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Database: UniProt
Entry: A0A1Y1HSY4_KLENI
LinkDB: A0A1Y1HSY4_KLENI
Original site: A0A1Y1HSY4_KLENI 
ID   A0A1Y1HSY4_KLENI        Unreviewed;       715 AA.
AC   A0A1Y1HSY4;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE            EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN   ORFNames=KFL_000460220 {ECO:0000313|EMBL:GAQ80111.1};
OS   Klebsormidium nitens (Green alga) (Ulothrix nitens).
OC   Eukaryota; Viridiplantae; Streptophyta; Klebsormidiophyceae;
OC   Klebsormidiales; Klebsormidiaceae; Klebsormidium.
OX   NCBI_TaxID=105231 {ECO:0000313|EMBL:GAQ80111.1, ECO:0000313|Proteomes:UP000054558};
RN   [1] {ECO:0000313|EMBL:GAQ80111.1, ECO:0000313|Proteomes:UP000054558}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-2285 {ECO:0000313|EMBL:GAQ80111.1,
RC   ECO:0000313|Proteomes:UP000054558};
RX   PubMed=24865297; DOI=10.1038/ncomms4978;
RA   Hori K., Maruyama F., Fujisawa T., Togashi T., Yamamoto N., Seo M.,
RA   Sato S., Yamada T., Mori H., Tajima N., Moriyama T., Ikeuchi M.,
RA   Watanabe M., Wada H., Kobayashi K., Saito M., Masuda T.,
RA   Sasaki-Sekimoto Y., Mashiguchi K., Awai K., Shimojima M., Masuda S.,
RA   Iwai M., Nobusawa T., Narise T., Kondo S., Saito H., Sato R., Murakawa M.,
RA   Ihara Y., Oshima-Yamada Y., Ohtaka K., Satoh M., Sonobe K., Ishii M.,
RA   Ohtani R., Kanamori-Sato M., Honoki R., Miyazaki D., Mochizuki H.,
RA   Umetsu J., Higashi K., Shibata D., Kamiya Y., Sato N., Nakamura Y.,
RA   Tabata S., Ida S., Kurokawa K., Ohta H.;
RT   "Klebsormidium flaccidum genome reveals primary factors for plant
RT   terrestrial adaptation.";
RL   Nat. Commun. 5:3978-3978(2014).
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};
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DR   EMBL; DF236995; GAQ80111.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y1HSY4; -.
DR   STRING; 105231.A0A1Y1HSY4; -.
DR   OrthoDB; 5480520at2759; -.
DR   Proteomes; UP000054558; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR   GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
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; 2.
DR   InterPro; IPR000569; HECT_dom.
DR   InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR   PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR   PANTHER; PTHR11254:SF446; HECT-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR   Pfam; PF00632; HECT; 1.
DR   SMART; SM00119; HECTc; 1.
DR   SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR   PROSITE; PS50237; HECT; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Ligase {ECO:0000313|EMBL:GAQ80111.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054558};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PROSITE-ProRule:PRU00104}.
FT   DOMAIN          396..715
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   REGION          1..199
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          267..337
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          213..247
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        34..59
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        138..152
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        302..321
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        322..337
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        682
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   715 AA;  78113 MW;  285BC11A2D8AAF1A CRC64;
     MEPNRKGAGG PRETSESIAE NAVHKLPMRL SRTMSDQARR KAEKDVRESE SKDKPAAKLT
     SGKAQRVLKD VTNQRSAKHA TELTKKASQQ SRPVPIAAIG AGQAPNVHHA TTASAKEAEV
     AVADTSEYKP ESASLLGRPQ EADSSQGPVE KGTTSVLPEG RSGLPFNTEE SPGIQVLEEG
     AGANADTERK ADSKASMKSK ALPLPVAVPL SDTRREQRKL AAAMKVFEQL EQQRLQQQEM
     ERKAQAKTLH VQQLLRKAMK GWKSIRSNAS LPANPSSLGV DEAGKLQAPG PSEQQTVNND
     IKGKQKVEEI TSEEGQVNHR PRQTGKRNGS TSMPAPKVEV QSPSQAFGSA AVAIVDQSIQ
     ELKEKRKKRV RTRGRQKQVE RVRMVESIIA LFSELKGEEL LDDFAVLFKG EEGMDAGGLT
     AELFYLFLLS CLRAEGPGTD KKEWANTFLQ IGKVFIKSIL DQVPLPRRLA STFFKFVLDC
     PLDLDDLGSF DPQLKRSYES ILAATSEDLD NMCLSFDSVG DPADAVTSEN RAQFVDQMVY
     EKLLGCRLEA LEALREGMSQ IGPLYDQLRT LSPAALEDRM CGTEVMNGRD VAVFLHFPPG
     ELSQAVHKEQ LLALLDAWDQ STLSDFLKFT TGLCVLPIGG LKNPDASPKH MIKVVSCTCA
     SCKKRSGPAK SPCTLLPQAS TCFWTLRLPV CSIAEELEKK LLVAFKWGNG SFGQL
//
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