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
//