ID A0A016WQD0_9BILA Unreviewed; 1049 AA.
AC A0A016WQD0;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=HECT domain-containing protein {ECO:0000259|PROSITE:PS50237};
GN Name=Acey_s0568.g55 {ECO:0000313|EMBL:EYC41467.1};
GN ORFNames=Y032_0568g55 {ECO:0000313|EMBL:EYC41467.1};
OS Ancylostoma ceylanicum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=53326 {ECO:0000313|EMBL:EYC41467.1, ECO:0000313|Proteomes:UP000024635};
RN [1] {ECO:0000313|Proteomes:UP000024635}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX PubMed=25730766; DOI=10.1038/ng.3237;
RA Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA Aroian R.V.;
RT "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT ceylanicum identify infection-specific gene families.";
RL Nat. Genet. 47:416-422(2015).
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:EYC41467.1}.
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DR EMBL; JARK01000168; EYC41467.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A016WQD0; -.
DR STRING; 53326.A0A016WQD0; -.
DR Proteomes; UP000024635; Unassembled WGS sequence.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR CDD; cd00078; HECTc; 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 Gene3D; 2.130.10.30; Regulator of chromosome condensation 1/beta-lactamase-inhibitor protein II; 2.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR009091; RCC1/BLIP-II.
DR InterPro; IPR000408; Reg_chr_condens.
DR PANTHER; PTHR22870; REGULATOR OF CHROMOSOME CONDENSATION; 1.
DR PANTHER; PTHR22870:SF437; X-LINKED RETINITIS PIGMENTOSA GTPASE REGULATOR-RELATED; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF00415; RCC1; 3.
DR Pfam; PF13540; RCC1_2; 3.
DR PRINTS; PR00633; RCCNDNSATION.
DR SMART; SM00119; HECTc; 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR SUPFAM; SSF50985; RCC1/BLIP-II; 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS00626; RCC1_2; 3.
DR PROSITE; PS50012; RCC1_3; 7.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000024635};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1049
FT /note="HECT domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001491556"
FT REPEAT 37..94
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 95..147
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 148..198
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 199..243
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 244..295
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 296..348
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 348..397
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT DOMAIN 720..1049
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT ACT_SITE 1017
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1049 AA; 116079 MW; 89EC963CA60B37CD CRC64;
MLLLVFHLCS FFRVLMPSSC CEVICDSEHF AKRVMRRELL GCGLSEDGQL GLGSRSAACV
KLPEQIVGAP LNAVGTAVTS VACGEKHTIL LAEDGKMWSV GGNEDGQLGR GGRGPGSFTI
YPVSFSGGVK MLQVAAGRSH SLAVAEDGRL FAWGSNEHGQ LAMPRHISWQ ETPKRVGELT
EVVQVACGPL HCIALLESGA VAVWGEQSDG AILHSPQIVT QLIGVPVVRV VAGGRHCVAI
SAGGGVYVWG HNEYGQLGTG DTLPRPTPFF LEGMSAMHII EAYCGDSHTL LLSQEGRLFA
FGSNAHGQIG GGKKFDKHTN PAAVTELMGS TVTRVACGRN HSVVVIGGRL YPFGQNANGQ
LGNGSALNQL IPRQTEELDH VVAVFAGFDQ TFILRSIGAP ALTAGPNCPL KVPLSLCKAN
VLDLLSRHEK LDLIGLLESV FSSISCINGS FLYEDERRFL SEGRVFGVDL DDVMETFGAL
GESSDARQYA DLIIDTCQMS VFGDFDPSAM CSVESLRVYL VLVWVQPFVT NVTRDVVARL
HLPFAESISK LRPHFRNALE KWWVVLPVRH FNRLATAMLT AVRCLVRDKV NPSECRAFLD
ILASLCAINK VTNKIPLENF YVHELADNYN LKMDYVNWAR AQEGREASAT CWSNYPFLMN
AAAKGELLYV EAVMSMQTSM NGARLTLFGF DLFVEQPFFE LTVRRQHIVQ DTINGLLSID
RRYLQRPLRV QFMSEEAEDA GGVKKEFFMI LFQKLLQSDY GMFVEDPDSH LVWFSGFDVE
EVNYYKMVGI LCGLAVYNCV LVAFPFPLAL YKMLLDQQPV LEDLTELSPV EGRSLQELLD
YQGDDFEDVF CLNFTISYAA FGSTETLDLK PGGADIAVTQ SNKADYVQRY VHHRLCVGRN
GEVGRQAAAF RDGFKMVLNS RIVAFFQPRE LMELVIGNEN YDWSELRKIV QYKGEYHANH
PTILAFWEAF FELNVDERKK FLQFLMGSTR LPVGGMSSLQ MYIQPTAPEV LPVAHTCFNL
LDLPNIADSK ELLRRLRVSI QHTQGFTLV
//
