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Database: UniProt
Entry: A0A0D0E223_9AGAM
LinkDB: A0A0D0E223_9AGAM
Original site: A0A0D0E223_9AGAM 
ID   A0A0D0E223_9AGAM        Unreviewed;       648 AA.
AC   A0A0D0E223;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN   ORFNames=PAXRUDRAFT_443087 {ECO:0000313|EMBL:KIK94519.1};
OS   Paxillus rubicundulus Ve08.2h10.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Boletales; Paxilineae; Paxillaceae; Paxillus.
OX   NCBI_TaxID=930991 {ECO:0000313|EMBL:KIK94519.1, ECO:0000313|Proteomes:UP000054538};
RN   [1] {ECO:0000313|EMBL:KIK94519.1, ECO:0000313|Proteomes:UP000054538}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ve08.2h10 {ECO:0000313|EMBL:KIK94519.1,
RC   ECO:0000313|Proteomes:UP000054538};
RG   DOE Joint Genome Institute;
RA   Kuo A., Kohler A., Jargeat P., Nagy L.G., Floudas D., Copeland A.,
RA   Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA   Lipzen A., Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA   Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA   Hua S.X.;
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000054538}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ve08.2h10 {ECO:0000313|Proteomes:UP000054538};
RG   DOE Joint Genome Institute;
RG   Mycorrhizal Genomics Consortium;
RA   Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA   Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA   Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT   "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001433};
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DR   EMBL; KN825101; KIK94519.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D0E223; -.
DR   STRING; 930991.A0A0D0E223; -.
DR   HOGENOM; CLU_000288_59_3_1; -.
DR   InParanoid; A0A0D0E223; -.
DR   OrthoDB; 1700376at2759; -.
DR   Proteomes; UP000054538; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:InterPro.
DR   CDD; cd12122; AMPKA_C; 1.
DR   CDD; cd14334; UBA_SNF1_fungi; 1.
DR   Gene3D; 3.30.310.80; Kinase associated domain 1, KA1; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR032270; AMPK_C.
DR   InterPro; IPR028375; KA1/Ssp2_C.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR013896; SNF1_UBA.
DR   PANTHER; PTHR24346; MAP/MICROTUBULE AFFINITY-REGULATING KINASE; 1.
DR   PANTHER; PTHR24346:SF82; SERINE_THREONINE-PROTEIN KINASE MARK-A-RELATED; 1.
DR   Pfam; PF16579; AdenylateSensor; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF08587; UBA_2; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF103243; KA1-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054538}.
FT   DOMAIN          16..267
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
SQ   SEQUENCE   648 AA;  72534 MW;  A821D431F85CD462 CRC64;
     MNEKTTVLPA SKLGEYTVIG DIAEGTFGKV KKAMHTITGQ QVAMKYISKA VIHMTKTKTR
     VQREVEYMRA LRHPHIIKLY EVISTPTDII IVLEYAGGEL FNYIVANGRM PEPRARKFFQ
     QLISGIEYSH KLKIVHRDLK PENVLLDDDL NVKIADFGLS NEIKDGDFLK TSCGSPNYAA
     PEVIRGGLYT GPEIDVWSCG VILYVMLCGR LPFEDDDVQT LFTKISQGSY HMPSHLGADA
     RGLINAMLAV DPVKRITVPE ITQHPFFTTD LPRYLTPLPP PPGPVLGTLS SLVTPAKVLD
     FEIIEGLGRI EEDVVDELAS RMDGVDKEDI WECLRRDDGV QGNAVKVAYM LLRDKRRAGR
     DLAEFEEQER DAKLAAMDPR NTMSPGALSP ASDLEENPFE VEFNGQYEDA DIDDGLDFST
     PLDGEINNFA VLNSSLPLPD QLPEQHHLAS YANAKRTWPA AKEKKQHRTK WHFGIRSRSP
     PMEVMLEIYR TLKTLGMEWK EKRNLGGLGG VRVQRQRSGT NGARIERARD LDGSEPVDLR
     VAASVYFVET RARVQDVVVL MNLQLYMVDS INYLVDFHHK KTYRASTEVG AGKFDMANIE
     TVLPETSSDG RSIKDKDSHS VKEDEVVSPF VFMDVACRLI LELAGGGE
//
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