ID K9HUW7_9PROT Unreviewed; 507 AA.
AC K9HUW7;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Deoxyribodipyrimidine photolyase {ECO:0000313|EMBL:EKV32051.1};
GN ORFNames=C882_3115 {ECO:0000313|EMBL:EKV32051.1};
OS Caenispirillum salinarum AK4.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Novispirillaceae; Caenispirillum.
OX NCBI_TaxID=1238182 {ECO:0000313|EMBL:EKV32051.1, ECO:0000313|Proteomes:UP000009881};
RN [1] {ECO:0000313|EMBL:EKV32051.1, ECO:0000313|Proteomes:UP000009881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK4 {ECO:0000313|EMBL:EKV32051.1,
RC ECO:0000313|Proteomes:UP000009881};
RX PubMed=23409257;
RA Khatri I., Singh A., Korpole S., Pinnaka A.K., Subramanian S.;
RT "Draft Genome Sequence of an Alphaproteobacterium, Caenispirillum salinarum
RT AK4(T), Isolated from a Solar Saltern.";
RL Genome Announc. 1:E00199-12(2013).
CC -!- COFACTOR:
CC Name=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate;
CC Xref=ChEBI:CHEBI:15636; Evidence={ECO:0000256|ARBA:ARBA00001932};
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 -!- 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:EKV32051.1}.
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DR EMBL; ANHY01000004; EKV32051.1; -; Genomic_DNA.
DR RefSeq; WP_009539312.1; NZ_ANHY01000004.1.
DR AlphaFoldDB; K9HUW7; -.
DR STRING; 1238182.C882_3115; -.
DR PATRIC; fig|1238182.3.peg.863; -.
DR eggNOG; COG0415; Bacteria.
DR OrthoDB; 9772484at2; -.
DR Proteomes; UP000009881; 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; 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 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 4: Predicted;
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:EKV32051.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009881}.
FT DOMAIN 4..133
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT REGION 475..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 210
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 264
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
SQ SEQUENCE 507 AA; 56226 MW; D8027B18CE402C29 CRC64;
MSRPVHIVWF KRDLRAADHA PLARAAAAGA VVPLYVIEPD LWRQPDASGR QWAFLRESLT
DLRRSLAALG APLVVRVGGV TEVLEDLRTS LGIAGLWSHE ETGSAWTYAR DRAVAAWARS
HGIRWTEWPQ TGVVRSLTRR DGWAKRWDGF MARPPTPTPH ALTPVPGLDP GPLPETVPVA
ADPCDGRQRG GRTAGLALLE GFLAGRGADY RRGMASPLTA PDACSRLSPH LAFGTVSLRE
VTQAAWHQRR TGAGGMGAAA LDSFTARLHW HCHFIQKLED APAHEVRNVH RGHDGLREDA
FDPALFPAWA EGRTGIPFVD ACMRFLTQTG WINFRMRAML TAFAAYQLWL HWRAPGLHLA
RLFTDYEPGI HWNQVQMQSG TTGINTLRVY NPVKQSREHD PDGTFIRRWV PELARVPAPL
IHTPWQLSPI ERADCGLAAA GYPPPVVDHE AAARRARERM HALRRSDAFR AEADAIQARH
GSRKSGIPSR SGRRRPAPDA RQMSLDV
//