UniProt: A0A0G4LLR9

Database: UniProt
Entry: A0A0G4LLR9_9PEZI

LinkDB:  A0A0G4LLR9_9PEZI 
Original site:  A0A0G4LLR9_9PEZI

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Ontology (8)   
   GO (8)   
Chemical reaction (2)   
   KEGG ENZYME (2)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (16)   
   InterPro (8)   
   Pfam (2)   
   PROSITE (5)   
   SMART (1)   
All databases (27)   

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ID   A0A0G4LLR9_9PEZI        Unreviewed;       822 AA.
AC   A0A0G4LLR9;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   RecName: Full=Multifunctional fusion protein {ECO:0000256|RuleBase:RU000587, ECO:0000256|RuleBase:RU361165};
DE   Includes:
DE     RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE              EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
DE   Includes:
DE     RecName: Full=Mitogen-activated protein kinase {ECO:0000256|RuleBase:RU361165};
DE              EC=2.7.11.24 {ECO:0000256|RuleBase:RU361165};
GN   ORFNames=BN1708_013571 {ECO:0000313|EMBL:CRK22992.1};
OS   Verticillium longisporum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX   NCBI_TaxID=100787 {ECO:0000313|EMBL:CRK22992.1, ECO:0000313|Proteomes:UP000044602};
RN   [1] {ECO:0000313|EMBL:CRK22992.1, ECO:0000313|Proteomes:UP000044602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VL1 {ECO:0000313|EMBL:CRK22992.1};
RA   Wang D.B., Wang M.;
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Allosteric enzyme that catalyzes the rate-limiting step in
CC       glycogen catabolism, the phosphorolytic cleavage of glycogen to produce
CC       glucose-1-phosphate, and plays a central role in maintaining cellular
CC       and organismal glucose homeostasis. {ECO:0000256|RuleBase:RU000587}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.24; Evidence={ECO:0000256|RuleBase:RU361165};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[(1->4)-alpha-D-glucosyl](n) + phosphate = [(1->4)-alpha-D-
CC         glucosyl](n-1) + alpha-D-glucose 1-phosphate; Xref=Rhea:RHEA:41732,
CC         Rhea:RHEA-COMP:9584, Rhea:RHEA-COMP:9586, ChEBI:CHEBI:15444,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58601; EC=2.4.1.1;
CC         Evidence={ECO:0000256|RuleBase:RU000587};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU361165};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|RuleBase:RU000587};
CC   -!- ACTIVITY REGULATION: Activated by threonine and tyrosine
CC       phosphorylation. {ECO:0000256|RuleBase:RU361165}.
CC   -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC       {ECO:0000256|ARBA:ARBA00006047, ECO:0000256|RuleBase:RU000587}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. MAP kinase subfamily. {ECO:0000256|RuleBase:RU361165}.
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DR   EMBL; CVQH01015002; CRK22992.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G4LLR9; -.
DR   STRING; 100787.A0A0G4LLR9; -.
DR   OrthoDB; 5473321at2759; -.
DR   Proteomes; UP000044602; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008184; F:glycogen phosphorylase activity; IEA:InterPro.
DR   GO; GO:0102250; F:linear malto-oligosaccharide phosphorylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004707; F:MAP kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0102499; F:SHG alpha-glucan phosphorylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 3.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011833; Glycg_phsphrylas.
DR   InterPro; IPR000811; Glyco_trans_35.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR003527; MAP_kinase_CS.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR035090; Pyridoxal_P_attach_site.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   NCBIfam; TIGR02093; P_ylase; 1.
DR   PANTHER; PTHR11468; GLYCOGEN PHOSPHORYLASE; 1.
DR   PANTHER; PTHR11468:SF3; GLYCOGEN PHOSPHORYLASE; 1.
DR   Pfam; PF00343; Phosphorylase; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
DR   PROSITE; PS01351; MAPK; 1.
DR   PROSITE; PS00102; PHOSPHORYLASE; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW   ECO:0000256|RuleBase:RU000587};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW   ECO:0000256|RuleBase:RU000587}; Kinase {ECO:0000256|RuleBase:RU361165};
KW   Magnesium {ECO:0000256|RuleBase:RU361165};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU000587};
KW   Reference proteome {ECO:0000313|Proteomes:UP000044602};
KW   Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU361165};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT   DOMAIN          20..385
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         50
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   822 AA;  94340 MW;  2632D574F735A74E CRC64;
     MAEFVRAQIF GTTFEITSRY SDLQPVGMGA FGLVCSARDQ LTNQNVAVKK IMKPFSTPVL
     AKRTYRELKL LKHLRHENVI SLSDIFISPL EDIYFVTELL GTDLHRLLTS RPLEKQFIQY
     FLYQIMRGLK YVHSAGVVHR DLKPSNILVN ENCDLKICDF GLARIQDPQM TGYVSTRYYR
     APEIMLTWQN LASLNYPAWG YGLRYRYGIF KQEIIDGYQV EVPDYWLDFN PWEFPRHDVI
     VDIQFYGHVN KSSDENGKSI AHWEGGETVQ AVAYDVPIPG YATPSTNNLR LWSSKAASGE
     FDFQKFNSGD YESSVADQQR AETISAVLYP NDNLERGKEL RLKQQYFWVA ASLYDIVRRF
     KKTKRAWKEF PDQVAIQLND THPTLAIVEL QRILIDLEKL EWDEAWDIVT ATFGYTNHTV
     LPEALEKWSV GLIQNLLPRH LQIIYDINLY FLQAVEKKFP GDRELLSRVS IIEESQPKMV
     RMAYLAVVGS HKVNGVAELH SDLIKTTIFK DFVNIYGPDK FTNVTNAITP RRWLHQANPR
     LSDLIAARTG SNEYLKDLTQ LNKLEQFVND KEFRKEWAEI KYANKVRLAK YIKSTTGVSV
     NPAALFDVQV KRIHEYKRQQ MNIFDIGDLL KVIFLEDYNV SKAEMIIPAS DLSEHISTAG
     TEASGTSNMK FVLNGGLIIG TCDGANIEIT REIGENNIFL FGNLAEDVED LRYAHNYGSH
     SLDSDLVKVF AEIEKGTFGS PHDFGALVSA VRDHGDYYLT SDDFHSYIET HALVDESYKN
     QEEWITKTIT SVARMGFFSS DRCINEYAEE IWNIEPLVVD DR
//

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