ID A0A0S8AA58_9GAMM Unreviewed; 472 AA.
AC A0A0S8AA58;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Deoxyribodipyrimidine photolyase {ECO:0000313|EMBL:KPJ96232.1};
GN ORFNames=AMJ53_01190 {ECO:0000313|EMBL:KPJ96232.1};
OS Gammaproteobacteria bacterium SG8_11.
OC Bacteria; Pseudomonadota; Gammaproteobacteria.
OX NCBI_TaxID=1703402 {ECO:0000313|EMBL:KPJ96232.1, ECO:0000313|Proteomes:UP000051175};
RN [1] {ECO:0000313|EMBL:KPJ96232.1, ECO:0000313|Proteomes:UP000051175}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_11 {ECO:0000313|EMBL:KPJ96232.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
CC -!- COFACTOR:
CC Name=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate;
CC Xref=ChEBI:CHEBI:15636; Evidence={ECO:0000256|ARBA:ARBA00001932};
CC -!- SIMILARITY: Belongs to the DNA photolyase class-1 family.
CC {ECO:0000256|ARBA:ARBA00005862}.
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:KPJ96232.1}.
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DR EMBL; LJNJ01000009; KPJ96232.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8AA58; -.
DR PATRIC; fig|1703402.3.peg.1899; -.
DR Proteomes; UP000051175; Unassembled WGS sequence.
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; IPR006050; DNA_photolyase_N.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR10211:SF0; DEOXYRIBODIPYRIMIDINE PHOTO-LYASE; 1.
DR PANTHER; PTHR10211; DEOXYRIBODIPYRIMIDINE PHOTOLYASE; 1.
DR Pfam; PF00875; DNA_photolyase; 1.
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 FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Lyase {ECO:0000313|EMBL:KPJ96232.1}.
FT DOMAIN 31..159
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
SQ SEQUENCE 472 AA; 54278 MW; 05B6128BC11AF319 CRC64;
MVVASPRRSN DSKVHPARIR VLNQRDFAGG EYVLYWMQQS QRAQENHALE YAVELANHLK
QPLLAVFGLT NSYPEANRRH FTFMLEGLQE TQKLLARRRI KLAVRAGHPV DVALEAGAQA
SVIVCDRGYL RHQKQWRQAV ARSAGCRVVQ VESDVVVPVD VVSSKAEYAA RTIRPKLHRL
LPEFLTGIRP TTVRRSSLDL PLDALSLRRI DPVMETLSID CSVEPVSGFY RGGTAAAKKC
FAGFLRNGLK HYDRHGNQPQ TDDVSHMSMY LHFGQVSPLY LALQAGKAER AGEKNRSAYL
EQLIVRRELA VNFVHQTPDY DSYGCLPHWA RQTLEDHRFD KRQHLYSRRQ LEKAATHDPY
WNAAMGEMKH TGFMHNYMRM YWGKKILEWS KTPRQAFETT LAINNKYFID GRDPNSYTGV
AWIYGLHDRP WVERPIFGKI RYMAASGLER KCDIQAYVRK VEKLKESAQN KQ
//
