ID A0A452I144_9SAUR Unreviewed; 1390 AA.
AC A0A452I144;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
OS Gopherus agassizii (Agassiz's desert tortoise).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Testudinidae; Gopherus.
OX NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000021205.1, ECO:0000313|Proteomes:UP000291020};
RN [1] {ECO:0000313|Proteomes:UP000291020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28562605;
RA Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT "The Agassiz's desert tortoise genome provides a resource for the
RT conservation of a threatened species.";
RL PLoS ONE 12:e0177708-e0177708(2017).
RN [2] {ECO:0000313|Ensembl:ENSGAGP00000021205.1}
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; 38772.ENSGAGP00000021205; -.
DR Ensembl; ENSGAGT00000024150.1; ENSGAGP00000021205.1; ENSGAGG00000015536.1.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000291020; 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; 2.60.40.150; 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; 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; 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:UP000291020};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 1..130
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 616..649
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 802..835
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 1055..1390
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 305..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 441..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 512..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 700..722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..323
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..402
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 704..722
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1358
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1390 AA; 157307 MW; C33D2DACF98E4391 CRC64;
GKIYISFFQG QGSRRLINFS LSDFQALGLK KGMFFNPDPY LKISIQPGKH SIFPALPHHG
QEKRSKITYN TVNPIWQGEQ FSFVSLPTDV LEIEVKDKFA KSRPIIKRFL GKLSMPVQRL
LERHAIGDRV VSYTLGRRLP TDHVSGQLQF RFEITSSIHP DDEEVSISAD PESAELQESP
VNSAAEEILG EPPCTGTVTS ESTAPEQLNG CNVNGVNVDS PGEVNQNSLN EELAGNREVD
AVPADAIESL ESIPGEVLPS LSAMDLSEQL ALLGHNDIFT SIEALDIDEV SADIQTVKDL
EKIQDEEGAS AQEEEDSKLQ LRTTGKRKNR PCSLPVSELE TVIASACGEP ETPRTHYIRI
HNLLHSLPSA QMSSDGEEEQ GGGEDEESTV KETSEKDVVS ESETLAADPP PESGTDEYFS
RGIVPRSTSV EHLSDLNEQL LDGEHPMTGS ESESSSRPYG DSECDTSCYS PSCYSTSCYS
TSCYSTSCYS PSCYDSNNRF SSHTRFSSVD SAKISESTVF SSQDDEEEEN SAFESVPDSM
QSPELDREQV DVSAQWPDEL VAHGGNPQRA TETLESTVAG PSNRREGDCP LLHNSQPVSQ
LPSLRSDHHH YPTIDEPLPP NWEARIDSHG RVFYVDHVNR TTTWQRPTAA ATPDGIRRSG
SIQQMEQLNR RYQNIQRTIA TERPEEDSIV NNRAERLSIG GGSDSEADFS QPNSEIRREG
SLSPVNSQKI TLLLQSPAVK FITNPEFFTV LHANYSAYRV FTNSTCLKHM ILKIRRDARN
FERYQHNRDL VNFINMFADT RLELPRGWEI KTDQQGKSFF VDHNSRATTF IDPRIPLQNG
RLPNHLTHRQ HLQRLRSYSA GEASEVSRNR SISLLTRPGN SLVTAIRNQH HHESLPLAYN
DKIVAFLRQP NIFEMLQERQ PSLARNHALR EKIHYIRTEG THGLEKLSCD ADLVILLSLF
EEDIMSYIPL QAAFHPGYSF SPRCSPCSSP QNSPGLQRAS ARAPSPYRRD FEAKLRNFYR
KLEAKGYGQG PGKIKLIIRR DHLLEGTFNQ VMAYSRKELQ RNKLYITFVG EEGLDYSGPS
REFFFLLSQE LFNPYYGLFE YSANDTYTVQ ISPMSAFVEN HLEWFKFSGR ILGLALIHQY
LLDAFFTRPF YKALLRLPCD LSDLEYLDEE FHQSLQWMKD NNITDILDLT FTVNEEVFGQ
VTERELKSGG SNTQVTEKNK KEYIERMVKW RVERGVVQQT EALVRGFYEV VDSRLVSIFD
ARELELVIAG TAEIDLNDWR NNTEYRGGYH DGHIVIRWFW AAVERFNNEQ RLRFLQFVTG
TSSVPYEGFA ALRGSNGLRR FCIEKWGKIT SLPRAHTCFN RLDLPPYPSY SMLYEKLLTA
VEETSTFGLE
//
