ID   A1CRK6_ASPCL            Unreviewed;       792 AA.
AC   A1CRK6;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   RecName: Full=DNA repair protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ACLA_030100 {ECO:0000313|EMBL:EAW08277.1};
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:EAW08277.1, ECO:0000313|Proteomes:UP000006701};
RN   [1] {ECO:0000313|EMBL:EAW08277.1, 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).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the DNA repair metallo-beta-lactamase (DRMBL)
CC       family. {ECO:0000256|ARBA:ARBA00010304}.
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DR   EMBL; DS027059; EAW08277.1; -; Genomic_DNA.
DR   RefSeq; XP_001269703.1; XM_001269702.1.
DR   AlphaFoldDB; A1CRK6; -.
DR   STRING; 344612.A1CRK6; -.
DR   EnsemblFungi; EAW08277; EAW08277; ACLA_030100.
DR   GeneID; 4701821; -.
DR   KEGG; act:ACLA_030100; -.
DR   VEuPathDB; FungiDB:ACLA_030100; -.
DR   eggNOG; KOG1361; Eukaryota.
DR   HOGENOM; CLU_013294_1_1_1; -.
DR   OMA; VFYFRAW; -.
DR   OrthoDB; 23465at2759; -.
DR   Proteomes; UP000006701; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR   Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR   InterPro; IPR011084; DRMBL.
DR   InterPro; IPR001279; Metallo-B-lactamas.
DR   InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR   PANTHER; PTHR23240; DNA CROSS-LINK REPAIR PROTEIN PSO2/SNM1-RELATED; 1.
DR   PANTHER; PTHR23240:SF39; REPAIR PROTEIN, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G04570)-RELATED; 1.
DR   Pfam; PF07522; DRMBL; 1.
DR   Pfam; PF12706; Lactamase_B_2; 1.
DR   SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
PE   3: Inferred from homology;
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006701}.
FT   DOMAIN          44..172
FT                   /note="Metallo-beta-lactamase"
FT                   /evidence="ECO:0000259|Pfam:PF12706"
FT   DOMAIN          453..481
FT                   /note="DNA repair metallo-beta-lactamase"
FT                   /evidence="ECO:0000259|Pfam:PF07522"
FT   REGION          522..598
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          622..755
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        527..541
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        571..589
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        652..689
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        716..733
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   792 AA;  87438 MW;  E022AFED1B6AF2E9 CRC64;
     MSTFDGIVPE FPFIQSELQA VIPVDETQLL KSFTVDYFRK NPDRPPPLAC FLSHVHSDHL
     QGLESFRAPF IYCSAATREM LLRIEKYPHR MNFSKGILES RRLHYKHLSR LLRPIPLNTP
     TEIELTPLLS IRVTLFDANH CAGAVMFLIE GDGNAILYTG DIRAEPWWVN SLIRHPVLIP
     YTLCGKRLDK IYIDTTFARA NHVCPSFPSK AEGLSELLQM VERYPQDTVF YFRAWTFGYE
     DVWVALSARL NSKIHVDRYQ VGLYRSLGSY SLGGTAEAPA LCGFELGNRF VPGCLSEDES
     ARVHSCEPGM HCSACRTQNT VYILPIVGRA RDGTRVPELG AGGGGGDLYQ THELELPDQS
     ALQQLERLCL EQIPDLETLS QTREVLAQAF KSKTKALSLD RFGMKDVADM PLEELVRILS
     RGRSDKELWS MNPEVSPSTL RDTAGNRLPK VIYFPYSRHS SYEELCTLVS AFKPKDVHPY
     TVDPHEWTED ISIRALFGHL CSGDDFAHDQ YMRATIAAAA ADGGDYNTPH PRKRTRHDDE
     VSSTQSSSIP IAIAMPDSID RASPSRARHE PPAAPDLPVP IPIPIPIPPS TAAAQKSKRN
     EIRRAWHLLH ALDPLAHPHI HPGALPSSWP TAEEDGFDQL DEKPTPGVDP DAESNSIPNS
     SCVDASQSPQ ASSSSSSSSS SSSSSAAASE EADVDAGIEP DAEAGAQAEV EAEAEPDQQP
     TSQISLSSSA FASQDQERER EPGSEPPPLH RSSSSFARRA AYLAARADSY ETWALAGLVS
     VGENHSREER EL
//