ID W8B1V6_CERCA Unreviewed; 716 AA.
AC W8B1V6;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 22-FEB-2023, entry version 26.
DE SubName: Full=E3 ubiquitin-protein ligase TRIM9 {ECO:0000313|EMBL:JAB92452.1};
DE Flags: Fragment;
GN Name=TRIM9 {ECO:0000313|EMBL:JAB92452.1};
OS Ceratitis capitata (Mediterranean fruit fly) (Tephritis capitata).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Tephritoidea;
OC Tephritidae; Ceratitis; Ceratitis.
OX NCBI_TaxID=7213 {ECO:0000313|EMBL:JAB92452.1};
RN [1] {ECO:0000313|EMBL:JAB92452.1}
RP NUCLEOTIDE SEQUENCE.
RA Geib S.;
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:JAB92452.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=24495485; DOI=10.1186/1471-2164-15-98;
RA Calla B., Hall B., Hou S., Geib S.M.;
RT "A genomic perspective to assessing quality of mass-reared SIT flies used
RT in Mediterranean fruit fly (Ceratitis capitata) eradication in
RT California.";
RL BMC Genomics 15:98-98(2014).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GAMC01014103; JAB92452.1; -; mRNA.
DR AlphaFoldDB; W8B1V6; -.
DR EnsemblMetazoa; XM_012301502.2; XP_012156892.1; LOC101463511.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd19803; Bbox1_TRIM9-like_C-I; 1.
DR CDD; cd19764; Bbox2_TRIM9-like; 1.
DR CDD; cd00063; FN3; 1.
DR CDD; cd12889; SPRY_PRY_TRIM67_9; 1.
DR Gene3D; 1.20.5.170; -; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 4.10.830.40; -; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR003649; Bbox_C.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR017903; COS_domain.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR000315; Znf_B-box.
DR PANTHER; PTHR24099; E3 UBIQUITIN-PROTEIN LIGASE TRIM36-RELATED; 1.
DR PANTHER; PTHR24099:SF15; E3 UBIQUITIN-PROTEIN LIGASE TRIM9; 1.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR SMART; SM00502; BBC; 1.
DR SMART; SM00336; BBOX; 2.
DR SMART; SM00060; FN3; 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; SSF49265; Fibronectin type III; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS51262; COS; 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS50119; ZF_BBOX; 2.
PE 2: Evidence at transcript level;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00024};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00024};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00024}.
FT DOMAIN 171..220
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 226..267
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 375..435
FT /note="COS"
FT /evidence="ECO:0000259|PROSITE:PS51262"
FT DOMAIN 450..543
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 525..713
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000259|PROSITE:PS50188"
FT REGION 1..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:JAB92452.1"
SQ SEQUENCE 716 AA; 77620 MW; D4F568BBB896C902 CRC64;
GGGGGGGGCL VHSHPLHGST ASHGNSITTT ATVHAHGGVG ASASVPTPQP PSSHPPSTRH
SSNSSAASTA SSATGSESVT SDQDQADKVS ILSEADSGVV CCSNTSRPVS YAGTAQLQGL
LQGAAAAAPP GAAFYLTCPL CRKLVFFDEG GVRNLPAYRT MESIVDRFCA REALRCQMCE
TDPKVASIVC EQCEIRYCDA CRELCHPARG PLAKHNLVKP RNAASQRESV CGEHEDTLSM
YCLVCKMPAC PQCIAEKQHP GHEVQSISVT CKAQKTELSH NLQQLSEKAR STTEFIQRLK
GMSDKVTESC MEFERLVTAQ CEALIQAIHD RREYLLEAIR MDKDTKIRIL KDQQSNCTGK
LQQTTGLIQF CIEALKETDS AAFLQVGSML INRVANTDMT WHQEVTNAAP RVSPIVDLTL
DDAALVRAID NLNFMQMKAV KDEEERLPAA PLAPTIVPED CSAENNSVTV AWHAPAHSFV
DGYVLELDDG SGGEFREVYC GKETICTVDG LHFNSMYNAR VKAFNNAGEG EYSELIGLQT
AEVAWFTFDP ILSGGAGSGL VFSNNNATVS VEGWEHRVAL GSVGFSRGIH YWEFTVDKYT
MDTDPAFGVA RIDVNRNKML GKDEKSFAMY IDGQRSWFQH NSVHERRVEG GITTGSTIGV
LLDLERHTLS FLVNEMPQGS VAFRDLYGVF YPAVSINRGV TLTLHTALVA PKMDYF
//
