ID G3T0F0_LOXAF Unreviewed; 494 AA.
AC G3T0F0;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 78.
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 Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000006439.4, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000006439.4, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000006439.4,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000006439.4}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000006439.4};
RG Ensembl;
RL Submitted (NOV-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 RefSeq; XP_003421569.1; XM_003421521.1.
DR AlphaFoldDB; G3T0F0; -.
DR STRING; 9785.ENSLAFP00000006439; -.
DR Ensembl; ENSLAFT00000007659.4; ENSLAFP00000006439.4; ENSLAFG00000007658.4.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000154647; -.
DR HOGENOM; CLU_013137_0_3_1; -.
DR InParanoid; G3T0F0; -.
DR OMA; QPQNGYW; -.
DR TreeFam; TF342569; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
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 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; 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; PF15227; zf-C3HC4_4; 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:UP000007646};
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..139
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 283..494
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000259|PROSITE:PS50188"
FT COILED 151..236
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 494 AA; 56865 MW; 1A95F503162D553D CRC64;
MASKILVNLE EGATCPICLE LLMEPISLDC GHSFCQACIT ADNKKSMVSQ EKESSCPVCR
IKYQPGNLRS NQHLASMVER LKEVKMSLEK EEKENYCVHH GEKLRLFCKL DGKFICWLCE
RSQEHHGHPT FLVEEVVPEY QKNLQAAFES LSKEQKKAEK WKADLREERD SWKKYIQTER
QSVRENFSQL RSILDNEEQK ELEELKSEEE SVMQNLSEAE NELGQQSDDV KKLMSDLQHR
LQGTTMEMLQ DVNDVIQGSK NTILEKPKTL PQKPRRIFQV PDMSLILCVM RELEDVQRYW
VNMTLNPINP ISNVVISEGG RQARIVPNSK SRNFCWSGSN DDDGIVGCLY IASGKHYWEV
DVSGKTSWIL GVCSDRCPEF SMLGAKQGVY LQNDYFRYQP KYGYWVIGLE NQSGYKVFEN
LCLGSQNLIF SLAVPPCRVG IFLDYEFGTV SFFNVTNYGF LIYKFSNCCF SGTVYPYFNP
MKCEVPMSLC LPSF
//
