ID E5FGA5_MACSY Unreviewed; 497 AA.
AC E5FGA5;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Tripartite motif-containing protein 5 {ECO:0000256|ARBA:ARBA00014825};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
DE AltName: Full=RING-type E3 ubiquitin transferase TRIM5 {ECO:0000256|ARBA:ARBA00033283};
DE AltName: Full=TRIM5alpha {ECO:0000256|ARBA:ARBA00032496};
GN Name=TRIM5 {ECO:0000313|EMBL:ADQ48010.1};
OS Macaca sylvanus (Barbary macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9546 {ECO:0000313|EMBL:ADQ48010.1};
RN [1] {ECO:0000313|EMBL:ADQ48010.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21103414; DOI=10.1371/journal.pone.0014019;
RA Dietrich E.A., Jones-Engel L., Hu S.-L.;
RT "Evolution of the antiretroviral restriction factor TRIMCyp in Old World
RT primates.";
RL PLoS ONE 5:e14019-e14019(2010).
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 -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family.
CC {ECO:0000256|ARBA:ARBA00008518}.
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DR EMBL; HM468429; ADQ48010.1; -; mRNA.
DR AlphaFoldDB; E5FGA5; -.
DR UniPathway; UPA00143; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd19761; Bbox2_TRIM5-like; 1.
DR CDD; cd16591; RING-HC_TRIM5-like_C-IV; 1.
DR CDD; cd15822; SPRY_PRY_TRIM5; 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; IPR003877; SPRY_dom.
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; PTHR24103; E3 UBIQUITIN-PROTEIN LIGASE TRIM; 1.
DR PANTHER; PTHR24103:SF416; TRIPARTITE MOTIF-CONTAINING PROTEIN 5; 1.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR PRINTS; PR01407; BUTYPHLNCDUF.
DR SMART; SM00336; BBOX; 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 2: Evidence at transcript level;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Antiviral defense {ECO:0000256|ARBA:ARBA00023118};
KW Autophagy {ECO:0000256|ARBA:ARBA00023006};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Immunity {ECO:0000256|ARBA:ARBA00022859};
KW Innate immunity {ECO:0000256|ARBA:ARBA00022588};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
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 15..60
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 92..133
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 283..497
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000259|PROSITE:PS50188"
FT COILED 141..171
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 497 AA; 57468 MW; 3667559B85F10C00 CRC64;
MASGILVNVK EEVTCPICLE LLTEPLSLPC GHSFCQACIT ANHKKSMLYK EGERSCPVCR
ISYQPENIRP NRHVANIVEK LREVKLSPEE GQKVDHCARH GEKLLLFCQE DRKVICWLCE
RSQEHRGHHT FLMEEVAQKY HMKLQTALEM LRQKQQEAEK LEADIREEKA SWKIQIEYDK
TNVSADFEQL REILDWEESN ELQNLEKEEE DILKSLMKSE TEMVQQTQYM RELISDLEHR
LQGSMMELLQ GVDGIIKRIE NMTLKKPKTF HKNQRRVFRA PDLKGMLDMF RELTDARCYW
VDVTLAPNNM SHAVIAEDKR QVSSRNPQIM YQTPGTLFMF PSLTNFNYCT GVLGSQSITS
GKHYWEVDVS KKSAWILGVC AGFQLDAMYN IEQNENYQPK YGYWVIGLQE GVKYSVFQDG
SSHTPFAPFI VPLSVIICPD RVGVFVDYEA CTVSFFNITN HGFLIYKFSQ CSFSKPVFPY
LNPRKCTVPM TLCSPSS
//
