ID A1CAN2_ASPCL Unreviewed; 446 AA.
AC A1CAN2;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=C3HC4 finger protein {ECO:0000313|EMBL:EAW12800.1};
GN ORFNames=ACLA_012280 {ECO:0000313|EMBL:EAW12800.1};
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:EAW12800.1, ECO:0000313|Proteomes:UP000006701};
RN [1] {ECO:0000313|EMBL:EAW12800.1, 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; DS027049; EAW12800.1; -; Genomic_DNA.
DR RefSeq; XP_001274226.1; XM_001274225.1.
DR AlphaFoldDB; A1CAN2; -.
DR STRING; 344612.A1CAN2; -.
DR EnsemblFungi; EAW12800; EAW12800; ACLA_012280.
DR GeneID; 4706436; -.
DR KEGG; act:ACLA_012280; -.
DR VEuPathDB; FungiDB:ACLA_012280; -.
DR eggNOG; ENOG502SBGS; Eukaryota.
DR HOGENOM; CLU_613903_0_0_1; -.
DR OMA; YSHIRTA; -.
DR OrthoDB; 75723at2759; -.
DR Proteomes; UP000006701; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:UniProt.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR14879; CASPASE REGULATOR, RING FINGER DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR14879:SF5; RING-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF13920; zf-C3HC4_3; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 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:PRU00175}.
FT DOMAIN 385..434
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 216..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..298
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..376
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 446 AA; 49065 MW; FD609273A299B7EF CRC64;
MDVQLPHPAI GEPSSMAPVL PNLQNNGSHG ALGSQNISQG APTGTTSGSS RPHFHGQNSN
TNMYTTPTFS GDFTFTAANN GQLNFQPVMQ LPTNTVAQPT QMEFSAPPQN TATFDQRQHG
NAIRYWHMQR PSYPQMRPTP IQPPNSTSIN GQPVLVQQAH HAQSQNSTAP NYRMTPQDTG
TNNIQAAHSA SGVGGRPIYP RPFYVQPSQY MPYPQSGVSP GITQNRRHSR TQSSTINSHS
TNISPGSPPQ HIRAGGQVGR RRTRPADEAN PQFARQISTS QVPRVPNTAT SSMGSESPMM
ETPRYFTYLT PEHRLHIQRL AELEALTNSI RSGHPVSGSH VRRSLDNDGY DLDDDLPETP
RGLDDAKDGR PEPKEDDELT VNLECKICMS QLVDTVMLPC GHAILCRWCA EQHMPSSRVD
RTWIKGQPVC PMCRAAVKSK IRIYLS
//
