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Database: UniProt
Entry: A0A2K6STW2_SAIBB
LinkDB: A0A2K6STW2_SAIBB
Original site: A0A2K6STW2_SAIBB 
ID   A0A2K6STW2_SAIBB        Unreviewed;      1606 AA.
AC   A0A2K6STW2;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE            EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN   Name=HECW1 {ECO:0000313|Ensembl:ENSSBOP00000010816.1};
OS   Saimiri boliviensis boliviensis (Bolivian squirrel monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Saimiriinae; Saimiri.
OX   NCBI_TaxID=39432 {ECO:0000313|Ensembl:ENSSBOP00000010816.1, ECO:0000313|Proteomes:UP000233220};
RN   [1] {ECO:0000313|Ensembl:ENSSBOP00000010816.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.26; Evidence={ECO:0000256|ARBA:ARBA00000885};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
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DR   STRING; 39432.ENSSBOP00000010816; -.
DR   Ensembl; ENSSBOT00000027594.1; ENSSBOP00000010816.1; ENSSBOG00000022224.1.
DR   GeneTree; ENSGT00940000158294; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000233220; Unplaced.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   CDD; cd08691; C2_NEDL1-like; 1.
DR   CDD; cd00078; HECTc; 1.
DR   CDD; cd00201; WW; 2.
DR   Gene3D; 2.20.70.10; -; 2.
DR   Gene3D; 2.60.40.2840; -; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
DR   Gene3D; 3.30.2160.10; Hect, E3 ligase catalytic domain; 1.
DR   Gene3D; 3.30.2410.10; Hect, E3 ligase catalytic domain; 1.
DR   Gene3D; 3.90.1750.10; Hect, E3 ligase catalytic domains; 1.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR037795; C2_HECW.
DR   InterPro; IPR000569; HECT_dom.
DR   InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR   InterPro; IPR040524; HECW1_helix.
DR   InterPro; IPR032348; HECW_N.
DR   InterPro; IPR001202; WW_dom.
DR   InterPro; IPR036020; WW_dom_sf.
DR   PANTHER; PTHR11254:SF79; E3 UBIQUITIN-PROTEIN LIGASE HECW1; 1.
DR   PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF00632; HECT; 1.
DR   Pfam; PF18436; HECW1_helix; 1.
DR   Pfam; PF16562; HECW_N; 1.
DR   Pfam; PF00397; WW; 1.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00119; HECTc; 1.
DR   SMART; SM00456; WW; 2.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR   SUPFAM; SSF51045; WW domain; 2.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS50237; HECT; 1.
DR   PROSITE; PS01159; WW_DOMAIN_1; 2.
DR   PROSITE; PS50020; WW_DOMAIN_2; 2.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000233220};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PROSITE-ProRule:PRU00104}.
FT   DOMAIN          183..319
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          829..862
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          1018..1051
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          1271..1606
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   REGION          350..414
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          479..539
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          573..672
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          730..815
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          894..938
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        358..375
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        479..515
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        649..665
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        747..761
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        920..938
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1574
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   1606 AA;  179440 MW;  51277F7B2CA9DB85 CRC64;
     MICAQTRAAK NLYQNRFLGL AAMASPSRNS QSRRRCKEPL RYSYNPDQFH NMDLRGGPHD
     GVTIPRSTSD TDLVTSDSRS TLMVSSSYYS IGHSQDLVIH WDIKEEVDAG DWIGMYLIDE
     VLSENFLDYK NRGVNGSHRG QIIWKIDASS YFVEPETKIC FKYYHGVSGA LRATTPSVTV
     KNSAAPIFKS IGSDETVQGQ GSRRLISFSL SDFQAMGLKK GMFFNPDPYL KISIQPGKHS
     IFPALPHHGQ ERRSKIIGNT VNPIWQAEQF SFVSLPTDVL EIEVKDKFAK SRPIIKRFLG
     KLSMPVQRLL ERHAIGDRVV SYTLGRRLPT DHVSGQLQFR FEITSSIHPD DEEISLSTEP
     ESAQIQDSPM NNVVENGSGD PRAEAPEPSE SWKPEQLGEG SVLDGPGNQS MELSRTTEEA
     AIITETGDQG MVSVGPEGAG ELLAQVQKDI QPAPSAEELA EQLDLGEEAS ALLLEDGDVP
     ASTKEEHVEE ETTAQSLAGR EEEKEREEEV GDVSALEQGE GRLQLRASVK RKSRPCSLPV
     SELETVIASA CGDPETPRTH YIRIHTLLHS MPSAQGSSVA EDEDGAEEST LKDSSEKDGL
     SEVDTVAADP SALEEDGEEP EGATPGTAPP GHTGDHFPSL ANGAAPDGDT HPSTGSESDS
     SPRQGGDHSC EGCDASCCSP SCYSSSCYST SCYSSSCYSA SCYSPSCYNG NRFASHTRFS
     SVDSAKISES TVFSSQDDDD EENSAFESVP DSMQSPELDP ESTNGAGPWQ DELAAPGGHV
     ERTPEGLESP VAGPSNRREG ECPILHNSQP VSQLPSLRPE HHHYPTIDEP LPPNWEARID
     SHGRVFYVDH VNRTTTWQRP TAAATPDGMR RSGSIQQMEQ LNRRYQNIQR TIATERPEED
     SGSQSCEQAP AGGGGGGGSD SEAESSQSSL DLRREGSLSP VNSQKITLLL QSPAVKFITN
     PEFFTVLHAN YSAYRVFTSS TCLKHMILKV RRDARNFERY QHNRDLVNFI NMFADTRLEL
     PRGWEIKTDQ QGKSFFVDHN SRATTFIDPR IPLQNGRLPN HLTHRQHLQR LRSYSAGEAS
     EVSRNRGASL LTRPGHSLVA AIRSQHQHES LPLAYNDKIV AFLRQPNIFE MLQERQPSLA
     RNHALREKIH YIRTEGNHGL EKLSCDADLV ILLSLFEEEI MSYVPLQAAF HPGYSFSPRC
     SPCSSPQNSP GLQRASARAP SPYRRDFEAK LRNFYRKLEA KGFGQGPGKI KLIIRRDHLL
     EGTFNQVMAY SRKELQRNKL YVTFVGEEGL DYSGPSREFF FLLSQELFNP YYGLFEYSAN
     DTYTVQISPM SAFVENHLEW FRFSGRILGL ALIHQYLLDA FFTRPFYKAL LRLPCDLSDL
     EYLDEEFHQS LQWMKDNNIT DILDLTFTVN EEVFGQVTER ELKSGGANTQ VTEKNKKEYI
     ERMVKWRVER GVVQQTEALV RGFYEVVDSR LVSVFDAREL ELVIAGTAEI DLNDWRNNTE
     YRGGYHDGHL VIRWFWAAVE RFNNEQRLRL LQFVTGTSSV PYEGFAALRG SNGLRRFCIE
     KWGKITSLPR AHTCFNRLDL PPYPSYSMLY EKLLTAVEET STFGLE
//
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