ID A0A2H0ZJX5_CANAR Unreviewed; 565 AA.
AC A0A2H0ZJX5;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Photolyase/cryptochrome alpha/beta domain-containing protein {ECO:0000259|PROSITE:PS51645};
GN ORFNames=B9J08_004445 {ECO:0000313|EMBL:PIS50617.1}, CA7LBN_004532
GN {ECO:0000313|EMBL:QWW25645.1};
OS Candida auris (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Metschnikowiaceae incertae sedis;
OC Candida/Metschnikowiaceae.
OX NCBI_TaxID=498019 {ECO:0000313|EMBL:PIS50617.1, ECO:0000313|Proteomes:UP000230249};
RN [1] {ECO:0000313|EMBL:PIS50617.1, ECO:0000313|Proteomes:UP000230249}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B8441 {ECO:0000313|EMBL:PIS50617.1,
RC ECO:0000313|Proteomes:UP000230249};
RX PubMed=27988485; DOI=.1093/cid/ciw691;
RA Lockhart S.R., Etienne K.A., Vallabhaneni S., Farooqi J., Chowdhary A.,
RA Govender N.P., Colombo A.L., Calvo B., Cuomo C.A., Desjardins C.A.,
RA Berkow E.L., Castanheira M., Magobo R.E., Jabeen K., Asghar R.J.,
RA Meis J.F., Jackson B., Chiller T., Litvintseva A.P.;
RT "Simultaneous emergence of multidrug-resistant Candida auris on 3
RT continents confirmed by whole-genome sequencing and epidemiological
RT analyses.";
RL Clin. Infect. Dis. 64:134-140(2017).
RN [2] {ECO:0000313|EMBL:PIS50617.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=B8441 {ECO:0000313|EMBL:PIS50617.1};
RA Munoz J.F., Gade L.G., Chow N.A., Litvintseva A.P., Loparev V.N.,
RA Cuomo C.A.;
RT "Candida auris genome assembly and annotation.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:QWW25645.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CA7LBN {ECO:0000313|EMBL:QWW25645.1};
RA Finianos M.;
RT "Candida auris outbreak in lebanese hospital.";
RL Submitted (JUN-2021) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRSR:PIRSR602081-1};
CC Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR602081-1};
CC -!- SIMILARITY: Belongs to the DNA photolyase class-1 family.
CC {ECO:0000256|ARBA:ARBA00005862}.
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DR EMBL; PEKT02000008; PIS50617.1; -; Genomic_DNA.
DR EMBL; CP076754; QWW25645.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H0ZJX5; -.
DR STRING; 498019.A0A2H0ZJX5; -.
DR EnsemblFungi; B9J08_004445-t37_1; B9J08_004445-t37_1-p1; B9J08_004445.
DR VEuPathDB; FungiDB:B9J08_004445; -.
DR VEuPathDB; FungiDB:CJI96_0005465; -.
DR VEuPathDB; FungiDB:CJI97_004509; -.
DR VEuPathDB; FungiDB:CJJ07_000349; -.
DR VEuPathDB; FungiDB:CJJ09_004970; -.
DR VEuPathDB; FungiDB:QG37_04432; -.
DR OMA; TPYKNAW; -.
DR OrthoDB; 124765at2759; -.
DR Proteomes; UP000230249; Unassembled WGS sequence.
DR Proteomes; UP000825438; Chromosome VI.
DR GO; GO:0097159; F:organic cyclic compound binding; IEA:UniProt.
DR GO; GO:0051716; P:cellular response to stimulus; IEA:UniProt.
DR GO; GO:0006139; P:nucleobase-containing compound metabolic process; IEA:UniProt.
DR GO; GO:0006950; P:response to stress; IEA:UniProt.
DR Gene3D; 1.25.40.80; -; 1.
DR Gene3D; 1.10.579.10; DNA Cyclobutane Dipyrimidine Photolyase, subunit A, domain 3; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR InterPro; IPR036134; Crypto/Photolyase_FAD-like_sf.
DR InterPro; IPR036155; Crypto/Photolyase_N_sf.
DR InterPro; IPR005101; Cryptochr/Photolyase_FAD-bd.
DR InterPro; IPR002081; Cryptochrome/DNA_photolyase_1.
DR InterPro; IPR018394; DNA_photolyase_1_CS_C.
DR InterPro; IPR006050; DNA_photolyase_N.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR11455; CRYPTOCHROME; 1.
DR PANTHER; PTHR11455:SF18; DEOXYRIBODIPYRIMIDINE PHOTO-LYASE, MITOCHONDRIAL; 1.
DR Pfam; PF00875; DNA_photolyase; 1.
DR Pfam; PF03441; FAD_binding_7; 1.
DR PRINTS; PR00147; DNAPHOTLYASE.
DR SUPFAM; SSF48173; Cryptochrome/photolyase FAD-binding domain; 1.
DR SUPFAM; SSF52425; Cryptochrome/photolyase, N-terminal domain; 1.
DR PROSITE; PS00394; DNA_PHOTOLYASES_1_1; 1.
DR PROSITE; PS00691; DNA_PHOTOLYASES_1_2; 1.
DR PROSITE; PS51645; PHR_CRY_ALPHA_BETA; 1.
PE 3: Inferred from homology;
KW Chromophore {ECO:0000256|ARBA:ARBA00022991};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR602081-1};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|PIRSR:PIRSR602081-
KW 1}; Reference proteome {ECO:0000313|Proteomes:UP000230249}.
FT DOMAIN 60..197
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT BINDING 296
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 348
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 351..358
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 449..451
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT SITE 383
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 436
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 459
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ SEQUENCE 565 AA; 65117 MW; A59910EF40D71FCD CRC64;
MSKKQKLEQL PKFSSKFYPK ELPTAVAATK YAKDENKPYN ILLNKVESTE KERSKIKPAN
CIAHWFVRDF RTFDNKGLSE ASKLAAKNKL PLVCFWVNCK EMTKAHGKSK FQMHYRVLSM
QKLHKKLADL NIAFVTINAE TRAKIIPSIL EFLQKHKVSH LFVNQEYEVD ELRLSTKLID
KALEKGINFQ VCHDTCVVQP GELVTKSSGK QFAVFSPWYR AWVDYVNAHY IDKGKIIVDS
PVKHEVGKED LIKQGHGLPT IKVDEKRFNK YWKDIGEDDA YAALEKWTES DAIKKYGDTR
NSLEGGASNL GVHISSGTLS PRTILWMLHE KELLTEANET AAPGITEYLR QVSWRDFYKH
ILCFWPHVSM FKPFHLEYSD LPWEYNKDHF LKWQEGNTGY PIVDASMRAL KETGHLNNRG
RLIVASFLTK HLLIDWRYGE QYFMSQLIDG DFASNNGGWG FSASTGVDPQ PYFRVFNPAS
QSERFDPKGA FIKKWCPELK DIESKLIHAP FDHAKSAQLA KQNKYPEPIV DYKMGRQRAL
DVFKETMQNG KEKLEEEVDD ADDGE
//
