ID U9W2B1_9CYAN Unreviewed; 553 AA.
AC U9W2B1;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Deoxyribodipyrimidine photolyase {ECO:0000313|EMBL:ESA34211.1};
GN ORFNames=N836_18355 {ECO:0000313|EMBL:ESA34211.1};
OS Leptolyngbya sp. Heron Island J.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae;
OC Leptolyngbya group; Leptolyngbya.
OX NCBI_TaxID=1385935 {ECO:0000313|EMBL:ESA34211.1, ECO:0000313|Proteomes:UP000017515};
RN [1] {ECO:0000313|EMBL:ESA34211.1, ECO:0000313|Proteomes:UP000017515}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Heron Island J {ECO:0000313|EMBL:ESA34211.1,
RC ECO:0000313|Proteomes:UP000017515};
RX PubMed=24503993;
RA Paul R., Jinkerson R.E., Buss K., Steel J., Mohr R., Hess W.R., Chen M.,
RA Fromme P.;
RT "Draft Genome Sequence of the Filamentous Cyanobacterium Leptolyngbya sp.
RT Strain Heron Island J, Exhibiting Chromatic Acclimation.";
RL Genome Announc. 2:e01166-e01113(2014).
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:ESA34211.1}.
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DR EMBL; AWNH01000080; ESA34211.1; -; Genomic_DNA.
DR AlphaFoldDB; U9W2B1; -.
DR STRING; 1385935.N836_18355; -.
DR PATRIC; fig|1385935.3.peg.5162; -.
DR eggNOG; COG0415; Bacteria.
DR Proteomes; UP000017515; 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:ESA34211.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000017515}.
FT DOMAIN 9..138
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT BINDING 216
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 228..232
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 370..372
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT SITE 301
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 357
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 380
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ SEQUENCE 553 AA; 63812 MW; A9464950389DC45F CRC64;
MARGEAAVNR TVVWFRRDLR IYDHEPLYRA ARRGAVVPVF VFDPSLLQHP ETGAARVSFM
VDCLRHLQQD LRRLGGCLIL RSGDPVEVLP RLVKETQAEG IYSYTDCERI YGRVRDARLN
QALAAQQIKI RWFEPPASRA ELMDYPQYRQ WWYQEMATPV VPAPAQVTVP SEVISEPLPG
LEQLGHCLDG KPIPQGSTRF ARQLLQQFLV EKAARYYWQL SYPSAEITTG LSPHIKFGAI
SVRECVQTIQ RADDRGDRRI QRSYHQLISR LRWGNGFTQR FRYLPQLELR SLYSIFDSDG
WAFDENLYQA WQQGQTGFPI VDAAARCLQA TGGYLSLNFR TRAIYASFLS NLLGMDWRYG
ALHFMRHLID GDCPIDHYQW AMQSGVTHCV DKTWTRIYNP QQVAVDRCDP EGLFIKRWVP
ELAHLAPEQL GAPPPTQGYP PPMLDYRQRR SQRVQQLEQQ RNAFLNTDNI VTYLSPMPES
ILPFGAERYV SEVSWAKIKA PQLFPTALDL DSLDAQQCRE LRTWFVAHVN ITPPKIRRRN
SKFSSDLQQL SLL
//
