ID Q9BL11_CAEEL Unreviewed; 1019 AA.
AC Q9BL11;
DT 01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2001, sequence version 2.
DT 27-MAR-2024, entry version 157.
DE SubName: Full=HECT domain-containing protein {ECO:0000313|EMBL:CCD73459.1};
GN Name=herc-1 {ECO:0000313|EMBL:CCD73459.1,
GN ECO:0000313|WormBase:Y48G8AL.1a};
GN ORFNames=CELE_Y48G8AL.1 {ECO:0000313|EMBL:CCD73459.1}, Y48G8AL.1
GN {ECO:0000313|WormBase:Y48G8AL.1a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000313|EMBL:CCD73459.1, ECO:0000313|Proteomes:UP000001940};
RN [1] {ECO:0000313|EMBL:CCD73459.1, ECO:0000313|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000313|EMBL:CCD73459.1,
RC ECO:0000313|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RA Sulson J.E., Waterston R.;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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DR EMBL; BX284601; CCD73459.1; -; Genomic_DNA.
DR RefSeq; NP_490834.1; NM_058433.3.
DR AlphaFoldDB; Q9BL11; -.
DR SMR; Q9BL11; -.
DR STRING; 6239.Y48G8AL.1a.1; -.
DR EPD; Q9BL11; -.
DR PaxDb; 6239-Y48G8AL-1; -.
DR PeptideAtlas; Q9BL11; -.
DR EnsemblMetazoa; Y48G8AL.1a.1; Y48G8AL.1a.1; WBGene00021685.
DR EnsemblMetazoa; Y48G8AL.1a.2; Y48G8AL.1a.2; WBGene00021685.
DR GeneID; 171700; -.
DR KEGG; cel:CELE_Y48G8AL.1; -.
DR UCSC; Y48G8AL.1; c. elegans.
DR AGR; WB:WBGene00021685; -.
DR WormBase; Y48G8AL.1a; CE29116; WBGene00021685; herc-1.
DR eggNOG; KOG0941; Eukaryota.
DR HOGENOM; CLU_002173_5_3_1; -.
DR InParanoid; Q9BL11; -.
DR OMA; GNQPEQI; -.
DR OrthoDB; 5475808at2759; -.
DR PhylomeDB; Q9BL11; -.
DR Reactome; R-CEL-1169408; ISG15 antiviral mechanism.
DR Reactome; R-CEL-936440; Negative regulators of DDX58/IFIH1 signaling.
DR Reactome; R-CEL-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR Reactome; R-CEL-9833482; PKR-mediated signaling.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00021685; Expressed in adult organism and 4 other cell types or tissues.
DR ExpressionAtlas; Q9BL11; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
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; PTHR45622:SF64; SECRETION-REGULATING GUANINE NUCLEOTIDE EXCHANGE FACTOR; 1.
DR PANTHER; PTHR45622; UBIQUITIN-PROTEIN LIGASE E3A-RELATED; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF00415; RCC1; 6.
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 1: Evidence at protein level;
KW Proteomics identification {ECO:0007829|EPD:Q9BL11,
KW ECO:0007829|PeptideAtlas:Q9BL11};
KW Reference proteome {ECO:0000313|Proteomes:UP000001940};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT REPEAT 3..59
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 60..112
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 113..163
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 164..208
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 209..260
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 261..313
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 313..362
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT DOMAIN 688..1019
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT ACT_SITE 987
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1019 AA; 114519 MW; 30BB47B056C3A957 CRC64;
MRAELLGCGH TGEGQLGVRL SESTIQVPER IIGAPNDMDG TAVTSVTCGE QHTVFLTKDG
KMWSVGSNMD GQLGRGSRTE GSFSIYPVSW TSSAKIIQIS AGRSHTVSVT DDGRVFAWGS
NEHGQLGMES KFTWQGTPRR VQEINDIVQV ASGSNHCIAL DEGGRVFVWG EQADGRCIHR
PEPVEQLSGV PIVRVLAGAR HCLALSASGA VFTWGQNNSG ELGIDDLRPQ TSVQHVHQMD
GLGVVEAACG DNHTVLLTHC GRTFSFGSDA LGQCGFGKKV EKRTNPTAVS DLIGSHVTRI
AAGACHTIAI CKGAPYPFGL NSSGQLGNGK IMTQSTPRKT DELDHVTGVF AGYHQTFFVR
SSGTIEQNEI VGPSCPMQYP IKLDHESLKK LLDEGDALEV MSLIESVFSS LASMNMSFLY
KDERRYNVGF CFERSHGIDM DQVMEAFMLF DEYPMKRQYM ELIVDSLKIA FQEWSENLKG
IECLRVLLML PWLPIFTENV NVQTIKNVHT PFVDAMCLIT GDLRAALEKW WTQLSTRHFR
RMVTVFKTAI KAMLKAKKGP RDCHKFILIM QKLSLINKTY HIIPLETFYI DELNTSVDLK
LEYVLELTRQ DPNKTELDYW THFPFLLNGV AKGELIFVEA WLMQTLRRQS SLFNTAHGTI
IFELPHLELT VRREFIVSDT MNQMAGLSES DLQKPLKVNI AGEDADDAGG VRKEFFILVM
RKILQSDYGM FSEDEESHLV WFSGLPSEFC DREQFHQLGR LVGLSIYNHS IVPFPFPLAL
YKYLLDTPPD LEDLCELSPS EGKGLKMLLS YEEDDVEDVF GLNFCISFNI LGETHTTELL
SGGTEKPVTN ANRDEYVRLY VHHRLELGYN GEIAQQALLF RKGFSESLHS RTLRFFQPCE
LKEMIVGNEN YDWNEFRDIL MYRGEYSSSH PTIQAFWKAF FALTDDERRK FLQFLTGSTR
IPVSGWEELH AAIQPSAPES LPVAHTCFNL LDLPNIADDV ELLRRLRISI EHTEGFTLA
//
