ID A0A2K6V1B5_SAIBB Unreviewed; 475 AA.
AC A0A2K6V1B5;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=TRIM5alpha {ECO:0000256|ARBA:ARBA00032496};
GN Name=TRIM62 {ECO:0000313|Ensembl:ENSSBOP00000037958.1};
OS Saimiri boliviensis boliviensis (Bolivian squirrel monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Saimiriinae; Saimiri.
OX NCBI_TaxID=39432 {ECO:0000313|Ensembl:ENSSBOP00000037958.1, ECO:0000313|Proteomes:UP000233220};
RN [1] {ECO:0000313|Ensembl:ENSSBOP00000037958.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBUNIT: Can form homodimers and homotrimers. In addition to lower-
CC order dimerization, also exhibits a higher-order multimerization and
CC both low- and high-order multimerizations are essential for its
CC restriction activity. Interacts with BTBD1 and BTBD2. Interacts with
CC PSMC4, PSMC5, PSMD7 and HSPA8/HSC70. Interacts (via B30.2/SPRY domain)
CC with HSPA1A/B. Interacts with PSMC2, MAP3K7/TAK1, TAB2 and TAB3.
CC Interacts with SQSTM1. Interacts with TRIM6 and TRIM34. Interacts with
CC ULK1 (phosphorylated form), GABARAP, GABARAPL1, GABARAPL2, MAP1LC3A,
CC MAP1LC3C and BECN1. {ECO:0000256|ARBA:ARBA00011109}.
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DR RefSeq; XP_010346417.1; XM_010348115.1.
DR AlphaFoldDB; A0A2K6V1B5; -.
DR SMR; A0A2K6V1B5; -.
DR STRING; 39432.ENSSBOP00000037958; -.
DR Ensembl; ENSSBOT00000054903.1; ENSSBOP00000037958.1; ENSSBOG00000035058.1.
DR GeneID; 101036674; -.
DR KEGG; sbq:101036674; -.
DR CTD; 55223; -.
DR GeneTree; ENSGT00940000158433; -.
DR OMA; WSRQEAQ; -.
DR OrthoDB; 3453019at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000233220; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0003713; F:transcription coactivator activity; IEA:Ensembl.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045087; P:innate immune response; IEA:Ensembl.
DR GO; GO:0010719; P:negative regulation of epithelial to mesenchymal transition; IEA:Ensembl.
DR GO; GO:0032897; P:negative regulation of viral transcription; IEA:Ensembl.
DR GO; GO:1905036; P:positive regulation of antifungal innate immune response; IEA:Ensembl.
DR GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; IEA:Ensembl.
DR GO; GO:0044314; P:protein K27-linked ubiquitination; IEA:Ensembl.
DR GO; GO:0046596; P:regulation of viral entry into host cell; IEA:Ensembl.
DR GO; GO:0019076; P:viral release from host cell; IEA:Ensembl.
DR CDD; cd19792; Bbox2_TRIM62_C-IV; 1.
DR CDD; cd16608; RING-HC_TRIM62_C-IV; 1.
DR CDD; cd13744; SPRY_PRY_TRIM62; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR003879; Butyrophylin_SPRY.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR006574; PRY.
DR InterPro; IPR035830; PRY/SPRY_TRIM62.
DR InterPro; IPR003877; SPRY_dom.
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; PTHR24103; E3 UBIQUITIN-PROTEIN LIGASE TRIM; 1.
DR PANTHER; PTHR24103:SF573; E3 UBIQUITIN-PROTEIN LIGASE TRIM62; 1.
DR Pfam; PF13765; PRY; 1.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR Pfam; PF15227; zf-C3HC4_4; 1.
DR PRINTS; PR01407; BUTYPHLNCDUF.
DR SMART; SM00589; PRY; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS50119; ZF_BBOX; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000233220};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00024}.
FT DOMAIN 11..54
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 88..128
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 277..475
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000259|PROSITE:PS50188"
FT COILED 129..166
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 208..235
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 475 AA; 54280 MW; 68A18B028C8495F2 CRC64;
MACSLKDELL CSICLSIYQD PVSLGCEHYF CRRCITEHWV RQEAQGARDC PECRRTFAEP
ALAPSLKLAN IVERYSAFPL DAILNARRAA RPCQAHDKVK LFCLTDRALL CFFCDEPALH
EQHQVTGIDD AFEELQRELK EQLQALQDSE REHTEALQLL KRQLAETKSS TKSLRTTIGE
AFERLHRLLR ERQKAMLEEL EADTARTLTD IEQKVQRYSQ QLRKVQEGAQ ILQERLAETD
RHTFLAGVAS LSERLKGKIH ETNLTYEDFP TSKYTGPLQY TIWKSLFQDI HPVPAALTLD
PGTAHQRLIL SDDCTIVAYG NLHPQPLQDS PKRFDVEVSV LGSEAFSSGV HYWEVVVAEK
TQWVIGLAHE AASRKGSIQI QPSRGFYCIV MHDGNQYSAC TEPWTRLNVR DKLDKVGVFL
DYDQGLLIFY NADDMSWLYT FREKFPGKLC SYFSPGQSHA NGKNVQPLRI NTVRI
//
