ID A0A1J1HVU8_9DIPT Unreviewed; 606 AA.
AC A0A1J1HVU8;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=CLUMA_CG005732, isoform A {ECO:0000313|EMBL:CRK92141.1};
GN ORFNames=CLUMA_CG005732 {ECO:0000313|EMBL:CRK92141.1};
OS Clunio marinus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Chironomoidea; Chironomidae;
OC Clunio.
OX NCBI_TaxID=568069 {ECO:0000313|EMBL:CRK92141.1, ECO:0000313|Proteomes:UP000183832};
RN [1] {ECO:0000313|EMBL:CRK92141.1, ECO:0000313|Proteomes:UP000183832}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Syromyatnikov M.Y., Popov V.N.;
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the SH3RF family.
CC {ECO:0000256|ARBA:ARBA00008649}.
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DR EMBL; CVRI01000024; CRK92141.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J1HVU8; -.
DR STRING; 568069.A0A1J1HVU8; -.
DR OrthoDB; 5407056at2759; -.
DR Proteomes; UP000183832; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0060255; P:regulation of macromolecule metabolic process; IEA:UniProt.
DR GO; GO:0009966; P:regulation of signal transduction; IEA:UniProt.
DR CDD; cd11787; SH3_SH3RF_2; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 3.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
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; PTHR14167; SH3 DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR14167:SF77; SH3 DOMAIN-CONTAINING PROTEIN 3; 1.
DR Pfam; PF00018; SH3_1; 2.
DR Pfam; PF14604; SH3_9; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00184; RING; 1.
DR SMART; SM00326; SH3; 3.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF50044; SH3-domain; 3.
DR PROSITE; PS50002; SH3; 3.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000183832};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 12..55
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 130..192
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 263..325
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 544..605
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 85..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 363..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 505..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 606 AA; 67852 MW; FB9638F7FC2D9360 CRC64;
MDFSLLDSII ECSVCLERLK QDARVLPCQH TFCLDCLKRV ANKNPQTPIA CPECRQQTNI
YDINLLPKNV FLIRLLDQIK QKANGSPDVK DEEISTPITT TNSSDKTKVV STGVSQSKPQ
QNEVKQHQQT SVPHAKALYD FQMNPLEDEG CLKFQKGMII QVTRRVDQNW AEGKLGESVG
IFPLSFVNMN QAATSLMQSY ATKWRLPASM PSTSNYEQAP TTSTNPLRQI PVLQPTPAHP
YLIRPTSPSN NNINQNKSNV LQDKSGIYIA LHNYTPQKPD ELELKKGLQY IVKEACQDGW
LKGCCSDNLF RKGVFPGNYV MPLAYHQKLM SAQRNSNFQT QKNQTNLNTQ QMRTTGAYTN
LGLSSIPPEL PQRNVIPSSR TSHSPLAHTN NTPESMASET TTAQTQKTDD NLNKLNKKET
VTEMLMKKLG YTRKSNDSSV YSMDNPVFED STTTSKVGSS NQLFYNHNRS GSCPIDLGIS
NSDIENLQTN SDTKSNAIVT KRHSINLSGP SSTTKHIQNT QIKTQHRKSS SLDTTSLEPN
NSTTQMARYR CVTKYPANSR FELSLNVGDI VILQKKRDNG WYKGELTRTG QVGLFPANFV
ELVENN
//