ID A0A015N574_RHIIW Unreviewed; 3013 AA.
AC A0A015N574;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=RirG_052520 {ECO:0000313|EMBL:EXX74283.1};
OS Rhizophagus irregularis (strain DAOM 197198w) (Glomus intraradices).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX NCBI_TaxID=1432141 {ECO:0000313|EMBL:EXX74283.1, ECO:0000313|Proteomes:UP000022910};
RN [1] {ECO:0000313|EMBL:EXX74283.1, ECO:0000313|Proteomes:UP000022910}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAOM197198w {ECO:0000313|Proteomes:UP000022910};
RA Lin K., Geurts R., Zhang Z., Limpens E., Saunders D.G., Mu D., Pang E.,
RA Cao H., Cha H., Lin T., Zhou Q., Shang Y., Li Y., Ivanov S., Sharma T.,
RA Velzen R.V., Ruijter N.D., Aanen D.K., Win J., Kamoun S., Bisseling T.,
RA Huang S.;
RT "Single nucleus genome sequencing reveals high similarity among nuclei of
RT an endomycorrhizal fungus.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001433};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
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:EXX74283.1}.
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; JEMT01013034; EXX74283.1; -; Genomic_DNA.
DR STRING; 1432141.A0A015N574; -.
DR HOGENOM; CLU_000466_0_0_1; -.
DR Proteomes; UP000022910; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd05170; PIKKc_SMG1; 1.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR InterPro; IPR003152; FATC_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR InterPro; IPR018936; PI3/4_kinase_CS.
DR InterPro; IPR031559; SMG1.
DR InterPro; IPR039414; SMG1_PIKKc.
DR PANTHER; PTHR11139; ATAXIA TELANGIECTASIA MUTATED ATM -RELATED; 1.
DR PANTHER; PTHR11139:SF71; SERINE_THREONINE-PROTEIN KINASE SMG1; 1.
DR Pfam; PF02260; FATC; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF15785; SMG1; 1.
DR SMART; SM01343; FATC; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SMART; SM01345; Rapamycin_bind; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51190; FATC; 1.
DR PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nonsense-mediated mRNA decay {ECO:0000256|ARBA:ARBA00023161};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000022910};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1569..1905
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2981..3013
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
FT REGION 1925..1947
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3013 AA; 346058 MW; 8F09D7C09F0CE934 CRC64;
MSRKPFFVQH QIQSAKFWLL QIHNGFHMDL SIQSVDEWFD GFLQTLAQWI PSIHPEVIYI
LINPDSALMK LRWNSYSARM SSDLLDMLHI VLQNQASFIP RSETDEMTLI HNITSEIGRM
MSILFHSDTS SRIPSQLHWS DILNRNEFKH DQTLVQFIES LRSLLNSNDS SLKDCSINIR
TATSILIFDI EILTDLAYSW HHNREIFWVF YVMSNKIGES GHFDVLVMCT LLKALRRTCR
SKNYFMTKIE IGSPLPSAFC AMVTILTAFL RFPNEISLST LALALDWFKE FLEFCGGYQF
HSKEIKENVR REIENIIISL VITARVVKSN DIRLQIPKII RGYFDVFGSL KLHKNAMIKI
AHRLFDSDIN IQSEFSRLID YLNPLYGTFR IDPLVDQFIV NFKTNVSATP HLGNFRPPHF
