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Database: UniProt
Entry: A0A1J1IN47_9DIPT
LinkDB: A0A1J1IN47_9DIPT
Original site: A0A1J1IN47_9DIPT 
ID   A0A1J1IN47_9DIPT        Unreviewed;       929 AA.
AC   A0A1J1IN47;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Zinc finger CCCH-type with G patch domain-containing protein {ECO:0000256|ARBA:ARBA00022414};
GN   ORFNames=CLUMA_CG014878 {ECO:0000313|EMBL:CRL01655.1};
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:CRL01655.1, ECO:0000313|Proteomes:UP000183832};
RN   [1] {ECO:0000313|EMBL:CRL01655.1, 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   -!- FUNCTION: Transcription repressor. {ECO:0000256|ARBA:ARBA00004062}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; CVRI01000056; CRL01655.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J1IN47; -.
DR   STRING; 568069.A0A1J1IN47; -.
DR   OrthoDB; 448298at2759; -.
DR   Proteomes; UP000183832; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   CDD; cd20384; Tudor_ZGPAT; 1.
DR   Gene3D; 2.30.30.1190; -; 1.
DR   Gene3D; 3.40.1810.10; Transcription factor, MADS-box; 1.
DR   InterPro; IPR000467; G_patch_dom.
DR   InterPro; IPR022102; HJURP_C.
DR   InterPro; IPR002100; TF_MADSbox.
DR   InterPro; IPR036879; TF_MADSbox_sf.
DR   InterPro; IPR000571; Znf_CCCH.
DR   PANTHER; PTHR46297:SF2; SMN (SURVIVAL OF MOTOR NEURON PROTEIN) RELATED; 1.
DR   PANTHER; PTHR46297; ZINC FINGER CCCH-TYPE WITH G PATCH DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF01585; G-patch; 1.
DR   Pfam; PF12347; HJURP_C; 1.
DR   Pfam; PF00319; SRF-TF; 1.
DR   PRINTS; PR00404; MADSDOMAIN.
DR   SMART; SM00443; G_patch; 1.
DR   SMART; SM00432; MADS; 1.
DR   SUPFAM; SSF55455; SRF-like; 1.
DR   PROSITE; PS50174; G_PATCH; 1.
DR   PROSITE; PS50066; MADS_BOX_2; 1.
DR   PROSITE; PS50103; ZF_C3H1; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000183832};
KW   Repressor {ECO:0000256|ARBA:ARBA00022491};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00723};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00723}.
FT   DOMAIN          131..158
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   DOMAIN          268..314
FT                   /note="G-patch"
FT                   /evidence="ECO:0000259|PROSITE:PS50174"
FT   DOMAIN          486..529
FT                   /note="MADS-box"
FT                   /evidence="ECO:0000259|PROSITE:PS50066"
FT   ZN_FING         131..158
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   REGION          223..249
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          547..576
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          633..705
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          795..819
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          848..929
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          417..444
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        633..652
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        848..899
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   929 AA;  103107 MW;  730AB6C37D65203D CRC64;
     MSNLNETTKQ DSCMISAYKH QLSQIKEALK KCENEEDLIN LQSLQNDLTE LIQLACLEEE
     SQESLSSEET SDINLDDFKN TFQSLINEKC RAPFKLKGQN ENYYNAFIAD VKNKTSEGDV
     IVQVFFLNPM EDKMKACDYF FSNTCTFEDN CRYSHGTLLP YSDLKPYHSS NYSLLKKGCH
     ALIKTEAGLW KPGIIMECNE DSRTCRVKMQ NGGKVVENCS YSDILPPLDN DSDSSDLSSD
     DSDEESGKFQ SSSVFIIEDN FGEWEKYTIG FGTKMLAKLG FINGQGLGKN SDGITQPVSA
     KMYIPGKSLD FNMEHNENKG QKTVEEKLRR QSLKHQKRNE RIQNRGNDVF DFINTIGSIN
     SPTPGNSKKE GFEVKTQSAA QLNIKNFKIE EEIKKVIKSL SQLKESLNRH KGDSIASKNI
     QKQITSKQNE IRDLERQLSD VNKEQIQHKD FCDLGNNGID FIFHFQALVL SKSSVMMKLI
     PYDVLRVTFN KRKFGVMKKA YELSVLCDCE IALIIFSSSN KLYQYASTDM DKVLLKYTEY
     NEPHESLTNK NIIEKENKNG QMSPESPEPD DSYTLTPRTE AKYNKIDEDF QMMMQRNQQL
     TSNRMGGGGS YTLPVSVPVG SYSDANMLQA SPQMAHQNIS PRPSSSETDS VYPSGGMLEM
     SNGYPSSPLG PSPSPSPVLG GHHNNKSHHI VHKQHSPVGP SRSTNLRVVI PTPTTSNMNS
     DDLSYAEHNR QSSSTLNTPV VALQTPIPGL NNYPVSTFGA QDFSMSSSDL NMITSWNSSH
     QNLGTLQHTR YGIPHLAVSN STPPPSSSSP APVKIKAEPI SPPRDQLLSQ HQQQTIVTSL
     GGGTSSVIGG VSHSSASSLG SNLNHSHMMN SRPSSTGGHL TPTPGSSTNP TSPGDMRHSQ
     SIGLSHLPDY DSPNAPHTKR PRISEGWST
//
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