ID A0A1S3MLM2_SALSA Unreviewed; 906 AA.
AC A0A1S3MLM2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Deoxyribodipyrimidine photo-lyase-like {ECO:0000313|RefSeq:XP_014004123.1};
GN Name=LOC106573523 {ECO:0000313|RefSeq:XP_014004123.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014004123.1};
RN [1] {ECO:0000313|RefSeq:XP_014004123.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014004123.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 class-1 family.
CC {ECO:0000256|ARBA:ARBA00005862}.
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DR RefSeq; XP_014004123.1; XM_014148648.1.
DR AlphaFoldDB; A0A1S3MLM2; -.
DR STRING; 8030.ENSSSAP00000016302; -.
DR PaxDb; 8030-ENSSSAP00000016302; -.
DR KEGG; sasa:106573523; -.
DR OrthoDB; 124765at2759; -.
DR Proteomes; UP000087266; Chromosome ssa16.
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:SF18; DEOXYRIBODIPYRIMIDINE PHOTO-LYASE, MITOCHONDRIAL; 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};
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:UP000087266}.
FT DOMAIN 271..412
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT REGION 121..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 234..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 854..906
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 855..873
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 517
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 529..533
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 560
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 660..662
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT SITE 594
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 647
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 670
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ SEQUENCE 906 AA; 101180 MW; CCBD143AEE609B0F CRC64;
MPVSGGEDPM SQVRQMLREL LVGRENAEGF FCLCVSVLGH NDTRTHFLPL IQLLATDHSS
LHTTLTSIYL EYFSKDEDDE LAVALALSLL EVKRQQQTDT KPLFPDPKLQ GQTDTQATAT
YRPQNSSIQS QSVSPNGSSS QPPPAPLPKG ASYAQLAAAG GRRQTQAQHQ DSTSPRRSSG
HGSSPQTERQ RGPTKTQKQT DIKWSNVTQD VCASIATSLT SNLNQTKDDV TVVECEVDQS
EKPKRSKNRR QRRKGYGQQV VGVPRCPSAP PPVLLWFRRD LRLHDNPAVI GSLEAGGPVI
PVFIWCPEEE EGPGVTVAMG GACKFWLHQA LSCLSSALEH IGSHLVFLRP DEEREGIGSS
LRALRSLVRE TGAQTVLASA LYEPWLRERD QVVVSALQKD RVEVNMVHSY CLRDPYTVTT
EGVGLRGIGS VSHFMSCCQM NPGPGLGVPL DPPISLPSPS VWPRGCPLEG LGLARMPCRK
DGTTIDWAAN IRSSWDFSEE GAQSRLEAFL NDGVYRYEKE SGRADAPNTS CLSPYLHFGQ
LSARWLLWDT KGARCRPPKF IRKLAWRDLA YWQLTLFPDL PWESLRPPYK ALRWSNERGH
LKAWQKGRTG YPLVDAAMRQ LWLTGWMNNY MRHVVASFLI AYLHLPWQEG YRWFQDTLVD
ADVAIDAMMW QNGGMCGLDH WNFVMHPVDA AMTCDPYGNY VRKWCTELAV LPDDLIHKPW
KCPASMLRRA GVVLGQSYPE RVVTDLEERR SQSLQDVALV RRRFGEYVDP CSGCDLVPLP
PRLVSEAMGG GMVSTGGQFL LPVITRMEFK HQSDDPDADA ASNPYNAVLK GYVSRRRNET
IAFLNQTDFT ASVINEGTER RERQERDQRR MEGLPRPLAA QGRGKRTPAA KDRFSTVPGG
VATSHR
//
