oxidized [electron-transfer flavoprotein]
Sequence Mass (Da): 67634
Sequence Length: 606
Subcellular Location: Mitochondrion... |
Q16134 | MLVPLAKLSCLAYQCFHALKIKKNYLPLCATRWSSTSTVPRITTHYTIYPRDKDKRWEGVNMERFAEEADVVIVGAGPAGLSAAVRLKQLAVAHEKDIRVCLVEKAAQIGAHTLSGACLDPGAFKELFPDWKEKGAPLNTPVTEDRFGILTEKYRIPVPILPGLPMNNHGNYIVRLGHLVSWMGEQAEALGVEVYPGYAAAEVLFHDDGSVKGIATNDVGIQKDGAPKATFERGLELHAKVTIFAEGCHGHLAKQLYKKFDLRANCEPQTYGIGLKELWVIDEKNWKPGRVDHTVGWPLDRHTYGGSFLYHLNEGEPLVA... | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Accepts electrons from ETF and reduces ubiquinone.
Catalytic Activity: a ubiquinone + reduced [electron-transfer flavoprotein] = a ubiquinol + H(+) + oxidized [electron-transfer flavoprotein]
Sequence Mass (Da): 68495
Sequence Length: 617
Subcellular Location: Mitochondrion... |
P55932 | SDIGGSMDYDVVIVGAGGAGLSAAILKQVNP | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Accepts electrons from ETF and reduces ubiquinone.
Catalytic Activity: a ubiquinone + reduced [electron-transfer flavoprotein] = a ubiquinol + H(+) + oxidized [electron-transfer flavoprotein]
Sequence Mass (Da): 2975
Sequence Length: 31
EC: 1.5.5.1
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P55931 | MMVPLAKLASPAYQCFHALKIKKNYLPLCATRWSSTCKVPRITTHYTIYPRDQDKRWEGVNMERFAEEADVVIVGAGPAGLSAATRLKQLAAQHEKDLRVCLVEKAAHIGAHTLSGACLDPRAFEELFPDWKEKGAPLNTPVTEDRFGILTEKYRIPVPILPGLPMNNHGNYVVRLGHLVSWMGEQAEALGVEVYPGYAAAEILFHEDGSVKGIATNDVGIQKDGAPKTTFERGLELHAKVTIFAEGCHGHLAKQLYKKFDLRANCEPQTYGIGLKELWVIDEKKWKPGRVDHTVGWPLDRHTYGGSFLYHLNEGEPLLA... | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Accepts electrons from ETF and reduces ubiquinone.
Catalytic Activity: a ubiquinone + reduced [electron-transfer flavoprotein] = a ubiquinol + H(+) + oxidized [electron-transfer flavoprotein]
Sequence Mass (Da): 68632
Sequence Length: 617
Subcellular Location: Mitochondrion... |
P87111 | MSYLSRSALARSVGAKHLTGVLRKIGRRGGRSMHVLPLASPSTLLKISSQTLRQDFTVLGARNFHSSSVRLNELTDNLRKLDTIEREVEDVDVCIVGAGPAGLSAAIRIKQQAAKANRDIRVVVLEKAAEPGNHSVSGAVIQPTALDELLPNWRDDPPENCTAVTHDKMKFLIPKLHFPIPVPPAMKNHGNYVMSLAEFTRWLAAKAEEYGVEIYPSFAASEVLYNKDGSVIGVATNDFGVDSKGLPKDNFERGMAFHAPVTLFAEGAHGSLSKSIIKRFNLRGNCEPQTYGLGVKEVWRVPDENFRKGEVAHTLGWPMR... | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Accepts electrons from ETF and reduces ubiquinone.
