Entry stringlengths 6 10 | Entry Name stringlengths 5 11 | Sequence stringlengths 2 35.2k | EC number stringlengths 7 127 ⌀ | Cofactor stringlengths 38 1.77k ⌀ | Gene Ontology (biological process) stringlengths 18 10.5k ⌀ | Gene Ontology (cellular component) stringlengths 17 1.89k ⌀ | Gene Ontology (molecular function) stringlengths 24 2.55k ⌀ | Pfam stringlengths 8 224 ⌀ | Gene3D stringlengths 10 250 ⌀ | Protein families stringlengths 9 237 ⌀ | Post-translational modification stringlengths 16 9.11k ⌀ | Subcellular location [CC] stringlengths 29 6.18k ⌀ | Catalytic activity stringlengths 65 35.7k ⌀ | Kinetics stringlengths 69 11.7k ⌀ | Pathway stringlengths 27 908 ⌀ | pH dependence stringlengths 64 955 ⌀ | Temperature dependence stringlengths 70 1.16k ⌀ | Function [CC] stringlengths 17 15.7k ⌀ | Organism stringlengths 8 196 | av_tokens listlengths 0 247 | av_text listlengths 0 247 | av_provenance listlengths 0 247 | nl_text stringlengths 42 15.3k |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
A0A023PYE4 | YE067_YEAST | MTQPLICAYRMCFVIDKYHSIFMCANYLNVYLERSTMVFSFLTVMPGDFIKCLFLRFFVKFKLRFPNGLLNIFQKMLFNMLVQVTHELLRMRICSITNFFRVLVRLV | null | null | null | membrane [GO:0016020] | null | null | null | null | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. | null | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | [
6727,
24930,
25105
] | [
"go_cc: membrane (GO:0016020)",
"subcellular_location: Membrane (SL-0162)",
"membrane_topology: Single-pass membrane protein (SL-9904)"
] | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB=ECO:0000255",
"UniProtKB=ECO:0000255"
] | Subcellular Location: Membrane
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 12901
Sequence Length: 107 |
A0A023PYE9 | YE087_YEAST | MVLFILVLYTCIQDGNGLLCGYISFSNTPMTSAKCWIGTVCFSIPCSFLVHFHCSSLHLFSNCFLHRSFSPHLMPRTSISTLGQLFEPTITHNGIPMACDNFILAPIPSFSLNWSRMSFCKFCMVGSFSSSDLTSCNLCEFSGLFGPVQIDTLYGAIIAGHLNPLESRPSSAIAPTSLLTPMP | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | [] | [] | [] | Sequence Mass (Da): 20007
Sequence Length: 183 |
A0A023PYF4 | YE145_YEAST | MAILLPLKSILPWCCITFSFLLSSSGSISHSTASSSITLTKSSKPTNVPSNSRFDCSTINTFWLIVLSMTSKGKISGRLILRASVYACECTCIRYACCETIYPPRKPFSLSLYFFYFNKKASILFCYPDAKTKPEHPGNKRAGSG | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | [] | [] | [] | Sequence Mass (Da): 16018
Sequence Length: 145 |
A0A023PYF7 | YE172_YEAST | MTVLLEHPLGPDSSRILCLALGKNMASKASCTSLSFLLCMATCSKQLGLNFSYHCSPPSSLILGRILDVSCLERKSFSVLLALRTGEVGLDELHFVICEPNELRLYCNKGRLFKFVLSISFRQEQT | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | [] | [] | [] | Sequence Mass (Da): 13972
Sequence Length: 126 |
A0A023PYG1 | YH002_YEAST | MLCFSGTLGCTKYGAFLLILSYRSPMARNDGSSLNESDSCLTTSVTAFFRVMCTEWLSMSAYNKEVKFFELISCLKREPQFSAKDTVKERVLKITLASCCSSLFSIRDITSCPLSSGSSFTKSQTSKMYCQLSLLNLGSVAFNSAFLILIADDDIFVNGFLR | null | null | null | membrane [GO:0016020] | null | null | null | null | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. | null | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | [
6727,
24930,
25105
] | [
"go_cc: membrane (GO:0016020)",
"subcellular_location: Membrane (SL-0162)",
"membrane_topology: Single-pass membrane protein (SL-9904)"
] | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB=ECO:0000255",
"UniProtKB=ECO:0000255"
] | Subcellular Location: Membrane
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 17933
Sequence Length: 162 |
A0A023PYG5 | YH046_YEAST | MNAENRNIAFNCQVSYFLAISSDLRIINDFVPFNLSFISSLGDESSSIFSSTISSLQFFSVFLRFVWLERLSSGTSIIFPLAQRVTTVFGAQVERTQAKFFYQDLMSL | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | [] | [] | [] | Sequence Mass (Da): 12274
Sequence Length: 108 |
A0A023PYH0 | YH070_YEAST | MTHRAVPCQPRAFSKIKVLVISFLFLMVAFLPFSSHGKLQEQIASYVSWKLETRAIHRFGGCNFAHQMQRNGIQRKIVCSDLERGNNTGMNACMQLVLSDLVARRVLLKTVHVHPWHLDGISGAFSVCCKDATEVS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | [] | [] | [] | Sequence Mass (Da): 15284
Sequence Length: 136 |
A0A023PYH5 | YH193_YEAST | MNMKMLLTRIHEMNALISSELNGRVDFFKNHRMFILSLVKILLVCTSRESLSVMYFRFDSFFDFLSGGASLPVLDSLEYALSDAAAIDGILKLLRRAGLLAQYTYLATENCRGLLRKGLVKRDI | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | [] | [] | [] | Sequence Mass (Da): 14085
Sequence Length: 124 |
A0A023PYH8 | YI047_YEAST | MNMLPMFTYSGLPVTLLCLIQLRRSVMILWIVVIWVQKPFHHLTTYLSRLHMTIILTVLPNLCPLTVGLSEEGPPCLRTFRDPFLGHMQLISKDQLSIPWMIGLPKQIVKVKWKVLCDLGWT | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | [] | [] | [] | Sequence Mass (Da): 14124
Sequence Length: 122 |
A0A023PYI2 | YI142_YEAST | MFTNTLAAGLSSGIDFRIVAPSFVTMQVLLDALCNNLSIPFGPNVLFTKSPTAMAPTNADKRAFSALSSVTWSPNICTLILNLLSFVRLTLLAYLMATFHPLFYCSALVF | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | [] | [] | [] | Sequence Mass (Da): 11940
Sequence Length: 110 |
A0A023PYI5 | YI036_YEAST | MLLPDFLHQRFHSRPVRDVEDTIDKFVCTVFSLQRLQTSFRSCYAVDDAFIVLFDNSFHQLQANPTGGTCNQNNLAHIPSLTDYKLFLLLLFATALISCIPSSFSALSFLATLRKRSKSEKKREKTMRNSMLP | null | null | null | membrane [GO:0016020] | null | null | null | null | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. | null | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | [
6727,
24930,
25105
] | [
"go_cc: membrane (GO:0016020)",
"subcellular_location: Membrane (SL-0162)",
"membrane_topology: Single-pass membrane protein (SL-9904)"
] | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB=ECO:0000255",
"UniProtKB=ECO:0000255"
] | Subcellular Location: Membrane
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 15235
Sequence Length: 133 |
A0A023PYJ0 | YM09A_YEAST | MKKKDRDSVFHRNIEIFITILINVVILKSFLLISSWVILVLLLVINDLPMYCYHHSLTYFLGCSKQTYFHRLGYPMQKLRHLLYFYYCYFLPRWKPRRRLTYHRYHPK | null | null | null | membrane [GO:0016020] | null | null | null | null | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. | null | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | [
6727,
24930,
25105
] | [
"go_cc: membrane (GO:0016020)",
"subcellular_location: Membrane (SL-0162)",
"membrane_topology: Single-pass membrane protein (SL-9904)"
] | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB=ECO:0000255",
"UniProtKB=ECO:0000255"
] | Subcellular Location: Membrane
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 13446
Sequence Length: 108 |
A0A023PYJ4 | YM153_YEAST | MLESHQSTTFGGKVFHYKSFHPNNQLFNLFNQLFLLLLACSLFFKSDSIELRTPLWIFPLFLKNNERPSFISSLRGFLKEVEFLETLNSALRTFEVTAFALAFSKIPSVFL | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | [] | [] | [] | Sequence Mass (Da): 12887
Sequence Length: 111 |
A0A023PYJ7 | YM304_YEAST | MIYGKMMGNTVLKNTGVFYQVIKPLKLHLLYDHSFSLFLKKQPNMGEISPFPYLLSYSYHVIVYLCVLCKVYILYSFVKDFSICLPFSYGSSLLYSLCSNLYIYIYAALPKSKIKL | null | null | null | membrane [GO:0016020] | null | null | null | null | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | [
6727,
24930,
25110
] | [
"go_cc: membrane (GO:0016020)",
"subcellular_location: Membrane (SL-0162)",
"membrane_topology: Multi-pass membrane protein (SL-9909)"
] | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB=ECO:0000255",
"UniProtKB=ECO:0000255"
] | Subcellular Location: Membrane
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13469
Sequence Length: 116 |
A0A023PYK2 | YP170_YEAST | MTERITTPNADRTVQHHALPVDTTGLIFFAVFASSFVLYRRGSCFESYLFFSFPLSYFSNNRKKSRVQSDKQFFSVFKKNDPEQQHLYYAALMQFLTQLVESPTLFCVCTQ | null | null | null | membrane [GO:0016020] | null | null | null | null | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. | null | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | [
6727,
24930,
25105
] | [
"go_cc: membrane (GO:0016020)",
"subcellular_location: Membrane (SL-0162)",
"membrane_topology: Single-pass membrane protein (SL-9904)"
] | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB=ECO:0000255",
"UniProtKB=ECO:0000255"
] | Subcellular Location: Membrane
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 12959
Sequence Length: 111 |
A0A023PZ94 | YA031_YEAST | MKDMNSIRYVFFFFSRDIKSCFYKVRSYLNLLLILEAILCPVDSLISIPNGIMVVSEPDSPFSHSNPSRRLFRKVNPSSCLSVLYLDLCCSGLIIAEAGIGG | null | null | null | membrane [GO:0016020] | null | null | null | null | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | [
6727,
24930,
25110
] | [
"go_cc: membrane (GO:0016020)",
"subcellular_location: Membrane (SL-0162)",
"membrane_topology: Multi-pass membrane protein (SL-9909)"
] | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB=ECO:0000255",
"UniProtKB=ECO:0000255"
] | Subcellular Location: Membrane
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 11414
Sequence Length: 102 |
A0A023PZ99 | YD008_YEAST | MFRSFMLAFQKACRQVHKQYLNKYYSVITYFLAFLTKFAILLESFTPFVSTPPLTSTPITPFNLSASPTFSGVSPPANIKCKLSGLSCLPTQSEIEFQSKSSPVPPASESNKGINE | null | null | null | membrane [GO:0016020] | null | null | null | null | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. | null | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | [
6727,
24930,
25105
] | [
"go_cc: membrane (GO:0016020)",
"subcellular_location: Membrane (SL-0162)",
"membrane_topology: Single-pass membrane protein (SL-9904)"
] | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB=ECO:0000255",
"UniProtKB=ECO:0000255"
] | Subcellular Location: Membrane
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 12837
Sequence Length: 116 |
A0A023PZA4 | YD154_YEAST | MKTSRSTTTDQVCCPWPTPVQTPTVLNSSSPPFHAHGWTVSMLSLVKLLTVTTSLRRLSPWVLLPVPPRLELLLPSPVNYNRSAWNNTAKIETNYSLLNYMYMYKVCVCMTINSYN | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | [] | [] | [] | Sequence Mass (Da): 13179
Sequence Length: 116 |
A0A023PZA9 | YD230_YEAST | MLHIYIGKRLKGPASTFCFPLVLFTRTCTISSQRRPEINSGYFVQTDSAFHFWRPPIAPAEMGHEGHYGALVFPFSPRFPLPIVRSGNFFVSLAYIAPIRQSSPVSESSSPNSWP | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | [] | [] | [] | Sequence Mass (Da): 12904
Sequence Length: 115 |
A0A023PZB3 | FMP49_YEAST | MYYFSRVAARTFCCCIFFCLATAYSRPDRNPRKIEKKDKKFFGASKNTNPANAMGNLFKAPTIEYVVEEVTRTHQPEQYDIPTDMSPLMTIAASESADKFTDKFFVDQSSIMKEKTSSKGNARTLL | null | null | null | mitochondrion [GO:0005739] | null | null | null | null | null | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14576278}. | null | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | [
6539,
24939
] | [
"go_cc: mitochondrion (GO:0005739)",
"subcellular_location: Mitochondrion (SL-0173)"
] | [
"UniProtKB-GO=ECO:0007005",
"UniProtKB=ECO:0000269"
] | Subcellular Location: Mitochondrion
Sequence Mass (Da): 14348
Sequence Length: 126 |
A0A023PZB8 | YE079_YEAST | MSLRMRFKPSIENFVNLFSFSCLSFLSHEPHVYLKKASLFGSLSFVSLVKTSFGLLEINLLVAATVIHLIAPTLFEAPTTHLLEWPATVYLIMLGLRIAVLLAKQLLLLLLR | null | null | null | membrane [GO:0016020] | null | null | null | null | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | [
6727,
24930,
25110
] | [
"go_cc: membrane (GO:0016020)",
"subcellular_location: Membrane (SL-0162)",
"membrane_topology: Multi-pass membrane protein (SL-9909)"
] | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB=ECO:0000255",
"UniProtKB=ECO:0000255"
] | Subcellular Location: Membrane
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 12599
Sequence Length: 112 |
A0A023PZC3 | YE133_YEAST | MYHLPINVMTSSYAQMMLCELSAQSFKPFHSGNLDKVSKMVHSLGLLHKQTSLRISPLLCFYFHHQINKSFSILNRWYYKDLSNRPLNGQFYFFLPTEIHRTGWPTGLRHQHT | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | [] | [] | [] | Sequence Mass (Da): 13357
Sequence Length: 113 |
A0A023PZC7 | YE152_YEAST | MGLRLRLVLLKGRNQRLEINRVVALLVDGGHFPLESRICEAIVDQEICWRDDERLPGIPVMWQGCLQKDVQHAIRSAAIQIQIVCPCPAPSPIFELKQLIIQKRTNLLSHPQGTFVRTVRQRMPVIGVVIVLPGLGPQYSRSRLNYCFSRQQPRARMALEEIDFLVFHYRLLARVVPCYSDAPPRFMC | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | [] | [] | [] | Sequence Mass (Da): 21595
Sequence Length: 188 |
A0A023PZD0 | YF036_YEAST | MTIVHFVGSLFFFFFFSYIFFYNDHGLYTWGCNFAMESPSPTSSPSLPTRFTPCPVAVLPSSSSPSWSFSTSCMPESTCSEISTSFFDTFNSSSDLFRSRICLLSDNRSFSIFSDSFTYFSFSISSCVSRSHSFVNLLSNFSMVSLTNSWIIAWLSSMYFSEISLDLSETLPNLSSPCSSVWTASFTHSINFEPDTLPSRLSPPLPFSVEPTTSRM | null | null | null | membrane [GO:0016020] | null | null | null | null | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. | null | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | [
6727,
24930,
25105
] | [
"go_cc: membrane (GO:0016020)",
"subcellular_location: Membrane (SL-0162)",