QIVMSHLGMK DLLSSQDEPD IINDDVYYKG QWRLRLFHSC QSVEGFDKGN PIEEEDDIKF
VYSESDIAGA IANSNDLLTF WSLWEVARYC VLSRLRTPFG GPKQTFDAFE KRLNDLLIQD
ATIVYKLDDT SIHDSLHNLN QLRDLLVLID RLELQIYNAA VGTALGQLPQ APRASIVFFK
TNRKVCDDWF SRIRSSIVKG SKIVGHDTLA IRHCLLSLAE RVNLLKQGVI KSRMTWIMEF
QQMLMDAVQC LQRINAVDSI IGLLIWSKRI CVSNEKSEPS LLGQPDDMQT GNKTNIAVLP
QSPTQRTLLQ RKPTNKTIPN SAHFYWMNSS HLFAEAKYES AAKESKEALN SLLKLDPEML
VISPQVQFLT SQIIDSYCKT NDLSSLAEWL NVFDLNGNIT DPLAQLNQHY LESLTKHYVG
EHFSAWELIE SKPPQISEHH INLRAANFIY SLCSFRGMLA RTLNVEASEP NHHFVYAILK
AASRYSFESS LINTIPLLAK ASIANSDVES IQTFLNEFVD YTKEYQHISF TDTFVSDLEI
WSALNSSIDQ LTLRNETSQS KQLQEKVDVF KLMMAKIARK SSAFQIANSL LDHWKQDSPP
EVVMEQAKTM YAQGQSQEAI IRACSVFGDN KNISAAFYDL QGFGQRIYLK IAKWLQNSEN
VISNETLSEI HFLLNATITK ETNETEPINY VESRSIVESC LSRAVEGDSS YDKAWFSYAT
YHYQRGRQIL EEIGSNKTTI NLITVPRNKI QELVTNDWKD SNHDNLVEFD VLFKGLFQLF
LRKFESRSKF ENDELEFKEI IPWISEKSTE EIIKIFHNLQ EEIFTSYKCA VEGYFKYLQL
AYGKKNERMN KFENVCNKPV EESDITTAAL RLFRLLVKYG TCLESQFTRG FDNIDYRAWE
KIIPQLFSRL DHPEPFVQQQ LCKLLCAIAI NSPQLVVYHT VVASNSSGAS EQNNQLLKKI
ADSLDYSNGA LIAEIRKVIK ELQHITVLWE EQWLNKISGL QLDINRRLHK VENEFERIND
NLNLTSDQRS KITKESYDAI MKPVISSFER LYNITIATAS TPHEQWFNQT FGSRIRNALE
KLRTPTSWNT YKEGWDLFRS VHKDLTKELH TSRTLKLSDV SPFLSKIKSS QITMPGLTTH
NETVFIQSFN DNVVILPTKT KPKKLVLLGS DGKQYGYLFK GLEDLHLDER IMQLLRITND
LFNRDKQSRS RKLRARHYAV IPLGDHSGMI QWVENATCMF VLYKKWQHRE HFAKLLQTNN
NAEIAGNPLR PSDMFFEKIG KALKKEGWAT SSSRRNWPKS VLKSVFLELI SETPSDLLEK
EVWSSCSSPS EWWDKNISLS RSLAVMSIIG YIIGLGDRHL DNILIDFNQG EVIHIDYNVC
FEKGKKLRVP ETIPFRLTQN LETALGITGV EGVFRIACEH ALRVMRENKE MLITLLEAFV
YDPLVDWNQD LSENKDKQIM ELEENIVLLT SRIAELRVPL ENNQKQLSSI VSDFLKSYEN
LRNNHNENDQ SIETPTNDPQ RSQSIQADRS LSNIEIIRQG VVKNVNNNQL EFESLKSTLS
KRASECALWH AQHEKAIQSV QGPLLQVMYN EAFASSSQIG SPLFGNFTQI ISTNDHLLQR
CSNINQEFFG WMNERNNAFK NCLERLQFYR ALILPIIQVL LSQDYYGKWP LLLGEFLDSG
FEKKDFQKIF ENVNLENPHH QFGNDGNDFK QNWETLQISC SNILQESLTI TEALVISSEN
GRLSDSTLHI MLNNLISEQN LKGQKFGRIL SLACTVNSLI ELKEKLVNPN GTMDEVFGFM
GFDDNFQQAV RNVLSNQVLD KSGFLTFIGT IFFIYHHIHF ATVTNPNDET LTHILSTTTE
LLQLTRFIYS LFNNFENIIL PKVFQMLCNS PNSLEPYNGI LCDLSNDTFN YWEMKNTEAH
SVVFSMNQSF KQICDMIYNE GSGNQAINGG ISIIINGFDE LFSELQNSIM KIQNLFKESL
GLQNVGEYLI SESVLDDFTV HKLNVISNVL LACEDFCKEN YQPNQNNAWI SSIAMTESFK
NSSDSLQRLY QVVYWCISDF FIPSIKHLLD ISINQLGNLF GAGIDANETD NTGAITTFSV
ENLINSGYFA NEEFQSQMQK VTQYCYLGSK INIVAMINMK KTEIEMELQQ RQMELMRFEW
INETLVGDES LIRKQFLENL KQDVNRFVRL DTLLQELVTQ YRAIEVDVAE LITKQFAGSD
VVILQSFNES ITNQQILFAQ EFERMQHIVS LCNSILHLES FRTVTEKTTA MDVDTLQLVK
RLEGIVYGEQ STTNSELDII QQLSALELDQ SMDKGISRKL EIIAKEFHNT FEEIRSLMLD
LILLIEPITN VEVDIDDNGK DIRSRAKEFM REWSKLDTEA DTIINNVLTV FDGNQKGRNN
AVADSENETI LENINRESIR AISDISDSLS RIFELLFTLC EASTSDQKNS RQQSPAGTNL
ENEEILAPPE IKHDQDNTSN GVEYTEQNEV YNNLISPQKD DQELSLKDNN NTVRRGSFVM
ADEGIQVTGN VGIAQARNSF AVSLIRRIKS KLEGKDFDLN TKMSVSEQVD KIIQQATDID
NLSVMYEGWT AWI
//