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Database: UniProt
Entry: A0A1L0CV94_9ASCO
LinkDB: A0A1L0CV94_9ASCO
Original site: A0A1L0CV94_9ASCO 
ID   A0A1L0CV94_9ASCO        Unreviewed;       549 AA.
AC   A0A1L0CV94;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   28-JUN-2023, entry version 17.
DE   SubName: Full=CIC11C00000004850 {ECO:0000313|EMBL:SGZ47026.1};
GN   ORFNames=SAMEA4029010_CIC11G00000004850 {ECO:0000313|EMBL:SGZ47026.1};
OS   [Candida] intermedia.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Metschnikowiaceae; Metschnikowiaceae incertae sedis;
OC   Candida/Metschnikowiaceae.
OX   NCBI_TaxID=45354 {ECO:0000313|EMBL:SGZ47026.1, ECO:0000313|Proteomes:UP000182334};
RN   [1] {ECO:0000313|EMBL:SGZ47026.1, ECO:0000313|Proteomes:UP000182334}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 141442 {ECO:0000313|EMBL:SGZ47026.1,
RC   ECO:0000313|Proteomes:UP000182334};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; LT635756; SGZ47026.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1L0CV94; -.
DR   STRING; 45354.A0A1L0CV94; -.
DR   OrthoDB; 124765at2759; -.
DR   Proteomes; UP000182334; Chromosome i.
DR   GO; GO:1901363; F:heterocyclic compound binding; IEA:UniProt.
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; SI:CH1073-390K14.1; 1.
DR   Pfam; PF00875; DNA_photolyase; 1.
DR   Pfam; PF03441; FAD_binding_7; 1.
DR   PRINTS; PR00147; DNAPHOTLYASE.
DR   SUPFAM; SSF48173; Cryptochrome/photolyase FAD-binding domain; 1.
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:UP000182334}.
FT   DOMAIN          58..195
FT                   /note="Photolyase/cryptochrome alpha/beta"
FT                   /evidence="ECO:0000259|PROSITE:PS51645"
FT   BINDING         292
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         344
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         347..354
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         445..447
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   SITE            379
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            432
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            455
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ   SEQUENCE   549 AA;  63519 MW;  900886531B1A3348 CRC64;
     MKRQKIEKLP SFSNLLYPSE LSLQAAAQYK NDQKKPYNVL NKKLAESETK RNSIKPRKVI
     AHWFVRDFRI SDNHGLSKAY EMAAKNKLPL VAFWVKCPKL SEAHGDSEFK KYYRSLSLQQ
     VHSKLAKLNI TLVTVEADEK KDIVPAIQSF CTKYDVSHLF ANLEYEVDEL RLFTSAHDNL
     LKSNTALMPY HDSCVVEPGE LKTKSKGTQF AVFTPWYKAW VKFVNDNYFS EKNFVYPDIQ
     KVESTIEVDE TTDFDVGNVD TDRFEKYWKL VGEDGAREAL TNYINSEQIK KYDEDRDFLD
     EDAPSQLSIH ISSGTLSTRT ILQELFNAKM LKSKLSSYNG VSEWVRQASW RDFYKHIMCN
     WPYICMYKPF QLELSDLHWE YNNDHFLLWC EGATGFPVVD ACMRCLNETG YLNNRGRLIV
     ACFLAKDLLI DWRYGEQYFM SKLVDGDLAS NNGGWGFAAS TGVDPQPYFR IFNPWTQSEK
     FDPEGNFIRK WVPELANLKG KAIHNPHSSN SDVEGYPTPI VEHKACRERA LERYKEAMAK
     GKEALKEVS
//
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