"membrane_topology: Single-pass membrane protein (SL-9904)"
] | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB=ECO:0000255",
"UniProtKB=ECO:0000255"
] | Subcellular Location: Membrane
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 24214
Sequence Length: 216 |
A0A023PZD5 | YH030_YEAST | MYSSASPIGAGASVVELAISFFTLNNKFSLLRSCWMEDLILRKLFQWSCKISLWRCSWESFEAEIAGLESQICVNESITSCLWPKIPSNCLSIFFSWPVCSELVVCANVEYLERSDSVCVSREMALPLMVTKDGCELMWCGCLSGIGLFPVSS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | [] | [] | [] | Sequence Mass (Da): 17065
Sequence Length: 153 |
A0A023PZE1 | YH063_YEAST | MFFFQGLYSSIMYVFFYIRIHTVFLRALYNSPFTALPVFKSLAVTLKAPSLLMLKIISTPLAFLIPNSINLVPKVYSFSLTTSGSSSDHSLSSSSSAFSSFGIGSKVFSSM | null | null | null | membrane [GO:0016020] | null | null | null | null | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | [
6727,
24930,
25110
] | [
"go_cc: membrane (GO:0016020)",
"subcellular_location: Membrane (SL-0162)",
"membrane_topology: Multi-pass membrane protein (SL-9909)"
] | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB=ECO:0000255",
"UniProtKB=ECO:0000255"
] | Subcellular Location: Membrane
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 12202
Sequence Length: 111 |
A0A023PZE2 | YA047_YEAST | MRSESEVSISTVFLGEYVGDDEKSLGILMGGSTSCMVGMNSAFVNDTIRLDLPTPSSPQITTRIVSLVIVLFNTLVFRSPLFLFSIFICLIYKFHSCFEGKPLYQMLKI | null | null | null | membrane [GO:0016020] | null | null | null | null | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | [
6727,
24930,
25110
] | [
"go_cc: membrane (GO:0016020)",
"subcellular_location: Membrane (SL-0162)",
"membrane_topology: Multi-pass membrane protein (SL-9909)"
] | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB=ECO:0000255",
"UniProtKB=ECO:0000255"
] | Subcellular Location: Membrane
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 12154
Sequence Length: 109 |
A0A023PZE4 | YH165_YEAST | MSNFLFPCNSTFFSALVSNSSRPGGGGGGGNVKSTISSAFISKLLGGGGGGGRNVSSFTDDGTIGLSSSSISYPGGGGGGGGSAKSLSSSKPGGGGGSPLIFL | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | [] | [] | [] | Sequence Mass (Da): 9601
Sequence Length: 103 |
A0A023PZE6 | YD048_YEAST | MSSLLQLLAVWSQSSSISMNSEVAQTNQKYKDHSFLVSQSFYSPFVNSCYWKLVNRRADLLKILFLRRKGDMHSHLFSYTFIFYFLLFKILSLHPFREPAKINI | null | null | null | membrane [GO:0016020] | null | null | null | null | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. | null | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | [
6727,
24930,
25105
] | [
"go_cc: membrane (GO:0016020)",
"subcellular_location: Membrane (SL-0162)",
"membrane_topology: Single-pass membrane protein (SL-9904)"
] | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB=ECO:0000255",
"UniProtKB=ECO:0000255"
] | Subcellular Location: Membrane
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 12316
Sequence Length: 104 |
A0A023PZE8 | YD57W_YEAST | MSETCSSSLALLHKILHIHSHTPSVYYNICISVRILTSERLQCFFFSFFPDPNITGSGLKVPGFLFFHTFFFSKSCCQALIDSFSSDYYQFKMLEKNRKAEKINKRTIFICSFTFEYKIKSCFSCFHLSTHTN | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | [] | [] | [] | Sequence Mass (Da): 15507
Sequence Length: 133 |
A0A023PZE9 | YI029_YEAST | MSHLTSAPGFEMSIFFEATHSNRQDSCMYLIEPLHLQGWKRGLSSVASPRQIRQVAPDGASSLKVAVSVSSFATLCSSSLNLETLTSESTSMTFTLLVSLIQLVVLLAKKTVFEISNKELFLT | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | [] | [] | [] | Sequence Mass (Da): 13443
Sequence Length: 123 |
A0A023PZF2 | YE009_YEAST | MNTLLKKYRKQRYAWLRFLLFSKIEGSLPVALRILLSLQPFCCNIYRKYYQENKKVKSTSGNTALKIIEKLESLVSNLRLKYSQMFSLLFLHSYNCLQSLATETFRIIKKREKNLLSLLIPGSCIEIARHFVLKE | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | [] | [] | [] | Sequence Mass (Da): 15939
Sequence Length: 135 |
A0A023PZF3 | YI070_YEAST | MNNKVTLLPPRVFFCLSWSVMVNIDRRKSDRSVNLDDQHSNKPPSESLISLLSLTSSMSISSLLSLLIIVAVLFPPLYISGLPWIMSFKSVFSFFSLSITSFIMVPFLLISLTILCKIELSSKCITSPSISKFNCPDIINFVNSSLISSKSIPSVDDK | null | null | null | membrane [GO:0016020] | null | null | null | null | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | [
6727,
24930,
25110
] | [
"go_cc: membrane (GO:0016020)",
"subcellular_location: Membrane (SL-0162)",
"membrane_topology: Multi-pass membrane protein (SL-9909)"
] | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB=ECO:0000255",
"UniProtKB=ECO:0000255"
] | Subcellular Location: Membrane
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 17541
Sequence Length: 158 |
A0A023PZF5 | YE046_YEAST | MQNIFYRSAYVHTVCPARLEYYLLLPLLLYYYYYYHHHEPDDPNCEAHFSYFTNPSWDTEGLIYTKLFLKSTRPMGLIISLSVSNNLSPRSRSGPMAASFAKDVISLPE | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | [] | [] | [] | Sequence Mass (Da): 12723
Sequence Length: 109 |
A0A023PZF9 | YI023_YEAST | MCYYLYYRGVSLVLIVTFLSSFIFIVWLPVALVSWFEFGLSSLSSVDDSSLAVLSLPAVFSSAASPDSCLVSLIEVKGEAFICVLELTFVLELTLGEDVLEGGCLLI | null | null | null | membrane [GO:0016020] | null | null | null | null | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. | null | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | [
6727,
24930,
25105
] | [
"go_cc: membrane (GO:0016020)",
"subcellular_location: Membrane (SL-0162)",
"membrane_topology: Single-pass membrane protein (SL-9904)"
] | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB=ECO:0000255",
"UniProtKB=ECO:0000255"
] | Subcellular Location: Membrane
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 11613
Sequence Length: 107 |
A0A023PZG0 | YE084_YEAST | MYLYVSFLINSLLLSYQSCSSFQINRFESYRNHLEFVLITWPPTMHLYISYFFPLCAISLGKICNQGKHPLVPFQFLCYFKNHPFIIYLYFFRPGLYQFIFRTFHISSNSAAHIFFHHDTGNRMGPWILAKQSLYSPVQNPQDICFPQQLQLQLINPMRKCRVYVIQDAF | null | null | null | membrane [GO:0016020] | null | null | null | null | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. | null | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | [
6727,
24930,
25105
] | [
"go_cc: membrane (GO:0016020)",
"subcellular_location: Membrane (SL-0162)",
"membrane_topology: Single-pass membrane protein (SL-9904)"
] | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB=ECO:0000255",
"UniProtKB=ECO:0000255"
] | Subcellular Location: Membrane
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 20288
Sequence Length: 170 |
A0A023PZG4 | YL236_YEAST | MHTICLRSPIDESSPLPYKSIRQPLENAHSCQALCSLMAVLCASAAHRLSETFPMRLVVAREYANWGAFQHAFTRRAGASVAATSAWFDAVAAGTENAHMQSAESCN | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | [] | [] | [] | Sequence Mass (Da): 11596
Sequence Length: 107 |
A0A023PZG5 | YE137_YEAST | MISIPFRSTMSRTLVFIILPTVLSCNPSSRLMNFSNSFNLCSYSTCNCDPSFCFEMINLARTSIACDNLTISFSVLFDDSHIPCYNNPRYSFNKLTMTILY | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | [] | [] | [] | Sequence Mass (Da): 11524
Sequence Length: 101 |
A0A023PZG9 | YM047_YEAST | MVFVTIIIIINISYNIYNIYTINENRFTFNAFLQSKKASFTFICIYVCISGGNMPLWAYILFRTFLHPSSSSNSVLCFRRHNQDYHNRIFFAFCCHHIWSLLPHHLSIFPIRRQFYLNSRQ | null | null | null | membrane [GO:0016020] | null | null | null | null | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | [
6727,
24930,
25110
] | [
"go_cc: membrane (GO:0016020)",
"subcellular_location: Membrane (SL-0162)",
"membrane_topology: Multi-pass membrane protein (SL-9909)"
] | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB=ECO:0000255",
"UniProtKB=ECO:0000255"
] | Subcellular Location: Membrane
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 14525
Sequence Length: 121 |
A0A023PZH1 | YE165_YEAST | MIVIFCVIVKCEFFCIFTFIFGCFIIEADLWPAVFVACCTIIKMGRCNMCIFITAIIFKLKCIFKGRHGSMPIAMKSSRHNYQLTFLFKVNCVFISLPGGNKGFLLRLLSLAQPPVNF | null | null | null | membrane [GO:0016020] | null | null | null | null | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | [
6727,
24930,
25110
] | [
"go_cc: membrane (GO:0016020)",
"subcellular_location: Membrane (SL-0162)",
"membrane_topology: Multi-pass membrane protein (SL-9909)"
] | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB=ECO:0000255",
"UniProtKB=ECO:0000255"
] | Subcellular Location: Membrane
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13421
Sequence Length: 118 |
A0A023PZH4 | YF052_YEAST | MDGLVTQAKIQLRLFQLRMVQVQVLLLLLHCPKKELPKVSLLVSLALNEKNVMKYKCVFPSLNIIILMSDALMFFLRSSICKYRHTHIYIFMCIILANKHF | null | null | null | membrane [GO:0016020] | null | null | null | null | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. | null | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | [
6727,
24930,
25105
] | [
"go_cc: membrane (GO:0016020)",
"subcellular_location: Membrane (SL-0162)",
"membrane_topology: Single-pass membrane protein (SL-9904)"
] | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB=ECO:0000255",
"UniProtKB=ECO:0000255"
] | Subcellular Location: Membrane
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 11822
Sequence Length: 101 |
A0A023PZH5 | YM290_YEAST | MAFKVGCDNFSSSNFSTQVVCSPSGAALFCFEVLFSSTTGSSVDSESLERLFDGVAILLLLILLSLSNYYSIQLSNSYVLKYRVYTIKSHLIAKANIEKKKKKKKKKQIKNFQFG | null | null | null | membrane [GO:0016020] | null | null | null | null | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | [
6727,
24930,
25110
] | [
"go_cc: membrane (GO:0016020)",
"subcellular_location: Membrane (SL-0162)",
"membrane_topology: Multi-pass membrane protein (SL-9909)"
] | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB=ECO:0000255",
"UniProtKB=ECO:0000255"
] | Subcellular Location: Membrane
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 12852
Sequence Length: 115 |
A0A023PZH9 | YH034_YEAST | MWVRSNYSCFSSEPVSCSISSSSFSGLITATSTVNSLSPKTLPLNSSALASISTFSPLKVTNAIPLLAESDVKILPVCWSLIFLIGKEMESASVPKNSATSSLVALNGTLLIYKVSFDLSIWSNGIFSLFCPLKPPLAPPLPLKFPLPLKPPL | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | [] | [] | [] | Sequence Mass (Da): 16290
Sequence Length: 153 |
A0A023PZI1 | OPI11_YEAST | MIFIHIIKIKSSFNHFSQSSDGRSNGGGSSSGDSVSTTSDGLLTTGTSPNTSSTSLDGLLTTERTIVSSVLLDFQLLDLSSQRGTITDTVLTSDTNLLSSFSPVFKKEKISKYVSKS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | [] | [] | [] | Sequence Mass (Da): 12402
Sequence Length: 117 |
A0A023PZI4 | YH069_YEAST | MDSCSSTPFVTGVLLPSAVFSFLFCTLVSSSFGLDEFNLTTCGIRGTLKMQFLKFLENTLIFLGSGNLTAHIGILVMKNDLSNSRIWRFTGGLYGNTPDILHELINLLNFWNTGSAIFMQ | null | null | null | membrane [GO:0016020] | null | null | null | null | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | [
6727,
24930,
25110
] | [
"go_cc: membrane (GO:0016020)",
"subcellular_location: Membrane (SL-0162)",
"membrane_topology: Multi-pass membrane protein (SL-9909)"
] | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB=ECO:0000255",
"UniProtKB=ECO:0000255"
] | Subcellular Location: Membrane
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13252
Sequence Length: 120 |
A0A023PZI9 | YH182_YEAST | MWPSFFRTTWHQRWTVTGTFLTTGDTRTNEKNTLLLQFFVTSIRIWEVRVTTIDDNITLFQKWDDLVDQSVNWSTSFNQKHDLSRSLQFGDEIFNGSSTDDRFALSFIGQEMVDLGLSSVVSTNSETVVSSVQDQILTHDGQTNQTEISRHFIVVFV | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | [] | [] | [] | Sequence Mass (Da): 18121
Sequence Length: 157 |
A0A023PZJ3 | YI030_YEAST | MMWHLVVQLGVFQEPARQARDQMHNFSLIMEMKITSLKILFGMRAEIILYSWKMKTLESTRTHSFIFFILFLFIFIFLTFSHNNSNSNKITSNIHTHINRHIFYFVLSYSEW | null | null | null | membrane [GO:0016020] | null | null | null | null | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. | null | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | [
6727,
24930,
25105
] | [
"go_cc: membrane (GO:0016020)",
"subcellular_location: Membrane (SL-0162)",
"membrane_topology: Single-pass membrane protein (SL-9904)"
] | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB=ECO:0000255",
"UniProtKB=ECO:0000255"
] | Subcellular Location: Membrane
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 13554
Sequence Length: 112 |
A0A023PZJ9 | YI115_YEAST | MIEDEFIINGTNNVHIAKYHYFAMFKFLKKSPICFFVFMANPTSTTLNPFMSFVIEEDASNDEAFLPFSSNCNLLTCSRNNLISFSKPSRARDSLASFATNGLSSNLLFFTVNNFKMFSNSSV | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | [] | [] | [] | Sequence Mass (Da): 13917
Sequence Length: 123 |
A0A023PZK4 | YI30A_YEAST | MSSICHTLSGLISSNLIGLCVKTAPKILRIFVRLCTYTFYNLLKSTGLALGLIISSYNKVVKKSLKILPVTSGKKYLAAKANLFFSPSGLAEANFAVSSFNILAVNSGVTLSPVSLKTTPCLTHWYN | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | [] | [] | [] | Sequence Mass (Da): 13675
Sequence Length: 127 |
