ID   M7C3H0_CHEMY            Unreviewed;       859 AA.
AC   M7C3H0;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE            EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN   ORFNames=UY3_03806 {ECO:0000313|EMBL:EMP38973.1};
OS   Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC   Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX   NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP38973.1, ECO:0000313|Proteomes:UP000031443};
RN   [1] {ECO:0000313|Proteomes:UP000031443}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23624526; DOI=10.1038/ng.2615;
RA   Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA   White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA   Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA   Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA   Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT   "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT   into the development and evolution of the turtle-specific body plan.";
RL   Nat. Genet. 45:701-706(2013).
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; KB518028; EMP38973.1; -; Genomic_DNA.
DR   AlphaFoldDB; M7C3H0; -.
DR   STRING; 8469.M7C3H0; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000031443; 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; cd00078; HECTc; 1.
DR   CDD; cd00201; WW; 1.
DR   Gene3D; 1.10.287.3160; -; 1.
DR   Gene3D; 2.20.70.10; -; 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; IPR035892; C2_domain_sf.
DR   InterPro; IPR000569; HECT_dom.
DR   InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR   InterPro; IPR001202; WW_dom.
DR   InterPro; IPR036020; WW_dom_sf.
DR   PANTHER; PTHR11254:SF282; E3 UBIQUITIN-PROTEIN LIGASE NEDD4; 1.
DR   PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR   Pfam; PF00632; HECT; 1.
DR   Pfam; PF00397; WW; 1.
DR   SMART; SM00119; HECTc; 1.
DR   SMART; SM00456; WW; 1.
DR   SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR   SUPFAM; SSF51045; WW domain; 1.
DR   PROSITE; PS50237; HECT; 1.
DR   PROSITE; PS01159; WW_DOMAIN_1; 1.
DR   PROSITE; PS50020; WW_DOMAIN_2; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000031443};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PROSITE-ProRule:PRU00104}.
FT   DOMAIN          326..359
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          524..858
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   REGION          1..84
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          315..334
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..40
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        68..84
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        826
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   859 AA;  98789 MW;  FACD93D2E5D855F4 CRC64;
     MRSDFAKDSR HQVSPAPPPL RHWSLSPGQK KQQPKQVPTA SFLLVRQPPT LPVPQLEPRP
     LPERTGQVTA PAPSTPAPQG PSSLVHVSSV VHTTVELRLL STPETFSTAR DLIMLTEPTP
     LQPAAPRVRM VTSKGKQSLI RLPSPSEAKW HWCWDQDRDG VLRRRLAAQG GQQASLDEAD
     SAAKTLASGI AMRRISWLQV SGLPPELQQT LQDLPVDGKG LFSEKMDSRL QSLKDSRIIM
     HSLGMRTPTE NPNMERPYTF KDFVLHPRSH KSRVKGHLRL KMTYLPKNNG SEEENTEQVE
     DLEPGWIILD QPDAACQPQQ QQQESPPLPP GWEERQDILG RTYFVNHESR RTQWKRPTAQ
     DNLADVDNGN IHLEAQHAFT HRRQISEETE NLDNRDSPEG MSTLAVDRCC GSRSTGGRCS
     SSSEDPLNQL PITFPLTLVF HQNKKYKEDP RLKIPAHLRK KTSLDPVDLG PLPAVPYSRD
     YKRKYEFFRK KLKKQSDIPN RFEMKLHRTT ILEDSYRRII AVKRADFLKA RLWIEFDGEK
     GLDYGGVARE WFFLLSKEMF NPYYGLFEYS ATDNYTLQIN PNSGLCNEDH LSYFKFIGRV
     AGMAVYHGKL LDGFFIRPFY KMMLQKPITL QDMESVDSEY YNSLRWILEN DPTELDLRFI
     VDEELFGQTH QHELKSGGSE IVVTNKNKRD YIHLVIQWRF VSRVQKQMAA FKEGFFELIS
     QDLIKIFDEN ELELLMCGLG DVDVADWKLY TKYKNGYSIN HQVIQWFWKA VLMMDSEKRI
     RLLQFVTGTS RVPMNGFAEL YGSNGPQLFT VEQWGTPEKL PRAHTCFNRL DLPPYESFED
     LWDKLLIAIE NTQGFDGVD
//