UniProt: A0A162P4Y5

Database: UniProt
Entry: A0A162P4Y5_9PEZI

LinkDB:  A0A162P4Y5_9PEZI 
Original site:  A0A162P4Y5_9PEZI

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Ontology (11)   
   GO (11)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (23)   
   InterPro (13)   
   Pfam (5)   
   PROSITE (3)   
   SMART (2)   
All databases (36)   

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ID   A0A162P4Y5_9PEZI        Unreviewed;      1076 AA.
AC   A0A162P4Y5;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Glutathione reductase {ECO:0000256|RuleBase:RU365016};
DE            EC=1.8.1.7 {ECO:0000256|RuleBase:RU365016};
GN   ORFNames=CI238_04216 {ECO:0000313|EMBL:KZL86685.1};
OS   Colletotrichum incanum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum spaethianum species complex.
OX   NCBI_TaxID=1573173 {ECO:0000313|EMBL:KZL86685.1, ECO:0000313|Proteomes:UP000076584};
RN   [1] {ECO:0000313|EMBL:KZL86685.1, ECO:0000313|Proteomes:UP000076584}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MAFF 238704 {ECO:0000313|EMBL:KZL86685.1,
RC   ECO:0000313|Proteomes:UP000076584};
RA   Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA   Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA   Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA   O'Connell R.J.;
RT   "Survival trade-offs in plant roots during colonization by closely related
RT   pathogenic and mutualistic fungi.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Maintains high levels of reduced glutathione in the cytosol.
CC       {ECO:0000256|RuleBase:RU365016}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 glutathione + NADP(+) = glutathione disulfide + H(+) +
CC         NADPH; Xref=Rhea:RHEA:11740, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:58349; EC=1.8.1.7;
CC         Evidence={ECO:0000256|RuleBase:RU365016};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|RuleBase:RU365016};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU365016}.
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532,
CC       ECO:0000256|RuleBase:RU003691}.
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:KZL86685.1}.
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DR   EMBL; LFIW01000399; KZL86685.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A162P4Y5; -.
DR   STRING; 1573173.A0A162P4Y5; -.
DR   Proteomes; UP000076584; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0004362; F:glutathione-disulfide reductase (NADP) activity; IEA:UniProtKB-EC.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR   CDD; cd17920; DEXHc_RecQ; 1.
DR   Gene3D; 3.30.390.30; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR004589; DNA_helicase_ATP-dep_RecQ.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR   InterPro; IPR006322; Glutathione_Rdtase_euk/bac.
DR   InterPro; IPR046952; GSHR/TRXR-like.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR   InterPro; IPR032284; RecQ_Zn-bd.
DR   NCBIfam; TIGR01421; gluta_reduc_1; 1.
DR   NCBIfam; TIGR00614; recQ_fam; 1.
DR   PANTHER; PTHR42737; GLUTATHIONE REDUCTASE; 1.
DR   PANTHER; PTHR42737:SF2; GLUTATHIONE REDUCTASE; 1.
DR   Pfam; PF00270; DEAD; 2.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF02852; Pyr_redox_dim; 1.
DR   Pfam; PF16124; RecQ_Zn_bind; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cytoplasm {ECO:0000256|RuleBase:RU365016};
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU003691};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU003691}; Helicase {ECO:0000313|EMBL:KZL86685.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   NADP {ECO:0000256|RuleBase:RU365016};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003691};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW   ECO:0000256|RuleBase:RU003691};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076584}.
FT   DOMAIN          34..186
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          238..384
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          470..489
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1076 AA;  119447 MW;  90BF15DD8C821301 CRC64;
     MPPLSRSNSC VDIDYTLRRQ FNKSTFRPQQ REIIAAALDG HDVFVQAATS FGKSLCFQLP
     ACIDHGRIDA SSLNSNTPTA ERDRINQDLA SGHPRIRLLY VTPELCSGDS FRRRIKLVYE
     QCELARIAVD EAHCISEWGH DFRKDFKRLS WFRETFPSVP IMCLTATANP TVRQDLLKTL
     GLLEQPGRLK SFVMTAHRPN LHIEIRYTKD QDDDRLADFL AWIRSVHERR KADPRKAELE
     AAGERLDNVS GIIYTISRDE CESLAAALRD EGVGARPFHA KLTKETKEQT LARWVNNEPG
     YDVIVATTAF GMGIDKNNVR FVVHWRLPKS FEGYYQEAGR AGRDGNASFC FLYYSREDLQ
     RVQSMIRKGN RDGSNWEAQA KSLQKLALYC EDTTACRHAQ ICKYFGESET PKCDFACDWH
     KDAQGLQRRM MRGLADEEWV STQAEYGRTS LTHTRANSLD TRFQTCNWSS NQSPDVAPPY
     ADSRSIPETH SPIADSAARI RTRISARRRP LRKKTYISYL PSPSPPYRIR AVLSFLQLSI
     FSPTNVHIEN YSPPPPSASA IISSPQHSMQ ALQAALYRTS TVAASRAAAP TTRLASIQRH
     LSSTARTMAP ITKETDFLVI GGGSGGLASA RKASGQFGAK ALIVEGSRLG GTCVNVGCVP
     KKVTFNAAAI AETIHQAKSY GFSVAETAPF DWSTFKTKRD AYIKRLNGIY ERNLNNDKVE
     YLHGWAKLTS RNEAEVTLDD GTKALVKAKK ILIAVGGNPT IPPTIPGSEL GTNSDGFFDI
     DTQPKKVALV GAGYIAVEFA GMFNALGTET HLFIRHDTFL RTFDPLIQET VTKEYERLGV
     NLHKRSQPTK VEKDAEGKLT IFYKDAEGKE TSEGGFDHLI WAIGRTPATK DIGLEEIGLK
     LNEKGHIPVD QYQNTNLDNI YALGDVTGQV ELTPVAIAAG RRLAERLYGG PEYSKAHLDY
     SNIPSVVFSH PEVGSIGLTE PQAIEKYGKD NIKVYKTNFT AMYYAMMEPE EKGPTAYKLI
     VAGPEEKVVG LHIAGLGSGE MLQGFGVAVK MGATKKDFDS CVAIHPTSAE ELVTLK
//

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