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Database: UniProt
Entry: A0A0G4H277_VITBC
LinkDB: A0A0G4H277_VITBC
Original site: A0A0G4H277_VITBC 
ID   A0A0G4H277_VITBC        Unreviewed;      1248 AA.
AC   A0A0G4H277;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=HECT domain-containing protein {ECO:0000259|PROSITE:PS50237};
GN   ORFNames=Vbra_19374 {ECO:0000313|EMBL:CEM37763.1};
OS   Vitrella brassicaformis (strain CCMP3155).
OC   Eukaryota; Sar; Alveolata; Colpodellida; Vitrellaceae; Vitrella.
OX   NCBI_TaxID=1169540 {ECO:0000313|EMBL:CEM37763.1, ECO:0000313|Proteomes:UP000041254};
RN   [1] {ECO:0000313|EMBL:CEM37763.1, ECO:0000313|Proteomes:UP000041254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Zhu J., Qi W., Song R.;
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CDMY01000954; CEM37763.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G4H277; -.
DR   STRING; 1169540.A0A0G4H277; -.
DR   VEuPathDB; CryptoDB:Vbra_19374; -.
DR   InParanoid; A0A0G4H277; -.
DR   OMA; ERIWHAV; -.
DR   OrthoDB; 276649at2759; -.
DR   PhylomeDB; A0A0G4H277; -.
DR   Proteomes; UP000041254; Unassembled WGS sequence.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR   GO; GO:0000209; P:protein polyubiquitination; 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; IPR044611; E3A/B/C-like.
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; PTHR45700:SF8; HECT DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR45700; UBIQUITIN-PROTEIN LIGASE E3C; 1.
DR   Pfam; PF00632; HECT; 1.
DR   Pfam; PF00415; RCC1; 4.
DR   PRINTS; PR00633; RCCNDNSATION.
DR   SMART; SM00119; HECTc; 1.
DR   SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR   SUPFAM; SSF50985; RCC1/BLIP-II; 2.
DR   PROSITE; PS50237; HECT; 1.
DR   PROSITE; PS50012; RCC1_3; 5.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000041254};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PROSITE-ProRule:PRU00104}.
FT   REPEAT          208..261
FT                   /note="RCC1"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT   REPEAT          262..313
FT                   /note="RCC1"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT   REPEAT          314..365
FT                   /note="RCC1"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT   REPEAT          366..419
FT                   /note="RCC1"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT   REPEAT          420..476
FT                   /note="RCC1"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT   DOMAIN          917..1248
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          146..179
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..45
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        161..175
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1216
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   1248 AA;  139994 MW;  B7544969A22D5636 CRC64;
     MEPDGTSLAR TVSHHPTYPP PRPPNQDTVS RAAPQAPQNE RSQSNISQIS EALRDENFFN
     FTDGSFVWTF GDNYCGQVLN EGTEPVRQPV LLTKLRKQRI LKVACGFETT WIIGDNGDVW
     AGGSNDSGQV TGLMDDEYDM AEQDEAMQPT EGPPTGENDN KRPRSAPTTS RGAPDSINHA
     KRLELRENQK VRTLQSGRDH TVAVLDSGVA LSFGSNEFGQ LGHGTPPSIQ RCKAGVMRVS
     PGSKVQSVAC GQGFTIVLMA TGQLLSCGDG GQGCLGHGSL ESRSALGPIP TLMGMPMNQV
     ACGVNHCMAL SITGEAYGWG KCRDGQLGLG DTVSDDKKLV PCRVPIERAK YVACGGAHSA
     IIARKGRLLM TGSNKYGQLG APTGLVEDRR EFAPVEALAE MKIRIAQLGL RHTLCITYMG
     TLLAFGCNQH GQLGIGSDEA LVCQPTEITF KDVPHQRQFF FSLSSGQDHA IAVATSDPPL
     RVKKGSGTRE IDEWLAKERS MIRTFSDYRN EKGLRLSDFP RYVSSDLSPM RKALRAFASS
     VESGTGVTAQ ELREVIDAHS LDIIPLKHQL HVILADVHTM NASFLVGVKR KLFDAEGLES
     AYRQLFALSQ IADIIPELIS HFEKCLMSVA TYEKELRTSD QLRFIMESNP RERERERQND
     RAIQKHAPCV MCVCARGCLQ IILQCPLFSV PTSLTVPLMA KLAEVTFKLS QRGKETLVRM
     AKEDTTPEVF GGRLVAHVVA YLNHQIEHHT PHYRQLERIW HAVHLLQLLY LANWECAKER
     KVDENGASRD FRIPLQRFHL DGITRFIDVV SECKMFYELF RDPKHQDQEG HRLAWRPQQV
     LTVSQLNHSN TFFLAHHNLC PLPYKRKALR VEAGRYQEEY MVRSLIQMEI PYFVVTVQRD
     NLLNTALARI MSVAQGSPHE FIKPLKIKFE NEEGVDEGGV LREFYRLITQ EVLNPDFGMF
     VYNEQIRTIW FNRLSLDDNL SMFAFVGILL GLALYNNVLL ELPFPLALYK LLQHEPIGLE
     DLADTFPDQA HSFQQILDHQ PGEEFDAAFG ELPFEVTFDY FGETKTVELT EGGSEKTLTY
     DNRQDYVELY TRYLLVDSVK EPIERFCKGF RGAAHSELIT VVTPSELQLL MCGTPQLDFE
     ELRKGARYDG GYTPDHPYIN TFWQILMSFD QEHKRKFLIF CTGSDRAPLG GLEDLRLLIQ
     RNGTEPTVRL PTAYTCYNAL LLPEYADGDK LQKLLVQAIE QAEGFGLR
//
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