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Database: UniProt
Entry: A0A077HJD7_9CORY
LinkDB: A0A077HJD7_9CORY
Original site: A0A077HJD7_9CORY 
ID   A0A077HJD7_9CORY        Unreviewed;       459 AA.
AC   A0A077HJD7;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Deoxyribodipyrimidine photolyase {ECO:0000313|EMBL:AIL96591.1};
GN   ORFNames=CUREI_04150 {ECO:0000313|EMBL:AIL96591.1};
OS   Corynebacterium ureicelerivorans.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=401472 {ECO:0000313|EMBL:AIL96591.1, ECO:0000313|Proteomes:UP000028939};
RN   [1] {ECO:0000313|EMBL:AIL96591.1, ECO:0000313|Proteomes:UP000028939}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMMIB RIV-2301 {ECO:0000313|EMBL:AIL96591.1,
RC   ECO:0000313|Proteomes:UP000028939};
RA   Tippelt A., Albersmeier A., Brinkrolf K., Ruckert C., Tauch A.;
RT   "Complete genome sequence of Corynebacterium ureicelerivorans DSM 45051, a
RT   lipophilic and urea-splitting isolate from a blood culture of a septicaemia
RT   patient.";
RL   Submitted (AUG-2014) 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 family.
CC       {ECO:0000256|RuleBase:RU004182}.
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DR   EMBL; CP009215; AIL96591.1; -; Genomic_DNA.
DR   RefSeq; WP_038610738.1; NZ_CP009215.1.
DR   AlphaFoldDB; A0A077HJD7; -.
DR   STRING; 401472.CUREI_04150; -.
DR   KEGG; cuv:CUREI_04150; -.
DR   HOGENOM; CLU_010348_2_2_11; -.
DR   OrthoDB; 9772484at2; -.
DR   Proteomes; UP000028939; Chromosome.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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; IPR006050; DNA_photolyase_N.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   PANTHER; PTHR11455; CRYPTOCHROME; 1.
DR   PANTHER; PTHR11455:SF9; CRYPTOCHROME-1; 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; PS51645; PHR_CRY_ALPHA_BETA; 1.
PE   3: Inferred from homology;
KW   Chromophore {ECO:0000256|RuleBase:RU004182};
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR602081-1};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|PIRSR:PIRSR602081-
KW   1}; Lyase {ECO:0000313|EMBL:AIL96591.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028939}.
FT   DOMAIN          5..118
FT                   /note="Photolyase/cryptochrome alpha/beta"
FT                   /evidence="ECO:0000259|PROSITE:PS51645"
FT   BINDING         215..219
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         253
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         379..381
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   SITE            287
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            366
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            389
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ   SEQUENCE   459 AA;  51208 MW;  BB0EB2905E676BA1 CRC64;
     MPTTPTTLVW FRDDLRVTDN PALAYAASRG DVAGVLIDDS STARPLGRAA AWWRERSAAA
     LSEKLPLIRE VGDPREIVPR LAREMDAEVV WNRRYDSVEL DAEVKRAVDA RTFPGFLLAE
     PWDIATGSGT PYRVFTPFYK AMQQHVAAHP PRPVAAPSLP GGTRLEVSAA PSWAEELAVH
     NTPGEDAALR RFHEFLDGLA DGHGYDNNDL TPGATSGLSA HLRFGELSPG YVWAETVAFA
     EEHPTAAPDA WAFLRQLVWR DFAWHRYYHL PDLAAHNVRE QFNRFEWAWS ANAAPWEHAA
     AFASAAMEPD ADAAQHLDQL AQWQRGATGV PLVDAGMHEL WRTGTMHNRV RMVVGSWLTK
     NLGIHWRHGE EWFWDTLVDA DAASNPFNWQ WVAGSGDDAA PYFRIFNPLT QQEKFDPAGA
     YVSRWAPEAL LPGYPEPMVD VKESRKVALA AYEDIKTSS
//
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