ID A0A093S7C8_9PASS Unreviewed; 1545 AA.
AC A0A093S7C8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
DE Flags: Fragment;
GN ORFNames=N305_04963 {ECO:0000313|EMBL:KFW78799.1};
OS Manacus vitellinus (golden-collared manakin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Pipridae; Manacus.
OX NCBI_TaxID=328815 {ECO:0000313|EMBL:KFW78799.1, ECO:0000313|Proteomes:UP000053258};
RN [1] {ECO:0000313|EMBL:KFW78799.1, ECO:0000313|Proteomes:UP000053258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N305 {ECO:0000313|EMBL:KFW78799.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-2014) 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}.
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DR EMBL; KL670320; KFW78799.1; -; Genomic_DNA.
DR STRING; 328815.ENSMVIP00005014762; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000053258; 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; 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:UP000053258};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 150..286
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 771..804
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 957..990
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 1210..1545
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 313..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 427..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 469..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 519..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 660..761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 834..877
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..339
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..447
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..554
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..582
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..617
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 660..674
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 859..877
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1513
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFW78799.1"
FT NON_TER 1545
FT /evidence="ECO:0000313|EMBL:KFW78799.1"
SQ SEQUENCE 1545 AA; 174291 MW; 561B0BA74D302A18 CRC64;
RRCKEPLRYS YNPDQFHNMD IRNNSHETVT IPRSTSDTDL VTSDSRSTLM VSSSYYSIGH
SQDLVIYWDI KEEVDAGDWI GMYLIDEVLS ENFLDYKNRG VNGSHRGQII WKIDASSYFV
EPETKICFKY YHGVSGALRA TTPSVTVKNN AAPIFKSITN EDSIQGQGNR RLISFSLSDF
QAFGLKKGMF FNPDPYLKIS IQPGKHSIFP ALPHHGQEKR SKIMCNTVNP IWQGEQFSFV
SLPTDVLEIE VKDKFAKSRP IIKRFLGKLS MPVQRLLERH AIGDRVVSYT LGRRLPTDHV
SGQLQFRFEI TSSIHPDPEP ADLQESPVNN PTEESLGEPP CINTVTSESA APEQLNGYSV
NSVDSPGAVK PPGEVNQNSL NEELAGDGEV DAVPVPEPLE SIPGEMLSSL SATDLTEQST
LMACMSPPET EVRENNKVNS GIQGDGGVTS IETLDIDEVS ADVHAGKDLE KSQEEDEGAS
AQEEEDNKLQ LRTTAKRKNR PCSLPVSELE TVIASACAQM SSDGEEEQDG GNGGENDEES
TVKEVLDKEV VSESETVAAE PPLENEAEEN FSQRTVPPET LDEQLSDLND GLLDGEPLRT
GSESESSSRP NGDNECETCD TSCYSPSCYS TSCYSTSCYS TSCYSTSCYD SNNRFSSHTR
FSSVDSAKIS ESTVFSSQDD DEEENSAFES VPDSVQSPEL DREQVDGSSQ WPDELVAHAG
NPQRATEGLD TPIAGPSSRR EGDCPLLHNS QPVSQLPSLR PDHHHYPTID EPLPPNWEAR
IDSHGRVFYV DHVNRTTTWQ RPTAAATPDG IHRSGSIQQM EQLNRRYQNI QRTIATERTD
DDAVVNNRVE RVPTGGGSDS EAEPSQPSSE IRREGSLSPV NSQKITLLLQ SPAVKFITNP
EFFTVLHANY SAYRVFTNST CLKHMILKIR RDARNFERYQ HNRDLVNFIN MFADTRLELP
RGWEIKTDQQ GKSFFVDHNS RATTFIDPRI PLQNGRLPNH LTHRQHLQRL RSYSAGEASE
VSRNRGVTLL ARPGNSLVTA IRNQHHHEAL PLAYNDKIVA FLRQPNIFEM LQERQPSLAR
NHALREKIHY IRTEGTHGLE KLSCDADLVI LLSLFEEDIM SYIPLQAAFH PGYSFSPRCS
PCSSPQNSPG LQRASARAPS PYRRDFEAKL RNFYRKLEAK GYGQGPGKIK LIIRRDHLLE
GTFNQVMAYS RKELQRNKLY VTFVGEEGLD YSGPSREFFF LLSQELFNPY YGLFEYSAND
TYTVQISPMS AFVENHLEWF RFSGRILGLA LIHQYLLDAF FTRPFYKALL RLPCDLSDLE
YLDEEFHQSL QWMKDNNITD ILDLTFTVNE EVFGQVTERE LKSGGANTAV TEKNKKEYIE
RMVKWRVERG VVQQTEALVR GFYEVVDSRL VSVFDARELE LVIAGTAEID LNDWRNNTEY
RGGYHDGHIV IRWFWAAVER FNNEQRLRLL QFVTGTSSVP YEGFAALRGS NGLRRFCIEK
WGKITSLPRA HTCFNRLDLP PYPSYSMLYE KLLTAVEETS TFGLE
//
