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
//