ID A0A372QHV9_9GLOM Unreviewed; 389 AA.
AC A0A372QHV9;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Kinase-like domain-containing protein {ECO:0000313|EMBL:RGB26899.1};
GN ORFNames=C1646_720024 {ECO:0000313|EMBL:RGB26899.1};
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:RGB26899.1, ECO:0000313|Proteomes:UP000263633};
RN [1] {ECO:0000313|EMBL:RGB26899.1, ECO:0000313|Proteomes:UP000263633}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUCL 43196 {ECO:0000313|EMBL:RGB26899.1,
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:RGB26899.1}.
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DR EMBL; QKKE01000576; RGB26899.1; -; Genomic_DNA.
DR STRING; 1803374.A0A372QHV9; -.
DR InParanoid; A0A372QHV9; -.
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: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; PS50011; PROTEIN_KINASE_DOM; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:RGB26899.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000263633};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 48..306
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 358..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..389
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 389 AA; 45623 MW; 392A87210EB76E1A CRC64;
MEDLEKRKQD NFKNWTSGNK DIDEFIQQSQ LNAVYFXKXL EWIPFENFEN ITYITRGGFG
KIYSAEWPEG YIRYWDIENQ KWDKDSNTEV ALKRLDNSSC LSTEFLNEIK SHLQIYLWDV
IQCYGITQDP NTKDYIMVLK YCEDGNLRNY YMNSELGYYS KINELQQIAR GLLDIHNAGK
IHKDFHSGNI LYNDDKFPYI SDLGMCQPAN NEKQSAKQEG IYGVLPYMAP EVLRGYQYTK
ASDIYSFGIM MNEYISEETP YNDIPHDHAL AIKIXLITKC WDAKAENRPT AKELYQILDK
WHHVILYSLN YGSEDFSQIN EYDDKIKLNR TSDKRSKNIQ THPQAIYTSR LLSFKNLPEP
VNSDSEGFDC QLDDSDLNEI NQNDDDNSE
//
