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Database: UniProt
Entry: A0A1E3PCX0_9ASCO
LinkDB: A0A1E3PCX0_9ASCO
Original site: A0A1E3PCX0_9ASCO 
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
//
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