ID A0A2P6V8H8_9CHLO Unreviewed; 1693 AA.
AC A0A2P6V8H8;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Deoxyribodipyrimidine photo-lyase {ECO:0000313|EMBL:PSC70387.1};
GN ORFNames=C2E20_6232 {ECO:0000313|EMBL:PSC70387.1};
OS Micractinium conductrix.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Chlorellales; Chlorellaceae; Chlorella clade; Micractinium.
OX NCBI_TaxID=554055 {ECO:0000313|EMBL:PSC70387.1, ECO:0000313|Proteomes:UP000239649};
RN [1] {ECO:0000313|EMBL:PSC70387.1, ECO:0000313|Proteomes:UP000239649}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAG 241.80 {ECO:0000313|EMBL:PSC70387.1,
RC ECO:0000313|Proteomes:UP000239649};
RX PubMed=29178410; DOI=10.1111/tpj.13789;
RA Arriola M.B., Velmurugan N., Zhang Y., Plunkett M.H., Hondzo H.,
RA Barney B.M.;
RT "Genome sequences of Chlorella sorokiniana UTEX 1602 and Micractinium
RT conductrix SAG 241.80: implications to maltose excretion by a green alga.";
RL Plant J. 93:566-586(2018).
CC -!- COFACTOR:
CC Name=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate;
CC Xref=ChEBI:CHEBI:15636; Evidence={ECO:0000256|ARBA:ARBA00001932};
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}.
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:PSC70387.1}.
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DR EMBL; LHPF02000020; PSC70387.1; -; Genomic_DNA.
DR STRING; 554055.A0A2P6V8H8; -.
DR Proteomes; UP000239649; Unassembled WGS sequence.
DR GO; GO:0003913; F:DNA photolyase activity; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0015074; P:DNA integration; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
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 Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR InterPro; IPR014133; Cry_DASH.
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; IPR001584; Integrase_cat-core.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR NCBIfam; TIGR02765; crypto_DASH; 1.
DR PANTHER; PTHR11455; CRYPTOCHROME; 1.
DR PANTHER; PTHR11455:SF22; CRYPTOCHROME DASH; 1.
DR Pfam; PF00875; DNA_photolyase; 1.
DR Pfam; PF03441; FAD_binding_7; 1.
DR Pfam; PF00665; rve; 1.
DR PRINTS; PR00147; DNAPHOTLYASE.
DR SUPFAM; SSF48173; Cryptochrome/photolyase FAD-binding domain; 1.
DR SUPFAM; SSF52425; Cryptochrome/photolyase, N-terminal domain; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS00394; DNA_PHOTOLYASES_1_1; 1.
DR PROSITE; PS50994; INTEGRASE; 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}; Lyase {ECO:0000313|EMBL:PSC70387.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000239649}.
FT DOMAIN 18..160
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT DOMAIN 785..951
FT /note="Integrase catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50994"
FT REGION 518..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 974..1016
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 273
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 327..334
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 426..428
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT SITE 360
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 413
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 436
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ SEQUENCE 1693 AA; 181879 MW; 10092F6554385DC9 CRC64;
MASSGSGSGA VAGGTGNRAV LWFRGTDLRL HDNPVVHEAA QRVAAGQVAE VLPVFCFDPR
FLRASAWGTP KTGPFRAQFL LESVADLKAQ LRAIGSDLLV AMGPPEEVLP RLLTERGSGH
SSVVLAQSEV TSEELGAERK VKSAVKGAGA KLELVWGSTM YHLDDLPFRE DLRDLPDMFT
PFKQKCEDRS RVRPCLPTPA RGALPLPPGA DAAALAYLPQ RVEDLKAVIP AGHPQLASPQ
KDARGVLDFK GGESVAQARL KYYTFDSNLI ATYFDTRNGM LGGDYSTKLA PWLAHGCLSA
RRAYHEIKRY EEKTGTANKS TYWVIFELTW RDFYRFFALK HGSRIFSPEG TAGGGPPGGW
VADEEGLRRW KEGRTGWPLV DANMRELAAT GFMSNRGRQN VASFLALDLG VDWRRGGDWF
ESLLLDYDVS SNWGNWVAAA ELTGGRVNKF NITKQSNDYD PQGDYIRTWV PELARVPARR
IHEPWLMSKD EQAAAGCGIG TDYPVPLKSR WKGFGGGFGG GERPPGYRQT GRASPYSRSG
RKLQQACTCT AVGDIGGLAF APFIGKMAVA GSGIIFNVPV TFAVGATVTA GGLNVQTGDV
TFQSGTKVKI TTGALPFTVD GASGMTVSGP GKIVLNSAIS VEATSGTSKL VVKTDSVEPK
ELSNRLLRQF HLEKTIDGKE VLLRSVSRND ELGIAVSRKV LVVAAEEVPA FFAKHHGIQG
QGWNSPARLF HHLHHAVPTQ LMPAPGGQPR LVHGAEGFTV ETAKAWCTEC PVRADMAAKK
PAEKRVVHPI VAIMTLMHLA ADLIDLGAGR DERYRYVLVV IDVFSRYCWL YPLASKTTIG
VARHLYFQFM RTQVPAKLQT DNGLEFCGKE VKELCELFNV RHAKSMPGHP ETNGCVERKN
RELKNKIRAL LMACPLFDWA FHVLTVMQMV NNSPTSALGG MAPTKALFGT LPSNMNLPLL
DDIVRLLGFT SSAEANDADT PPAPATRKGS AAQPKRRRTL SELVLPSDSE DEASDDAALD
EATLQIAATA SPLGRRSTRT NAGGRLSQLV ADELLDEAGE VPTRALPQRA TAMRSPSGKR
RAATSLLDQL AAIAAECDAA DELDKVDDSS DGAGTSADAE AAAILTAHHG AHQEQVLALH
VRNRQRIRSQ GGKGGAEFDI GDAVLLKPAS MGKVGTSTIQ RKRLTCRVVG VAEQTGKYHL
RCNTGLLKGT YGGGEIRPGK VITSWLDGVE DGKEIRAESW LGIKSGDNVR SSNDLGVFRS
AAIGLATKTK ATLGSTGKVL HIHGDAWVGN EVLFDGAGRP TRRTFLTRVR PGKVSISWPN
PGEPIDVLPY KLPMPECSLG RKSSDPPTDP NLVVWGSANI SASTALTAGV AGRVLSVHGE
GWYGPWAPQG VPTFLTRVRV GRVTTSWPPP GWKTGQPFAA QEAYIGKRPA DGPVAPQLYT
YGTASLVDGA QIRPGKVITS WLDGVEDGKE IRAESWLGIK SGDNVRSSND LGVFRSAAIG
LATKTKATLG STGKVLHIHG DAWVGNEVLF DGAGRPTRRT FLTRVRPGKV SISWPNPGEP
IDVLPYKLPM PECSLGRKSS DPPTDPNLVV WGSANISAST ALTAGVAGRV LSVHGEGWYG
PWAPQGVPTF LTRVRVGRVT TSWPPPGWKT GQPFAAQEAY IGKRPADGPV APQLYTYGTA
SLVDGAQVFL AKP
//
