ID A0A0P7YTN5_SCLFO Unreviewed; 1335 AA.
AC A0A0P7YTN5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN ORFNames=Z043_110110 {ECO:0000313|EMBL:KPP71015.1};
OS Scleropages formosus (Asian bonytongue) (Osteoglossum formosum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Osteoglossidae; Scleropages.
OX NCBI_TaxID=113540 {ECO:0000313|EMBL:KPP71015.1, ECO:0000313|Proteomes:UP000034805};
RN [1] {ECO:0000313|EMBL:KPP71015.1, ECO:0000313|Proteomes:UP000034805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Aro1 {ECO:0000313|EMBL:KPP71015.1};
RA Tan M.H., Gan H.M., Croft L.J., Austin C.M.;
RT "The genome of the Asian arowana (Scleropages formosus).";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPP71015.1}.
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DR EMBL; JARO02003181; KPP71015.1; -; Genomic_DNA.
DR STRING; 113540.ENSSFOP00015016031; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000034805; Unassembled WGS sequence.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd00078; HECTc; 1.
DR CDD; cd00201; WW; 2.
DR Gene3D; 2.20.70.10; -; 2.
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; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR040524; HECW1_helix.
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; PF00632; HECT; 1.
DR Pfam; PF18436; HECW1_helix; 1.
DR Pfam; PF00397; WW; 1.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00456; WW; 2.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR SUPFAM; SSF51045; WW domain; 2.
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:UP000034805};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 571..604
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 750..783
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 1000..1335
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 134..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 403..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 471..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 633..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 927..948
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..359
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 637..651
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1303
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1335 AA; 149757 MW; C60DD0750D08605A CRC64;
MVAFSVSTGI GITLTVHPEG LGSGTTAQAG QQPMQGAGGQ KMRRFNFVSL PTDVLEIEVK
DKFSKSRPII KRFLGKLSMP VQRLLEKHAI GYTLGRRLPT DHVSGQLQFR FEITSSIHPD
DEEASLCTEP DCEQVENPEA NHPCEPYPDD ADTLSLGPEM PELPADGVTV DTEADSVPPA
PSPTELSPAE PGGSESFWAE TGGVEPVGTE PGGVESVGTE PGRVESVGTE PEGAEFAGAE
SGEVGPLEAK CQDVEPEGEE SVDMESVGTL TLREDDGDEE CSSPCLRSFP KRRSRPCSLP
VSELETVIAS VCGEPETPRT HYIRIHHLLH SLPSAQHSQD TDPDPDSEEM TLRPSEDKEN
GEQEEEDEGA SEGQDGPGPC CRRTLPRSLS IERLSDLNQL LESEPPCLDS ESETGGQRQP
RDSECDLCDT SCYSTSCYST SCYSTSCYST SGHEGRNRFC SHTRFSSVDS ARLSESNVFS
SQEEEEESSA FESVADSMQG LEVRDPGSAP WQEEQALGEG SPGSTEGSRG SPMAGPSERT
EGSCPLPCSH PAVSQPPALR PDPHHYPTVD EPLPPNWEAR IDSHGRVFYV DHVNRTTTWQ
HPCTAGLANG IHRSGSIQQM EQLNRRYQNI QRTMATEDES NGRRSERINS TDAEMDSPPP
AGELRRESPS SPINSQKMGL LLQCPAVKFI AHPEFFTVLH ANYGAYRMFT NSTCLKHMIL
KIRRDARNFE RYQHNRDLVA FLNKFADTQL ELPRGWEIKS DQQGKFFFVD HNSRATTFID
PRIPLQNGRL PNHLTHRQHL QRLRSYSAGE ASEVSRSRGA SLLARPGNSL VAAIRSQHHQ
DPMPLAYNDK IVAFLRQPHI FDMLQERQPS LARNHALREK IHYIRTEGTQ GVEKLSCDAD
LVILLSLFEE DIMSYIPPHS FHPGYGFSPR CSPGSSPQNS PGLQRARAPA PYRRDFEAKL
RNFYRKLEAK GYGQGPGKIK LLVRRDHLLE GTFNQVMAYS RKELQRNKLY VTFVGEEGLD
YSGPSREFFF LLSQELFNPY YGLFEYSAND TYMVQISPMS AFVENHLEWF RFSGRILGLA
LIHQYLLDAF FTRPFYKALL RLPTDLSDLE YLDEEFHQSL QWMKDNDITD ILDLTFTVNE
EVFGQVTERE LKSGGANIQV TEKNKKEYME RLVKWRVERG VVQQTEALVR GFYEVVDSRL
VSVFDARELE LVIAGTAEID LNDWRNNTEY RGGYHDGHIV IRWFWGAVER FNNEQRLRLL
QFVTGTSSVP YEGFAALRGS NGLRRFCIEK WGKISSLPRA HTCFNRLDLP AYPSYTMLYE
KLLIAVEETS TFGLE
//
