ID A0A2K6BZ20_MACNE Unreviewed; 380 AA.
AC A0A2K6BZ20;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Cryptochrome circadian regulator 2 {ECO:0000313|Ensembl:ENSMNEP00000016651.1};
GN Name=CRY2 {ECO:0000313|Ensembl:ENSMNEP00000016651.1};
OS Macaca nemestrina (Pig-tailed macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000016651.1, ECO:0000313|Proteomes:UP000233120};
RN [1] {ECO:0000313|Ensembl:ENSMNEP00000016651.1}
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; A0A2K6BZ20; -.
DR Ensembl; ENSMNET00000040868.1; ENSMNEP00000016651.1; ENSMNEG00000032337.1.
DR GeneTree; ENSGT00940000159073; -.
DR Proteomes; UP000233120; Unplaced.
DR Bgee; ENSMNEG00000032337; Expressed in skeletal muscle tissue and 12 other cell types or tissues.
DR Gene3D; 1.25.40.80; -; 1.
DR Gene3D; 1.10.579.10; DNA Cyclobutane Dipyrimidine Photolyase, subunit A, domain 3; 1.
DR InterPro; IPR036134; Crypto/Photolyase_FAD-like_sf.
DR InterPro; IPR005101; Cryptochr/Photolyase_FAD-bd.
DR InterPro; IPR002081; Cryptochrome/DNA_photolyase_1.
DR PANTHER; PTHR11455; CRYPTOCHROME; 1.
DR PANTHER; PTHR11455:SF15; CRYPTOCHROME-2; 1.
DR Pfam; PF03441; FAD_binding_7; 1.
DR SUPFAM; SSF48173; Cryptochrome/photolyase FAD-binding domain; 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:UP000233120}.
FT DOMAIN 94..292
FT /note="Cryptochrome/DNA photolyase FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF03441"
FT REGION 320..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..367
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 40
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 95..102
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 193..195
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT SITE 126
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 180
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 203
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ SEQUENCE 380 AA; 43173 MW; 21A0FF7838A6CD1E CRC64;
MTWKGFPTEG LGPAVWQGGE TEALARLDKH LERKAWVANY ERPRMNANSL LASPTGLSPY
LRFGCLSCRL FYYRLWDLYK KVKRNSTPPL SLFGQLLWRE FFYTAATNNP RFDRMEGNPI
CIQIPWDRNP EALAKWAEGK TGFPWIDAIM TQLRQEGWIH HLARHAVACF LTRGDLWVSW
ESGVRVFDEL LLDADFSVNA GSWMWLSCSA FFQQFFHCYC PVGFGRRTDP SGDYIRRYLP
KLKGFPSRYI YEPWNAPESI QKAAKCIIGV DYPRPIVNHA ETSRLNIERM KQIYQQLSRY
RGLCLLASVP SCVEDLSHPV AEPSSSQAGS VNSAGPRPLP SGPASPKRKL EAAEEPPGEE
LSKRAKVAEL PTPELPSKDA
//