A0A023PZK9 | YL458_YEAST | MSPQTFCILLIFSLSLEKTSLIVWNIFVNLRLGVFLLLVRIFSSVFLSVTFLGLFRTLLPVGRICFLLLLKADRFLTSSRDPYSRFLPSSRIPKKSFHSPCTDFSILPMSIIVPFSSEYLLVHVQQ | null | null | null | membrane [GO:0016020] | null | null | null | null | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | [
6727,
24930,
25110
] | [
"go_cc: membrane (GO:0016020)",
"subcellular_location: Membrane (SL-0162)",
"membrane_topology: Multi-pass membrane protein (SL-9909)"
] | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB=ECO:0000255",
"UniProtKB=ECO:0000255"
] | Subcellular Location: Membrane
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 14447
Sequence Length: 126 |
A0A023PZL2 | YM119_YEAST | MRLLVQKVILIYLARYAKSMKEIQYYGPADVLPFARIAEFLWVYVGSALAYVVGVKFMGTVRFILFQIVNNSLRTFAWYLKEVFRLGALALITIARAFCVAHINIIIINQVFFLWEMFELKLYL | null | null | null | membrane [GO:0016020] | null | null | null | null | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | [
6727,
24930,
25110
] | [
"go_cc: membrane (GO:0016020)",
"subcellular_location: Membrane (SL-0162)",
"membrane_topology: Multi-pass membrane protein (SL-9909)"
] | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB=ECO:0000255",
"UniProtKB=ECO:0000255"
] | Subcellular Location: Membrane
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 14510
Sequence Length: 124 |
A0A023PZL7 | YM294_YEAST | MKYEISKIRAENRNYHKKEKNKVSKGYQALISSSFYQTIPSSSSFAFPQSVRVVVADTLLVHHTFDWKHHPLAVAYRSHRKSQQHQTQGNQVLRGTRKLESPTVGPRPGLRRQHTRNFL | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | [] | [] | [] | Sequence Mass (Da): 13839
Sequence Length: 119 |
A0A023PZM3 | YP050_YEAST | MKPIPSYKFRAAEFSTSVSNMISSQCSLCILSMAISTSFFAMPCPRYVDSTASIPIYPLSLTFLCGSILHTMQPMGMLGVPLLLSTAMYVNSGHWFKKYLYTYIEYGSDRSASISFLILANCSSLRMSNGLYTISMS | null | null | null | membrane [GO:0016020] | null | null | null | null | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | [
6727,
24930,
25110
] | [
"go_cc: membrane (GO:0016020)",
"subcellular_location: Membrane (SL-0162)",
"membrane_topology: Multi-pass membrane protein (SL-9909)"
] | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB=ECO:0000255",
"UniProtKB=ECO:0000255"
] | Subcellular Location: Membrane
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 15156
Sequence Length: 137 |
A0A023UA23 | PHAT_AMAFU | PAWLVDCPCVGDDVNRLLARGEK | null | null | null | null | null | null | null | MSDIN fungal toxin family | PTM: Processed by the macrocyclase-peptidase enzyme POPB to yield a toxic cyclic heptapeptide (By similarity). POPB first removes 10 residues from the N-terminus (By similarity). Conformational trapping of the remaining peptide forces the enzyme to release this intermediate rather than proceed to macrocyclization (By s... | null | null | null | null | null | null | FUNCTION: Major toxin that belongs to the bicyclic heptapeptides called phallotoxins (PubMed:24613547). Although structurally related to amatoxins, phallotoxins have a different mode of action, which is the stabilization of F-actin (PubMed:24613547). Phallotoxins are poisonous when administered parenterally, but not or... | Amanita fuliginea (East Asian brown death cap) | [] | [] | [] | Function: Major toxin that belongs to the bicyclic heptapeptides called phallotoxins. Although structurally related to amatoxins, phallotoxins have a different mode of action, which is the stabilization of F-actin. Phallotoxins are poisonous when administered parenterally, but not orally because of poor absorption.
PTM... |
A0A023UBA8 | PHAT_AMARI | PAWLVDCPCVGDDISRLLTRGEK | null | null | null | null | null | null | null | MSDIN fungal toxin family | PTM: Processed by the macrocyclase-peptidase enzyme POPB to yield a toxic cyclic heptapeptide (By similarity). POPB first removes 10 residues from the N-terminus (By similarity). Conformational trapping of the remaining peptide forces the enzyme to release this intermediate rather than proceed to macrocyclization (By s... | null | null | null | null | null | null | FUNCTION: Major toxin that belongs to the bicyclic heptapeptides called phallotoxins (PubMed:24613547). Although structurally related to amatoxins, phallotoxins have a different mode of action, which is the stabilization of F-actin (PubMed:24613547). Phallotoxins are poisonous when administered parenterally, but not or... | Amanita rimosa | [] | [] | [] | Function: Major toxin that belongs to the bicyclic heptapeptides called phallotoxins. Although structurally related to amatoxins, phallotoxins have a different mode of action, which is the stabilization of F-actin. Phallotoxins are poisonous when administered parenterally, but not orally because of poor absorption.
PTM... |
A0A023UBX6 | PHAT1_AMAEX | PAWLVDCPCVGDDVNRLLTRGER | null | null | null | null | null | null | null | MSDIN fungal toxin family | PTM: Processed by the macrocyclase-peptidase enzyme POPB to yield a toxic cyclic heptapeptide (By similarity). POPB first removes 10 residues from the N-terminus (By similarity). Conformational trapping of the remaining peptide forces the enzyme to release this intermediate rather than proceed to macrocyclization (By s... | null | null | null | null | null | null | FUNCTION: Toxin that belongs to the bicyclic heptapeptides called phallotoxins (PubMed:24613547). Although structurally related to amatoxins, phallotoxins have a different mode of action, which is the stabilization of F-actin (PubMed:24613547). Phallotoxins are poisonous when administered parenterally, but not orally b... | Amanita exitialis (Guangzhou destroying angel) | [] | [] | [] | Function: Toxin that belongs to the bicyclic heptapeptides called phallotoxins. Although structurally related to amatoxins, phallotoxins have a different mode of action, which is the stabilization of F-actin. Phallotoxins are poisonous when administered parenterally, but not orally because of poor absorption.
PTM: Proc... |
A0A023UBY3 | PHAT_AMAPH | PAWLVDCPCVGDDINRLLTRGEK | null | null | null | null | null | null | null | MSDIN fungal toxin family | PTM: Processed by the macrocyclase-peptidase enzyme POPB to yield a toxic cyclic heptapeptide (By similarity). POPB first removes 10 residues from the N-terminus (By similarity). Conformational trapping of the remaining peptide forces the enzyme to release this intermediate rather than proceed to macrocyclization (By s... | null | null | null | null | null | null | FUNCTION: Major toxin that belongs to the bicyclic heptapeptides called phallotoxins (PubMed:24613547). Although structurally related to amatoxins, phallotoxins have a different mode of action, which is the stabilization of F-actin (PubMed:24613547). Phallotoxins are poisonous when administered parenterally, but not or... | Amanita phalloides (Death cap) | [] | [] | [] | Function: Major toxin that belongs to the bicyclic heptapeptides called phallotoxins. Although structurally related to amatoxins, phallotoxins have a different mode of action, which is the stabilization of F-actin. Phallotoxins are poisonous when administered parenterally, but not orally because of poor absorption.
PTM... |
A0A023UCA6 | AAMA2_AMAFL | IWGIGCNPCVGDEVTALITRGEA | null | null | null | null | null | null | null | MSDIN fungal toxin family | PTM: Processed by the macrocyclase-peptidase enzyme POPB to yield a toxic cyclic decapeptide (PubMed:24613547). POPB first removes 10 residues from the N-terminus (By similarity). Conformational trapping of the remaining peptide forces the enzyme to release this intermediate rather than proceed to macrocyclization (By ... | null | null | null | null | null | null | FUNCTION: Major toxin belonging to the bicyclic octapeptides amatoxins that acts by binding non-competitively to RNA polymerase II and greatly slowing the elongation of transcripts from target promoters (PubMed:24613547). {ECO:0000305|PubMed:24613547}. | Amanita fuligineoides | [] | [] | [] | Function: Major toxin belonging to the bicyclic octapeptides amatoxins that acts by binding non-competitively to RNA polymerase II and greatly slowing the elongation of transcripts from target promoters.
PTM: Processed by the macrocyclase-peptidase enzyme POPB to yield a toxic cyclic decapeptide. POPB first removes 10 ... |
A0A023UCC1 | PHAT_AMAFL | PAWLVDCPCVGDDVNFILTRGQK | null | null | null | null | null | null | null | MSDIN fungal toxin family | PTM: Processed by the macrocyclase-peptidase enzyme POPB to yield a toxic cyclic heptapeptide (By similarity). POPB first removes 10 residues from the N-terminus (By similarity). Conformational trapping of the remaining peptide forces the enzyme to release this intermediate rather than proceed to macrocyclization (By s... | null | null | null | null | null | null | FUNCTION: Major toxin that belongs to the bicyclic heptapeptides called phallotoxins (PubMed:24613547). Although structurally related to amatoxins, phallotoxins have a different mode of action, which is the stabilization of F-actin (PubMed:24613547). Phallotoxins are poisonous when administered parenterally, but not or... | Amanita fuligineoides | [] | [] | [] | Function: Major toxin that belongs to the bicyclic heptapeptides called phallotoxins. Although structurally related to amatoxins, phallotoxins have a different mode of action, which is the stabilization of F-actin. Phallotoxins are poisonous when administered parenterally, but not orally because of poor absorption.
PTM... |
A0A023VXA2 | GUN_MAREN | MPRMLAASAAIIATTLAPLSAQAAGCEMTLHGINLSGAEFGQPGDPYGQGYIYPSESTIKAFADDGFNAVRLPFLWERLQPTLNGTLDATELSRIKDTVETLRDNGMVVILDVHNYARYHGEMIGTPNVPVAAFADFWKRLSAVFANDDDVIFGLMNEPHDISAPAWLAAANAAIDAIRTIGAGNLVLVPGTAWTGAHSWSQTFYGPSNASVMAQVVDSSNNFAYEVHQYTDDDFSGKNADCSKIDDAVSALNDFTSWLNANDVQGFLGEFGTTEQIQCLRGLKQMVDVVQQNPRAWLGWAYWAGGDWWPKDSPMIIHSN... | 3.2.1.4 | null | glucan catabolic process [GO:0009251] | null | cellulase activity [GO:0008810] | PF00150; | 3.20.20.80; | Glycosyl hydrolase 5 (cellulase A) family | null | null | CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4; Evidence={ECO:0000269|PubMed:33523417}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.5 with CMC as substrate. {ECO:0000269|PubMed:33523417}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius with CMC as substrate. Retains 50% of its activity at temperatures ranging from 30 to 60 degrees Celsius. {ECO:0000269|PubMed:33523417}; | FUNCTION: Shows highest activity on carboxymethyl cellulose (CMC). Shows weak activity on xylan, and no activity against avicel, laminarin and chitin. {ECO:0000269|PubMed:33523417}. | Martelella endophytica | [
241,
1602,
8322,
10224,
13891,
14008,
20650
] | [
"ec: EC 3.2.1.4",
"go_bp: glucan catabolic process (GO:0009251)",
"go_mf: cellulase activity (GO:0008810)",
"interpro: Glycoside hydrolase, family 5 (IPR001547)",
"interpro: Glycoside hydrolase superfamily (IPR017853)",
"interpro: Glycoside hydrolase, family 5, conserved site (IPR018087)",
"pfam: Cellul... | [
"UniProtKB=ECO:0000269",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000269",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match:Pfam"
] | Function: Shows highest activity on carboxymethyl cellulose (CMC). Shows weak activity on xylan, and no activity against avicel, laminarin and chitin.
Catalytic Activity: Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
EC: 3.2.1.4
Sequence Mass (Da): 37840
Sequence ... |
A0A023VZF1 | TX41F_ETHRU | LLVCLFVCWNAVGAQDARSAFSSEETAQDQHVMEERIFINPCRKPGKNACMENCRSSPNCKTMSFVQSSIRP | null | null | null | extracellular region [GO:0005576] | null | null | null | Scoloptoxin-04 family | PTM: Contains 2 disulfide bonds. {ECO:0000305}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24602922}. Note=The mature toxins are clearly liberated from the multidomain precursors in the venom gland prior to venom expulsion and not by venom proteases upon secretion. {ECO:0000269|PubMed:24602922}. | null | null | null | null | null | null | Ethmostigmus rubripes (Giant centipede) | [
6485,
24983
] | [
"go_cc: extracellular region (GO:0005576)",
"subcellular_location: Secreted (SL-0243)"
] | [
"UniProtKB-GO=ECO:0000269",
"UniProtKB=ECO:0000269"
] | Subcellular Location: Secreted
PTM: Contains 2 disulfide bonds.