Catalytic Activity: a ubiquinone + reduced [electron-transfer flavoprotein] = a ubiquinol + H(+) + oxidized [electron-transfer flavoprotein]
Sequence Mass (Da): 69472
Sequence Length: 632
Subcellular Location: Mitochondrion... |
Q08822 | MIKFTNENLIRGIRMTISAKSRHLALGTDMTRKFSLSCRFLNKANLTEEEKELLNEPRARDYVDVCIVGGGPAGLATAIKLKQLDNSSGTGQLRVVVLEKSSVLGGQTVSGAILEPGVWKELFPDEKSDIGIPLPKELATLVTKEHLKFLKGKWAISVPEPSQMINKGRNYIVSLNQVVGYLGEKAEEVGVEVYPGIAVSDLIYDENNAVKGVITKDAGISKSGKPKETFERGMEFWARQTVLAEGCHGSLTKQALAKYDLRKGRQHQTYGLGIKEVWEVKPENFNKGFAAHTMGYPLTNDVYGGGFQYHFGDGLVTVGL... | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Accepts electrons from ETF and reduces ubiquinone.
Catalytic Activity: a ubiquinone + reduced [electron-transfer flavoprotein] = a ubiquinol + H(+) + oxidized [electron-transfer flavoprotein]
Sequence Mass (Da): 69634
Sequence Length: 631
Subcellular Location: Mitochondrion... |
O22854 | MHRFLVKLSSSSSPFSNQLRSLKNQRLILPLLPSSKPFTSSSVSPPPSPLNASNRFGYPYSADLFRNLSPLNPNSRILGVNGITSSRCISSEAVRESIEYDVLIVGAGPAGLSAAIRLKQLSQEKNIDLSVCVVEKGAEVGGHIISGNVFEPLALDELLPHWRQEHAPIEIPASSDKFWFLTKDRAFSLPSPFDNKGNYVISLSQLVRWLGGKAEELGTEIYPGFSASEVLFDASDKVVGIATKDMGISKDGSKKENFQPGVDIKGRVTLFAEGCRGSLSERIIKKYKLREEVNAQHQTYALGIKEVWEIDESKHNPGEV... | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Accepts electrons from ETF and reduces ubiquinone. May act downstream of IVD and D2HGDH in the degradation of phytol or chlorophyll during dark-induced senescence and sugar starvation.
Catalytic Activity: a ubiquinone + reduced [electron-transfer flavoprotein] = a ubiquinol... |
Q0AZ32 | MIFGFHPLEGGYDVPMRVVGANIPYEWLIYVIMLIPVSVFLFGFWKKLEVWLLAKGEIHRNDKIAQRIWSWFVFSFAQARVIRKPLAGWMHAFLFWGFLVLFLAAGIDAMHNMISWPHLEGNFYIGFSWVVDVLGFLALIGVMVLGFVRYFQKPERLNDTKSSDGWIILLIFAILLTGYFIEGLRIAAQIKLSTTMQQIAYERAASPFGWMFASFFGSMSVDAMLMWHRLLWWFHMAIAFLFIALVPFTKLWHIFASMLNYTFRDLEPSANRMVYNIEEAETFGVENIEDFGWKDLLDLDSCIRCGRCQENCPAYNTGKH... | Cofactor: Binds 2 [4Fe-4S] clusters per subunit.
Function: Oxidoreductase involved in syntrophic growth of S.wolfei with butyrate. Is presumed to link the electron flow from butyryl-CoA dehydrogenases to the membrane, in conjunction with the electron transfer flavoprotein EtfAB. May transfer electrons to the menaquinon... |
Q8Y7U4 | MNEQELKQMIEGILTEMSGGKTTDTVAAVPTKSVVETVVTEGSIPDITEVDIKKQLLVPEPADREGYLKMKQMTPARLGLWRAGPRYKTETILRFRADHAVAQDSVFSYVSEDLVKEMNFIPVNTKCQDKDEYLTRPDLGREFDDEMVEVIRANTTKNAKLQIVVGDGLSSAAIEANIKDILPSIKQGLKMYNLDFDNIIFVKHCRVPSMDKIGEITGADVVCLLVGERPGLVTAESMSAYIAYKPTVGMPEARRTVISNIHSGGTPPVEAGAYIAELIHNMLEKKCSGIDLK | Cofactor: Binds between the large and small subunits.
Function: Catalyzes the deamination of various vicinal amino-alcohols to oxo compounds. Allows this organism to utilize ethanolamine as the sole source of nitrogen and carbon in the presence of external vitamin B12.
