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Database: UniProt
Entry: A0A443HZH4_BYSSP
LinkDB: A0A443HZH4_BYSSP
Original site: A0A443HZH4_BYSSP 
ID   A0A443HZH4_BYSSP        Unreviewed;       806 AA.
AC   A0A443HZH4;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=DNA repair protein {ECO:0000313|EMBL:RWQ97131.1};
GN   ORFNames=C8Q69DRAFT_462445 {ECO:0000313|EMBL:RWQ97131.1};
OS   Byssochlamys spectabilis (Paecilomyces variotii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Thermoascaceae; Paecilomyces.
OX   NCBI_TaxID=264951 {ECO:0000313|EMBL:RWQ97131.1, ECO:0000313|Proteomes:UP000283841};
RN   [1] {ECO:0000313|EMBL:RWQ97131.1, ECO:0000313|Proteomes:UP000283841}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 101075 {ECO:0000313|EMBL:RWQ97131.1,
RC   ECO:0000313|Proteomes:UP000283841};
RX   PubMed=30619145; DOI=10.3389/fmicb.2018.03058;
RA   Urquhart A.S., Mondo S.J., Makela M.R., Hane J.K., Wiebenga A., He G.,
RA   Mihaltcheva S., Pangilinan J., Lipzen A., Barry K., de Vries R.P.,
RA   Grigoriev I.V., Idnurm A.;
RT   "Genomic and genetic insights into a cosmopolitan fungus, Paecilomyces
RT   variotii (Eurotiales).";
RL   Front. Microbiol. 9:3058-3058(2018).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RWQ97131.1}.
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DR   EMBL; RCNU01000003; RWQ97131.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A443HZH4; -.
DR   STRING; 264951.A0A443HZH4; -.
DR   OrthoDB; 23465at2759; -.
DR   Proteomes; UP000283841; 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:UP000283841}.
FT   DOMAIN          29..150
FT                   /note="Metallo-beta-lactamase"
FT                   /evidence="ECO:0000259|Pfam:PF12706"
FT   DOMAIN          425..463
FT                   /note="DNA repair metallo-beta-lactamase"
FT                   /evidence="ECO:0000259|Pfam:PF07522"
FT   REGION          405..427
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          501..612
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          651..700
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          717..806
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        411..427
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        501..536
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        552..593
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        726..741
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        742..765
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   806 AA;  91022 MW;  68B9CE1E735F0692 CRC64;
     MSTFDGIVEE FPFIRIDYFR KNPDRPSPLA CFLSHVHSDH LQGLESLRSP FIYCSAATRE
     LLLRIEKYPH RMNFSKGILE SRKQHYNHLA KLLRPIPLNT PTEIELTPRL RIRVTLLDAN
     HCLGAVMFLI EGDGKAVLYT GDIRAETWWV NSLIRHPVLI PYTLGNKRLN KVYLDTTFAI
     KSDVYRSFPS KAEGIKELLD KVYAYPDDTV FYLRAWTFGY EDVWLALSAA LNSKIHVDRY
     QRRLYQSLHP RNDGKVPEAA FLCGFELGNN FSPGCLTGDE SCRIHSCEPG MFCPVIASGR
     AVYITPIVTR SDDVEVPEVG AGGGGGDLYQ SHELELPDES SVEQLEKLCL QHIHDPNILT
     RTKGALIEAF RSKKKTLSLD RYGLKDENDI SLQRLVDVLS RGQSLDTTGS NQYEDKERAA
     GGRTESKRQL PRKITFPYSR HSSYAELCEL IAAFRPKDIY PCTVDPETWS EDVSMARLFG
     HLCSGDIFSH DEYMYKFLSE QQRPQQQMQD ISSSTQPSQQ SSEQSSQISH ALFSQPATGP
     TEHDRVPKTH TRQLPTGPSS DSSHTRNDAQ PSNSTTTSLQ KSAAPTSEHH SPSMNHEPPP
     IPERTEKARK HRNSIRRTWY KIEELRRQGK WHFHNEPLPT WWPTEEEDLY HAEEPSSDEA
     SDVSDPDTPF LVTEDPSITD VNNIAPIDPI DTDVDADADA DLPYSQTSTL SISLSMSMSE
     SAFDSQEQPP PPPPPPDSTP QTTPNINDSN NNRITNGSNG NNKRKRLPDP SIRNRIRAYH
     AARSGSWSDV SLLSAGNNHT EEEQEL
//
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