ID A0A180GIF6_PUCT1 Unreviewed; 694 AA.
AC A0A180GIF6;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=CAMK/CAMKL/AMPK protein kinase {ECO:0000313|EMBL:OAV92354.1};
GN ORFNames=PTTG_02247 {ECO:0000313|EMBL:OAV92354.1};
OS Puccinia triticina (isolate 1-1 / race 1 (BBBD)) (Brown leaf rust fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=630390 {ECO:0000313|EMBL:OAV92354.1};
RN [1] {ECO:0000313|EMBL:OAV92354.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1-1 BBBD Race 1 {ECO:0000313|EMBL:OAV92354.1};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J.,
RA Yandava C., Izard J., Baranova O.V., Blanton J.M., Tanner A.C.,
RA Dewhirst F.E., Haas B., Nusbaum C., Birren B.;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OAV92354.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1-1 BBBD Race 1 {ECO:0000313|EMBL:OAV92354.1};
RA Cuomo C.A., Bakkeren G., Szabo L., Khalil H., Joly D., Goldberg J.,
RA Young S., Zeng Q., Fellers J.;
RT "Comparative analysis highlights variable genome content of wheat rusts and
RT divergence of the mating loci.";
RL Submitted (MAY-2016) 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:OAV92354.1}.
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DR EMBL; ADAS02000065; OAV92354.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A180GIF6; -.
DR SMR; A0A180GIF6; -.
DR STRING; 630390.A0A180GIF6; -.
DR VEuPathDB; FungiDB:PTTG_02247; -.
DR OrthoDB; 1700376at2759; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd12122; AMPKA_C; 1.
DR CDD; cd14079; STKc_AMPK_alpha; 1.
DR Gene3D; 3.30.310.80; Kinase associated domain 1, KA1; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR032270; AMPK_C.
DR InterPro; IPR028375; KA1/Ssp2_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24346; MAP/MICROTUBULE AFFINITY-REGULATING KINASE; 1.
DR PANTHER; PTHR24346:SF82; SERINE_THREONINE-PROTEIN KINASE MARK-A-RELATED; 1.
DR Pfam; PF16579; AdenylateSensor; 2.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF103243; KA1-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:OAV92354.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Transferase {ECO:0000313|EMBL:OAV92354.1}.
FT DOMAIN 35..286
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 309..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 404..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 566..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..440
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..497
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 694 AA; 78220 MW; 049A01E7D48623A0 CRC64;
MPPSTTATRS PSSRKRHESL STQRESAATK SIGEFEIVKT LGHGSFGKVK LAKHKLTRLN
VAMKFLSKKK ILTQEMRDRV KREIEYLSFL RHPHIIKLYD VIQDNTDIVM VIEYLKGELF
DYIVHVGKMP EHDARRFFQQ IICAVEYCHL HNIVHRDLKP ENLLLDHNLN VKIADFGLSN
IMRDGDFLKT SCGSPNYAAP EVISGKLYAG PEIDIWSCGV ILFVMLCGRL PFDDDHIPML
FKKINSGLYS LPPHLSSGSR HLLSRMLVVD VNKRITIPEI RELDWFKQDL PEYLKQTARP
IIVNLDESRK SSISDTPDPS HQAQHEPEDT SPIDSNEIRA PGLGILDPRV INDLCNLIGD
RITADDIYNA LMNDLDKNIK ISYQLARDYR RMKEGTAYMD DVAHSNEAPL GRSNSLRSRG
LSTSLNAPQS QSSTTGECPL NASLDLPEDT GPSHIRILPH TLPPTAVSGQ GDGLSRLKQS
LMNTQSSPLN NLNKPFTPAE PSKRPTDRVA ESSHRTLTGS GRVKKAPKTK WHFGIRSKSP
PMTVMLEIYR TLQTLGFEFK RKDLHSSALE EPPEEAPAES EGEKRRRRRK AEEEKVKQAQ
DLYFIETRCR LDNVVVRMDL QLYQIEVNNY LVDFRNLGYK PIEPSAQTAT TREEAAANRR
RAASMGGGAT SSPFLFLECA CRLIVELAVG PSES
//