Sequence Mass (Da): 8069
Sequence Length: 72 |
A0A023VZM6 | TX41C_ETHRU | MTRHLIFAAVLLVCLFVCWNAVGAQDARSAFSSEETAQDQHVMEERIFINPAGNREKNACLENCRSSPNCKNYEFCSK | null | null | null | extracellular region [GO:0005576] | null | null | null | Scoloptoxin-04 family | PTM: Contains 2 disulfide bonds. {ECO:0000305}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24602922}. Note=The mature toxins are clearly liberated from the multidomain precursors in the venom gland prior to venom expulsion and not by venom proteases upon secretion. {ECO:0000269|PubMed:24602922}. | null | null | null | null | null | null | Ethmostigmus rubripes (Giant centipede) | [
6485,
24983
] | [
"go_cc: extracellular region (GO:0005576)",
"subcellular_location: Secreted (SL-0243)"
] | [
"UniProtKB-GO=ECO:0000269",
"UniProtKB=ECO:0000269"
] | Subcellular Location: Secreted
PTM: Contains 2 disulfide bonds.
Sequence Mass (Da): 8815
Sequence Length: 78 |
A0A023VZR2 | TX81A_CORWE | MIFRVNLLFSCFCFVLFVFDFSNASKYDQGSLNIAKRLWRDWEREANAKDMERKEVKADAEGNAQMERERRLWRDWEASQAKPLERRAWVEAVEASDQNEREKRLWRDWEGNQANDLERRAMEGLMEANEENQRAKRLWRNWEANHEYEIERKRDLPELKRRKRLWRNEDQEVACTTKCSCSDNEIFSKVDHELTTSETKRVPCCC | null | null | null | extracellular region [GO:0005576] | null | null | null | Scoloptoxin-08 family | PTM: Contains 3 disulfide bonds. {ECO:0000305}. | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:24602922}. | null | null | null | null | null | null | Cormocephalus westwoodi (Westwood's green centipede) | [
6485,
24983
] | [
"go_cc: extracellular region (GO:0005576)",
"subcellular_location: Secreted (SL-0243)"
] | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB=ECO:0000305"
] | Subcellular Location: Secreted
PTM: Contains 3 disulfide bonds.
Sequence Mass (Da): 24947
Sequence Length: 206 |
A0A023W082 | TX41B_ETHRU | MTRHLIFAAVLLVCLFVCWNAVGAQDARSAFSSEETAQDQHVMEERIFINPAGNREKNACMENCRSSPNCKNYEFCSK | null | null | null | extracellular region [GO:0005576] | null | null | null | Scoloptoxin-04 family | PTM: Contains 2 disulfide bonds. {ECO:0000305}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24602922}. Note=The mature toxins are clearly liberated from the multidomain precursors in the venom gland prior to venom expulsion and not by venom proteases upon secretion. {ECO:0000269|PubMed:24602922}. | null | null | null | null | null | null | Ethmostigmus rubripes (Giant centipede) | [
6485,
24983
] | [
"go_cc: extracellular region (GO:0005576)",
"subcellular_location: Secreted (SL-0243)"
] | [
"UniProtKB-GO=ECO:0000269",
"UniProtKB=ECO:0000269"
] | Subcellular Location: Secreted
PTM: Contains 2 disulfide bonds.
Sequence Mass (Da): 8833
Sequence Length: 78 |
A0A023W090 | TX41E_ETHRU | MTRHLIFAAMLLVCLFVCWNAVGARDARSAFSLEETAQDEHVMEERVFINPAGNREKNACLENCKSLPNCKNYEFCSK | null | null | null | extracellular region [GO:0005576] | null | null | null | Scoloptoxin-04 family | PTM: Contains 2 disulfide bonds. {ECO:0000305}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24602922}. Note=The mature toxins are clearly liberated from the multidomain precursors in the venom gland prior to venom expulsion and not by venom proteases upon secretion. {ECO:0000250|UniProtKB:A0A023VZM6}. | null | null | null | null | null | null | Ethmostigmus rubripes (Giant centipede) | [
6485,
24983
] | [
"go_cc: extracellular region (GO:0005576)",
"subcellular_location: Secreted (SL-0243)"
] | [
"UniProtKB-GO=ECO:0000269",
"UniProtKB=ECO:0000269"
] | Subcellular Location: Secreted
PTM: Contains 2 disulfide bonds.
Sequence Mass (Da): 8886
Sequence Length: 78 |
A0A023W0B6 | TX85A_ETHRU | MKTNCEFPLLCLLIVLVANVEGEVEDTGLKMVKRLWRNWEDPEQRQLLDQGTELEKQREKRLWRNWEDLELRQLLNEFAENQREKRLWRNWERRQVANEDDGEKAKELWRNWEDLKRRQVADLNDEQETQRDKRLWRNWEDNHATLRKRSADSLSRQKRLGKERGKE | null | null | null | extracellular region [GO:0005576] | null | null | null | Scoloptoxin-08 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24602922}. Note=The mature toxins are clearly liberated from the multidomain precursors in the venom gland prior to venom expulsion and not by venom proteases upon secretion. {ECO:0000269|PubMed:24602922}. | null | null | null | null | null | null | Ethmostigmus rubripes (Giant centipede) | [
6485,
24983
] | [
"go_cc: extracellular region (GO:0005576)",
"subcellular_location: Secreted (SL-0243)"
] | [
"UniProtKB-GO=ECO:0000269",
"UniProtKB=ECO:0000269"
] | Subcellular Location: Secreted
Sequence Mass (Da): 20636
Sequence Length: 167 |
A0A023W0C3 | TX85D_ETHRU | MKTNCEFPLLCLLIVLVANVEGEVEDNELKMVKRLWRNWEDPEQRQLLDQEAEQEKQREKRLWRNWEDLELRQLLNEFAENQREKRLWRNWERRQVANEDDGEKPKELWRNWEDLKRRQVGRFE | null | null | null | extracellular region [GO:0005576] | null | null | null | Scoloptoxin-08 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:24602922}. | null | null | null | null | null | null | Ethmostigmus rubripes (Giant centipede) | [
6485,
24983
] | [
"go_cc: extracellular region (GO:0005576)",
"subcellular_location: Secreted (SL-0243)"
] | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB=ECO:0000305"
] | Subcellular Location: Secreted
Sequence Mass (Da): 15590
Sequence Length: 124 |
A0A023W0U0 | TX41D_ETHRU | MTRHLIFAAMLLVCLFVCWNAVGARDARSAFSLEETAQDEHVMEERIFINPAGNREKNACLENCRSSPNCENYEFCSK | null | null | null | extracellular region [GO:0005576] | null | null | null | Scoloptoxin-04 family | PTM: Contains 2 disulfide bonds. {ECO:0000305}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24602922}. Note=The mature toxins are clearly liberated from the multidomain precursors in the venom gland prior to venom expulsion and not by venom proteases upon secretion. {ECO:0000269|PubMed:24602922}. | null | null | null | null | null | null | Ethmostigmus rubripes (Giant centipede) | [
6485,
24983
] | [
"go_cc: extracellular region (GO:0005576)",
"subcellular_location: Secreted (SL-0243)"
] | [
"UniProtKB-GO=ECO:0000269",
"UniProtKB=ECO:0000269"
] | Subcellular Location: Secreted
PTM: Contains 2 disulfide bonds.
Sequence Mass (Da): 8903
Sequence Length: 78 |
A0A023W0V6 | TX93A_SCOMO | MNANSIFLCFFIMLIGCTLTHSCPSGCYCDQVDGNKCRPEEGTNPHLCLGKYCKTPDSSSVITGNQDEKTQAKG | null | null | null | extracellular region [GO:0005576] | null | null | null | Scoloptoxin-09 family | PTM: Contains 3 disulfide bonds. {ECO:0000305}. | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:24602922}. | null | null | null | null | null | null | Scolopendra morsitans (Tanzanian blue ringleg centipede) | [
6485,
24983
] | [
"go_cc: extracellular region (GO:0005576)",
"subcellular_location: Secreted (SL-0243)"
] | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB=ECO:0000305"
] | Subcellular Location: Secreted
PTM: Contains 3 disulfide bonds.
Sequence Mass (Da): 8023
Sequence Length: 74 |
A0A023W0V9 | TX85C_ETHRU | MKTNCEFPLLCLLIVLVANVEGEVEDTGLKMVKRLWRNWEDPEQRQLLDQEAEQEKQLEKRLWRNWEDLELRQLLNEFAENQREKRLWRNWERRQVAKEDDGEKPKELWRNWEDLKRRQVVDLNDEQKTQRDKRLWRNWEDNHATLRKRSADSLSRQKRLGRERGKE | null | null | null | extracellular region [GO:0005576] | null | null | null | Scoloptoxin-08 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:24602922}. | null | null | null | null | null | null | Ethmostigmus rubripes (Giant centipede) | [
6485,
24983
] | [
"go_cc: extracellular region (GO:0005576)",
"subcellular_location: Secreted (SL-0243)"
] | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB=ECO:0000305"
] | Subcellular Location: Secreted
Sequence Mass (Da): 20745
Sequence Length: 167 |
A0A023W0W9 | TX85A_SCOMO | MSYTCMKGLLCFCLVLMFFELTDGSDESQRQDMKRLWRHWEEEQQKDREKRLWRNWEDQEQKERERRLWRNWEDENQREKRLWRNWEDEEQVPRQKRLWRNWEESEQKEKRSFPEVKYEIEQNQELPQVKRKKRFWRDEEESERS | null | null | null | extracellular region [GO:0005576] | null | null | null | Scoloptoxin-08 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:24602922}. | null | null | null | null | null | null | Scolopendra morsitans (Tanzanian blue ringleg centipede) | [
6485,
24983
] | [
"go_cc: extracellular region (GO:0005576)",
"subcellular_location: Secreted (SL-0243)"
] | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB=ECO:0000305"
] | Subcellular Location: Secreted
Sequence Mass (Da): 18904
Sequence Length: 145 |
A0A023W123 | TX41A_ETHRU | MTRHLIFAAVLLVCLFVCWNAIGAQDARSAFSSEETAQDQHVMEERIFINPAGNREKNACLENCRSSPNCKNYEFCSK | null | null | null | extracellular region [GO:0005576] | null | null | null | Scoloptoxin-04 family | PTM: Contains 2 disulfide bonds. {ECO:0000305}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24602922}. Note=The mature toxins are clearly liberated from the multidomain precursors in the venom gland prior to venom expulsion and not by venom proteases upon secretion. {ECO:0000269|PubMed:24602922}. | null | null | null | null | null | null | Ethmostigmus rubripes (Giant centipede) | [
6485,
24983
] | [
"go_cc: extracellular region (GO:0005576)",
"subcellular_location: Secreted (SL-0243)"
] | [
"UniProtKB-GO=ECO:0000269",
"UniProtKB=ECO:0000269"
] | Subcellular Location: Secreted
PTM: Contains 2 disulfide bonds.
Sequence Mass (Da): 8829
Sequence Length: 78 |
A0A023W140 | TXX1A_ETHRU | MASQVVLSFALVVVLAVFVGQVDSCPSDCKCDYRSSQCRPANDDVHPNVCIDHYCVVMNLAKREQRPELSPGAWDDSSEEKDNEASLA | null | null | null | extracellular region [GO:0005576] | null | null | null | Scoloptoxin-XY family | PTM: Contains 3 disulfide bonds. {ECO:0000305}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24602922}. Note=The mature toxins are clearly liberated from the multidomain precursors in the venom gland prior to venom expulsion and not by venom proteases upon secretion. {ECO:0000269|PubMed:24602922}. | null | null | null | null | null | null | Ethmostigmus rubripes (Giant centipede) | [
6485,
24983
] | [
"go_cc: extracellular region (GO:0005576)",
"subcellular_location: Secreted (SL-0243)"
] | [
"UniProtKB-GO=ECO:0000269",
"UniProtKB=ECO:0000269"
] | Subcellular Location: Secreted
PTM: Contains 3 disulfide bonds.
Sequence Mass (Da): 9661
Sequence Length: 88 |
A0A023W145 | TXX1B_ETHRU | MASQVVLSFALVVVLAVFVGQVDSCPSDCKCDYRSSQCRPANDDVHPNVCIDHYCVVMNLAKREQRPELSPGALDDSSEEKDNEASLA | null | null | null | extracellular region [GO:0005576] | null | null | null | Scoloptoxin-XY family | PTM: Contains 3 disulfide bonds. {ECO:0000305}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24602922}. Note=The mature toxins are clearly liberated from the multidomain precursors in the venom gland prior to venom expulsion and not by venom proteases upon secretion. {ECO:0000269|PubMed:24602922}. | null | null | null | null | null | null | Ethmostigmus rubripes (Giant centipede) | [
6485,
24983
] | [
"go_cc: extracellular region (GO:0005576)",
"subcellular_location: Secreted (SL-0243)"
] | [
"UniProtKB-GO=ECO:0000269",
"UniProtKB=ECO:0000269"
] | Subcellular Location: Secreted
PTM: Contains 3 disulfide bonds.
