GenomeNet

Database: UniProt
Entry: X5J8I3_9BACT
LinkDB: X5J8I3_9BACT
Original site: X5J8I3_9BACT 
ID   X5J8I3_9BACT            Unreviewed;       476 AA.
AC   X5J8I3;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Deoxyribodipyrimidine photo-lyase {ECO:0000313|EMBL:CDG50032.1};
DE            EC=4.1.99.3 {ECO:0000313|EMBL:CDG50032.1};
GN   Name=phr {ECO:0000313|EMBL:CDG50032.1};
GN   ORFNames=CHV_d0039 {ECO:0000313|EMBL:CDG50032.1};
OS   Cardinium endosymbiont cBtQ1 of Bemisia tabaci.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Amoebophilaceae;
OC   Cardinium.
OX   NCBI_TaxID=1354314 {ECO:0000313|EMBL:CDG50032.1, ECO:0000313|Proteomes:UP000024482};
RN   [1] {ECO:0000313|EMBL:CDG50032.1, ECO:0000313|Proteomes:UP000024482}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cBtQ1 {ECO:0000313|Proteomes:UP000024482};
RX   DOI=10.1093/gbe/evu077;
RA   Santos-Garcia D., Rollat-Farnier P.A., Beitia F., Zchori-Fein E., Vavre F.,
RA   Mouton L., Moya A., Latorre A., Silva F.J.;
RT   "The genome of Cardinium cBtQ1 provides insights into genome reduction,
RT   symbiont motility and its settlement in Bemisia tabaci.";
RL   Genome Biol. Evol. Evol.0:0-0(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   -!- SIMILARITY: Belongs to the DNA photolyase family.
CC       {ECO:0000256|RuleBase:RU004182}.
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:CDG50032.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CBQZ010000004; CDG50032.1; -; Genomic_DNA.
DR   RefSeq; WP_034577450.1; NZ_CBQZ010000004.1.
DR   AlphaFoldDB; X5J8I3; -.
DR   STRING; 1354314.CHV_d0039; -.
DR   eggNOG; COG0415; Bacteria.
DR   Proteomes; UP000024482; Unassembled WGS sequence.
DR   GO; GO:0003904; F:deoxyribodipyrimidine photo-lyase activity; IEA:UniProtKB-EC.
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:CDG50032.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000024482}.
FT   DOMAIN          3..132
FT                   /note="Photolyase/cryptochrome alpha/beta"
FT                   /evidence="ECO:0000259|PROSITE:PS51645"
FT   BINDING         237
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         282
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         285..292
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   SITE            317
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            370
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            393
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ   SEQUENCE   476 AA;  55158 MW;  1C2E3337CB082DB1 CRC64;
     MAQVAIVWLR RNLRLQDNKP FAAALRHFDK VLPIFIFDTT ILKQFPNPYD RRLSFLAHTL
     CLLHDTLKML QGALSVFHGT PLEIIPKLVN HLKVEAIYAD EDYEPANIER DRAIQKVLAP
     HCKLHLYCDH LLIKPGIILT QSNQPYKVYT PYMKAFRAYV VHQGVLAQNR LLIEYKYALE
     GRLFTSSLPD GNSIDLNLGV EAVLKQIGYI YKKDGLWDPK NACNRLDGFL INQIDHYKAN
     RDLLDLNGTS RCGPYLRFGL ISIRSCYRKA FALASNVGVT TWINELIWRE FYANILYHFP
     NIIYEAFQEK YRNTIPWNSK QEDYDRFVCG QTGYPIVDAA IQQLLCEGWM HNRARMIVAS
     FFSKNLLLDW SKGESFFAQH LMDYELASNV GGWQWSSACG VDAPPYFRVF NPYLQGKKFD
     PDGQYVKKYL PSLQKVPGHI IHTVDFHTLH IDYPKPMVDY RLSRIRAIET LKKIGP
//
DBGET integrated database retrieval system