GenomeNet

Database: UniProt
Entry: W5J3L0_ANODA
LinkDB: W5J3L0_ANODA
Original site: W5J3L0_ANODA 
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
//
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