ID A0A2K5CYS7_AOTNA Unreviewed; 614 AA.
AC A0A2K5CYS7;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=TRIM5alpha {ECO:0000256|ARBA:ARBA00032496};
GN Name=TRIM41 {ECO:0000313|Ensembl:ENSANAP00000013849.1};
OS Aotus nancymaae (Ma's night monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae;
OC Aotus.
OX NCBI_TaxID=37293 {ECO:0000313|Ensembl:ENSANAP00000013849.1, ECO:0000313|Proteomes:UP000233020};
RN [1] {ECO:0000313|Ensembl:ENSANAP00000013849.1}
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_012306960.1; XM_012451537.1.
DR AlphaFoldDB; A0A2K5CYS7; -.
DR Ensembl; ENSANAT00000031677.1; ENSANAP00000013849.1; ENSANAG00000024834.1.
DR GeneID; 105716745; -.
DR CTD; 90933; -.
DR GeneTree; ENSGT00940000154294; -.
DR OrthoDB; 3453019at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000233020; Unplaced.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd19762; Bbox2_TRIM7-like; 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; 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:SF659; E3 UBIQUITIN-PROTEIN LIGASE TRIM41; 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; SM00336; BBOX; 1.
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; 2.
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:UP000233020};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00024}.
FT DOMAIN 20..61
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 225..266
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 416..614
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000259|PROSITE:PS50188"
FT REGION 51..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 148..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 506..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 288..315
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 51..76
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..170
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 614 AA; 69654 MW; E721D1E4ACA46EF4 CRC64;
MAAVAMTPNP VQTLQEEAVC AICLDYFTDP VSIGCGHNFC RVCVTQLWGG EDEEDRDELD
REEEEEDGEE EEVEVEAVGA GAGWDTPMRD DDYEGDMEEE VEEEEEGVFW TSGMGRSGWG
HMDYVWEEEE EEEEEDLDYY LGDIEEDLRG EDEEDEEEVL EEDEEEELDP VTPVPPPPVP
RRCFTCPQCR KSFPRRSFRP NLQLANMVQV IRQMHPTPGR GSRVTDQGIC PKHQEALKLF
CEVDEEAICV VCRESRSHKQ HSVVPLEEVV QEYKAKLQGH VEPLRKHLEA VQKMKAREER
RVTELKSQMK SELAAVASEF GRLTRFLAEE QAGLERRLRE MHEAQLGRAG AAASRLAEQA
AQLSRLLAEA QERSQQGGLR LLQDIKETFN RCEEVQLQPP EVWSPDPCQP HSHDFLTDAI
VRKMSRMFCQ AARVDLTLDP DTAHPALMLS PDRRGVRLAE RRQEVADHPK CFLADCCVLG
AQGFRSGRHY WEVEVGGRRG WAVGAAREST HHKEKVGPGG SSVGSGDASS SRHHHRRRRL
HLPQQPLLQR EVWCVGTNGK RYQAQSSTEQ TLLSPSEKPR RFGVYLDYEA GRLGFYNAET
LAHVHTFSAA FLGA
//