Sequence Mass (Da): 9588
Sequence Length: 88 |
A0A023W157 | TX85B_ETHRU | MKTNCEFPLLCLLIVLVANVEGEVEDTGLKMVKRLWRNWEDPEQRQLLDQETELEKQREKRLWRNWEDLELRQLLNEFAENQREKRLWRNWERRQVANEDDGEKAKELWRNWEDLKRRQVADLNDEQETQRDKRLWRNWEDNHATLRKRSADSLSRQKRLGKERGKE | null | null | null | extracellular region [GO:0005576] | null | null | null | Scoloptoxin-08 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24602922}. Note=The mature toxins are clearly liberated from the multidomain precursors in the venom gland prior to venom expulsion and not by venom proteases upon secretion. {ECO:0000269|PubMed:24602922}. | null | null | null | null | null | null | Ethmostigmus rubripes (Giant centipede) | [
6485,
24983
] | [
"go_cc: extracellular region (GO:0005576)",
"subcellular_location: Secreted (SL-0243)"
] | [
"UniProtKB-GO=ECO:0000269",
"UniProtKB=ECO:0000269"
] | Subcellular Location: Secreted
Sequence Mass (Da): 20708
Sequence Length: 167 |
A0A023W163 | TX85E_ETHRU | MKTNCEFPLLCLLIVLVANVEGEVEDNELKMVKRLWRNWEDPEQRQLLDQEAEQEKQREKRLWRNWEDLELRQLLNEFAENQREKRLWRNWERRQVANEDDGEKPKELWRNWEDLKRRQVVDLNDEQKTTG | null | null | null | extracellular region [GO:0005576] | null | null | null | Scoloptoxin-08 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:24602922}. | null | null | null | null | null | null | Ethmostigmus rubripes (Giant centipede) | [
6485,
24983
] | [
"go_cc: extracellular region (GO:0005576)",
"subcellular_location: Secreted (SL-0243)"
] | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB=ECO:0000305"
] | Subcellular Location: Secreted
Sequence Mass (Da): 16301
Sequence Length: 131 |
A0A023W168 | TX85A_SCOAL | MIFSRIMRGLLCLCLVLTVFELINGSDEFEHQDSLHLVKRLWRNWEEDQQKDREKRLWRNWEEEEQKDREKRLWRNWEEEEQKEKRNLPELKYEMEKNQEVPQLKRKRGILEKIWIPNEIGR | null | null | null | extracellular region [GO:0005576] | null | null | null | Scoloptoxin-08 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:24602922}. | null | null | null | null | null | null | Scolopendra alternans (Florida Keys giant centipede) | [
6485,
24983
] | [
"go_cc: extracellular region (GO:0005576)",
"subcellular_location: Secreted (SL-0243)"
] | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB=ECO:0000305"
] | Subcellular Location: Secreted
Sequence Mass (Da): 15405
Sequence Length: 122 |
A0A023W421 | DTD_BACAM | MKLVVQRVTDASVTVDGAVAGRIGPGIMALVGVTHEDTEEDAAYLADKIVNLRIFDDESGKMNLSLLDTGGEILSVSQFTLYGETKKGRRPNFMNAAKPDQALLLYEKWNELLREKGVKVETGIFGAMMDVQLTNSGPVTLIMDSKQ | 3.1.1.96 | null | D-amino acid catabolic process [GO:0019478] | cytoplasm [GO:0005737] | D-tyrosyl-tRNA(Tyr) deacylase activity [GO:0051500]; Gly-tRNA(Ala) deacylase activity [GO:0106026]; Ser(Gly)-tRNA(Ala) hydrolase activity [GO:0043908]; tRNA binding [GO:0000049] | PF02580; | 3.50.80.10; | DTD family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00518}. | CATALYTIC ACTIVITY: Reaction=glycyl-tRNA(Ala) + H2O = tRNA(Ala) + glycine + H(+); Xref=Rhea:RHEA:53744, Rhea:RHEA-COMP:9657, Rhea:RHEA-COMP:13640, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57305, ChEBI:CHEBI:78442, ChEBI:CHEBI:78522; EC=3.1.1.96; Evidence={ECO:0000255|HAMAP-Rule:MF_00518}; CATALYTIC ACTIVITY: R... | null | null | null | null | FUNCTION: An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active si... | Bacillus amyloliquefaciens (Bacillus velezensis) | [
205,
2351,
6538,
7507,
11062,
14867,
20029,
20425,
21953,
24883
] | [
"ec: EC 3.1.1.96",
"go_bp: D-amino acid catabolic process (GO:0019478)",
"go_cc: cytoplasm (GO:0005737)",
"go_mf: tRNA binding (GO:0000049)",
"interpro: D-aminoacyl-tRNA deacylase DTD (IPR003732)",
"interpro: D-aminoacyl-tRNA deacylase-like superfamily (IPR023509)",
"rhea: a D-aminoacyl-tRNA + H2O = a t... | [
"UniProtKB=ECO:0000255",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match",
"UniProtKB=ECO:0000255",
"UniProtKB=ECO:0000255",
"InterPro=match:Pfam",
"UniProtKB=ECO:0000255"
] | Function: An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active si... |
A0A023YYV9 | NLEB2_ECOLR | MLSPIRTTFHNSVNIVQSSPCQTVSFAGKEYELKVIDEKTPILFQWFEPNPERYKKDEVPIVNTKQHPYLDNVTNAARIESDRMIGIFVDGDFSVNQKTAFSKLERDFENVMIIYREDVDFSMYDRKLSDIYHDIICEQRLRTEDKRDEYLLNLLEKELREISKAQDSLISMYAKKRNHAWFDFFRNLALLKAGEIFRCTYNTKNHGISFGEGGIYLDMDMILTGKLGTIYAPDGISMHVDRRNDSVNIENSAIIVNRSNHPALLEGLSFMHSKVDAHPYYDGLGKGVKKYFNFTPLHNYNHFCDFIEFNHPNIIMNTSQ... | 2.4.1.- | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:B7UI21}; | null | extracellular region [GO:0005576]; host cell [GO:0043657] | protein-arginine N-acetylglucosaminyltransferase activity [GO:0106362] | PF24688; | 3.90.550.20; | Glycosyltransferase NleB family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:A0A482PDI9}. Host cell {ECO:0000250|UniProtKB:A0A482PDI9}. Note=Secreted via the type III secretion system (T3SS). {ECO:0000250|UniProtKB:A0A482PDI9}. | CATALYTIC ACTIVITY: Reaction=L-arginyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = N(omega)-(N-acetyl-beta-D-glucosaminyl)-L-arginyl-[protein] + UDP + H(+); Xref=Rhea:RHEA:66632, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:17079, ChEBI:CHEBI:15378, ChEBI:CHEBI:29965, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:167322... | null | null | null | null | FUNCTION: Protein-arginine N-acetylglucosaminyltransferase effector that catalyzes the transfer of a single N-acetylglucosamine (GlcNAc) to a conserved arginine residue of host target proteins. In contrast to NleB1, not able to disrupt TNF signaling in infected cells. Shows a lower enzymatic activity than NleB1. {ECO:0... | Escherichia coli O145:H28 (strain RM12581) | [
6485,
7141,
19930,
24983,
25057
] | [
"go_cc: extracellular region (GO:0005576)",
"go_cc: host cell (GO:0043657)",
"cofactor: Mn(2+) (CHEBI:29035)",
"subcellular_location: Secreted (SL-0243)",
"subcellular_location: Host cell (SL-0427)"
] | [
"UniProtKB-GO=ECO:0000250",
"UniProtKB-GO=ECO:0000250",
"UniProtKB=ECO:0000250",
"UniProtKB=ECO:0000250",
"UniProtKB=ECO:0000250"
] | Function: Protein-arginine N-acetylglucosaminyltransferase effector that catalyzes the transfer of a single N-acetylglucosamine (GlcNAc) to a conserved arginine residue of host target proteins. In contrast to NleB1, not able to disrupt TNF signaling in infected cells. Shows a lower enzymatic activity than NleB1.
Cataly... |
A0A024B2V6 | FRA18_FRAAN | MGVFTYETEFTSVIPPPRLYKAFVLDADNLIPKIAPQAVKSAEIVQGDGGVGTIKKIHLGEGSEYSYVKHQIDGLDKDNFVYNYSIIEGDAIGDKVEKISYEIKLVASPSGGSIIKSTSHYHCKGEVEIKEEHVKAGKEKAAGLFKIIENHLLANPEAYN | 3.1.27.- | null | abscisic acid-activated signaling pathway [GO:0009738]; defense response [GO:0006952] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | abscisic acid binding [GO:0010427]; protein phosphatase inhibitor activity [GO:0004864]; signaling receptor activity [GO:0038023] | PF00407; | 3.30.530.20; | BetVI family | PTM: Phosphorylated in vivo. Phosphorylation prevents its activity as ribonuclease. {ECO:0000269|PubMed:30572279}. | null | null | null | null | null | null | FUNCTION: Possesses ribonuclease activity in vitro. {ECO:0000269|PubMed:30572279}. | Fragaria ananassa (Strawberry) (Fragaria chiloensis x Fragaria virginiana) | [
1190,
1707,
6494,
6538,
8017,
8368,
8877,
9890,
14837,
15041,
18533,
20867
] | [
"go_bp: defense response (GO:0006952)",
"go_bp: abscisic acid-activated signaling pathway (GO:0009738)",
"go_cc: nucleus (GO:0005634)",
"go_cc: cytoplasm (GO:0005737)",
"go_mf: protein phosphatase inhibitor activity (GO:0004864)",
"go_mf: abscisic acid binding (GO:0010427)",
"go_mf: signaling receptor a... | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match:Pfam"
] | Function: Possesses ribonuclease activity in vitro.
PTM: Phosphorylated in vivo. Phosphorylation prevents its activity as ribonuclease.
EC: 3.1.27.-
Sequence Mass (Da): 17525
Sequence Length: 160 |
A0A024B3D0 | FRA14_FRAAN | MGVFTYETEFTSVIPPPRLFKAFILDADNLIPKIAPQAVKCAEIIEGDGGVGTIKKITFGEGSQFGSVTHKIDGIDKDNFAYSYSLVEGDALSDKIEKISYETKLVASSDGGSVIKSTSNYHTKGDVEIKEEHVKAGKEKASHLFKLVEDYLLANPNEYC | 3.1.27.- | null | abscisic acid-activated signaling pathway [GO:0009738]; defense response [GO:0006952] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | abscisic acid binding [GO:0010427]; protein phosphatase inhibitor activity [GO:0004864]; signaling receptor activity [GO:0038023] | PF00407; | 3.30.530.20; | BetVI family | PTM: Phosphorylated in vivo. Phosphorylation prevents its activity as ribonuclease. {ECO:0000269|PubMed:30572279}. | null | null | null | null | null | null | FUNCTION: Possesses ribonuclease activity in vitro. {ECO:0000269|PubMed:30572279}. | Fragaria ananassa (Strawberry) (Fragaria chiloensis x Fragaria virginiana) | [
1190,
1707,
6494,
6538,
8017,
8368,
8877,
9890,
14837,
15041,
18533,
20867
] | [
"go_bp: defense response (GO:0006952)",
"go_bp: abscisic acid-activated signaling pathway (GO:0009738)",
"go_cc: nucleus (GO:0005634)",
"go_cc: cytoplasm (GO:0005737)",
"go_mf: protein phosphatase inhibitor activity (GO:0004864)",
"go_mf: abscisic acid binding (GO:0010427)",
"go_mf: signaling receptor a... | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match:Pfam"
] | Function: Possesses ribonuclease activity in vitro.
PTM: Phosphorylated in vivo. Phosphorylation prevents its activity as ribonuclease.
EC: 3.1.27.-
Sequence Mass (Da): 17471
Sequence Length: 160 |
A0A024B3G5 | FRA16_FRAAN | MGVFTYETEFTSVIPPPRLFKAFILDADNLIPKIAPQAVKCAEIVEGDGGVGTIKKITFGEGSQFGSVTHKIDGIDKENFVYSYSLVEGDALSDKIEKISYETKLVASSDGGSVIKSTSNYHTKGDVEIKEEHVKAGKEKASHLFKLVEDYLLANPNEYC | 3.1.27.- | null | abscisic acid-activated signaling pathway [GO:0009738]; defense response [GO:0006952] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | abscisic acid binding [GO:0010427]; protein phosphatase inhibitor activity [GO:0004864]; signaling receptor activity [GO:0038023] | PF00407; | 3.30.530.20; | BetVI family | null | null | null | null | null | null | null | FUNCTION: Possesses ribonuclease activity in vitro. {ECO:0000269|PubMed:30572279}. | Fragaria ananassa (Strawberry) (Fragaria chiloensis x Fragaria virginiana) | [
1190,
1707,
6494,
6538,
8017,
8368,
8877,
9890,
14837,
15041,
18533,
20867
] | [
"go_bp: defense response (GO:0006952)",
"go_bp: abscisic acid-activated signaling pathway (GO:0009738)",
"go_cc: nucleus (GO:0005634)",
"go_cc: cytoplasm (GO:0005737)",
"go_mf: protein phosphatase inhibitor activity (GO:0004864)",
"go_mf: abscisic acid binding (GO:0010427)",
"go_mf: signaling receptor a... | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match:Pfam"
] | Function: Possesses ribonuclease activity in vitro.
EC: 3.1.27.-
Sequence Mass (Da): 17499
Sequence Length: 160 |
A0A024B404 | FRA15_FRAAN | MGVFTYETEFTSVIPPPRLFKAFILDADNLIPKIAPQAVKCAEIIEGDGGVGTIKKITFGEGSQFGSVTHKIDGIDKDNFVYSYSLVEGDALSDKIEKISYETKLVASSDGGSIIKSTSNYHTKGDVEIKEEHVKAGKEKASHLFKLVEGYLLANPNEYC | 3.1.27.- | null | abscisic acid-activated signaling pathway [GO:0009738]; defense response [GO:0006952] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | abscisic acid binding [GO:0010427]; protein phosphatase inhibitor activity [GO:0004864]; signaling receptor activity [GO:0038023] | PF00407; | 3.30.530.20; | BetVI family | PTM: Phosphorylated in vivo. Phosphorylation prevents its activity as ribonuclease. {ECO:0000269|PubMed:30572279}. | null | null | null | null | null | null | FUNCTION: Possesses ribonuclease activity in vitro. {ECO:0000269|PubMed:30572279}. | Fragaria ananassa (Strawberry) (Fragaria chiloensis x Fragaria virginiana) | [
1190,
1707,
6494,
6538,
8017,
8368,
8877,
9890,
14837,
15041,
18533,
20867
] | [
"go_bp: defense response (GO:0006952)",
"go_bp: abscisic acid-activated signaling pathway (GO:0009738)",
"go_cc: nucleus (GO:0005634)",
"go_cc: cytoplasm (GO:0005737)",
"go_mf: protein phosphatase inhibitor activity (GO:0004864)",
"go_mf: abscisic acid binding (GO:0010427)",
"go_mf: signaling receptor a... | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match:Pfam"
] | Function: Possesses ribonuclease activity in vitro.
PTM: Phosphorylated in vivo. Phosphorylation prevents its activity as ribonuclease.
