ID H0YUB0_TAEGU Unreviewed; 1614 AA.
AC H0YUB0;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 73.
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:ENSTGUP00000001878.2};
OS Taeniopygia guttata (Zebra finch) (Poephila guttata).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC Estrildinae; Taeniopygia.
OX NCBI_TaxID=59729 {ECO:0000313|Ensembl:ENSTGUP00000001878.2, ECO:0000313|Proteomes:UP000007754};
RN [1] {ECO:0000313|Ensembl:ENSTGUP00000001878.2, ECO:0000313|Proteomes:UP000007754}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20360741; DOI=10.1038/nature08819;
RA Warren W.C., Clayton D.F., Ellegren H., Arnold A.P., Hillier L.W.,
RA Kunstner A., Searle S., White S., Vilella A.J., Fairley S., Heger A.,
RA Kong L., Ponting C.P., Jarvis E.D., Mello C.V., Minx P., Lovell P.,
RA Velho T.A., Ferris M., Balakrishnan C.N., Sinha S., Blatti C., London S.E.,
RA Li Y., Lin Y.C., George J., Sweedler J., Southey B., Gunaratne P.,
RA Watson M., Nam K., Backstrom N., Smeds L., Nabholz B., Itoh Y., Whitney O.,
RA Pfenning A.R., Howard J., Volker M., Skinner B.M., Griffin D.K., Ye L.,
RA McLaren W.M., Flicek P., Quesada V., Velasco G., Lopez-Otin C.,
RA Puente X.S., Olender T., Lancet D., Smit A.F., Hubley R., Konkel M.K.,
RA Walker J.A., Batzer M.A., Gu W., Pollock D.D., Chen L., Cheng Z.,
RA Eichler E.E., Stapley J., Slate J., Ekblom R., Birkhead T., Burke T.,
RA Burt D., Scharff C., Adam I., Richard H., Sultan M., Soldatov A.,
RA Lehrach H., Edwards S.V., Yang S.P., Li X., Graves T., Fulton L.,
RA Nelson J., Chinwalla A., Hou S., Mardis E.R., Wilson R.K.;
RT "The genome of a songbird.";
RL Nature 464:757-762(2010).
RN [2] {ECO:0000313|Ensembl:ENSTGUP00000001878.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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; 59729.ENSTGUP00000001878; -.
DR Ensembl; ENSTGUT00000001896.2; ENSTGUP00000001878.2; ENSTGUG00000001817.2.
DR GeneTree; ENSGT00940000158294; -.
DR HOGENOM; CLU_002173_14_0_1; -.
DR InParanoid; H0YUB0; -.
DR OMA; SGSQNCE; -.
DR TreeFam; TF313938; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000007754; Chromosome 2.
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:UP000007754};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 182..318
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 840..873
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 1026..1059
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 1279..1614
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 349..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 460..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 502..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 582..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 729..840
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 906..947
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..517
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..618
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..646
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..682
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 729..743
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 928..947
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1582
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1614 AA; 181942 MW; 6DA8A40FF0D83952 CRC64;
MLLHLCSVKN LYQNRFLGLA AMASPSRNSQ NRRRCKEPLR YSYNPDQFHN MDIRNNSHET
VTIPRSTSDT DLVTSDSRST LMVSSSYYSI GHSQDLVIYW DIKEEVDAGD WIGMYLIDEV
LSENFLDYKN RGVNGSHRGQ IIWKIDASSY FVEPETKICF KYYHGVSGAL RATTPSVTVK
NNAAPIFKSI TNEDSVQGQG SRRLISFSLS DFQAFGLKKG MFFNPDPYLK ISIQPGKHSI
FPALPHHGQE KRSKIICNTV NPVWQGEQFS FVSLPTDVLE IEVKDKFAKS RPIIKRFLGK
LSMPVQRLLE RHAIGDRVVS YTLGRRLPTD HVSGQLQFRF EITSSIHPDD EEVSISADPE
PADLPESPVN NPTEESLGEP PCINTVTSES AAPEQLNGYS VNSVDSPGAV KPPGEVNQNS
LNEELAGDGE VDAVPVPEPL ESIPGEVLLL SATDLMEQSD PTACMSPPEP EVRENDKVNS
GMQGDGGVLT SVETVDIDEV SADVHAGKDL EKSQEEEEEG ASAQEEEDSK LQLRTTAKRK
NRPCSLPVSE LETVIASACG EPETPRTHYI RIHNLLHSLP SAQMSSDGEE EQDGGNGREN
DEESTVKEVM DKEVVSESET MAAEPPLENE AEENFSQNTV PPGTLDEQLS DLNDGLLDGE
PPRTGSESES SSRPNGDNEC EACDTSCYSP SCYSPSCYST SCYSTSCYST SCYSTSCYDS
NNRFSSHTRF SSVDSAKISE STVFSSQDDD EEENSAFESV PDSVQSPELD REQVDGSSQW
PDELVAHGGN PQRATEGLDT PVAGPSSRRE GDCPLLHNSQ PVSQLPSLRP DHHHYPTIDE
PLPPNWEARI DSHGRVFYVD HVNRTTTWQR PTAAATPDGI HRSGSIQQME QLNRRYQNIQ
RTIATERTED DAVVNNRVER VPTGGGSDSE AEPSQPSPEI RREGSLSPVN SQKITLLLQS
PAVKFITNPE FFTVLHANYS AYRVFTNSTC LKHMILKIRR DARNFERYQH NRDLVNFINM
FADTRLELPR GWEIKTDQQG KSFFVDHNSR ATTFIDPRIP LQNGRLPNHL THRQHLQRLR
SYSAGEASEV SRNRGVTLLA RPGNSLVTAI RNQHHHEALP LAYNDKIVAF LRQPNIFEML
QERQPSLARN HALREKIHYI RTEGTHGLEK LSCDADLVIL LSLFEEDIMS YIPLQAAFHP
GYSFSPRCSP CSSPQNSPGL QRASARAPSP YRRDFEAKLR NFYRKLEAKG YGQGPGKIKL
IIRRDHLLEG TFNQVMAYSR KELQRNKLYV TFVGEEGLDY SGPSREFFFL LSQELFNPYY
GLFEYSANDT YTVQISPMSA FVENHLEWFR FSGRILGLAL IHQYLLDAFF TRPFYKALLR
LPCDLSDLEY LDEEFHQSLQ WMKDNNITDI LDLTFTVNEE VFGQVTEREL KSGGANTAVT
EKNKKEYIER MVKWRVERGV VQQTEALVRG FYEVVDSRLV SVFDARELEL VIAGTAEIDL
NDWRNNTEYR GGYHDGHIVI RWFWAAVERF NNEQRLRLLQ FVTGTSSVPY EGFAALRGSN
GLRRFCIEKW GKITSLPRAH TCFNRLDLPP YPSYSMLYEK LLTAVEETST FGLE
//
