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Database: UniProt
Entry: A0A060S7U6_PYCCI
LinkDB: A0A060S7U6_PYCCI
Original site: A0A060S7U6_PYCCI 
ID   A0A060S7U6_PYCCI        Unreviewed;      2103 AA.
AC   A0A060S7U6;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=Phosphoglycerate kinase {ECO:0000256|ARBA:ARBA00016471, ECO:0000256|RuleBase:RU000532};
DE            EC=2.7.2.3 {ECO:0000256|ARBA:ARBA00013061, ECO:0000256|RuleBase:RU000532};
GN   ORFNames=BN946_scf184636.g9 {ECO:0000313|EMBL:CDO70577.1};
OS   Pycnoporus cinnabarinus (Cinnabar-red polypore) (Trametes cinnabarina).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Polyporaceae; Trametes.
OX   NCBI_TaxID=5643 {ECO:0000313|EMBL:CDO70577.1, ECO:0000313|Proteomes:UP000029665};
RN   [1] {ECO:0000313|EMBL:CDO70577.1, ECO:0000313|Proteomes:UP000029665}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRFM137 {ECO:0000313|EMBL:CDO70577.1,
RC   ECO:0000313|Proteomes:UP000029665};
RA   Levasseur A., Lomascolo A., Ruiz-Duenas F.J., Uzan E., Piumi F., Kues U.,
RA   Ram A.F.J., Murat C., Haon M., Benoit I., Arfi Y., Chevret D., Drula E.,
RA   Kwon M.J., Gouret P., Lesage-Meessen L., Lombard V., Mariette J.,
RA   Noirot C., Park J., Patyshakuliyeva A., Wieneger R.A.B., Wosten H.A.B.,
RA   Martin F., Coutinho P.M., de Vries R., Martinez A.T., Klopp C.,
RA   Pontarotti P., Henrissat B., Record E.;
RT   "The genome of the white-rot fungus Pycnoporus cinnabarinus: a
RT   basidiomycete model with a versatile arsenal for lignocellulosic biomass
RT   breakdown.";
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl
CC         phosphate + ADP; Xref=Rhea:RHEA:14801, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:57604, ChEBI:CHEBI:58272, ChEBI:CHEBI:456216; EC=2.7.2.3;
CC         Evidence={ECO:0000256|ARBA:ARBA00000642,
CC         ECO:0000256|RuleBase:RU000532};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|RuleBase:RU000696}.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC       {ECO:0000256|ARBA:ARBA00008982, ECO:0000256|RuleBase:RU000532}.
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:CDO70577.1}.
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DR   EMBL; CCBP010000086; CDO70577.1; -; Genomic_DNA.
DR   STRING; 5643.A0A060S7U6; -.
DR   HOGENOM; CLU_232353_0_0_1; -.
DR   OrthoDB; 2784357at2759; -.
DR   Proteomes; UP000029665; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140680; F:histone H3K36me/H3K36me2 demethylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004618; F:phosphoglycerate kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006096; P:glycolytic process; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00318; Phosphoglycerate_kinase; 1.
DR   Gene3D; 2.60.120.650; Cupin; 1.
DR   Gene3D; 3.40.50.1260; Phosphoglycerate kinase, N-terminal domain; 3.
DR   Gene3D; 2.60.120.470; PITH domain; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR   HAMAP; MF_00145; Phosphoglyc_kinase; 1.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR041070; JHD.
DR   InterPro; IPR003347; JmjC_dom.
DR   InterPro; IPR001576; Phosphoglycerate_kinase.
DR   InterPro; IPR015911; Phosphoglycerate_kinase_CS.
DR   InterPro; IPR015824; Phosphoglycerate_kinase_N.
DR   InterPro; IPR036043; Phosphoglycerate_kinase_sf.
DR   InterPro; IPR010400; PITH_dom.
DR   InterPro; IPR037047; PITH_dom_sf.
DR   InterPro; IPR006597; Sel1-like.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   PANTHER; PTHR11406; PHOSPHOGLYCERATE KINASE; 1.
DR   PANTHER; PTHR11406:SF0; PHOSPHOGLYCERATE KINASE; 1.
DR   Pfam; PF17811; JHD; 1.
DR   Pfam; PF02373; JmjC; 1.
DR   Pfam; PF00162; PGK; 1.
DR   Pfam; PF06201; PITH; 1.
DR   Pfam; PF08238; Sel1; 7.
DR   PRINTS; PR00477; PHGLYCKINASE.
DR   SMART; SM00558; JmjC; 1.
DR   SMART; SM00671; SEL1; 7.
DR   SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF81901; HCP-like; 1.
DR   SUPFAM; SSF53748; Phosphoglycerate kinase; 1.
DR   PROSITE; PS51184; JMJC; 1.
DR   PROSITE; PS00111; PGLYCERATE_KINASE; 1.
DR   PROSITE; PS51532; PITH; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU000532};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029665};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000532}.
