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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//