ID A0A372RQ91_9GLOM Unreviewed; 422 AA.
AC A0A372RQ91;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE SubName: Full=Kinase-like domain-containing protein {ECO:0000313|EMBL:RGB41517.1};
GN ORFNames=C1646_810652 {ECO:0000313|EMBL:RGB41517.1};
OS Rhizophagus sp. MUCL 43196.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX NCBI_TaxID=1803374 {ECO:0000313|EMBL:RGB41517.1, ECO:0000313|Proteomes:UP000263633};
RN [1] {ECO:0000313|EMBL:RGB41517.1, ECO:0000313|Proteomes:UP000263633}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUCL 43196 {ECO:0000313|EMBL:RGB41517.1,
RC ECO:0000313|Proteomes:UP000263633};
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:RGB41517.1}.
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; QKKE01000037; RGB41517.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A372RQ91; -.
DR STRING; 1803374.A0A372RQ91; -.
DR InParanoid; A0A372RQ91; -.
DR Proteomes; UP000263633; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
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; PS50011; PROTEIN_KINASE_DOM; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:RGB41517.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000263633};
KW Transferase {ECO:0000313|EMBL:RGB41517.1}.
FT DOMAIN 69..339
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
SQ SEQUENCE 422 AA; 49038 MW; 909706CE0BB09A1A CRC64;
MDKCEKCGES YKGFFNIKYK WCKPCQINRL KNYIKISGDK KIDEFIQEIN SKINCYSDPL
FEWIPYNQFN DVELIGKGGF SIVCSAIWKD GPLNYDVNKM EWTTRKERVN KKVALKCLID
SQNITSEFLN EIKIHKIMNS RHILKAFGIS QNPETKEYIM VFEFVEGGSL NDWINKNFID
LSWKNKLKSL LNIFNALDEL HQKGFVHHDF HTGNILIKNG NFPHISDMGL CREASNNDET
KIFGVMPYLD PNVLKGNPYT QASDVYSAGM IMYFIATGRQ PFANCPHDEF LAINICKGDR
PVINKTEAPK CYVELMEKCW DSSPDKRPKI AELKKEILIF YASYTKNESG FKTLMKTEKK
KEHYEIENQF KEAEEHRKSL SSESNPHSQA IYTSRLLNSF TKNIPKYDNI NNNSVEIIDF
TM
//