ID A0A2U9BXG1_SCOMX Unreviewed; 1273 AA.
AC A0A2U9BXG1;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Putative E3 ubiquitin-protein ligase HERC4-like {ECO:0000313|EMBL:AWP08934.1};
GN ORFNames=SMAX5B_015379 {ECO:0000313|EMBL:AWP08934.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP08934.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWP08934.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus speckle {ECO:0000256|ARBA:ARBA00004324}.
CC -!- SIMILARITY: Belongs to the EGR C2H2-type zinc-finger protein family.
CC {ECO:0000256|ARBA:ARBA00005682}.
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DR EMBL; CP026252; AWP08934.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U9BXG1; -.
DR STRING; 52904.ENSSMAP00000026190; -.
DR Proteomes; UP000246464; Chromosome 10.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 2.
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; 1.
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 InterPro; IPR000976; Wilms_tumour_N.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR45622:SF73; E3 UBIQUITIN-PROTEIN LIGASE HERC4-LIKE ISOFORM X1-RELATED; 1.
DR PANTHER; PTHR45622; UBIQUITIN-PROTEIN LIGASE E3A-RELATED; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF00415; RCC1; 3.
DR Pfam; PF13540; RCC1_2; 1.
DR Pfam; PF02165; WT1; 1.
DR Pfam; PF00096; zf-C2H2; 1.
DR PRINTS; PR00633; RCCNDNSATION.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00355; ZnF_C2H2; 2.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 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; 5.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Reference proteome {ECO:0000313|Proteomes:UP000246464};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT DOMAIN 284..313
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 314..339
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REPEAT 355..406
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 407..459
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 460..511
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 512..563
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 564..619
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT DOMAIN 970..1273
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT ACT_SITE 1242
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1273 AA; 142086 MW; 27630CAD91431D60 CRC64;
MGSDVRDLNS LLPPVPAGPS PGCPALPVST APQWAPVLDF HTAASPYSSL AAPHTSLGSH
SFIKQEPTWG ATGDPHVHDA DPHCGLSAFT VHFSGQFTGT GACRMFSNPP YLTNCMDTQQ
AARNQTGYSA FDGAGNYGHT PTHHGSQFSN HSFKHEDALT QQNSMGEQQY PVPPPVYGCH
TPSDSCTGSQ ALLLRNPYNS GDNLYQMSSQ LECVAWSPVN TLASTVKSHA TGYDSDPNTP
MVYSCSTQYR IHTHGVFRGL QDVRRVPSIA PALVRSETSE KRPFMCAYPG CNKRYFKLSH
LQMHSRKHTG EKPYQCDFTD CGRRFSRSDQ LKRHQRRHTE FLKCKEKIKA LSCGDDVVAL
LSERGSVLCV DTTRHPFTPR PLDVLCNIPV RQVACGSQHS MALTNDGQVY TWGQDSRGQL
GLGKGKSGAN SPQHLRSLSA IPLLRVAAGG EQSFALSVSG GVFGWGRNDR GQLGLGDNAD
KHTPTPVKCL DMKRSVQISC GRDHTATLTK DGAVFTFGSG QHGQLGHNSF RDELRPRLVA
ELLGAKVTDV ACGMHHTLVL TDSKKVYSFG RGEQGQLGHG GETHPSVPLP VQLPQGSGDG
PKITNVFAGG NCSFATCTSD EEESGADSVG SVTPCRLDDM IDKWTTPCDS KSWKKIKQEI
HRTFSSASCM NQSFIEQRKD KHFQTSTKNP GLNLLLARNA FKKLAKKDDV LSEVEAAVLH
LLHSFDTNPV GVEGLRIFLL LNELLRVMQT HKRQRSTKLA EAVAAAVLTL SAENLQVIGD
WWTTLPASTM SKYVKVWKKA LSVNLSSQPV PRNSGVRNLL LVLQYMYNAN SRTAESRRMP
ESDFHLVIDT KFLQEDLRFW ILQSKPEIGF AEPLILCGFP IVMDLQSKKM AFDMHASYSK
EETMGAYWRN IYVLGGYSAL PQQLFFDLDL RRASISEDTF EKLGAVCHSN YKRPLLVYLD
GAPTPSYVYT KDFFHEVFHE IVSAESGMFL FNDSKTLAWF PSRQATQDHH RYFLFGVLCG
LAFYNQCIIH LPFPMALFKK LLGVKPSLED MMEFSPSIGK SLKATLEDYN DDDIKNLDMC
FSISWDGTDV DLDPQNPEKA VTSQNKKEFV DAYVNHAFNT SVENVFLEFK RGFFKVCDRN
LVKLFRPKEL QEMLVGKDFI DWERLKQNTA YEAPFHPDHP NILMFWEVFD ELTEDQKKSF
IWFVTGFERV PVLKTENIQM TVRVKQGSDG SDDHFYPETL TCYSFLDLPL YSTKEIMRTM
LTVALSNRRG THK
//