EC: 3.1.27.-
Sequence Mass (Da): 17455
Sequence Length: 160 |
A0A024B4E4 | FRA17_FRAAN | MGVFTYETEFTSVIPPPRLYKAFVLDTDNLIPKIAPQAVKSTELVQGDGGVGTIKKIHLGEGSEYSYVKHQIDGLDKDNFVYNYSIIEGDAIGDKVEKISYEIKLVASPSGGSIIKSTSHYHCKGEVEIKEEHVKAGKERAAGLFKIIENYLLGNPDAYN | 3.1.27.- | null | abscisic acid-activated signaling pathway [GO:0009738]; defense response [GO:0006952] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | abscisic acid binding [GO:0010427]; protein phosphatase inhibitor activity [GO:0004864]; signaling receptor activity [GO:0038023] | PF00407; | 3.30.530.20; | BetVI family | PTM: Phosphorylated in vivo. Phosphorylation prevents its activity as ribonuclease. {ECO:0000269|PubMed:30572279}. | null | null | null | null | null | null | FUNCTION: Possesses ribonuclease activity in vitro. {ECO:0000269|PubMed:30572279}. | Fragaria ananassa (Strawberry) (Fragaria chiloensis x Fragaria virginiana) | [
1190,
1707,
6494,
6538,
8017,
8368,
8877,
9890,
14837,
15041,
18533,
20867
] | [
"go_bp: defense response (GO:0006952)",
"go_bp: abscisic acid-activated signaling pathway (GO:0009738)",
"go_cc: nucleus (GO:0005634)",
"go_cc: cytoplasm (GO:0005737)",
"go_mf: protein phosphatase inhibitor activity (GO:0004864)",
"go_mf: abscisic acid binding (GO:0010427)",
"go_mf: signaling receptor a... | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match:Pfam"
] | Function: Possesses ribonuclease activity in vitro.
PTM: Phosphorylated in vivo. Phosphorylation prevents its activity as ribonuclease.
EC: 3.1.27.-
Sequence Mass (Da): 17611
Sequence Length: 160 |
A0A024B7I0 | SCL7_POPEU | MAYMCADSGNLMAIAQQVIKQKQQQEQQQQQSHHPQQQFLGLNPFSLNPWPSTTMSANPNLGYGLSGPAAFSDPFQSGPDTGDPPGFSFSNMEHQHSGGFRFPDFTGAGGEFDSDEWMDSLMNGGDSTDSSNLPSGCDAWQNNADFGIYPSDPFNTSPSRLTVGCSPPSDLNRVISDSLWADPSPQEIKPKTSPPQQPPPTAKNEVVVGSKEVVELSSSPVLKAFVECAQLVESKVDQAVKSLIKLKESVSENGDPGERVGFYFVQGLCRRVAVGELDDLKNFHQTTSEEFTLSYKALNDACPYSKFAHLTANQAILEAT... | null | null | null | nucleus [GO:0005634] | null | PF03514; | null | GRAS family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20616154}. | null | null | null | null | null | FUNCTION: Probable transcription factor involved in plant development (By similarity). Involved in environmental abiotic stress resistance. May increase the expression of stress-responsive genes (PubMed:20616154). Binds DNA in vitro (By similarity). {ECO:0000250|UniProtKB:Q53K16, ECO:0000250|UniProtKB:Q9SCR0, ECO:00002... | Populus euphratica (Euphrates poplar) | [
6494,
11474,
22287,
24954
] | [
"go_cc: nucleus (GO:0005634)",
"interpro: Transcription factor GRAS (IPR005202)",
"pfam: GRAS (PF03514)",
"subcellular_location: Nucleus (SL-0191)"
] | [
"UniProtKB-GO=ECO:0000269",
"InterPro=match",
"InterPro=match:Pfam",
"UniProtKB=ECO:0000269"
] | Function: Probable transcription factor involved in plant development (By similarity). Involved in environmental abiotic stress resistance. May increase the expression of stress-responsive genes. Binds DNA in vitro (By similarity).
Subcellular Location: Nucleus
Domain: The GRAS domain is involved in DNA-binding.
Sequen... |
A0A024B7W1 | POLG_ZIKVF | MKNPKKKSGGFRIVNMLKRGVARVSPFGGLKRLPAGLLLGHGPIRMVLAILAFLRFTAIKPSLGLINRWGSVGKKEAMEIIKKFKKDLAAMLRIINARKEKKRRGADTSVGIVGLLLTTAMAAEVTRRGSAYYMYLDRNDAGEAISFPTTLGMNKCYIQIMDLGHMCDATMSYECPMLDEGVEPDDVDCWCNTTSTWVVYGTCHHKKGEARRSRRAVTLPSHSTRKLQTRSQTWLESREYTKHLIRVENWIFRNPGFALAAAAIAWLLGSSTSQKVIYLVMILLIAPAYSIRCIGVSNRDFVEGMSGGTWVDVVLEHGGC... | 2.1.1.56; 2.1.1.57; 2.7.7.48; 3.4.21.91; 3.6.1.15; 3.6.4.13 | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; negative regulation of innate immune response [GO:0045824]; proteolysis [GO:0006508]; symbiont-mediated activation of host autophagy [GO:0039520]; symbiont-mediated suppression of host J... | centrosome [GO:0005813]; extracellular region [GO:0005576]; host cell cytoplasm [GO:0030430]; host cell endoplasmic reticulum membrane [GO:0044167]; host cell nucleolus [GO:0044196]; host cell nucleus [GO:0042025]; host cell perinuclear region of cytoplasm [GO:0044220]; viral capsid [GO:0019028]; viral envelope [GO:001... | 4 iron, 4 sulfur cluster binding [GO:0051539]; 5'-3' RNA polymerase activity [GO:0034062]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; double-stranded RNA binding [GO:0003725]; GTP binding [GO:0005525]; lipid binding [GO:0008289]; metal ion binding [GO:0046872]; methyltransferase cap1 activity [GO:0... | PF20907;PF01003;PF07652;PF21659;PF02832;PF00869;PF01004;PF00948;PF01005;PF01002;PF01350;PF01349;PF00972;PF20483;PF01570;PF01728;PF00949; | 1.10.10.930;1.10.260.90;1.20.1280.260;2.40.10.120;2.60.40.350;1.10.8.970;2.60.260.50;3.30.70.2840;3.40.50.300;2.60.98.10;3.40.50.150;3.30.67.10;3.30.387.10; | Class I-like SAM-binding methyltransferase superfamily, mRNA cap 0-1 NS5-type methyltransferase family | PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins. Cleavages in the lumen of endoplasmic reticulum are performed by host signal peptidase, whereas cleavages in the cytoplasmic side are performed by serine protease NS3. Signal cleavage at the 2K-4B site requires a prior NS3 protease-m... | SUBCELLULAR LOCATION: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000269|PubMed:36594413}. Host cytoplasm {ECO:0000250|UniProtKB:P06935}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P06935}. Host nucleus, host nucleolus {ECO:0000250|UniProtKB:Q01299}.; SUBCELLULAR LO... | CATALYTIC ACTIVITY: [RNA-directed RNA polymerase/Methyltransferase NS5]: Reaction=a 5'-end (5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:67008, Rhea:RHEA-COMP:17166, Rhea:RHEA-C... | null | null | null | null | FUNCTION: [Capsid protein C]: Capsid protein C self-assembles to form an icosahedral capsid about 30 nm in diameter. The capsid encapsulates the genomic RNA (Probable). Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of the mature virus p... | Zika virus (isolate ZIKV/Human/French Polynesia/10087PF/2013) (ZIKV) | [
290,
298,
1009,
2310,
3395,
4007,
6485,
6579,
6766,
6828,
7072,
7146,
7220,
7610,
7611,
7673,
7773,
8085,
8167,
8168,
8245,
8563,
8804,
9015,
9033,
9140,
9175,
10276,
10796,
12042,
12459,
13329,
13415,
15266,
15446,
17640,
20013,
20168,
202... | [
"ec: EC 3.6.1.15",
"ec: EC 3.6.4.13",
"go_bp: proteolysis (GO:0006508)",
"go_bp: virion attachment to host cell (GO:0019062)",
"go_bp: symbiont-mediated suppression of host type I interferon-mediated signaling pathway (GO:0039502)",
"go_bp: negative regulation of innate immune response (GO:0045824)",
"g... | [
"UniProtKB=ECO:0000250,none",
"UniProtKB=ECO:0000250,none",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000314",
"UniProtKB-GO=ECO:0000250",
"UniProtKB-GO=ECO:0000314",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000250",
"UniProtKB-G... | Catalytic Activity: RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) + diphosphate; Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala.; a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + phosphate + H(+); ATP + H2... |
A0A024BTN9 | OXLA_BOTSC | SCADDRNPLEECFQETDYEEFLEIARNGLKATSNPKHVVIVGAGMSGLSAAYVLAGAGHQVTVLEASERAGGRVRTYRNDKEGWYANLGPMRLPEKHRIVREYITKFGLQLNEFSQENENAWYFIKNIRKRVGEVKKDPGLLQYPVKPSEEGKSAGQLYEESLGKVVEELKRTNCSYILDKYDTYSTKEYLIKEGNLSPGAVDMIGDLLNEDSGYYVSFIESLKHDNIFGYEKRFNEIVDGMDKLPTSMYQAIEEKVRFNARVIKIQQNDNEVTVTYQTSENEMSPVTADYVIVCTTSRAARRITFEPPLPPKKAHALRS... | 1.4.3.2 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:P81382}; | amino acid catabolic process [GO:0009063] | extracellular region [GO:0005576] | L-amino-acid oxidase activity [GO:0001716] | PF01593; | 3.90.660.10;3.50.50.60;1.10.405.10; | Flavin monoamine oxidase family, FIG1 subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24875315}. | CATALYTIC ACTIVITY: Reaction=an L-alpha-amino acid + O2 + H2O = a 2-oxocarboxylate + H2O2 + NH4(+); Xref=Rhea:RHEA:13781, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35179, ChEBI:CHEBI:59869; EC=1.4.3.2; Evidence={ECO:0000269|PubMed:24875315}; CATALYTIC ACTIVITY: Reaction=L-l... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=16.37 uM for L-Leu {ECO:0000269|PubMed:24875315}; Vmax=0.39 umol/min/mg enzyme {ECO:0000269|PubMed:24875315}; | null | null | null | FUNCTION: Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme (PubMed:24875315). Shows activity on L-Leu (PubMed:24875315). Damage cell membranes of the Gram-positive bacteria S.aureu... | Bothriechis schlegelii (Eyelash palm pitviper) | [
36,
1574,
6485,
7571,
10824,
16307,
18534,
19943,
20026,
20447,
21615,
24983
] | [
"ec: EC 1.4.3.2",
"go_bp: amino acid catabolic process (GO:0009063)",
"go_cc: extracellular region (GO:0005576)",
"go_mf: L-amino-acid oxidase activity (GO:0001716)",
"interpro: Amine oxidase (IPR002937)",
"interpro: FAD/NAD(P)-binding domain superfamily (IPR036188)",
"interpro: L-amino-acid oxidase-lik... | [
"UniProtKB=ECO:0000269",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000269",
"UniProtKB-GO=ECO:0000269",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"UniProtKB=ECO:0000250",
"UniProtKB=ECO:0000269",
"UniProtKB=ECO:0000269",
"InterPro=match:Pfam",
"UniProtKB=ECO:0000269"
] | Function: Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme. Shows activity on L-Leu. Damage cell membranes of the Gram-positive bacteria S.aureus (MIC=4 ug/ml and MBC=8 ug/ml) and ... |
A0A024CI64 | C80F1_ATRBE | MNIENTSEIFTIFFTHILLPFLSFFIIRCVISSRKKLPLPPGPFPWPIIGHLFHLGNKPHVSLAKLAHVHGPDLMSIRLGGRLVIVASSPVATAEVLKTHDRLLSGRFVPHPMRVEGSYIRNLATETLEECDENWKKVRSMYQIVLFSHKAVESQVNIREKKVMELVNFVASKEGQLVNIKDIAFVTILNILSNSTISIDLVDFEGKGIGEGMRQWIRNYTKLEGVPQLADLFPILDGCSWDFQGTYKKLKDTFERISDVWRDIINKKRKEISGKCYEGEDFADALIRNGFEDKQINALLMELYSAGTETTITTVEWTLV... | 1.14.14.195 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P04798}; | tropane alkaloid biosynthetic process [GO:0009710] | endoplasmic reticulum [GO:0005783]; membrane [GO:0016020] | heme binding [GO:0020037]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen [GO:0016705] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9SP06}. | CATALYTIC ACTIVITY: Reaction=(R)-littorine + reduced [NADPH--hemoprotein reductase] + O2 = hyoscyamine aldehyde + oxidized [NADPH--hemoprotein reductase] + 2 H2O + H(+); Xref=Rhea:RHEA:85415, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CH... | null | PATHWAY: Alkaloid biosynthesis; tropane alkaloid biosynthesis. {ECO:0000250|UniProtKB:Q1A1B0}. | null | null | FUNCTION: Cytochrome P450 monooxygenase involved in the biosynthesis of tropane alkaloids natural products (By similarity). Catalyzes the oxidation of (R)-littorine with rearrangement to form hyoscyamine aldehyde, a putative precursor to hyoscyamine by an alcohol dehydrogenase, and without rearrangement to form 3'-hydr... | Atropa belladonna (Belladonna) (Deadly nightshade) | [