Catalytic Activity: ethanolamine = acetaldehyde + ... |
Q02SJ2 | MNDKHLPDASAENPWLPLRQLTPARIALGRTGTSLPTRPQLDFQYAHAQARDAVHLPFDHAAISDGLRQRGRDSLLLHSAAADRHVYLQRPDLGRRLDEASVQRLREHAAGYDGQIDLAIVVADGLSALAVQRHTLPFLERLEEQALAEGWSLSPVVLVEQGRVAVADEIGELLRAKMSVILIGERPGLSSPDSLGLYFTWAPRVGLTDAYRNCISNVRLEGLSYGMAAHRLLYLMREACRRQLSGVNLKDEAEVQALEGEAPRTGNFLLARD | Cofactor: Binds between the large and small subunits.
Function: Catalyzes the deamination of various vicinal amino-alcohols to oxo compounds. Allows this organism to utilize ethanolamine as the sole source of nitrogen and carbon in the presence of external vitamin B12.
Catalytic Activity: ethanolamine = acetaldehyde + ... |
C3K2P6 | MKEPPVQLDLPDNPWLELRRLTPARIALGRTGTSIPTNAQLDFQFAHAQARDAVHLPFDPAGLSSQLAERGRDSLLLHSAAADRHSYLQRPDLGRRLSDESAQALRDHASANPGGVDLAVVVADGLSALAVHKHTLPFLTRMEEQTHAEGWSLSPVILVEQGRVAVADEIGQLLGAKMVVILIGERPGLSSPDSLGLYFTYNPKVGLTDAYRNCISNVRLEGLSYGMAAHRLLYLMREACRRQLSGVNLKDEAQVQTLESDDPDLMKGNFLLSSPDD | Cofactor: Binds between the large and small subunits.
Function: Catalyzes the deamination of various vicinal amino-alcohols to oxo compounds. Allows this organism to utilize ethanolamine as the sole source of nitrogen and carbon in the presence of external vitamin B12.
Catalytic Activity: ethanolamine = acetaldehyde + ... |
P22794 | MPTDMEHTGHYLHLAFLMTTVFSLSPGTKANYTRLWANSTSSWDSVIQNKTGRNQNENINTNPITPEVDYKGNSTNMPETSHIVALTSKSEQELYIPSVVSNSPSTVQSIENTSKSHGEIFKKDVCAENNNNMAMLICLIIIAVLFLICTFLFLSTVVLANKVSSLRRSKQVGKRQPRSNGDFLASGLWPAESDTWKRTKQLTGPNLVMQSTGVLTATRERKDEEGTEKLTNKQIG | Function: May complex with itself or/and other proteins within the membrane, to function as part of a cell-surface receptor.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 26213
Sequence Length: 236
Subcellular Location: Membrane
|
P34910 | MDPKYFILILFCGHLNNTFFSKTETITTEKQSQPTLFTSSMSQVLANSQNTTGNPLGQPTQFSDTFSGQSISPAKVTAGQPTPAVYTSSEKPEAHTSAGQPLAYNTKQPTPIANTSSQQAVFTSARQLPSARTSTTQPPKSFVYTFTQQSSSVQIPSRKQITVHNPSTQPTSTVKNSPRSTPGFILDTTSNKQTPQKNNYNSIAAILIGVLLTSMLVAIIIIVLWKCLRKPVLNDQNWAGRSPFADGETPDICMDNIRENEISTKRTSIISLTPWKPSKSTLLADDLEIKLFESSENIEDSNNPKTEKIKDQVNGTSEDS... | Function: Required for granulocyte differentiation and functionality of hematopoietic progenitor cells through the control of cell cycle progression and survival of hematopoietic progenitor cells.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 48666
Sequence Length: 448
Subcellular Location:... |
O60447 | MVTNKMTAAFRNPSGKQVATDKVAEKLSSTLSWVKNTVSHTVSQMASQVASPSTSLHTTSSSTTLSTPALSPSSPSQLSPDDLELLAKLEEQNRLLETDSKSLRSVNGSRRNSGSSLVSSSSASSNLSHLEEDSWILWGRIVNEWEDVRKKKEKQVKELVHKGIPHHFRAIVWQLLCSAQSMPIKDQYSELLKMTSPCEKLIRRDIARTYPEHNFFKEKDSLGQEVLFNVMKAYSLVDREVGYCQGSAFIVGLLLMQMPEEEAFCVFVKLMQDYRLRELFKPSMAELGLCMYQFECMIQEHLPELFVHFQSQSFHTSMYA... | Function: Functions as a regulator of cell cycle progression by stabilizing the FBXO5 protein and promoting cyclin-A accumulation during interphase. May play a role in cytokinesis.
