GenomeNet

Database: UniProt
Entry: A0A101R3C4_9ACTN
LinkDB: A0A101R3C4_9ACTN
Original site: A0A101R3C4_9ACTN 
ID   A0A101R3C4_9ACTN        Unreviewed;       458 AA.
AC   A0A101R3C4;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Deoxyribodipyrimidine photolyase {ECO:0000313|EMBL:KUN40945.1};
GN   ORFNames=AQJ30_03325 {ECO:0000313|EMBL:KUN40945.1};
OS   Streptomyces longwoodensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=68231 {ECO:0000313|EMBL:KUN40945.1, ECO:0000313|Proteomes:UP000053271};
RN   [1] {ECO:0000313|EMBL:KUN40945.1, ECO:0000313|Proteomes:UP000053271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 41677 {ECO:0000313|EMBL:KUN40945.1,
RC   ECO:0000313|Proteomes:UP000053271};
RA   Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT   "Draft genome sequence of Streptomyces longwoodensis DSM 41677, type strain
RT   for the species Streptomyces longwoodensis.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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:KUN40945.1}.
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; LMWS01000005; KUN40945.1; -; Genomic_DNA.
DR   RefSeq; WP_067228331.1; NZ_KQ948549.1.
DR   AlphaFoldDB; A0A101R3C4; -.
DR   STRING; 68231.AQJ30_03325; -.
DR   Proteomes; UP000053271; Unassembled WGS sequence.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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; PS00691; DNA_PHOTOLYASES_1_2; 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}; Lyase {ECO:0000313|EMBL:KUN40945.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053271}.
FT   DOMAIN          2..131
FT                   /note="Photolyase/cryptochrome alpha/beta"
FT                   /evidence="ECO:0000259|PROSITE:PS51645"
FT   BINDING         218
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         230..234
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         363..365
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   SITE            294
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            350
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            373
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ   SEQUENCE   458 AA;  50869 MW;  119D20D1DE935C6E CRC64;
     MHVSVVLFTA DLRLHDHPPM RAALDASDAV VPLFVRDRAV TAAGFDPPNR RAFLADCLAD
     LDASLRERGG RLVVRSGDLV EEVCRVVTEA DADEIHMAAG HTAFAARREE RLRRALEADG
     RRLFVHDAVT VAVPPGTVTP ASADHFAVFT PYFRQWDRLV LRPVAPPPRR VSVPGHVTGE
     PLPARGDVGG VSPALAAGGE AAGRRRMTAY WRKGLDAYDD TRDDLAADTT SRFSPHLHFG
     TLSAVELVHR ARKQGGPGAD ALVRQLAWRD FHRQVLAARP GAARADYRTK RDSWRSRRTA
     AADIEAWETG RTGYPVIDAA MRQLRHEGWM HNRARLLTAS FLAKTLYVDW RIGAAHFLHW
     LVDGDVANNQ LNWQWVAGTG TDTRPNRVLN PLTQAKKYDP DGTYVRRWVP ELAGVDAPAV
     HEPWKLAGPD RAALDYPEPV VELSAGLYRF RQARERAR
//
DBGET integrated database retrieval system