ID R7Q2P4_CHOCR Unreviewed; 1417 AA.
AC R7Q2P4;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Photolyase/cryptochrome alpha/beta domain-containing protein {ECO:0000259|PROSITE:PS51645};
GN ORFNames=CHC_T00001385001 {ECO:0000313|EMBL:CDF32158.1};
OS Chondrus crispus (Carrageen Irish moss) (Polymorpha crispa).
OC Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae; Gigartinales;
OC Gigartinaceae; Chondrus.
OX NCBI_TaxID=2769 {ECO:0000313|EMBL:CDF32158.1, ECO:0000313|Proteomes:UP000012073};
RN [1] {ECO:0000313|Proteomes:UP000012073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Stackhouse {ECO:0000313|Proteomes:UP000012073};
RX PubMed=23503846; DOI=10.1073/pnas.1221259110;
RA Collen J., Porcel B., Carre W., Ball S.G., Chaparro C., Tonon T.,
RA Barbeyron T., Michel G., Noel B., Valentin K., Elias M., Artiguenave F.,
RA Arun A., Aury J.M., Barbosa-Neto J.F., Bothwell J.H., Bouget F.Y.,
RA Brillet L., Cabello-Hurtado F., Capella-Gutierrez S., Charrier B.,
RA Cladiere L., Cock J.M., Coelho S.M., Colleoni C., Czjzek M., Da Silva C.,
RA Delage L., Denoeud F., Deschamps P., Dittami S.M., Gabaldon T.,
RA Gachon C.M., Groisillier A., Herve C., Jabbari K., Katinka M., Kloareg B.,
RA Kowalczyk N., Labadie K., Leblanc C., Lopez P.J., McLachlan D.H.,
RA Meslet-Cladiere L., Moustafa A., Nehr Z., Nyvall Collen P., Panaud O.,
RA Partensky F., Poulain J., Rensing S.A., Rousvoal S., Samson G.,
RA Symeonidi A., Weissenbach J., Zambounis A., Wincker P., Boyen C.;
RT "Genome structure and metabolic features in the red seaweed Chondrus
RT crispus shed light on evolution of the Archaeplastida.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:5247-5252(2013).
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 EMBL; HG001459; CDF32158.1; -; Genomic_DNA.
DR RefSeq; XP_005711823.1; XM_005711766.1.
DR EnsemblPlants; CDF32158; CDF32158; CHC_T00001385001.
DR GeneID; 17319557; -.
DR Gramene; CDF32158; CDF32158; CHC_T00001385001.
DR KEGG; ccp:CHC_T00001385001; -.
DR OrthoDB; 1719at2759; -.
DR Proteomes; UP000012073; 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:SF18; DEOXYRIBODIPYRIMIDINE PHOTO-LYASE, MITOCHONDRIAL; 1.
DR Pfam; PF00875; DNA_photolyase; 1.
DR Pfam; PF03441; FAD_binding_7; 1.
DR SUPFAM; SSF48173; Cryptochrome/photolyase FAD-binding domain; 2.
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:UP000012073}.
FT DOMAIN 84..213
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT REGION 1..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 841..896
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 919..957
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1132..1164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1184..1308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 851..865
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 872..896
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1186..1207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1224..1245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1266..1308
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 319..323
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 463
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 563..565
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT SITE 497
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 550
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 573
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ SEQUENCE 1417 AA; 156816 MW; EF892B50AEA27A40 CRC64;
MSQANAARMH NPSPSPSALT QAPITNASRR IRRRAASPPA KRRRTASSTE DADSVSPPAS
PSPELRQPPS QATAPQGAKW FRKPSVVWYR GNDLRVEDHP ALLAASQRGG PVVPLFIWDP
SDSFGSDLGH VKQWWLRESL SCLQRDLKRL GVQLYTRTGK STEELRNFLC DTGADAVFWN
RCYEPDLLTR DEELRDELLS EGLTAESFKA ELLVEPWELK NTEVNPRYET FRSYMRAWMT
FAPPPEPFPC PSRLTAITSE VKSVGISALA FDIPHTLEEV LQKTWTPGSV QANAQLEKFL
IEVFPAFGDN RCRRHFDGTS RLSPHIRFGE LSPRRMYHST RMRVSRWDQG SMLSLAASRK
WSLAMSNGGT KQEWKRASLL ESLESGREVN REREPQGDTR SSPLTSGTHA KQEESVGDKG
GRGRPQPTPP EKPPKTNFRH MMRSAAAVQR PALPPISQSA RAFLRNLCLR DFSYHILFHN
PDFHAKPLIP EYVNFPWAED KGSFTAWQTA KTGYPIIDAA MRELRATGWI HNRMRFLLAC
FLTKYLLLPW SRGLKEFYGL LLDGDHSSNA LGWQWTAGSN TYAATLRNLL NPVKSASQHD
PHGSYVRQWL PELANLPTNF VHEPWKAPPD VLHAAGVELG TTYPNRIVML KEARVRAFEA
MRLMRQIFSA SGVSRKLEVE DEEDLVMGWR EDHSEVFPVE ESAVTGTKRT LLPCLWALLQ
SDQEPTYLSN SSSGSDPLIA RDTASLTEGA LAVPMDDQQE SIENALLTAH NHGPPPEVLV
IPLEAVTADD QALGDPIYPQ EKNCETEGMM VGPGSDNLPV GHLGEPLKYH DSEVCAFPES
ENVSDRQAPM EADGSRVRTD SARARTRPPD TVQVGAPNTC RGSAAQALNP SVPFPHQPQY
QLQQFQQLQQ LHKFQLQNHM HVHQQQQRQE TQQHQRAAQQ QRTSQHTSPH QHIHYPNSAL
PQRQQPHVHA MADAIYGQQG CSNGSLPSTS LAGVPMPGAP VMMGPATGSQ DLSANAMFTG
GDRGSSVYAH PLGFGQFYGF PPVMPILNAP AANGGERNDG ILSSATTDMS KLPAPGMMAM
PYGMYPGNMF EQNVLGGAHQ AGNNHYASSL PQMQDGRQSP YRYSPQMYFP HTTPEISPAQ
GNGHVPHRPS PSIPPQSRHL DMPSVANAPN ATAAAAVAGR EREAAQVASS NANTRTLPKS
EQLTDVARNT PGLKPGFGVA SRSVDTTKPL NSKVTNANTR LGQGRPRGRN NARSKAALKR
KGSASNGIAK NRNEVKSSSN GRGQGSEGRS STAQEKGPKE DTQPQGTTLK ARQEMLASVL
GKEDHQFHGF AKYLSSTYEL TASTDRKTSK DYIRLCNLKD DYHKQCKSDK LKIYGIKSFF
SKVLNLDVTG EWDRHNHGGV RGPYVYGIRP RRSTNPS
//
