ID U9V817_RHIID Unreviewed; 902 AA.
AC U9V817;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN ORFNames=GLOINDRAFT_14812 {ECO:0000313|EMBL:ESA24041.1};
OS Rhizophagus irregularis (strain DAOM 181602 / DAOM 197198 / MUCL 43194)
OS (Arbuscular mycorrhizal fungus) (Glomus intraradices).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX NCBI_TaxID=747089 {ECO:0000313|EMBL:ESA24041.1};
RN [1] {ECO:0000313|EMBL:ESA24041.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DAOM 197198 {ECO:0000313|EMBL:ESA24041.1};
RG DOE Joint Genome Institute;
RA Tisserant E., Malbreil M., Kuo A., Kohler A., Symeonidi A., Balestrini R.,
RA Charron P., Duensing N., Frei-dit-Frey N., Gianinazzi-Pearson V.,
RA Gilbert B., Handa Y., Hijri M., Kaul R., Kawaguchi M., Krajinski F.,
RA Lammers P., Lapierre D., Masclaux F.G., Murat C., Morin E., Ndikumana S.,
RA Pagni M., Petitpierre D., Requena N., Rosikiewicz P., Riley R., Saito K.,
RA San Clemente H., Shapiro H., van Tuinen D., Becard G., Bonfante P.,
RA Paszkowski U., Shachar-Hill Y., Young J.P., Sanders I.R., Henrissat B.,
RA Rensing S.A., Grigoriev I.V., Corradi N., Roux C., Martin F.;
RT "The genome of an arbuscular mycorrhizal fungus provides insights into the
RT evolution of the oldest plant symbiosis.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the sel-1 family.
CC {ECO:0000256|ARBA:ARBA00038101}.
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DR EMBL; KI274261; ESA24041.1; -; Genomic_DNA.
DR AlphaFoldDB; U9V817; -.
DR eggNOG; KOG0192; Eukaryota.
DR eggNOG; KOG1550; Eukaryota.
DR HOGENOM; CLU_000288_7_12_1; -.
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; SEL-1-LIKE PROTEIN; 1.
DR PANTHER; PTHR11102:SF163; SEL1 DOMAIN PROTEIN REPEAT-CONTAINING PROTEIN; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF08238; Sel1; 12.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00671; SEL1; 11.
DR SUPFAM; SSF81901; HCP-like; 4.
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}.
FT DOMAIN 37..293
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 312..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..327
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 64
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 902 AA; 103698 MW; FA3ECBCFEE8F1909 CRC64;
MSKEMKETDL KESNYYIDWL EKSIANEYLN YYEYSEFKNL KPLGSGSYGS VVRVNWKNAL
FALKTFNNDK ITLKEVVNEI ILQKKVDFHE NILRLCGITK IEAEKKYSLV LEYADNGTLK
TYLNEEFNEL VWNDKYQLSF QLASAVAFLH ENDIIHRDLH ADNVLVHQKK IKLADFGLSK
KIAKASSNRS QICGIIPFVD PRSLNDHDYK LNEKSDVYSI GVLMWQISSG IRPFSDLNYD
AGLMLSIVNG KREEIIDNTP IEYSNLYSEC WKDEPDERPY MQEVVLALKS IIFPDQYCVN
NHCNDDPLQE SLDISGNSNM NDNQDINDDS SDVNDDLDIN DFSDIIPNNI GNLQDQASIK
SVRVMRFKSN QSSTSIQTDL SKDSSDSKFD IINYSFIDKL ITFIIKKHDK GYTFDQIQQL
LDQITLQFDQ ITNNLIINWL TKNQDKSAYI WLFGLLYYYG IGIEENDDKS FELFLKAAEN
NYSIAQVYLA KCYNDGYGTE VNKNLAFNWY QKGAENKSIV GQFYLGYCYE FNIGTKNNEN
KFIEWYQKAA DNGNITAKLY LANCYRLGKG IKKNESKAFE YYKILAEKKS QMLNINLEIV
IIMELEQKLI KIKLLIVIYF EGLIFVGESN YFGVGMKQNY KKAFYYFQKA AKGGNNFAQY
CLGYCYENGK ELGYCYSFGI GTEINNSKAF DLYKLAAEKG HLYAQYLLGI CYNIGIGTEI
DNSKAFELYK IAAEKSHLDA LYQLGYCYDK GIGTEINKTK AFEIYITAAD KNHLDAQYQL
GRCYNEGIGT GVNKTKAFEI YITAADKNHL DAQYQLGNCY YEGIGTEIDK TKAFKLYEIA
AEKGYLKAQY QLGNCYYEGI GTEIDKTKAF KLYEIVAEKG HIIAQNKLEF LYVSCEAIEK
DL
//
