ID K9IKG3_DESRO Unreviewed; 480 AA.
AC K9IKG3;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=Tripartite motif-containing protein 10 {ECO:0000256|ARBA:ARBA00014653};
OS Desmodus rotundus (Vampire bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Phyllostomidae;
OC Desmodontinae; Desmodus.
OX NCBI_TaxID=9430 {ECO:0000313|EMBL:JAA47720.1};
RN [1] {ECO:0000313|EMBL:JAA47720.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Salivary gland {ECO:0000313|EMBL:JAA47720.1};
RA Francischetti I.M.B., Assumpcao T.C.F., Ma D., Vicente E.C.,
RA Ribeiro J.M.C.;
RT "The Vampirome: Transcriptome and Proteome Analysis of the Submandibular
RT and Accessory Glands of the Vampire Bat and Vector of Human Rabies,
RT Desmodus rotundus.";
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Interacts with IFNAR1; this interaction prevents association
CC of IFNAR1 with TYK2. {ECO:0000256|ARBA:ARBA00025816}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family.
CC {ECO:0000256|ARBA:ARBA00008518}.
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DR EMBL; GABZ01005805; JAA47720.1; -; mRNA.
DR AlphaFoldDB; K9IKG3; -.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd16593; RING-HC_TRIM10_C-IV; 1.
DR CDD; cd15827; SPRY_PRY_TRIM10; 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; IPR042784; TRIM10_RING-HC.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
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:SF329; TRIPARTITE MOTIF-CONTAINING PROTEIN 10; 1.
DR Pfam; PF13765; PRY; 1.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR Pfam; PF00097; zf-C3HC4; 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; 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 Coiled coil {ECO:0000256|SAM:Coils}; Ligase {ECO:0000313|EMBL:JAA47720.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00024}.
FT DOMAIN 16..61
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 93..134
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 291..480
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000259|PROSITE:PS50188"
FT COILED 142..169
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 480 AA; 55261 MW; 34F4F484954E6629 CRC64;
MASATSVTSL EDEVNCPICQ GSLREPVTIG CGHNFCRGCL TRYCEIPGAD PEEPPTCPLC
KEPFRPGSFR PNWQLASVVE NIERLKLVSR PSPEEDVCRE HGEKVYFFCE DDEMQLCVVC
REAEEHRAHT VRFLEEAAKP YREQIQKCLE CLRREREEIQ EIQSRENQRL RVLLSQVATK
RQRVIFEFAH LSQFLDEQHG TLLAQLERLD GDILKQQDEF DVLVAGEMCR FTALIKELEE
KKERPARELL TNIRSTLIRC ETRKCRKPEA VSPELGQRIR DFPQQVSLLQ REMELFLEKL
CFELDYEPAH ISLDPKTSHP KLLLSEDHQG ARFSYKWQNS PDNPQRFDWA TCVLAHGGFT
GGRHTWVVNV DLAHGGSCTV GVVREDVRRK GELQLRPEEG VWALRLAWGF VSALGSFPTR
LTLKEHPRQV RVSLDYEVGW VTFLNAVTQE PIYTFTTSFT QKVFPFFGLW GRGSSFSLSS
//
