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Database: UniProt
Entry: A0A3B3CR57_ORYME
LinkDB: A0A3B3CR57_ORYME
Original site: A0A3B3CR57_ORYME 
ID   A0A3B3CR57_ORYME        Unreviewed;      1611 AA.
AC   A0A3B3CR57;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
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:ENSOMEP00000020363.1};
OS   Oryzias melastigma (Marine medaka).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC   Oryzias.
OX   NCBI_TaxID=30732 {ECO:0000313|Ensembl:ENSOMEP00000020363.1, ECO:0000313|Proteomes:UP000261560};
RN   [1] {ECO:0000313|Ensembl:ENSOMEP00000020363.1}
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; 30732.ENSOMEP00000020363; -.
DR   PaxDb; 30732-ENSOMEP00000020363; -.
DR   Ensembl; ENSOMET00000036074.1; ENSOMEP00000020363.1; ENSOMEG00000022347.1.
DR   GeneTree; ENSGT00940000158294; -.
DR   OrthoDB; 5480520at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000261560; 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; 2.
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   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PROSITE-ProRule:PRU00104}.
FT   DOMAIN          185..318
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          856..889
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          1023..1056
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          1276..1611
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   REGION          368..555
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          585..644
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          757..837
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          885..908
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          920..947
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1202..1224
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        399..441
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        525..550
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        588..615
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        932..947
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1205..1219
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1579
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   1611 AA;  180028 MW;  47C1F233325EF297 CRC64;
     MIHRQVLLPQ NLYQNRLLSL AAMASPTRSG PTRQRCKDVA RHSYGAETYN VNGLNQEAFL
     LGLSRSTSDT DLVSPDARST LTVSSSHYTI GQSEDLVISW DIKEEVDAGD WIGMYQVDEV
     LSENFLDYKN RGISGSHKGQ IVWKIESGAN FSDVETQVCF RYYHGVTGAL RATTPSVTIK
     KSAPPVSKPV VSPEVNHGMG NRRLINFWLS DLQAVGLKKG MFFNPDPYLK LSIQPGKHSI
     FPSLPHHGQE KRSRVVCNTI NPQWTTERFN FVSLPTDVLE IEVKDKFAKS RPIIKRFLGK
     LSVPVQRLLE KHAIGDRVVS YSLGRRVPTD HVCGQLLFRF ELTSSIHPDD EEVSLVIETA
     CAEAANAADD AGGAADDDTL SVGPDMPNLP LDAPPEAENS PPTHEEETHP AEREEEEGGA
     QVEQGGTEEE EDRREEPPAI QQQEENEEQQ EANGIQEEGG EARAEEEQRQ EVAPQSPAVE
     SKDGDEEELG ASSGGAAAVE APSEESATGA GEGAPKGETE GGERSSPPCS CQPPSSNLNS
     NASSRRKNRP CSLPVSELET VIASACGEPE TPRSHYIRIH HLLHSLPSAQ QRAPSQEGED
     TSSTVDATSP TLKTSKEENG PEEEEEDDDT TQSPSQVPEC PGPCCRRSLP RSLSIERLSE
     LNQLLEGDGG RGHPVMRRIS PSCLDSEEGD SSNGGRRVCG GTHRPLGENE CEFCDTSCYS
     TSCYSTSCYS TSCYSNSGFE GRGRFCSHNR LSSVDSNRLS GSTVFSSQDE EDEEESAFES
     VPDFAHPEGQ NLGGPEGGRT PPSGCKENRR GEQGEPAVAG PSDRNGIGSD SSPPVDHLPV
     LRPSHDLNHF PAATDQALPP NWEARIDSHG RVFYVDHVNR TTTWQRPSHS TKCNHGIPRS
     SSTQQMEQLN RRYQNIQRTM ATEEDGGSRS SDGDSDSPQT GPSSPVNQQK ITHLLQSPAV
     KFVTHPEFFT VLHSNYAAYR MFTSSSCVKH MVLKVRRDAR NFERYQHNRD LVVFINKFAD
     TQLELPRGWE IKTDPQGKSF FVDHNSRATT FIDPRIPLQN GRLPGHLAHK QHLQRLRSYS
     AGEASEVSRS RGASLMVRPG NSLVAAIRSQ HQPDSQPLSA PSYNDKIVAF LRQPNIFDML
     QERQPSLSRN HALREKIHYI RTEGTQGVEK LSCDADLVIL LSLFEEEIMS YAPPHPIHPG
     FSFSPRCSPA SSPQNSPGLQ RARAPAPYRR DFEAKLRNFY RKLEAKGYGQ GPGKIKLLIR
     REHLLEGTFN QVMAYSRKEL QRNKLYVTFL GEEGLDYSGP SREFFFLLSQ ELFNPYYGLF
     EYSANDTYTV QISPMSAFVE NHLEWFRFSG RILGLALIHQ YLLDAFFTRP FYKALLRLPT
     DLSDLEYLDE EFHQSLQWMK DNDITDILEL TFTVNEEVFG QVTERELKSG GSNLQVTEKN
     KKDYIERMTK WRVERGVVQQ TEALVRGFYE VVDSRLVSVF DARELELVIA GTVEIDLNDW
     RSNTEYRGGY HDGHIVMRWF WAAVERFNNE QRLRLLQFVT GTSSVPYEGF AALRGSNGLR
     RFCIEKWGKV TSLPRAHTCF NRLDLPPYPS YTILYEKLLI AVEETSTFGL E
//
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