GenomeNet

Database: UniProt
Entry: A0A180GIF6_PUCT1
LinkDB: A0A180GIF6_PUCT1
Original site: A0A180GIF6_PUCT1 
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}.
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; 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
//
DBGET integrated database retrieval system