ID A1CPR3_ASPCL Unreviewed; 802 AA.
AC A1CPR3;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE SubName: Full=RING finger ubiquitin ligase (Tul1), putative {ECO:0000313|EMBL:EAW07634.1};
GN ORFNames=ACLA_023480 {ECO:0000313|EMBL:EAW07634.1};
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:EAW07634.1, ECO:0000313|Proteomes:UP000006701};
RN [1] {ECO:0000313|EMBL:EAW07634.1, 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; EAW07634.1; -; Genomic_DNA.
DR RefSeq; XP_001269060.1; XM_001269059.1.
DR AlphaFoldDB; A1CPR3; -.
DR STRING; 344612.A1CPR3; -.
DR EnsemblFungi; EAW07634; EAW07634; ACLA_023480.
DR GeneID; 4700888; -.
DR KEGG; act:ACLA_023480; -.
DR VEuPathDB; FungiDB:ACLA_023480; -.
DR eggNOG; KOG0828; Eukaryota.
DR HOGENOM; CLU_010475_0_0_1; -.
DR OMA; LEGWMRF; -.
DR OrthoDB; 51730at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000006701; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
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; PTHR22763; RING ZINC FINGER PROTEIN; 1.
DR PANTHER; PTHR22763:SF165; TRANSMEMBRANE E3 UBIQUITIN-PROTEIN LIGASE 1; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Ligase {ECO:0000313|EMBL:EAW07634.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Reference proteome {ECO:0000313|Proteomes:UP000006701};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..802
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002633084"
FT TRANSMEM 386..405
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 417..438
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 444..465
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 551..569
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 575..593
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 614..632
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 732..796
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 478..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 514..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 802 AA; 90267 MW; 77FB99BD1F037CF2 CRC64;
MDNRGSFFFF LIVFYLLLSS QSRPPLIDQD REHQREVARE RDALRLLNET NYGDFDPQAD
KWLPFTGVRK NDSYAWDILP HAQDRARHQL RNAILDAGLE PPKVLEDPEA SPPLNFTQLL
LPVYRNVTGK LRGEWVRRKQ DGEHPKLNTT AIALENEYFT HEFSLNITGS SGTFYLDLRE
GGGEELRVDD GHVREIRATL AVESDDLWEN TWYLSLFGVH FPESGGIILT STSEKYGGLF
ALPHLTLSPD AYELSHRLLM KSLSDTLSEK ANRPPTLFPW PSLVGSEQVE FPAPKCEHVV
YIQQHPVSIH GSLADKPLID QIEQELRYPI GAPIPSAPLM VMSAVVFSPD CGYILETKGT
PDFPPSEALY LSGPKIEEFG KYSARLVFLV CGVFAAQITL LLRQIKEAST PSTRSRISFY
TIALMAIGDA FVLVFILLEL YPSVSFLVMT TASFLTFLSV SYIGMKFMME IWAVQAPERR
EQERRSNPTP NQRTGGLPLP ATMARDTGAT PIIVTPDQDP PAEENDLPTN RGTAPTAQET
RNDVGAMYAR FYFTLFVMLI ISIWSFLWPN RLGALYARAL AFVYLSFWVP QIGRNVMRNC
RKALRWDFVV GQSLLRLFPF IYFLTVRGNV LFVRPDTTTA MALAGWIWAQ VWILASQDIL
GPRFFVPRGW APPAYDYHPV LRDSTDPEAD LESGGVLPIG ALRADERDIS TDSKDGEDKP
RSKDRKKAVF DCAICMQEIE VPVLAALGAA GGSSVTDGAT SILSRRTYMI TPCRHIFHST
CLESWMRLRL QCPICRESIP PV
//
