GenomeNet

Database: UniProt
Entry: A3TJ93_9MICO
LinkDB: A3TJ93_9MICO
Original site: A3TJ93_9MICO 
ID   A3TJ93_9MICO            Unreviewed;       455 AA.
AC   A3TJ93;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   SubName: Full=Phr {ECO:0000313|EMBL:EAQ00907.1};
GN   ORFNames=JNB_12049 {ECO:0000313|EMBL:EAQ00907.1};
OS   Janibacter sp. HTCC2649.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC   Janibacter.
OX   NCBI_TaxID=313589 {ECO:0000313|EMBL:EAQ00907.1, ECO:0000313|Proteomes:UP000005063};
RN   [1] {ECO:0000313|EMBL:EAQ00907.1, ECO:0000313|Proteomes:UP000005063}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2649 {ECO:0000313|EMBL:EAQ00907.1,
RC   ECO:0000313|Proteomes:UP000005063};
RX   PubMed=21075932; DOI=10.1128/JB.01298-10;
RA   Thrash J.C., Cho J.C., Bertagnolli A.D., Ferriera S., Johnson J.,
RA   Vergin K.L., Giovannoni S.J.;
RT   "Genome sequence of the Marine Janibacter Sp. Strain HTCC2649.";
RL   J. Bacteriol. 193:584-585(2011).
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:EAQ00907.1}.
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; AAMN01000001; EAQ00907.1; -; Genomic_DNA.
DR   RefSeq; WP_009776712.1; NZ_CH672413.1.
DR   AlphaFoldDB; A3TJ93; -.
DR   STRING; 313589.JNB_12049; -.
DR   eggNOG; COG0415; Bacteria.
DR   HOGENOM; CLU_010348_2_2_11; -.
DR   OrthoDB; 9772484at2; -.
DR   Proteomes; UP000005063; Unassembled WGS sequence.
DR   GO; GO:0097159; F:organic cyclic compound binding; IEA:UniProt.
DR   GO; GO:0051716; P:cellular response to stimulus; IEA:UniProt.
DR   GO; GO:0006139; P:nucleobase-containing compound metabolic process; IEA:UniProt.
DR   GO; GO:0006950; P:response to stress; IEA:UniProt.
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; IPR018394; DNA_photolyase_1_CS_C.
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; PS00394; DNA_PHOTOLYASES_1_1; 1.
DR   PROSITE; PS51645; PHR_CRY_ALPHA_BETA; 1.
PE   3: Inferred from homology;
KW   Chromophore {ECO:0000256|ARBA:ARBA00022991, 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}; Reference proteome {ECO:0000313|Proteomes:UP000005063}.
FT   DOMAIN          1..126
FT                   /note="Photolyase/cryptochrome alpha/beta"
FT                   /evidence="ECO:0000259|PROSITE:PS51645"
FT   BINDING         215
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         227..231
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         259
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         262..269
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         359..361
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
SQ   SEQUENCE   455 AA;  50369 MW;  19F1A555D0644279 CRC64;
     MTSVLWLRRD LRRADHPALL AARDAAGGEL VVAYVIDPAL WAGAGAVRRA WLAAALEATR
     EEFDDGLTLL WGDPREVVPA LAKRVGATSV HVTRETTPFG RRRDETVASS LAAQGIEWVE
     TGTPYAVGPG LVQNLSGAPY KVFTPFAKAW RGHGWPDPAP RPSELPLRHV RNDAKATQAI
     EEALAAPDLP DLPAAGERAA MARWREFCET GLTAYATDRD LPATDGTSRL SPYLKLGVVH
     PRTLLADLAG RRGEGAQTYI NELGWREFYA DVLWHNPSSA WKDLRDPLAG MAYDEPADAI
     EAWQTGTTGY PIVDAGMRQL LAQGWMHNRV RMITASFLTK DLHVWWPVGA RHFLELLIDG
     DIASNNHGWQ WVAGTGTDAS PYFRVFNPVT QGEKFDVDGD YVREWVPELA HLAGKAAHQP
     WEHPDGYAHG YPQRIVDHAE ERREALRRLG ELKDS
//
DBGET integrated database retrieval system