1698,
6563,
6727,
7856,
8157,
8525,
8657,
10002,
10647,
13954,
16401,
19936,
20574,
24892,
24930,
25105
] | [
"go_bp: tropane alkaloid biosynthetic process (GO:0009710)",
"go_cc: endoplasmic reticulum (GO:0005783)",
"go_cc: membrane (GO:0016020)",
"go_mf: monooxygenase activity (GO:0004497)",
"go_mf: iron ion binding (GO:0005506)",
"go_mf: oxidoreductase activity, acting on paired donors, with incorporation or re... | [
"UniProtKB-GO=ECO:0000250",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000250",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"UniProtKB=ECO:0000250",
... | Function: Cytochrome P450 monooxygenase involved in the biosynthesis of tropane alkaloids natural products (By similarity). Catalyzes the oxidation of (R)-littorine with rearrangement to form hyoscyamine aldehyde, a putative precursor to hyoscyamine by an alcohol dehydrogenase, and without rearrangement to form 3'-hydr... |
A0A024F8Y4 | VLMB_LECSP | MEVKKLEFIGPRVMPGGQKEMDYFCQVPEFQQRCQSGNAVVIPRRDQVADGRGSTGKLFSQTLNTADTIPHCIVMFEDTYTAQSSTQPWLPISTCSVFYQLGEGVCGFGNICHGGIQTTLLDDVMGVLGVLNARLQDGIIPSKVPGAYWPRNNPGMVDLTKSLFATQGIEVKFLRPLRTPQVIEVSAQLVDMDVSGGSFTVQCVIRDMKGKQYAVANANWVIHTPRPRSRL | null | null | null | null | null | null | 3.10.129.10; | null | null | null | null | null | PATHWAY: Secondary metabolite biosynthesis. {ECO:0000269|PubMed:24848421}. | null | null | FUNCTION: Part of the gene cluster that mediates the biosynthesis of verlamelin, a lipopeptide that exhibits antifungal activity against plant pathogenic fungi (PubMed:24848421). Verlamelin is a cyclic hexadepsipeptide and is bridged by ester bonding between a 5-hydroxytetradecanoic acid moiety and a carboxyl group on ... | Lecanicillium sp | [
15451
] | [
"interpro: HotDog domain superfamily (IPR029069)"
] | [
"InterPro=match"
] | Function: Part of the gene cluster that mediates the biosynthesis of verlamelin, a lipopeptide that exhibits antifungal activity against plant pathogenic fungi. Verlamelin is a cyclic hexadepsipeptide and is bridged by ester bonding between a 5-hydroxytetradecanoic acid moiety and a carboxyl group on the terminal Val o... |
A0A024F910 | VLMS_LECSP | MDAPDIQAPSGSCRTTLGKVAADIFEMNVETLDWDMSFIQMGGDSILAIDFIVRCRDEGIWVDMMDLLTVDTLAELADSIDEQNGVTADVANSSDLNEHETHQENGENINATLPVADRPLRFASMEIAHVKDASLVSSALESLITRHSALRSVWSVSSTGEYTLTTKPTAMAYESQPFFLAEASEPTKMNDAFELLKNALRSDGAPPLGCLFISNNATTASSIIVLAADANLVDSLSMRILRTEFREFILGHALDAPPGFQFSNWVAAKCQSTTARPRTLQQPQRAMERAIATKLSSSTSSADSSSNEATITTFQITHST... | 6.3.2.- | null | amino acid activation for nonribosomal peptide biosynthetic process [GO:0043041]; secondary metabolite biosynthetic process [GO:0044550] | cytoplasm [GO:0005737] | catalytic activity [GO:0003824]; phosphopantetheine binding [GO:0031177] | PF00501;PF00668;PF00550; | 3.30.300.30;3.40.50.980;1.10.1200.10;3.30.559.10;2.30.38.10;3.40.50.12780;3.30.559.30; | NRP synthetase family | null | null | null | null | PATHWAY: Secondary metabolite biosynthesis. {ECO:0000269|PubMed:24848421}. | null | null | FUNCTION: Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of verlamelin, a lipopeptide that exhibits antifungal activity against plant pathogenic fungi (PubMed:24848421). Verlamelin is a cyclic hexadepsipeptide and is bridged by ester bonding between a 5-hydroxytetradecanoic aci... | Lecanicillium sp | [
3796,
6538,
7628,
9863,
10062,
11759,
12505,
12563,
14491,
14513,
14804,
16550,
17485,
18019,
20939,
20970,
21063
] | [
"go_bp: secondary metabolite biosynthetic process (GO:0044550)",
"go_cc: cytoplasm (GO:0005737)",
"go_mf: catalytic activity (GO:0003824)",
"interpro: AMP-dependent synthetase/ligase domain (IPR000873)",
"interpro: Condensation domain (IPR001242)",
"interpro: Phosphopantetheine attachment site (IPR006162)... | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"Inter... | Function: Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of verlamelin, a lipopeptide that exhibits antifungal activity against plant pathogenic fungi. Verlamelin is a cyclic hexadepsipeptide and is bridged by ester bonding between a 5-hydroxytetradecanoic acid moiety and a car... |
A0A024F9J0 | VLMC_LECSP | MIFTQPSFVPALPSPLPLGETIGDFCMSERLAKVGNDAVEEQPIPFIDAAIDKSWTTDEINTRVAQLTRALATEWNIAPGEKWHKQVAVLASNCVSIFMDTLILTWAIHRLGGGCLMLQPTSSVEEMAAHIDHVPPFAMFVTLDLVTLGQETIQKSSQSADLPFYKFSKVYGPPAKNAPDTSNVKSLDALLEKSKDQAPIEKLLLAEGEGSKRVAYYCTTSGTGGFQRIVAITHENIIASILQAGLFTGITKEKSEIALVFTPFNHIYGLLTAHTLMWLGHSTVIHRGFNMLEVLMSIPKRRITTLYLVPPIINAMSRNA... | 6.3.2.- | null | null | null | CoA-ligase activity [GO:0016405] | PF00501;PF13193; | 3.30.300.30;3.40.50.12780; | ATP-dependent AMP-binding enzyme family | null | null | null | null | PATHWAY: Secondary metabolite biosynthesis. {ECO:0000269|PubMed:24848421}. | null | null | FUNCTION: AMP-dependent ligase; part of the gene cluster that mediates the biosynthesis of verlamelin, a lipopeptide that exhibits antifungal activity against plant pathogenic fungi (PubMed:24848421). Verlamelin is a cyclic hexadepsipeptide and is bridged by ester bonding between a 5-hydroxytetradecanoic acid moiety an... | Lecanicillium sp | [
8500,
9863,
15051,
17485,
18019,
20939,
23640
] | [
"go_mf: CoA-ligase activity (GO:0016405)",
"interpro: AMP-dependent synthetase/ligase domain (IPR000873)",
"interpro: AMP-binding enzyme, C-terminal domain (IPR025110)",
"interpro: ANL, N-terminal domain (IPR042099)",
"interpro: AMP-binding enzyme domain superfamily (IPR045851)",
"pfam: AMP-binding (PF005... | [
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match:Pfam",
"InterPro=match:Pfam"
] | Function: AMP-dependent ligase; part of the gene cluster that mediates the biosynthesis of verlamelin, a lipopeptide that exhibits antifungal activity against plant pathogenic fungi. Verlamelin is a cyclic hexadepsipeptide and is bridged by ester bonding between a 5-hydroxytetradecanoic acid moiety and a carboxyl group... |
A0A024FA41 | VLMA_LECSP | MPSTTQTTVQSIDSIDSIPTTIKRRQNDKTKTPKTKPVSKIPICPKNSSIPRLDQPSQHKFILLQSLLPITVHQLTTLVLSISRYDDYVHPFLLRLCVIIGYGYAFRFLLRREGLAIRTLGKKLGYLDGDHHPRDKVPRDSTRLNWSLPLTVGSRTVMCVLVAYDPSQQPINYLASLKWWAWLAVYLSLYPIILDFYYYCVHRAWHEVPCLWRFHRRHHTIKRPSILFTAYADSEQELFDIVGTPLLTFFTLKALHLPMDFYTWWICIQYIAYTEVMGHSGLRIYTTPPISCSWLLQRFGVELVIEDHDLHHRQGYRQAR... | 1.-.-.- | null | lipid biosynthetic process [GO:0008610] | membrane [GO:0016020] | iron ion binding [GO:0005506] | PF04116; | null | Sterol desaturase family, TMEM195 subfamily | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. | null | null | PATHWAY: Secondary metabolite biosynthesis. {ECO:0000269|PubMed:24848421}. | null | null | FUNCTION: Fatty acid hydroxylase; part of the gene cluster that mediates the biosynthesis of verlamelin, a lipopeptide that exhibits antifungal activity against plant pathogenic fungi (PubMed:24848421). Verlamelin is a cyclic hexadepsipeptide and is bridged by ester bonding between a 5-hydroxytetradecanoic acid moiety ... | Lecanicillium sp | [
1556,
6727,
8157,
11953,
18548,
22452,
24930,
25110
] | [
"go_bp: lipid biosynthetic process (GO:0008610)",
"go_cc: membrane (GO:0016020)",
"go_mf: iron ion binding (GO:0005506)",
"interpro: Fatty acid hydroxylase (IPR006694)",
"interpro: Sterol desaturase-related (IPR050307)",
"pfam: FA_hydroxylase (PF04116)",
"subcellular_location: Membrane (SL-0162)",
"me... | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match",
"InterPro=match:Pfam",
"UniProtKB=ECO:0000255",
"UniProtKB=ECO:0000255"
] | Function: Fatty acid hydroxylase; part of the gene cluster that mediates the biosynthesis of verlamelin, a lipopeptide that exhibits antifungal activity against plant pathogenic fungi. Verlamelin is a cyclic hexadepsipeptide and is bridged by ester bonding between a 5-hydroxytetradecanoic acid moiety and a carboxyl gro... |
A0A024QYT3 | OST2A_ONCMY | MKSLTLLTICAVLSVSLSMNDLALDVVLDPAPDPATEPAPAADSSASSSASSSSSSASDSSASASDSSDSDSSSASSSSSSSESASAEVTTEDPAAATEPEVVIMKRDLASVLLRRKRAAGQAAAAFTLTQVESLSEVCELNLACEHMAETAGIVAAYTAYYGPPPF | null | null | bone development [GO:0060348]; osteoblast differentiation [GO:0001649]; regulation of cellular response to insulin stimulus [GO:1900076]; response to vitamin K [GO:0032571] | extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; hydroxyapatite binding [GO:0046848]; structural constituent of bone [GO:0008147] | PF25890; | null | Osteocalcin/matrix Gla protein family | PTM: Gamma-carboxyglutamate residues are formed by vitamin K dependent carboxylation. These residues are essential for the binding of calcium. {ECO:0000255|PROSITE-ProRule:PRU00463}. | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. | null | null | null | null | null | FUNCTION: Binds strongly to apatite and calcium. {ECO:0000305}. | Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri) | [
535,
4865,
6485,
8159,
9574,
16199,
17065,
19707,
24720,
24983
] | [
"go_bp: osteoblast differentiation (GO:0001649)",
"go_bp: bone development (GO:0060348)",
"go_cc: extracellular region (GO:0005576)",
"go_mf: calcium ion binding (GO:0005509)",
"interpro: Gamma-carboxyglutamic acid-rich (GLA) domain (IPR000294)",
"interpro: Gamma-carboxyglutamic acid-rich (GLA) domain sup... | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match:Pfam",
"UniProtKB=ECO:0000305"
] | Function: Binds strongly to apatite and calcium.
Subcellular Location: Secreted
PTM: Gamma-carboxyglutamate residues are formed by vitamin K dependent carboxylation. These residues are essential for the binding of calcium.
