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Database: UniProt
Entry: A1CQL9_ASPCL
LinkDB: A1CQL9_ASPCL
Original site: A1CQL9_ASPCL 
ID   A1CQL9_ASPCL            Unreviewed;       752 AA.
AC   A1CQL9;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   24-JAN-2024, entry version 82.
DE   SubName: Full=CHY zinc finger domain protein {ECO:0000313|EMBL:EAW07940.1};
GN   ORFNames=ACLA_026570 {ECO:0000313|EMBL:EAW07940.1};
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612 {ECO:0000313|EMBL:EAW07940.1, ECO:0000313|Proteomes:UP000006701};
RN   [1] {ECO:0000313|EMBL:EAW07940.1, ECO:0000313|Proteomes:UP000006701}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1
RC   {ECO:0000313|Proteomes:UP000006701};
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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DR   EMBL; DS027059; EAW07940.1; -; Genomic_DNA.
DR   RefSeq; XP_001269366.1; XM_001269365.1.
DR   AlphaFoldDB; A1CQL9; -.
DR   STRING; 344612.A1CQL9; -.
DR   EnsemblFungi; EAW07940; EAW07940; ACLA_026570.
DR   GeneID; 4701136; -.
DR   KEGG; act:ACLA_026570; -.
DR   VEuPathDB; FungiDB:ACLA_026570; -.
DR   eggNOG; KOG1940; Eukaryota.
DR   HOGENOM; CLU_013368_4_3_1; -.
DR   OMA; STKCDCP; -.
DR   OrthoDB; 325136at2759; -.
DR   Proteomes; UP000006701; Unassembled WGS sequence.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd16464; RING-H2_Pirh2-like; 1.
DR   Gene3D; 2.20.28.10; -; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR039512; RCHY1_zinc-ribbon.
DR   InterPro; IPR008913; Znf_CHY.
DR   InterPro; IPR037274; Znf_CHY_sf.
DR   InterPro; IPR017921; Znf_CTCHY.
DR   InterPro; IPR037275; Znf_CTCHY_sf.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR21319:SF0; AND RING FINGER DOMAIN PROTEIN, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G08900)-RELATED; 1.
DR   PANTHER; PTHR21319; RING FINGER AND CHY ZINC FINGER DOMAIN-CONTAINING PROTEIN 1; 1.
DR   Pfam; PF05495; zf-CHY; 1.
DR   Pfam; PF13639; zf-RING_2; 1.
DR   Pfam; PF14599; zinc_ribbon_6; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF161219; CHY zinc finger-like; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF161245; Zinc hairpin stack; 1.
DR   PROSITE; PS51266; ZF_CHY; 1.
DR   PROSITE; PS51270; ZF_CTCHY; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006701};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00601}.
FT   DOMAIN          318..385
FT                   /note="CHY-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51266"
FT   DOMAIN          387..453
FT                   /note="CTCHY-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51270"
FT   DOMAIN          454..496
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          22..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          221..313
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          574..600
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          655..684
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          704..752
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        221..235
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        247..286
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        585..600
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        710..745
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   752 AA;  83391 MW;  88166964DB797D1B CRC64;
     MSGRISSLLI EPVVRQACRL SQQLDSHPPY DDDLGDSQTS IRDRSSLIGP NSTDLAVINN
     GLESERAVLH PSKGQAELDH TAPFTQPEQS LHESSGRHDD YGESFFAIQP TTGIPIASSS
     NQPVLTGPMH DDGNYSDPAV VGIAAGVNSI PAQNLVQETN RSVQGTNLSP ASGNDTDIIG
     AQYLLPEDDG MGVLRRKIHA IRDLESTNDA KARMIHELMT ERYHASREKK EDTTPSPPRP
     ASPSSSWAFE RPITPRSHQS SPSLDREPVT PVSTASIRQP RTEISHNLTA EDLMPTFFPR
     PVPDSPAGDR EDGDIEDVEE PCLGCRHYKR NVKLQCFACK KWYTCRFCHD EAEDHHLNRP
     KTENMLCMLC GHPQPAAQVC RQCGEHAAQY YCDICKLWDN DSNKSIYHCN DCGICRIGQG
     LGKDFFHCKT CSVCLPISIE NTHRCIERST QCDCPICGDY MFTSPETVVF MRCGHSIHQK
     CLSEYSKSSY RCPICSKTIA NMESTFRNLD RTIQSQPMPA EFKDTHALIH CNDCGAKSVV
     KYHWLGLKCD MCESYNTAQV QLLHSDALDA LEQENEENRN DLTSRLRSSS HGAENIAPSL
     SSIQSRIDTE TLSGANLSPR FRAASSTEPT ARFSSYSLTR GRAVSPVISN YFGLPPDRET
     DRSRSTTSFF GGLTSKAGDD HSGGELSLWG TRIRYKYGFL DRDTESVDGV SDAQEDDVDD
     DDDDNSTEDA ERPGGEDDDD DDDESIDIFG HR
//
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