PTM: Probably phosphorylated by PLK1; may be required for degradation during mitosis.
Sequence Mass (Da): 92949
Sequence Length: 810
Subcel... |
P97366 | MVTTKMTAAFRNPNRRQVATDKVAEKLSSTLSWVKNTVSHTVSQMASQVASPSASLHTTSSSTTLSTPTQSPSSPSKLSPDDLELLAKLEEQNRLIETDSKSLRSVNGSRRNSGSSLVSSSSASSNLSHLEEDSWILWGRIVNEWDDVRKKKEKQVKELVRKGIPHHFRAIVWQLLCNAQSMTIKDQYSELLKMTSPCEKLIRRDIARTYPEHNFFKEKDSLGQEVLFNVMKAYSLVDRELVTVRAVLSSLDCCCMQMPEEEAFCVFVKLMQDYRLRELFKPSMAELGLCMYQFECMIQEYLPELFVHFQSQSFHTSMYA... | Function: Functions as a regulator of cell cycle progression by stabilizing the FBXO5 protein and promoting cyclin-A accumulation during interphase. May play a role in cytokinesis (By similarity).
PTM: Probably phosphorylated by PLK1; may be required for degradation during mitosis.
Sequence Mass (Da): 92943
Sequence Le... |
Q9UI08 | MSEQSICQARASVMVYDDTSKKWVPIKPGQQGFSRINIYHNTASNTFRVVGVKLQDQQVVINYSIVKGLKYNQATPTFHQWRDARQVYGLNFASKEEATTFSNAMLFALNIMNSQEGGPSSQRQVQNGPSPDEMDIQRRQVMEQHQQQRQESLERRTSATGPILPPGHPSSAASAPVSCSGPPPPPPPPVPPPPTGATPPPPPPLPAGGAQGSSHDESSMSGLAAAIAGAKLRRVQRPEDASGGSSPSGTSKSDANRASSGGGGGGLMEEMNKLLAKRRKAASQSDKPAEKKEDESQMEDPSTSPSPGTRAASQPPNSSE... | Function: Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance and lamellipodial and filopodial dynamics in migrating cells. EVL enhances actin nucleation and polymerization.
PTM: Phosphorylated by PKA; phosphorylat... |
P70429 | MSEQSICQARASVMVYDDTSKKWVPIKPGQQGFSRINIYHNTASSTFRVVGVKLQDQQVVINYSIVKGLKYNQATPTFHQWRDARQVYGLNFASKEEATTFSNAMLFALNIMNSQEGGPSTQRQVQNGPSPEEMDIQRRQVMEQQHRQESLERRISATGPILPPGHPSSAASTTLSCSGPPPPPPPPVPPPPTGSTPPPPPPLPAGGAQGTNHDESSASGLAAALAGAKLRRVQRPEDASGGSSPSGTSKSDANRASSGGGGGGLMEEMNKLLAKRRKAASQTDKPADRKEDESQTEDPSTSPSPGTRATSQPPNSSEAG... | Function: Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance and lamellipodial and filopodial dynamics in migrating cells. EVL enhances actin nucleation and polymerization.