FT   DOMAIN          664..823
FT                   /note="JmjC"
FT                   /evidence="ECO:0000259|PROSITE:PS51184"
FT   DOMAIN          1942..2103
FT                   /note="PITH"
FT                   /evidence="ECO:0000259|PROSITE:PS51532"
FT   REGION          406..463
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          492..513
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          920..953
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1053..1124
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1141..1556
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        435..454
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        931..945
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1053..1073
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1141..1230
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1281..1295
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1319..1342
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1349..1365
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1422..1487
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1512..1526
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2103 AA;  231531 MW;  292426B746AFF928 CRC64;
     MSIANKLSIT DLDLKGKRVL IRVDFNVPMQ DGKVTNPARI VAALPTIKYA VENGASKVIL
     MSHLGRPDGK PNPKYSLEPV SKELEKHLGK SVIFVHECVG PDVEKTVNEA PEGSVILLEN
     LRFHIEEEGS SKDKDGKKVK ADPAKVQEFR EGLTRLGDVY VNDAFGTAHR AHSSMVGVKL
     SQRAAGFLMK KELDYFAKAL EHPERPFLAI LGGAKVSDKI QLIDNMLDKV DSLIICGGMA
     FTFKKTLNNV KIGQSLFDAP GAEKVASLVE KAKQRNIKIV FPVDYVIADK FDKDAKTGVA
     TDEEGIPDDW MGLDAGPKSR ELFRQTVLES KTILWNGPPG VFEFPAFSAG SKALLDATIE
     AAQKGAIVIV GGGDTATVVA NYGAEDKLSH VSTGGGASLE LLEGKTLPGV AELSEKQTQK
     TPDAGGATDD DAQTPQHGQE GEDVREDDYD KCPSCQEGDP TGEEVAADKE KWVRFCRGCL
     DTDPARVITM KPPARKSARK KTQRDYAGLN TGQEADPSRF LRMMEGRLIK KDPFRRMRGS
     EVGVEWLESD ESAMKEPIVV EDAEGLGMKM PPSSFTVDDV VEALGEDHPV EVIGAFKVQA
     ADGDSAHARY PEDYTKLMSV SWCSSSDVAT QSNSPNWTLG KWLEYWHTEP SKRDKIRNVI
     SLEISGSELA NQVLPPRIVR ELDWVEKFWP NTKKGKGHNY PKVQLYCLMG VGGAWTDWHI
     DFAGSSVYYH IINGAKVFYF IRPTPANLAA YERWSGTEVQ NHSWLGDMCD EVFKVELKTG
     DTMIIPTGWI HAVYTPVDTL VFGGNFLHSY NVPTQLRVRE IEIATHVPKK FRFPYFTKLC
     WYAAEKYLRD FKAKEEFPPR VLESVEALAD FLVAEARTME RGNDTAKRQA KEEVPGDRIK
     DAPALARELR WRVRHAAGYS SDDDGRSARK SKGTANGNGE SATNGVGSKR KRVALESSEE
     SVELFRNFKR PPWDRVEERP TGRESMVVKV RRPDTQSQGW VQDWVSGSGD AEVEDGEDAQ
     VERKRDVIVK VRKTAKGLER QRVERVLEEW AWNGGTSTSP PRSSKTEPPT VDVTMTSEDR
     PPXXXXXXXP PATEAKAEPA EQDAVMRDAA PALPGDSVLS PTTSTRTHDI HRSLVTVLGP
     SLNVMSDAQD NQHQPTDRQS RRQGILSADS QQYWNGQALQ TQNDYAGYQT EGQHNGNHSP
     PSGQDNFNQP LMRHQNRSVP TINTQIPPDQ YGEHDTVPPL PPPYDPNSVA DQFGNMHLTQ
     HGPPSRGPPA SDPIPRAGTS MSMRSMHSMQ SPQRMAPPMN GGLPISPDAM RRQPPGRIDN
     AMRSNSVHSG GSGTSGNVSM YSEGHDSLPY DASNETDTTS LYSAHDDPMF QPVQNGYHHG
     GGLPPPVPRW HGHGQQPQYN VSPPPNEFNH LYAAASDVLG MGPPPGPAPP APPPVNHQYA
     PGPAASPYPP PPGPSHTPYP PPGSTASPYP HPGPSPAPYP PQGYPQGLGP IPASQSGSYL
     GAAPYQPGPS GPYPASSQSH LARGPSNASS FHAPPPPPLE EAEFELNRPP LHRTETAASV
     APRTQKTKAI DLSAPPYTKE YIDQYRQRIK DDPDPEAQFQ YAKYLIDAAK KIGAEAKDQR
     SLRKYRDSLI QESLKVIRRL ATQGQPYDEA QFFLANCHGT GMLGLQVDHE RAYHLYLQAA
     KQNHPAACYR VAVCNEIGAG TKADPQRAAA FYRKAASLGD TAAMYKLGVI LLRGLLKQQP
     NPREAIGWLR RAAEQADEEN PHALHELAML YENPNNGVVP YDPAYAKELY TRAAHLGYTH
     SQFKLGQCYE YGTLTCPVDP RRSIAWYTKA AEKGHAEAEL ALSGWYLTGS EGVLKQSDSE
     AYLWARRAAN KGLSKAEYAV GYYAEVGIGV KQDIEFAKRW YMRAAAQGNK RAMARLTEMK
     RNGNKRANMA RPTRQDAKDD ADDDAMAETE VSLLEHLDLS QLTCLNETQE HNLKGIVADK
     KKNTGSAYLE SDADEQLLLT LPFNQAVKIR AIAIQSSNVS QAPRKIKLVT NKPTLDFDDL
     EDGGAVVQEL ELSEDDVREG RKVPLRFVKF QSVNSLHVST CALEIHRPVH YALGMLSELS
     MRC
//
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