ID Q3MJK4_PIG Unreviewed; 492 AA.
AC Q3MJK4;
DT 25-OCT-2005, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2005, sequence version 1.
DT 27-MAR-2024, entry version 109.
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};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|EMBL:AAY40468.1};
RN [1] {ECO:0000313|EMBL:AAY40468.1}
RP NUCLEOTIDE SEQUENCE.
RA Smith T.P.L., Uenishi H.;
RT "Complete CDS sequence of porcine tripartite motif protein TRIM5.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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; AY970971; AAY40468.1; -; mRNA.
DR RefSeq; NP_001037997.1; NM_001044532.1.
DR AlphaFoldDB; Q3MJK4; -.
DR SMR; Q3MJK4; -.
DR GeneID; 733579; -.
DR KEGG; ssc:733579; -.
DR OrthoDB; 3453019at2759; -.
DR Genevisible; Q3MJK4; SS.
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 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 282..492
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000259|PROSITE:PS50188"
FT COILED 134..175
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 492 AA; 56756 MW; FE926F980FE26940 CRC64;
MASGILENIR EEVTCPICLE LLKEPLSLDC GHSFCQDCLT VNSKKSMMGL EGKSNCPVCR
VSYQPGNLRL NRHVANIVER LRKVSLSPEV AQKGNLCVHH EEKLLFFCKE DGKVICWICE
RSQQHCDHQT FLVEEVAQEY QKKLQDALER LQEEQKEAEK LEAQVREEVS SWKNQIQSEQ
QSVQAEFMRL RGILENEELK EMQMLKDEEK VILSDLADSK DELAQQTQLV GELISEVERR
LLGSKLEMLQ DVNDILKRSE TLTLKKPKAF PKEQRRVFRA PDLREILCVF NKLTDVRRYW
VHVTLNNLKI KSDVTISVDR RQVRYARKFG LSSTCPNGDF EDCSVLGYPL ISSGKHYWEV
DVSGKRAWIL GVYGRKLSNC LFCFSKSNQH PYWRYKPKYG YWVIWLNDKG EYNTFEESSS
SDSGPLTLSL GVPPRRIGVF LEYEAGTVSF FNITNHGSLI YRFSSCPFSQ ATFPYFNPMK
CHIPMILCSP GS
//