PTM: Phosphorylated by PKA; phosphorylat... |
Q64GL0 | MSEQSICQARASVMIYDDTSKKWVPIKPGQQGFSRINIYHNTANNTFRVVGVKLQDQQVVINYSLVKGLKYNQATPTFHQWRDARQVYGLNFASKEEATTFSNAMLFALNIMNSQDGGPAAQRQAQNIQNGPSPDDMEIQRRQMLEQQQRQETLERRTSTTVSTLQINVSSSPSHCQSPPPDYSNFSASPSTGAVPPPSYAKVISSAAASPELSSKSTNKSSNRTSEPPELQNSHCGSEPSTSQSSAFSPIRPSNGTVSRSIKQISLSPPPAPGSHSPLSLHQSVRHPSLSFSPCSSSPPVSVTSSVQKNISPQSPIPVV... | Function: Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance and lamellipodial and filopodial dynamics in migrating cells. Evl enhances actin nucleation and polymerization (By similarity).
Sequence Mass (Da): 7392... |
F4J4C8 | MKTTATSFVTGERVVVFVVVSRILLSLPLSLISHGFSLFLLSLSAFLVEIRVETSPFLLSHFSSRRGASSGILLGAVTLPSVMISKLVQLSRAISIHEAEQDELAHVTMQYWAASASCCAILIYLSVIMSQVRKDESLSSSSIWLTRVSLTGTVLYGVACFVSLSMISHTGLNTSLKMLWMLFHGLAAVKLIRHLLCTFPSCASIGEALLVTSGLVLYFGDFLACTIAKIFEKLIPVDLVSISYGIKRTETGIIVQGLLLGLLLFPMVFRFVLHIYESSLRKRDARQRNCSDAAKSVLFFVSLLFFMVVAVPSWMQFVHD... | Function: Essential for pollen development. Involved in protein N-glycosylation in the endoplasmic reticulum (ER), especially in the female gametophyte. Mediates pollen tube (PT) reception in synergids through protein glycosylation.
Catalytic Activity: CTP + di-trans,poly-cis-dolichol = a dolichyl phosphate + CDP + H(+... |
B8I3A9 | MNRVYSVSDINNYIKQLVSNDIILSDVSIRGEISNFKHHYTGHMYFTIKDKNSLLKCVMFRSQAVSLRFSPENGMKVIVSGYISVFERDGQYQLYASSMQPDGVGALHIAFEQLKEKLQREGLFDPENKKKIPVLPGSIGVVTSSTGAVIRDIINVTYRRNSKMKLVLYPVAVQGQQAAGQIAEAIKCLNEQNKVDVIIVARGGGSLEELWAFNEEIVARSIYASNIPVISAVGHETDFTICDFVSDMRAPTPSAAAELAVPDMEVLLYKLESYNMRMKSSLAKKVTTLKNQLQKLNARPFFAQPYDRVNQQRQTLDNLT... | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 4524... |
A1AX20 | MFNIDEIYTISNFLFLCNKTIEDKIPTCWLQGEISNLTRPESGHWYFSLKDSKAQVYCVLFRFNQRHIKFNPKNGMEVLVHVTPTLYKARGNFQLIIQHLEPVGIGNLNLAFEQLKNKLVNEGLFDNIHKKPLPNIINTIGVISSSTGAVIQDIIKVLNNRYPFSDILLFDSMVQGQGSVKKLTNALNAADQSGKCDVIIIARGGGSLEDLWAFNEETLARAIFKASTPIISAIGHETDTTISDFVCDICAPTPSAAAMLVTPDRLELLANTDKLYMRLHQSYQQTLHDYQSVLNQLKLRIPISNKQIAFFSQKLDHVSI... | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 5220... |
A9MHM3 | MLSSQTSSIFTVSRLNQTVRLLLEQEMGQVWISGEISNFTQPASGHWYFTLKDDTAQVRCAMFRNSNRRVTFRPQHGQQVLVRANITLYEPRGDYQIIVESMQPAGEGLLQQKYEQLKAKLQAEGLFDQQYKHPLPSPAYCVGVITSKTGAALHDILHVLKRRDPSLPVIIYPAAVQGEDAPGQIVRAITLANARKECDVLIVGRGGGSLEDLWSFNDERVARAIFASTIPVVSAVGHETDVTIADFVADLRAPTPSAAAEVVSRNQQELLRQMQTACQRLEMAMDYYLANRQRRFSQLYHRLQQQHPQLRLARQQTTLE... | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 5156... |
Q2S4K5 | MLSVAELTRGLSDLVEDRYDDVWVEGELSDFTRAASGHCYFSLKDEDAQIRCVMWKHLTQYVYFEPEEGMQVRVNGHASVYERRGDLQIQAQAMRQAGKGAQQKAFEELKQTLQAEGLFAPERKQALPAFPDTIGVVTSGQGAAIHDIQSGLARRFPPAEVVLCPVKVQGLDAPRAVADAVAAFNDLPADDAQRPDLLIVGRGGGSTEDLWAFNEEVVARALDASNLPVVSAVGHESDVTIADLVADERAATPSAAAERVVPDRRDVADRVRALHDRLRSRVTGRLQDARQRVDALVASRAFHAPARRLEQHRQHLDALV... | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 4390... |
