ID A0A1E3PCX0_9ASCO Unreviewed; 251 AA.
AC A0A1E3PCX0;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=C3H1-type domain-containing protein {ECO:0000259|PROSITE:PS50103};
GN ORFNames=NADFUDRAFT_53528 {ECO:0000313|EMBL:ODQ63256.1};
OS Nadsonia fulvescens var. elongata DSM 6958.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetales incertae sedis; Nadsonia.
OX NCBI_TaxID=857566 {ECO:0000313|EMBL:ODQ63256.1, ECO:0000313|Proteomes:UP000095009};
RN [1] {ECO:0000313|EMBL:ODQ63256.1, ECO:0000313|Proteomes:UP000095009}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6958 {ECO:0000313|EMBL:ODQ63256.1,
RC ECO:0000313|Proteomes:UP000095009};
RX PubMed=27535936; DOI=10.1073/pnas.1603941113;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goeker M.,
RA Salamov A.A., Wisecaver J.H., Long T.M., Calvey C.H., Aerts A.L.,
RA Barry K.W., Choi C., Clum A., Coughlan A.Y., Deshpande S., Douglass A.P.,
RA Hanson S.J., Klenk H.-P., LaButti K.M., Lapidus A., Lindquist E.A.,
RA Lipzen A.M., Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J.L.,
RA Peng Y., Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C.,
RA Stielow J.B., Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V.,
RA Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:9882-9887(2016).
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DR EMBL; KV454415; ODQ63256.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E3PCX0; -.
DR STRING; 857566.A0A1E3PCX0; -.
DR OrthoDB; 23913at2759; -.
DR Proteomes; UP000095009; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IEA:InterPro.
DR GO; GO:0043170; P:macromolecule metabolic process; IEA:UniProt.
DR Gene3D; 4.10.1000.10; Zinc finger, CCCH-type; 1.
DR InterPro; IPR045877; ZFP36-like.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR PANTHER; PTHR12547; CCCH ZINC FINGER/TIS11-RELATED; 1.
DR PANTHER; PTHR12547:SF18; PROTEIN TIS11; 1.
DR Pfam; PF00642; zf-CCCH; 1.
DR SMART; SM00356; ZnF_C3H1; 2.
DR SUPFAM; SSF90229; CCCH zinc finger; 2.
DR PROSITE; PS50103; ZF_C3H1; 2.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00723}; Reference proteome {ECO:0000313|Proteomes:UP000095009};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00723};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00723}.
FT DOMAIN 178..212
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 225..251
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT ZN_FING 178..212
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 225..251
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 132..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 251 AA; 28327 MW; EAEC86659755B900 CRC64;
MKDSYNPYTY TRPAHRHFPT APSSTSSLVS NISLSTAASS SHWDTLLPDV WGDLSDETEE
ASRLCPKSRL WSSRRDCSPE FSLDFVDDAS PDQDLPEFNQ HILNSVNDLM AHLDLEIPMG
PQDSTTAQDF WSLSTLSPDP QSSTLPSTSP VADIDPTPKK KKKRSKNRKK SPKTNADLYK
TEPCVAYAQS LKTKRVGKCP YGDKCQFAHG PEELRSVAET LRPQNYRSKR CVNWAKYGVC
VYNDRCCFRH E
//