Sequence Mass (Da): 16746
Sequence Length: 167 |
A0A024R1R8 | TMA7B_HUMAN | MSSHEGGKKKALKQPKKQAKEMDEEEKAFKQKQKEEQKKLEVLKAKVVGKGPLATGGIKKSGKK | null | null | null | null | null | PF09072; | null | TMA7 family | null | null | null | null | null | null | null | null | Homo sapiens (Human) | [] | [] | [] | Sequence Mass (Da): 7091
Sequence Length: 64 |
A0A024RBG1 | NUD4B_HUMAN | MMKFKPNQTRTYDREGFKKRAACLCFRSEQEDEVLLVSSSRYPDQWIVPGGGMEPEEEPGGAAVREVYEEAGVKGKLGRLLGIFEQNQDRKHRTYVYVLTVTEILEDWEDSVNIGRKREWFKVEDAIKVLQCHKPVHAEYLEKLKLGCSPANGNSTVPSLPDNNALFVTAAQTSGLPSSVR | 3.6.1.52 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q96G61}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q96G61}; Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q96G61}; | adenosine 5'-(hexahydrogen pentaphosphate) catabolic process [GO:1901911]; diadenosine hexaphosphate catabolic process [GO:1901909]; diadenosine pentaphosphate catabolic process [GO:1901907]; diphosphoinositol polyphosphate metabolic process [GO:0071543] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | bis(5'-adenosyl)-hexaphosphatase activity [GO:0034431]; bis(5'-adenosyl)-pentaphosphatase activity [GO:0034432]; diphosphoinositol-polyphosphate diphosphatase activity [GO:0008486]; endopolyphosphatase activity [GO:0000298] | PF00293; | 3.90.79.10; | Nudix hydrolase family, DIPP subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9NZJ9}. | CATALYTIC ACTIVITY: Reaction=diphospho-myo-inositol polyphosphate + H2O = myo-inositol polyphosphate + phosphate.; EC=3.6.1.52; Evidence={ECO:0000250|UniProtKB:Q9NZJ9}; | null | null | null | null | FUNCTION: Cleaves a beta-phosphate from the diphosphate groups in PP-InsP5 (diphosphoinositol pentakisphosphate), PP-InsP4 and [PP]2-InsP4 (bisdiphosphoinositol tetrakisphosphate), suggesting that it may play a role in signal transduction. Also able to catalyze the hydrolysis of dinucleoside oligophosphate Ap6A, but no... | Homo sapiens (Human) | [
293,
6494,
6538,
8286,
9483,
13567,
14402,
18161,
19924,
19930,
20772,
24883
] | [
"ec: EC 3.6.1.52",
"go_cc: nucleus (GO:0005634)",
"go_cc: cytoplasm (GO:0005737)",
"go_mf: diphosphoinositol-polyphosphate diphosphatase activity (GO:0008486)",
"interpro: NUDIX hydrolase domain (IPR000086)",
"interpro: NUDIX hydrolase-like domain superfamily (IPR015797)",
"interpro: NUDIX hydrolase, co... | [
"UniProtKB=ECO:0000250",
"UniProtKB-GO=ECO:0000318",
"UniProtKB-GO=ECO:0000250",
"UniProtKB-GO=ECO:0000250",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"UniProtKB=ECO:0000250",
"UniProtKB=ECO:0000250",
"InterPro=match:Pfam",
"UniProtKB=ECO:0000250"
] | Function: Cleaves a beta-phosphate from the diphosphate groups in PP-InsP5 (diphosphoinositol pentakisphosphate), PP-InsP4 and [PP]2-InsP4 (bisdiphosphoinositol tetrakisphosphate), suggesting that it may play a role in signal transduction. Also able to catalyze the hydrolysis of dinucleoside oligophosphate Ap6A, but no... |
A0A024RXP8 | GUX1_TRIR3 | MYRKLAVISAFLATARAQSACTLQSETHPPLTWQKCSSGGTCTQQTGSVVIDANWRWTHATNSSTNCYDGNTWSSTLCPDNETCAKNCCLDGAAYASTYGVTTSGNSLSIGFVTQSAQKNVGARLYLMASDTTYQEFTLLGNEFSFDVDVSQLPCGLNGALYFVSMDADGGVSKYPTNTAGAKYGTGYCDSQCPRDLKFINGQANVEGWEPSSNNANTGIGGHGSCCSEMDIWEANSISEALTPHPCTTVGQEICEGDGCGGTYSDNRYGGTCDPDGCDWNPYRLGNTSFYGPGSSFTLDTTKKLTVVTQFETSGAINRY... | 3.2.1.91 | null | glucan catabolic process [GO:0009251] | extracellular region [GO:0005576] | cellulose 1,4-beta-cellobiosidase activity [GO:0016162]; cellulose binding [GO:0030248] | PF00734;PF00840; | 2.70.100.10; | Glycosyl hydrolase 7 (cellulase C) family | PTM: N-glycosylated. A high mannose glycan is attached to Asn-287 (predominantly Man(8)GlcNAc(2)) and single GlcNAc occupancy is observed at Asn-62 and Asn-401 with some site heterogeneity depending on strains and fermentation conditions. {ECO:0000269|PubMed:11270873}.; PTM: O-glycosylated. Within the linker domain, al... | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P62694}. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains.; EC=3.2.1.91; Evidence={ECO:0000250|UniProtKB:P62694}; | null | null | null | null | FUNCTION: Exocellobiohydrolases (CBH) that catalyzes the hydrolysis of 1,4-beta-D-glucosidic bonds in cellulose to release the disaccharide cellobiose. The degradation of cellulose involves an interplay between different cellulolytic enzymes. Hydrolysis starts with endoglucanases (EGs), which cut internal beta-1,4-gluc... | Trichoderma reesei (strain ATCC 56765 / BCRC 32924 / NRRL 11460 / VTT-D-86271 / Rut C-30) (Hypocrea jecorina) | [
257,
1602,
6485,
8481,
8683,
9557,
10313,
13148,
16198,
16693,
21109,
21177,
24983
] | [
"ec: EC 3.2.1.91",
"go_bp: glucan catabolic process (GO:0009251)",
"go_cc: extracellular region (GO:0005576)",
"go_mf: cellulose 1,4-beta-cellobiosidase activity (GO:0016162)",
"go_mf: cellulose binding (GO:0030248)",
"interpro: Cellulose-binding domain (IPR000254)",
"interpro: Glycoside hydrolase, fami... | [
"UniProtKB=ECO:0000250",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000250",
"UniProtKB-GO=ECO:0000250",
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match:Pfam",
"InterPro=match:Pfam",
"UniProtKB=ECO:0000... | Function: Exocellobiohydrolases (CBH) that catalyzes the hydrolysis of 1,4-beta-D-glucosidic bonds in cellulose to release the disaccharide cellobiose. The degradation of cellulose involves an interplay between different cellulolytic enzymes. Hydrolysis starts with endoglucanases (EGs), which cut internal beta-1,4-gluc... |
A0A024SC78 | CUTI1_TRIR3 | MRSLAILTTLLAGHAFAYPKPAPQSVNRRDWPSINEFLSELAKVMPIGDTITAACDLISDGEDAAASLFGISETENDPCGDVTVLFARGTCDPGNVGVLVGPWFFDSLQTALGSRTLGVKGVPYPASVQDFLSGSVQNGINMANQIKSVLQSCPNTKLVLGGYSQGSMVVHNAASNLDAATMSKISAVVLFGDPYYGKPVANFDAAKTLVVCHDGDNICQGGDIILLPHLTYAEDADTAAAFVVPLVS | 3.1.1.74 | null | carbohydrate catabolic process [GO:0016052] | extracellular region [GO:0005576] | cutinase activity [GO:0050525] | PF01083; | 3.40.50.1820; | Cutinase family | PTM: The 2 disulfide bonds play a critical role in holding the catalytic residues in juxta-position; reduction of the disulfide bridges results in the complete inactivation of the enzyme. {ECO:0000250|UniProtKB:P11373}. | SUBCELLULAR LOCATION: Secreted {ECO:0000255|RuleBase:RU361263}. | CATALYTIC ACTIVITY: Reaction=cutin + H2O = cutin monomers.; EC=3.1.1.74; Evidence={ECO:0000269|PubMed:25219509}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4-7. {ECO:0000269|PubMed:25219509}; | null | FUNCTION: Catalyzes the hydrolysis of complex carboxylic polyesters found in the cell wall of plants (PubMed:25219509). Degrades cutin, a macromolecule that forms the structure of the plant cuticle (PubMed:25219509). {ECO:0000269|PubMed:25219509}. | Trichoderma reesei (strain ATCC 56765 / BCRC 32924 / NRRL 11460 / VTT-D-86271 / Rut C-30) (Hypocrea jecorina) | [
2190,
6485,
9095,
9761,
12755,
15442,
17658,
17659,
21325,
24983
] | [
"go_bp: carbohydrate catabolic process (GO:0016052)",
"go_cc: extracellular region (GO:0005576)",
"go_mf: cutinase activity (GO:0050525)",
"interpro: Cutinase/acetylxylan esterase (IPR000675)",
"interpro: Cutinase, monofunctional (IPR011150)",
"interpro: Alpha/Beta hydrolase fold (IPR029058)",
"interpro... | [
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000314",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match:Pfam",
"UniProtKB=ECO:0000255"
] | Function: Catalyzes the hydrolysis of complex carboxylic polyesters found in the cell wall of plants. Degrades cutin, a macromolecule that forms the structure of the plant cuticle.
Catalytic Activity: cutin + H2O = cutin monomers.
Subcellular Location: Secreted
Domain: In contract to classical cutinases, possesses a li... |
A0A024SH20 | GUN2_TRIR3 | MNKSVAPLLLAASILYGGAAAQQTVWGQCGGIGWSGPTNCAPGSACSTLNPYYAQCIPGATTITTSTRPPSGPTTTTRATSTSSSTPPTSSGVRFAGVNIAGFDFGCTTDGTCVTSKVYPPLKNFTGSNNYPDGIGQMQHFVNDDGMTIFRLPVGWQYLVNNNLGGNLDSTSISKYDQLVQGCLSLGAYCIVDIHNYARWNGGIIGQGGPTNAQFTSLWSQLASKYASQSRVWFGIMNEPHDVNINTWAATVQEVVTAIRNAGATSQFISLPGNDWQSAGAFISDGSAAALSQVTNPDGSTTNLIFDVHKYLDSDNSGTH... | 3.2.1.4 | null | glucan catabolic process [GO:0009251] | extracellular region [GO:0005576] | cellulase activity [GO:0008810]; cellulose binding [GO:0030248] | PF00734;PF00150; | 3.20.20.80; | Glycosyl hydrolase 5 (cellulase A) family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P07982}. | CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4; Evidence={ECO:0000250|UniProtKB:P07982}; | null | null | null | null | FUNCTION: Endoglucanase (EG) that cleaves the internal beta-1,4-glucosidic bonds in cellulose. The degradation of cellulose involves an interplay between different cellulolytic enzymes. Hydrolysis starts with EGs, which cut internal glycosidic linkages to reduce the polymerization degree of the substrate and creates ne... | Trichoderma reesei (strain ATCC 56765 / BCRC 32924 / NRRL 11460 / VTT-D-86271 / Rut C-30) (Hypocrea jecorina) | [
241,
1602,
6485,
8322,
8683,
9557,
10224,
13891,
14008,
16198,
20650,
21109,
24983
] | [
"ec: EC 3.2.1.4",
"go_bp: glucan catabolic process (GO:0009251)",
"go_cc: extracellular region (GO:0005576)",
"go_mf: cellulase activity (GO:0008810)",
"go_mf: cellulose binding (GO:0030248)",
"interpro: Cellulose-binding domain (IPR000254)",
"interpro: Glycoside hydrolase, family 5 (IPR001547)",
"int... | [
"UniProtKB=ECO:0000250",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000250",
"UniProtKB-GO=ECO:0000250",
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match:Pfam",
"InterPro=match:Pfam",
"UniProtKB=ECO:0000... | Function: Endoglucanase (EG) that cleaves the internal beta-1,4-glucosidic bonds in cellulose. The degradation of cellulose involves an interplay between different cellulolytic enzymes. Hydrolysis starts with EGs, which cut internal glycosidic linkages to reduce the polymerization degree of the substrate and creates ne... |
A0A024SH76 | GUX2_TRIR3 | MIVGILTTLATLATLAASVPLEERQACSSVWGQCGGQNWSGPTCCASGSTCVYSNDYYSQCLPGAASSSSSTRAASTTSRVSPTTSRSSSATPPPGSTTTRVPPVGSGTATYSGNPFVGVTPWANAYYASEVSSLAIPSLTGAMATAAAAVAKVPSFMWLDTLDKTPLMEQTLADIRTANKNGGNYAGQFVVYDLPDRDCAALASNGEYSIADGGVAKYKNYIDTIRQIVVEYSDIRTLLVIEPDSLANLVTNLGTPKCANAQSAYLECINYAVTQLNLPNVAMYLDAGHAGWLGWPANQDPAAQLFANVYKNASSPRAL... | 3.2.1.91 | null | cellulose catabolic process [GO:0030245] | extracellular region [GO:0005576] | cellulose 1,4-beta-cellobiosidase activity [GO:0016162]; cellulose binding [GO:0030248] | PF00734;PF01341; | 3.20.20.40; | Glycosyl hydrolase 6 (cellulase B) family | PTM: Asn-334 contains mainly a high-mannose-type glycan (Hex(7-9)GlcNAc(2)) in a 3:1 ration with a single GlcNAc. Asn-313 was primarily unglycosylated with a small fraction (18%) bearing a single GlcNAc at this site. {ECO:0000269|PubMed:12499406}. | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P07987}. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains.; EC=3.2.1.91; Evidence={ECO:0000250|UniProtKB:P07987}; | null | null | null | null | FUNCTION: Exocellobiohydrolases (CBH) that catalyzes the hydrolysis of 1,4-beta-D-glucosidic bonds in cellulose to release the disaccharide cellobiose. The degradation of cellulose involves an interplay between different cellulolytic enzymes. Hydrolysis starts with endoglucanases (EGs), which cut internal beta-1,4-gluc... | Trichoderma reesei (strain ATCC 56765 / BCRC 32924 / NRRL 11460 / VTT-D-86271 / Rut C-30) (Hypocrea jecorina) | [
257,
2554,
6485,
8481,
8683,
9557,
16198,
21109,
24983
] | [
"ec: EC 3.2.1.91",
"go_bp: cellulose catabolic process (GO:0030245)",
"go_cc: extracellular region (GO:0005576)",
"go_mf: cellulose 1,4-beta-cellobiosidase activity (GO:0016162)",
"go_mf: cellulose binding (GO:0030248)",
"interpro: Cellulose-binding domain (IPR000254)",
"interpro: Cellulose-binding doma... | [
"UniProtKB=ECO:0000250",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000250",
"UniProtKB-GO=ECO:0000250",
"UniProtKB-GO=ECO:0000501",
"InterPro=match",
"InterPro=match",
"InterPro=match:Pfam",
"UniProtKB=ECO:0000250"
] | Function: Exocellobiohydrolases (CBH) that catalyzes the hydrolysis of 1,4-beta-D-glucosidic bonds in cellulose to release the disaccharide cellobiose. The degradation of cellulose involves an interplay between different cellulolytic enzymes. Hydrolysis starts with endoglucanases (EGs), which cut internal beta-1,4-gluc... |
A0A024SIB3 | XYN3_TRIR3 | MKANVILCLLAPLVAALPTETIHLDPELAALRANLTERTADLWDRQASQSIDQLIKRKGKLYFGTATDRGLLQREKNAAIIQADLGQVTPENSMKWQSLENNQGQLNWGDADYLVNFAQQNGKSIRGHTLIWHSQLPAWVNNINNADTLRQVIRTHVSTVVGRYKGKIRAWDVVNEIFNEDGTLRSSVFSRLLGEEFVSIAFRAARDADPSARLYINDYNLDRANYGKVNGLKTYVSKWISQGVPIDGIGSQSHLSGGGGSGTLGALQQLATVPVTELAITELDIQGAPTTDYTQVVQACLSVSKCVGITVWGISDKDSW... | 3.2.1.8 | null | xylan catabolic process [GO:0045493] | extracellular region [GO:0005576] | endo-1,4-beta-xylanase activity [GO:0031176] | PF00331; | 3.20.20.80; | Glycosyl hydrolase 10 (cellulase F) family | PTM: Not glycosylated. {ECO:0000250|UniProtKB:Q9P973}. | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9P973}. | CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.; EC=3.2.1.8; Evidence={ECO:0000250|UniProtKB:Q9P973}; | null | PATHWAY: Glycan degradation; xylan degradation. {ECO:0000255|PROSITE-ProRule:PRU01096}. | null | null | FUNCTION: Glycoside hydrolase involved in the hydrolysis of xylan, a major plant cell wall hemicellulose made up of 1,4-beta-linked D-xylopyranose residues. Catalyzes the endohydrolysis of the main-chain 1,4-beta-glycosidic bonds connecting the xylose subunits yielding various xylooligosaccharides and xylose. Produces ... | Trichoderma reesei (strain ATCC 56765 / BCRC 32924 / NRRL 11460 / VTT-D-86271 / Rut C-30) (Hypocrea jecorina) | [
242,
3908,
6485,
8735,
9934,
13891,
17791,
20803,
24983
] | [
"ec: EC 3.2.1.8",
"go_bp: xylan catabolic process (GO:0045493)",
"go_cc: extracellular region (GO:0005576)",
"go_mf: endo-1,4-beta-xylanase activity (GO:0031176)",
"interpro: Glycoside hydrolase family 10 domain (IPR001000)",
"interpro: Glycoside hydrolase superfamily (IPR017853)",
"interpro: Glycoside ... | [
"UniProtKB=ECO:0000250,ECO:0000255",
"UniProtKB-GO=ECO:0000501",
"UniProtKB-GO=ECO:0000250",
"UniProtKB-GO=ECO:0000250",
"InterPro=match",
"InterPro=match",
"InterPro=match",
"InterPro=match:Pfam",
"UniProtKB=ECO:0000250"
] | Function: Glycoside hydrolase involved in the hydrolysis of xylan, a major plant cell wall hemicellulose made up of 1,4-beta-linked D-xylopyranose residues. Catalyzes the endohydrolysis of the main-chain 1,4-beta-glycosidic bonds connecting the xylose subunits yielding various xylooligosaccharides and xylose. Produces ... |
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