A9ANA4 | MAKTASPGATPPGNGAEPLPDNYETALAELETLVARMEGGALSLEDSLAAYRRGAALVAFCQQQLEKVEQQVRVLDGATLKPAAATDGEDDDL | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 9672... |
Q8RAC8 | MEKEFNFEEDLKRLEEIVDTLEKGNLMLEESFNLFKEGVEISKRLEKMLKEVEGKITMLISEDEEIEFKEEENNV | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 8987... |
Q3AAM6 | MTFEEAMNRLNEIVERLERGNVGLEESLALFEEGLKLHRFCSEKLKELELKLVEVQEDEAGEVTFEEIVEMEDDLPF | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 9017... |
Q9K1A5 | MKKNAPKSFEEALSRLESLTQSMQGEMPLEDALAAYQEGNELVRYCQTKLAQVEQKLQVLDTDGLKELNLESDE | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 8375... |
Q82VD5 | MRKKSSSNKEETALHPPPENFETATAELEQIVAGMETGQMSLEDALSAYKRGVELLQYCQNILKNSQQQIKILEADMLKHFSPAEHDAS | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 9976... |
B2IWI8 | MVKRKGASSSEEGWNYEAKVAEIEGIITRIEAGELELEAVFEQFASAVEYLRQCESFLQQRQQQVDLLIETLSEE | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 8583... |
Q8YW43 | MVKRKNSDNSDTVAHGNYEAKVAEIEAIISRIESGELELEAVFEQFANAVEYLRQCDTFLQQRQQQMDLLIETLNDEDNSEL | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 9436... |
Q2G632 | MGTVPELASLSFEEALKELENVVRRLESGEAPLDESIELYARGDALRAHCQARLDAAQARIEAIVADRDGKAQGLRPFDETVG | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 9037... |
Q30Z97 | MTGTGTTGFEEQLARLQEIVRRLETGELPLEEGVALYKEGLELAAGCRKRLQTARNDIKVFSDGVLKDFDMPEDSPAADD | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 8814... |
Q6MDK5 | MNNPSDQEPTASFETALCRLEEILEKMNSGTVSLDESLKLYEEADQLIIICNKRLNDAERKIEILVKNRSGELTLGNDDKPIIQDFKIASTS | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 1035... |
Q8L1H9 | MSDIQTLSFEEAMRELEATVGKLETGEATLEDSIALYERGAALRAHCETRLREAEERVEKITLAANGQPSGTEPAEGL | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 8492... |
Q6D842 | MPKKTEQPVSFESSLNELEKIVTRLESGELPLDDALNEFEHGIQLARQGQQKLQQAEQRVQILLSDDPDAPLSPFTPDNDTL | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 9229... |
Q03FZ3 | MAEEKTFEENLQELQQVVSNLEQGDIPLEKALTEFQKGIQLSSELQETLKNAEKTLTKVMQDNGEETNLDLGTDGENE | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 8784... |
A5D2Z3 | MAEKEMNFEEALARLEAVVKELEDGRLPLQKALELFAEGIGLSRICNRYLEDAEQRIAILTADEKGGVVLRELGPSPAAREDTNDEL | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 9670... |
B4RGV8 | MSEPADIAAMTFEQALAELEQIVARLESGQAPLEDSIRMYERGAALKAHCETRLEAARLRVEKIVMGAGGAPASEPAEFG | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 8559... |
Q6H676 | MAKSCTLVLLLVALVGLSLLVSPIACSRKLSKPKPKPKPSMKKPVVRAHNNYTGSPSVTVTTGWAAAGATYYGAPNGDGSDGGACGYQTAVGQRPFSSMIAAGSPSLYKGGKGCGACYEVKCTTNAACSGQPATVVITDECPGGICLAGAAHFDMSGTSMGAMAKPGMADKLRAAGILQVQYRRVPCKYSGVNIAFRVDQGANPFYFEVLIEFEDGDGDLNAVDLMEAGCGWTPMVQNWGALWRYNSNTGKALKAPFSLRLTSDSGKVLVANNVIPASWKPGVTYRSLVNYS | Function: May cause loosening and extension of plant cell walls by disrupting non-covalent bonding between cellulose microfibrils and matrix glucans. No enzymatic activity has been found. May be required for rapid internodal elongation in deepwater rice during submergence (By similarity).
