ID A0A452EAP6_CAPHI Unreviewed; 1127 AA.
AC A0A452EAP6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN Name=TRIM33 {ECO:0000313|Ensembl:ENSCHIP00000009078.1};
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925 {ECO:0000313|Ensembl:ENSCHIP00000009078.1, ECO:0000313|Proteomes:UP000291000};
RN [1] {ECO:0000313|Ensembl:ENSCHIP00000009078.1, ECO:0000313|Proteomes:UP000291000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT "Polished mammalian reference genomes with single-molecule sequencing and
RT chromosome conformation capture applied to the Capra hircus genome.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCHIP00000009078.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
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DR EMBL; LWLT01000004; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_005678048.2; XM_005677991.3.
DR AlphaFoldDB; A0A452EAP6; -.
DR SMR; A0A452EAP6; -.
DR STRING; 9925.ENSCHIP00000009078; -.
DR Ensembl; ENSCHIT00000016846.1; ENSCHIP00000009078.1; ENSCHIG00000012017.1.
DR GeneID; 102180642; -.
DR KEGG; chx:102180642; -.
DR CTD; 51592; -.
DR GeneTree; ENSGT00940000156361; -.
DR OrthoDB; 56754at2759; -.
DR Proteomes; UP000291000; Chromosome 3.
DR Bgee; ENSCHIG00000012017; Expressed in testis and 17 other cell types or tissues.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0070410; F:co-SMAD binding; IEA:Ensembl.
DR GO; GO:0070412; F:R-SMAD binding; IEA:Ensembl.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; IEA:Ensembl.
DR GO; GO:0016567; P:protein ubiquitination; IEA:Ensembl.
DR GO; GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
DR CDD; cd19847; Bbox1_TIF1g_C-VI; 1.
DR CDD; cd19830; Bbox2_TIF1g_C-VI; 1.
DR CDD; cd05502; Bromo_tif1_like; 1.
DR CDD; cd15624; PHD_TIF1gamma; 1.
DR CDD; cd16766; RING-HC_TIF1gamma; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR003649; Bbox_C.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR027370; Znf-RING_euk.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR45915:SF3; E3 UBIQUITIN-PROTEIN LIGASE TRIM33; 1.
DR PANTHER; PTHR45915; TRANSCRIPTION INTERMEDIARY FACTOR; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00502; BBC; 1.
DR SMART; SM00336; BBOX; 2.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00249; PHD; 2.
DR SMART; SM00184; RING; 2.
DR SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS50119; ZF_BBOX; 2.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035}; Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000291000};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00024}.
FT DOMAIN 125..185
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 212..259
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 271..312
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 887..934
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 974..1046
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 1..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 536..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 609..629
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 641..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 673..692
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 703..781
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1091..1127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 309..390
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 100..118
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 703..771
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1106..1127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1127 AA; 122524 MW; 99ECAC76443F678C CRC64;
MAENKGGGEA ESGGGGSSSA PVTAGAAGLA AQEAEPPLAA VLVEEEEEEG GRAGAESGAA
GPDDGGVAAA SSGSAPAASA PAASMGPGVP GGAVSTPAPA PASAPAPGPS AGPPPGPPAS
LLDTCAVCQQ SLQSRREAEP KLLPCLHSFC LRCLPEPERQ LNVPIPGGSN GDIQQVGVIR
CPVCRQECRQ IDLVDNYFVK DTSETPSSSD EKSEQVCTSC EDNASAVGFC VECGEWLCKT
CIEAHQRVKF TKDHLIRKKE DVSESVGASG QRPVFCPVHK QEQLKLFCET CDRLTCRDCQ
LLEHKEHRYQ FLEEAFQNQK GAIENLLAKL LEKKNYVHFA ATQVQNRIKE VNETNKRVEQ
EIKVAIFTLI NEINKKGKSL LQQLENVTKE RQMKLLQQQN DITGLSRQVK HVMNFTNWAI
ASGSSTALLY SKRLITFQLR HILKARCDPV PAANGAIRFH CDPTFWAKNV VNLGNLVIES
KPAPGYTPNV VVGQVPPGTN HISKTPGQIN LAQLRLQHMQ QQVYAQKHQQ LQQMRMQQPP
APVPTTTTAT QQHSRQAAPQ MLQQQPPRLI SVQAMQRGNM NCGAFQAHQM RLAQNAARIP
GIPRHSGPQY SMMQPHLQRQ HSNPGHAGPF PVVSVHNNPV NPTSPTTATM ANANRGPTSP
SVTAIELIPS VTNPENLPSL PDIPPIQLED AGSSSLDNLL SRYISGSHLP PQPTSTMNPS
PGPSALSPGS SGLSNSHTPV RPPSTSSTGS RGSCGSSGRT AEKTSLSFKS DPVKVKQEPG
TEDEICSFSG AVKQEKTEDG RRSACMLSSP ESSLTPPLST NLHLESELDA LTSLENHVKT
EPADLNESCK QSGLNSLVNG KSPVRSLMHR SARIGGDGSS KDDDPNEDWC AVCQNGGDLL
CCEKCPKVFH LTCHVPTLLS FPSGDWICTF CRDIGKPEVE YDCDNLQHSK KGKTAQGLSP
VDQRKCERLL LYLYCHELSI EFQEPVPASI PNYYKIIKKP MDLSTVKKKL QKKHSQHYQI
PDDFVADVRL IFKNCERFNE MMKVVQVYAE TQEINLKADS EVAQAGKAVA LYFEDKLTEI
YSDRTFAPLP EFEQEEDDGE VTEDSDEDFI QPRRKRLKSD ERPVHIK
//
