ID A0A2K6CHA8_MACNE Unreviewed; 580 AA.
AC A0A2K6CHA8;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
DE AltName: Full=TRIM5alpha {ECO:0000256|ARBA:ARBA00032496};
GN Name=TRIM45 {ECO:0000313|Ensembl:ENSMNEP00000023039.1};
OS Macaca nemestrina (Pig-tailed macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000023039.1, ECO:0000313|Proteomes:UP000233120};
RN [1] {ECO:0000313|Ensembl:ENSMNEP00000023039.1}
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};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family.
CC {ECO:0000256|ARBA:ARBA00008518}.
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DR RefSeq; XP_011735221.1; XM_011736919.1.
DR AlphaFoldDB; A0A2K6CHA8; -.
DR SMR; A0A2K6CHA8; -.
DR STRING; 9545.ENSMNEP00000023039; -.
DR Ensembl; ENSMNET00000047300.1; ENSMNEP00000023039.1; ENSMNEG00000035138.1.
DR GeneID; 105479104; -.
DR KEGG; mni:105479104; -.
DR CTD; 80263; -.
DR GeneTree; ENSGT00940000154334; -.
DR OrthoDB; 2916643at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000233120; Unplaced.
DR Bgee; ENSMNEG00000035138; Expressed in skeletal muscle tissue and 9 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0045171; C:intercellular bridge; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0060348; P:bone development; IEA:Ensembl.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; IEA:Ensembl.
DR CDD; cd19809; Bbox1_TRIM45_C-X; 1.
DR CDD; cd19785; Bbox2_TRIM45_C-X; 1.
DR CDD; cd16588; RING-HC_TRIM45_C-VII; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR003649; Bbox_C.
DR InterPro; IPR017868; Filamin/ABP280_repeat-like.
DR InterPro; IPR001298; Filamin/ABP280_rpt.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR047153; TRIM45/56/19.
DR InterPro; IPR027370; Znf-RING_euk.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR25462; BONUS, ISOFORM C-RELATED; 1.
DR PANTHER; PTHR25462:SF291; TRIPARTITE MOTIF-CONTAINING PROTEIN 45; 1.
DR Pfam; PF00630; Filamin; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR SMART; SM00502; BBC; 1.
DR SMART; SM00336; BBOX; 2.
DR SMART; SM00557; IG_FLMN; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50194; FILAMIN_REPEAT; 1.
DR PROSITE; PS50119; ZF_BBOX; 2.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000233120};
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 29..98
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 130..176
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 186..222
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT REPEAT 394..497
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT COILED 249..316
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 580 AA; 64230 MW; 415423DDEB8AB489 CRC64;
MSENRKPLLG IVSKLPNGTA LGNSGKTHCP LCLGLFKAPR LLPCLHTVCT TCLEQLEPFS
VVDIRGGDSD TSSEGSIFQE LKPRSLQSQI GILCPVCDAQ VDLPMGGVKA LTIDHLAVND
VMLESLRGEG QGLVCDLCND REVEKRCQTC KANLCHFCCQ AHRRQKKTTY HTMVDLKDLK
GYSRIGKPIL CPIHPAEELR LFCEFCDRPV CRDCVVGEHR EHPCDFTSNV IHKHGDSVRE
LLKGTQPHVE ALEEALAQIN IMNSALQKRV EAVAADVQTF SEGYIKAIEE HRDKLLKQLE
DIRIQKENSL QLQKAQLEQL LADMRTGVEF TEHLLTSGSD LEILITKGVV VERLRKLNKV
QYSARPGVND KIRFCPQEKA GQCHGYEIYG TINTKEVDPA KCVLQGEDLH RAREKQTASF
TLLCKDAAGE IMGRGGDNIQ VAVLPKDKKD SPVRPMVQDN KDGTYYISYT PKEPGVYTVW
VCVKEQHVQG SPFTVTVRRK HRPHPGVFHC CTFCSSGGQK TARCACGGTM PGGYLGCGHG
HKGHPGRPHW SCCGKFNEKS ECTWTGGQSA PRSLLRTVAL
//