Location Topology: Peripheral ... |
Q10G40 | MAAFEPHRLQLLYFIAITVLASVFQPCTSIELHRELSGWSNGIATWYGDPNGAGSEGGACGYQYAVDQPPFSSRIAAGSPYIYDSGKGCGSCYRVVCAGNEACSGIPVTVVITDQGPGGPCLEELVDGQCMNEAAHFDMSGTAFGAMARPGQADQLRGAGLLQIQYTRVECEWTGVGLTFVVDSGSNPNYLALLVEYDDNDSDLAAVDIMPIGAGASGSWIPMQQSWGAVWRLNSGSALQGPFSVRLTFSSGQMFVASNAIPAGWNPGMAYQPGGVAMRVRGRNGGRRGYEAVGMLGGLCHLLLLLLLMLFEL | Function: May cause loosening and extension of plant cell walls by disrupting non-covalent bonding between cellulose microfibrils and matrix glucans. No enzymatic activity has been found. May be required for rapid internodal elongation in deepwater rice during submergence (By similarity).
Location Topology: Peripheral ... |
Q6H677 | MALAAKLLPSIVAFVALACCVLRSSVASVDHHRKLSGWSIGGATWYGPANGSGTDGGACGYQGDVGQPPFNSMIAAGSPSIYESGKGCGSCYQVKCSGNPSCSGKPVTVVLTDLCPGGACLEEPVHFDLSGTAFGAMAKPGQDDQLRNAGKLPVQYARVPCKWQGVDIAFRVDAGSNQYYLAVLVEDEDGDGDLSAVDLMQSGGSGGGGSWAAMQQSWGAVWKYNSGPAPLQAPMSIRLTSGSGRTLVASNVIPAGWQPGGTYRSIVNFRRED | Function: May cause loosening and extension of plant cell walls by disrupting non-covalent bonding between cellulose microfibrils and matrix glucans. No enzymatic activity has been found. May be required for rapid internodal elongation in deepwater rice during submergence (By similarity).
Location Topology: Peripheral ... |
Q0DZ85 | MAAFSSSSSAPMLIRSVLFVSLLSAAFVFDSGEAGAAHRVVDPEWHPATATWYGSADGDGSDGGACGYGTLVDVVPMKTRVGAVSPVLFKGGEGCGACYKVRCLDASICSRRAVTVIVTDECPGGVCAFGRTHFDLSGAAFARLAVAGHGGQLQNRGEISVVYRRTACKYGGKNIAFHVNEGSTTFWLSLLVEFEDGDGDIGSMQLKQANSAQWQDMKHIWGATWSLTPGPLVGPFSVRLTTLTTRQTLSAQDVIPKNWTPKATYTSRLNFA | Function: May cause loosening and extension of plant cell walls by disrupting non-covalent bonding between cellulose microfibrils and matrix glucans. No enzymatic activity has been found. May be required for rapid internodal elongation in deepwater rice during submergence (By similarity).
