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Database: UniProt
Entry: A0A2K5ZNA0_MANLE
LinkDB: A0A2K5ZNA0_MANLE
Original site: A0A2K5ZNA0_MANLE 
ID   A0A2K5ZNA0_MANLE        Unreviewed;       488 AA.
AC   A0A2K5ZNA0;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 28.
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|Ensembl:ENSMLEP00000029253.1};
OS   Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Mandrillus.
OX   NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000029253.1, ECO:0000313|Proteomes:UP000233140};
RN   [1] {ECO:0000313|Ensembl:ENSMLEP00000029253.1}
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   -!- 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   AlphaFoldDB; A0A2K5ZNA0; -.
DR   Ensembl; ENSMLET00000052808.1; ENSMLEP00000029253.1; ENSMLEG00000038751.1.
DR   GeneTree; ENSGT00940000154647; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000233140; Unplaced.
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   3: Inferred from homology;
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   Reference proteome {ECO:0000313|Proteomes:UP000233140};
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          273..488
FT                   /note="B30.2/SPRY"
FT                   /evidence="ECO:0000259|PROSITE:PS50188"
FT   COILED          137..171
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   488 AA;  56082 MW;  71A07714B2CEAD9F CRC64;
     MASGILLNVK EEVTCPICLE LLTEPLSLPC GHSFCQACIT ANHRKSMLYK EGERSCPVCR
     ISYQPENIQP NRHVANIVEK LREVKLSPEE GQKVDHCARH GEKLLLFCQE DSKVICWLCE
     RSQEHRGHHT FLMEEVAQEY HVKLQTALEM LRQKQQEAEK LEADIREEKA SWKIQIDYDK
     TNVLADFQQL REILDLEESN ELQNLEKEEE DILKSLTKSE TEMVQQTQYM RELISDLEHR
     LQGSMMELLQ GVDGIIKRIE NMTLKKPKTF HKNQRRVFRA PDLKGMLDMF RVDVTLAPNN
     ISHAVIAEDK RQVSSRNPQI MYQAPGTLFS FPSHTNFNYC TGVLGSQSIT SGKHYWEVDV
     SKKSAWILGV CAGFQLDAMY NIEQNENYQP KYGYWVIGLQ KGVKYSVFQD GSSHTPFAPF
     IVPLSVIICP DRVGVFVDYE ACTVSFFNIT NHGFLIYKFS QCSFSKPVFP YLNPRKCTVP
     MTLCSPSS
//
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