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Database: UniProt
Entry: A0A0A1TS11_9HYPO
LinkDB: A0A0A1TS11_9HYPO
Original site: A0A0A1TS11_9HYPO 
ID   A0A0A1TS11_9HYPO        Unreviewed;       719 AA.
AC   A0A0A1TS11;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   SubName: Full=Putative NEDD4-binding protein 2 {ECO:0000313|EMBL:CEJ95035.1};
GN   ORFNames=VHEMI10538 {ECO:0000313|EMBL:CEJ95035.1};
OS   [Torrubiella] hemipterigena.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae;
OC   Clavicipitaceae incertae sedis; 'Torrubiella' clade.
OX   NCBI_TaxID=1531966 {ECO:0000313|EMBL:CEJ95035.1, ECO:0000313|Proteomes:UP000039046};
RN   [1] {ECO:0000313|EMBL:CEJ95035.1, ECO:0000313|Proteomes:UP000039046}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Horn F., Habel A., Scharf D.H., Dworschak J., Brakhage A.A., Guthke R.,
RA   Hertweck C., Linde J.;
RT   "Draft Genome Sequence and Gene Annotation of the Entomopathogenic Fungus
RT   Verticillium hemipterigenum.";
RL   Genome Announc. 3:e01439-e01414(2015).
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DR   EMBL; CDHN01000008; CEJ95035.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A1TS11; -.
DR   STRING; 1531966.A0A0A1TS11; -.
DR   HOGENOM; CLU_015244_0_0_1; -.
DR   Proteomes; UP000039046; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0043170; P:macromolecule metabolic process; IEA:UniProt.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; IEA:InterPro.
DR   Gene3D; 3.30.1370.110; -; 1.
DR   Gene3D; 4.10.1000.10; Zinc finger, CCCH-type; 1.
DR   InterPro; IPR013899; DUF1771.
DR   InterPro; IPR002625; Smr_dom.
DR   InterPro; IPR036063; Smr_dom_sf.
DR   InterPro; IPR045124; Su(sable)-like.
DR   InterPro; IPR000571; Znf_CCCH.
DR   InterPro; IPR036855; Znf_CCCH_sf.
DR   PANTHER; PTHR13119:SF12; PROTEIN SUPPRESSOR OF SABLE; 1.
DR   PANTHER; PTHR13119; ZINC FINGER CCCH DOMAIN-CONTAINING PROTEI; 1.
DR   Pfam; PF08590; DUF1771; 1.
DR   Pfam; PF14608; zf-CCCH_2; 2.
DR   SMART; SM01162; DUF1771; 1.
DR   SMART; SM00463; SMR; 1.
DR   SMART; SM00356; ZnF_C3H1; 2.
DR   SUPFAM; SSF90229; CCCH zinc finger; 1.
DR   SUPFAM; SSF160443; SMR domain-like; 1.
DR   PROSITE; PS50828; SMR; 1.
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:UP000039046};
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          281..308
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   DOMAIN          311..333
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   DOMAIN          591..672
FT                   /note="Smr"
FT                   /evidence="ECO:0000259|PROSITE:PS50828"
FT   ZN_FING         281..308
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   ZN_FING         311..333
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   REGION          58..94
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          372..504
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        397..412
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        484..503
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   719 AA;  77862 MW;  14B7ED76A00C7BE7 CRC64;
     MISDEHYEIC LPILQDSTLE DEDKTDRMEE LLKKETNLTG SSLEHVILDA LWRFREGAGG
     SASPPPIRQS ILRRPSPASW RGPGTPLSGS PRLAVSPLAP PGYVPASFNR TKSSAPSPFS
     SPRASPRLAF ATPVIPHSPS LNAYEFASDP TPATEILGDY QAENVEWLVN DDAASVSSVG
     TTSSALNAAA PEFSFTTTQQ LDMSPYDMLR SILGQTRTDE EIETALASHG YDLSATIAAI
     MESKAQQASF AAASPPEEPK SVLIGKSISN ESRPSTPHSQ SKSSIICKFY MSTGQCLRAD
     CRFSHDLSNH ICKYWVMGNC LAGETCVFSH DPAKLMKEMS IDGSSTPPIN ANLQLQDLNS
     FPSLQSGGPD GFGGHHIYTG AMTPPPGLRT FHPAESPLSR SRPSSRQQQV KEVAVPAPSL
     DDNEAFPSLG SASLKQGKKH GGKRGGHGHK ENVVPNSLAD IVKMSPSPSP ASPRLAAKRP
     GTNGASRNGE NSAASQAIPS PQQIPWLETG DRANKAYLKA RQEAIKHGGL RNKFLQSAAQ
     AWNRNDARAA KALSLRGQSE NDLMRKAHRE AAKELYEERN RNPSGTSEIY VDLHGLHPEE
     AVEYLEKVLL ENSRETGAIY AITGTGHHSK NGKDKVGRAI RNFLNEWRYA YREFSVPGDR
     NNMGGILGID ARSWDKSLAR EEPAQEDKDV DILSQGVEIG DGNVRLLVRE TPKGPSGKR
//
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