ID A0A2Z6QI62_9GLOM Unreviewed; 661 AA.
AC A0A2Z6QI62;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN ORFNames=RclHR1_11060006 {ECO:0000313|EMBL:GBB84501.1};
OS Rhizophagus clarus.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX NCBI_TaxID=94130 {ECO:0000313|EMBL:GBB84501.1, ECO:0000313|Proteomes:UP000247702};
RN [1] {ECO:0000313|EMBL:GBB84501.1, ECO:0000313|Proteomes:UP000247702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HR1 {ECO:0000313|EMBL:GBB84501.1,
RC ECO:0000313|Proteomes:UP000247702};
RA Kobayashi Y.;
RT "The genome of Rhizophagus clarus HR1 reveals common genetic basis of
RT auxotrophy among arbuscular mycorrhizal fungi.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the sel-1 family.
CC {ECO:0000256|ARBA:ARBA00038101}.
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:GBB84501.1}.
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DR EMBL; BEXD01000121; GBB84501.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z6QI62; -.
DR STRING; 94130.A0A2Z6QI62; -.
DR Proteomes; UP000247702; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 3.
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; IPR006597; Sel1-like.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR11102:SF147; FIBRONECTIN TYPE-II DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR11102; SEL-1-LIKE PROTEIN; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF08238; Sel1; 8.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00671; SEL1; 8.
DR SUPFAM; SSF81901; HCP-like; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00022707};
KW Myristate {ECO:0000256|ARBA:ARBA00022707};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Reference proteome {ECO:0000313|Proteomes:UP000247702}.
FT DOMAIN 52..313
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 81
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 661 AA; 75277 MW; B6F389E142363899 CRC64;
MFSAVSPFFL KKTAIKINYI KMQGINNANN WTNLIEDAIS KNHIKYYEYD HFYNIKEVGS
GSFGKVYRAN WKNSQKYLVL KSFVNVNKTS IKEIVHERDV DFYENVIRFY GITSYNKENQ
DDNSKEYLLV MEYADSGTLQ DHLKEHFKSL NWKDKFDLAI QLAHAVSCLH DEGIMHRGLH
SKNVLIHQNT IKLTDFGLSK KVDEELKSRS DSSGIIPYVD PKKFKLQKYS LSKKSDVYSI
GVLLWEISSG RPPFKERLTS DSSDLIVQIQ KGLREVPISD TPSAYVDLYT KCWNGEPDNR
PTIHQVVTKL KELKENKIND DFRVIVDEIV NLSNKIEDNV DEEEKQNILD YFNNHNVTSQ
EIYNWSLNNQ NYSNSIVLLG DFNYLGIEIN VNKNKAFELY QTAAILGNII AQYNLGCCYK
YGKGVDKDYD KAFNIFKKSA EKSHPKGINH LGYCYKYGLG TNVNEKKAFE LYKKAANLGN
VFGLVNLGNC YFSGIGTSAD EEMVFKLHQE ATNLGNTYGM INLGSCYKTG IGTRVDKQKA
FELFQKAANL GNTNGIINLG NCYRRGIGTC ADEEKAFELY QKAADIGNIF GIINLGVCYQ
NGIGTSVNMQ KAFELYQKAA NLENVDGINY LGNCYRYGIG TNVDERKAFE LYQKAENLGV
R
//
