ID W5J3L0_ANODA Unreviewed; 1068 AA.
AC W5J3L0;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE SubName: Full=DNA photolyase {ECO:0000313|EMBL:ETN58942.1};
GN ORFNames=AND_009461 {ECO:0000313|EMBL:ETN58942.1};
OS Anopheles darlingi (Mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=43151 {ECO:0000313|EMBL:ETN58942.1};
RN [1] {ECO:0000313|EMBL:ETN58942.1, ECO:0000313|Proteomes:UP000000673}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=20920257; DOI=10.1186/1471-2164-11-529;
RA Mendes N.D., Freitas A.T., Vasconcelos A.T., Sagot M.F.;
RT "Combination of measures distinguishes pre-miRNAs from other stem-loops in
RT the genome of the newly sequenced Anopheles darlingi.";
RL BMC Genomics 11:529-529(2010).
RN [2] {ECO:0000313|EMBL:ETN58942.1}
RP NUCLEOTIDE SEQUENCE.
RA Almeida L.G., Nicolas M.F., Souza R.C., Vasconcelos A.T.R.;
RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ETN58942.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23761445;
RA Marinotti O., Cerqueira G.C., de Almeida L.G., Ferro M.I., Loreto E.L.,
RA Zaha A., Teixeira S.M., Wespiser A.R., Almeida E Silva A.,
RA Schlindwein A.D., Pacheco A.C., Silva A.L., Graveley B.R., Walenz B.P.,
RA Lima Bde A., Ribeiro C.A., Nunes-Silva C.G., de Carvalho C.R., Soares C.M.,
RA de Menezes C.B., Matiolli C., Caffrey D., Araujo D.A., de Oliveira D.M.,
RA Golenbock D., Grisard E.C., Fantinatti-Garboggini F., de Carvalho F.M.,
RA Barcellos F.G., Prosdocimi F., May G., Azevedo Junior G.M., Guimaraes G.M.,
RA Goldman G.H., Padilha I.Q., Batista Jda S., Ferro J.A., Ribeiro J.M.,
RA Fietto J.L., Dabbas K.M., Cerdeira L., Agnez-Lima L.F., Brocchi M.,
RA de Carvalho M.O., Teixeira Mde M., Diniz Maia Mde M., Goldman M.H.,
RA Cruz Schneider M.P., Felipe M.S., Hungria M., Nicolas M.F., Pereira M.,
RA Montes M.A., Cantao M.E., Vincentz M., Rafael M.S., Silverman N.,
RA Stoco P.H., Souza R.C., Vicentini R., Gazzinelli R.T., Neves Rde O.,
RA Silva R., Astolfi-Filho S., Maciel T.E., Urmenyi T.P., Tadei W.P.,
RA Camargo E.P., de Vasconcelos A.T.;
RT "The genome of Anopheles darlingi, the main neotropical malaria vector.";
RL Nucleic Acids Res. 41:7387-7400(2013).
RN [4] {ECO:0000313|EnsemblMetazoa:ADAC009461-PA}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2015) 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 EMBL; ADMH02002109; ETN58942.1; -; Genomic_DNA.
DR AlphaFoldDB; W5J3L0; -.
DR STRING; 43151.W5J3L0; -.
DR EnsemblMetazoa; ADAC009461-RA; ADAC009461-PA; ADAC009461.
DR VEuPathDB; VectorBase:ADAC009461; -.
DR VEuPathDB; VectorBase:ADAR2_009961; -.
DR eggNOG; KOG0133; Eukaryota.
DR HOGENOM; CLU_010348_3_1_1; -.
DR OMA; FIHEPWN; -.
DR OrthoDB; 124765at2759; -.
DR Proteomes; UP000000673; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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; 2.
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:SF30; 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}; Lyase {ECO:0000313|EMBL:ETN58942.1};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000000673};
KW Transcription {ECO:0000256|ARBA:ARBA00023015};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 106..260
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT REGION 1..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 701..786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 880..911
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 942..1068
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..99
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 717..786
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 885..909
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 947..1005
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1027..1055
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 416..423
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 514..516
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT SITE 447
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 501
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 524
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ SEQUENCE 1068 AA; 120676 MW; 49F7A065D116BC61 CRC64;
MGMTKQTSSG VSGHYSGSGG HTGMNSMATG SGNAEKQQQP SSNLPHQQQQ QQASRHGQGS
KGQAQHQQHH LHQPLHAHHP LHHHLQQQQQ QQQQQQHPTA GKLRDKHTVH WFRKGLRLHD
NPALREGVRG ATSFRCVFVI DPWFAGSSNV GINKWRYWTH SAFANHVADN VSESLPEVTY
LFLLQCLDDL DRNLRKLNSR LFVIRGQPAD ALPKLFKEWS TTCLTFEEDP EPFGRVRDHN
ISEMCKELGI EVISAASHTL YNLERIIEKN GGRAPLTYHQ FQAIIASMDA PPQPETTITL
EAIGGATTPL YDDHDDKYGV PTLEELGFET EALRPPVWIG GETEALARLE RHLERKAWVA
SFGRPKMTPQ SLLASQTGLS PYLRFGCLST RLFYYQLTDL YKKIKKACPP LSLHGQLLWR
EFFYCAATKN PTFDKMAGNP ICVQIPWDRN SEALAKWASG QTGFPWIDAI MTQLREEGWI
HHLARHAVAC FLTRGDLWIS WEEGMKVFEE LLLDADWSVN AGMWMWLSCS SFFQQFFHCY
CPVKFGRKAD PNGDYIRRYL PVLKNFPTRF IHEPWNAPEN VQRAAKCLIG KDYPLPMVNH
AIASRANMER IKQVYQHLAK YRSPGVCYEG DCVEKGGSAI AGVMTAAKMQ HMNASSMNDS
PSPTTILTSV NSSGNYMCRS NPSAQSDPNA KVLTYHPLAM DGPTSIDGRA RSGSVVSGLG
TGDNANDGSS NTMDGKGRML TMQESVLQQQ QQQQQQHQRQ QQLQRQQRHA LQDGRPSNTV
QEAYGNLPTS DYASLKTDSG LGTMIRGGNL TGGRFTNLQD QLSNSLLSLE CEVMATKLEP
NNYDFERNQN MYNSQFKVEY SDNFNSGYGL RNAVFYGRKR EDEQDNEQDE DEGTGDDNND
QEESYNDEDD DRLATIAMSP LQDGVAARSL DHYQPGEPQI KQEATPLHSD MFREPKLLKG
SSLRTRTEEH QQQRAEQEER QCEDVVRPQA STNEHGEDKH TKRSAELPSN SMLTDCDYDS
ESHKMVTDYS RQQQQQQQQQ QRQSAVQLQN DQPMQDTAAK EEKLDCAD
//