Location Topology: Peripheral ... |
Q7X6J9 | MAAASSRSFSLCVLLLLLLLAPPISASFLFDGGKSKSAAAAAAVDMEWRPATATWYGDAEGDGSTGGACGYGSLVDVVPMKARVGSVSPVLFKDGEGCGACYKVKCLDHGICSRRAVTVIVTDECPGGLCAFGRTHFDLSGAAFSRMAVAGAGGHLRDRGQLSVVYRRTACKYGGKNIAFRVNEGSTNFWLSLLVEFEDGQGDIGSMQIKQANSVEWLDMKHVWGATWCLVRGPLVGPFSVRLTTLSAQKALTARDVIPRNWKPTATYTSRLNFEAAL | Function: May cause loosening and extension of plant cell walls by disrupting non-covalent bonding between cellulose microfibrils and matrix glucans. No enzymatic activity has been found. May be required for rapid internodal elongation in deepwater rice during submergence (By similarity).
Location Topology: Peripheral ... |
Q5W6Z9 | MNSKFQLILSTFVVIAAFTLLPRPCASIEFHRKLSSWSNGGATWYGAANGAGSDGGACGYQAAVDQAPFSSMIAAGSPSIYKSGLGCGSCYQVKCSGNSACSGNPVTVVLTDECPGGPCLSEPVHFDLSGTAFGAMANPGQADQLRAAGVLQIQYNRVPCNWGGVMLTFAVDAGSNPSYFAVLVKYENGDGDLSGMDLMQTGAGAAWTPMQQSWGAVWKLSAGAALQAPLSIRLTSSSGKTLVASNVIPSGWKPGASYTSTVNY | Function: May cause loosening and extension of plant cell walls by disrupting non-covalent bonding between cellulose microfibrils and matrix glucans. No enzymatic activity has been found. May be required for rapid internodal elongation in deepwater rice during submergence (By similarity).
Location Topology: Peripheral ... |
O52043 | MESLQQLQQQLGLMAWPLFICSALTVMLLAERLFQVLLSLTVGKGAIRHALQATSPKNPKQLAELTEHFASKRPVLYRGVAMLLAHHQFDKSLREDAAGIWLQEQRHQFNSGLRLLTLIGVISPLLGLLGTVLGLIEMFKGVAATTGSITPNVLADGLGVAMYTTAAGLLIAVPAVAGAQLLSLWADRTMAKLEHTLNYVNLWLEGMTLHADASLTVVTPQEATTENL | Function: Involved in the TonB-dependent energy-dependent transport of various receptor-bound substrates. Protects ExbD from proteolytic degradation and functionally stabilizes TonB (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 24684
Sequence Length: 228
Subcellular Location: Cell ... |
O67637 | MMEEIKELIDYGIMGTLLFMSFVALAVGIERYLSIRSTKVENFKSKAQLEKELTKRLYIIATVASNAPYVGLLGTVLGILLTFYIIGEKGIVNTKEIMVGLALALKATALGLIVAIPSTILYNFLVRKVREKLLDWEAIHGECSSSHE | Function: Involved in the TonB-dependent energy-dependent transport of various receptor-bound substrates. Protects ExbD from proteolytic degradation and functionally stabilizes TonB (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 16396
Sequence Length: 148
Subcellular Location: Cell ... |
P0ABU8 | MGNNLMQTDLSVWGMYQHADIVVKCVMIGLILASVVTWAIFFSKSVEFFNQKRRLKREQQLLAEARSLNQANDIAADFGSKSLSLHLLNEAQNELELSEGSDDNEGIKERTSFRLERRVAAVGRQMGRGNGYLATIGAISPFVGLFGTVWGIMNSFIGIAQTQTTNLAVVAPGIAEALLATAIGLVAAIPAVVIYNVFARQIGGFKAMLGDVAAQVLLLQSRDLDLEASAAAHPVRVAQKLRAG | Function: Involved in the TonB-dependent energy-dependent transport of various receptor-bound substrates. Protects ExbD from proteolytic degradation and functionally stabilizes TonB (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26287
Sequence Length: 244
Subcellular Location: Cell ... |
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