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Database: UniProt
Entry: A0A397U0W5_9GLOM
LinkDB: A0A397U0W5_9GLOM
Original site: A0A397U0W5_9GLOM 
ID   A0A397U0W5_9GLOM        Unreviewed;       463 AA.
AC   A0A397U0W5;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   SubName: Full=Kinase-like domain-containing protein {ECO:0000313|EMBL:RIB02818.1};
GN   ORFNames=C2G38_841768 {ECO:0000313|EMBL:RIB02818.1};
OS   Gigaspora rosea.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC   Glomeromycetes; Diversisporales; Gigasporaceae; Gigaspora.
OX   NCBI_TaxID=44941 {ECO:0000313|EMBL:RIB02818.1, ECO:0000313|Proteomes:UP000266673};
RN   [1] {ECO:0000313|EMBL:RIB02818.1, ECO:0000313|Proteomes:UP000266673}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DAOM 194757 {ECO:0000313|EMBL:RIB02818.1,
RC   ECO:0000313|Proteomes:UP000266673};
RA   Morin E., San Clemente H., Chen E.C.H., De La Providencia I., Hainaut M.,
RA   Kuo A., Kohler A., Murat C., Tang N., Roy S., Loubradou J., Henrissat B.,
RA   Grigoriev I.V., Corradi N., Roux C., Martin F.M.;
RT   "Comparative genomics reveals the genomic features of Rhizophagus
RT   irregularis, R. cerebriforme, R. diaphanum and Gigaspora rosea, and their
RT   symbiotic lifestyle signature.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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:RIB02818.1}.
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DR   EMBL; QKWP01002580; RIB02818.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A397U0W5; -.
DR   STRING; 44941.A0A397U0W5; -.
DR   Proteomes; UP000266673; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   PANTHER; PTHR23257:SF975; DUAL SPECIFICITY PROTEIN KINASE SPLA-RELATED; 1.
DR   PANTHER; PTHR23257; SERINE-THREONINE PROTEIN KINASE; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:RIB02818.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000266673};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          120..405
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         148
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   463 AA;  53026 MW;  9EA4F5B4C03098A1 CRC64;
     MTCIKYIKIF LIIYIFYKFK NYINLKDNKF KVYGLTQNTT TKEYILVFDE FGSKRDFKHG
     KCSYCNRYNT SPAWCQTCDP QRMIQGWTSG NKDIDNYIKG FQLAATEYEN VIEWIPFDKL
     DNFQKIGEGG FGSVYSAIWS SGKRIIGKIP KYTQQRTQSY VVALKTLPGP QKNFLDEFKN
     YMKSRLLEQP DIIEPKYRPI NNQLEVYGLT KDAVTNEFLM VFQYVNRGSL NNFLASNFQN
     LSWKKKLELL LGISKDLAKI HDAGYIHCDI HSGNILINEC INGNIISYIS DLGLSRTTDE
     LSLEDGIYGV LPYIAPEVLI KQPYTTAADI YSFGIIMSEI STGKLPYCDV KHNEDLAIKI
     YAGLRPEFAK GTPECYIQLA NQCMDANPSN RPSASEICKK LEDWYLKIRA EAINEDAKNL
     KKAFASADVM IKTLSTKLQD YPQVRSKLVE FLNVSEPESM PVI
//
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