ID A0A3P8X3J1_CYNSE Unreviewed; 697 AA.
AC A0A3P8X3J1;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Cryptochrome-2-like {ECO:0000313|Ensembl:ENSCSEP00000033422.1};
OS Cynoglossus semilaevis (Tongue sole).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Cynoglossidae;
OC Cynoglossinae; Cynoglossus.
OX NCBI_TaxID=244447 {ECO:0000313|Ensembl:ENSCSEP00000033422.1, ECO:0000313|Proteomes:UP000265120};
RN [1] {ECO:0000313|Ensembl:ENSCSEP00000033422.1, ECO:0000313|Proteomes:UP000265120}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=24487278;
RA Chen S., Zhang G., Shao C., Huang Q., Liu G., Zhang P., Song W., An N.,
RA Chalopin D., Volff J.N., Hong Y., Li Q., Sha Z., Zhou H., Xie M., Yu Q.,
RA Liu Y., Xiang H., Wang N., Wu K., Yang C., Zhou Q., Liao X., Yang L.,
RA Hu Q., Zhang J., Meng L., Jin L., Tian Y., Lian J., Yang J., Miao G.,
RA Liu S., Liang Z., Yan F., Li Y., Sun B., Zhang H., Zhang J., Zhu Y., Du M.,
RA Zhao Y., Schartl M., Tang Q., Wang J.;
RT "Whole-genome sequence of a flatfish provides insights into ZW sex
RT chromosome evolution and adaptation to a benthic lifestyle.";
RL Nat. Genet. 46:253-260(2014).
RN [2] {ECO:0000313|Ensembl:ENSCSEP00000033422.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; A0A3P8X3J1; -.
DR STRING; 244447.ENSCSEP00000033422; -.
DR Ensembl; ENSCSET00000033856.1; ENSCSEP00000033422.1; ENSCSEG00000021440.1.
DR GeneTree; ENSGT00940000159073; -.
DR InParanoid; A0A3P8X3J1; -.
DR Proteomes; UP000265120; Chromosome 6.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0005667; C:transcription regulator complex; IEA:Ensembl.
DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IEA:Ensembl.
DR GO; GO:0009416; P:response to light stimulus; IEA:Ensembl.
DR GO; GO:0009266; P:response to temperature stimulus; IEA:Ensembl.
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:SF15; CRYPTOCHROME-2; 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 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:UP000265120}.
FT DOMAIN 3..132
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT REGION 509..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 601..697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..527
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 601..637
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 651..668
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..686
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 289..296
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 387..389
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT SITE 320
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 374
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 397
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ SEQUENCE 697 AA; 79464 MW; 1E2E132BB3F8F5ED CRC64;
MAVNSVHWFR KCLRLHDNPA LQEAVNAAHT LRCVYILDPW FAGAANVGIN RWRFLGEALE
DLDNSLKKFN SRLFVIRGQP TDVFPRLFKE WKVTRLTFEY DPEPYGKERD GAIIKMAQEF
GVETVVRNSH TLYNLDRIIE MNNNSPPLTF KRFQTIVSRL ELPRRPLPVI TQQQMEKCCT
KISENHEQLY SIPSLEELGF RTERLPPAVW RGGESEALDR LNKHLDKKVW VANLEHSRIN
TCSLYASPTG LSPYLRFGCL SCRVLYYNLR ELYMKLRKHS SPPPSLFGQL LWREFFYTAA
TNNPNFDRME GNPICVQIPW DQNPEALAKW AEGRTGFPWI DAIMTQLRQE GWIHHLARHA
VACFLTRGDL WISWESGMKV FEELLLDADW SVNAGSWMWL SCSAFFQQFF HCYCPVGFGR
RTDPSGDYIR RYVPILKDYP NRYIYEPWNA PESVQKAANC VVGVDYPKPM INHAEGSRLN
IERMKQVYQQ LSHYRGLSQL ASVPTIQEEA EPPMTDESQT SSGPGKRKPL SRSHMINLSA
HLMWNVLRFF FFSDSPPAGG ALTEAAGCSI LPDSSTLCPT VVTAHQSSDC PQTSAAVTST
SASVNADPLK PPSPCSSSSS PCGTTSPPST SAQTLTKRKG PAHKIRRSMR QRGHQGAEER
REDEEDKGRE ERMEDDDDEN EESMEQDATG EMSGHRQ
//