ID A0A0L6VFR5_9BASI Unreviewed; 1357 AA.
AC A0A0L6VFR5;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=IRE protein kinase {ECO:0000313|EMBL:KNZ59631.1};
GN ORFNames=VP01_1690g2 {ECO:0000313|EMBL:KNZ59631.1};
OS Puccinia sorghi.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=27349 {ECO:0000313|EMBL:KNZ59631.1, ECO:0000313|Proteomes:UP000037035};
RN [1] {ECO:0000313|EMBL:KNZ59631.1, ECO:0000313|Proteomes:UP000037035}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RO10H11247 {ECO:0000313|EMBL:KNZ59631.1,
RC ECO:0000313|Proteomes:UP000037035};
RA Rochi L., Burguener G., Darino M., Turjanski A., Kreff E., Dieguez M.J.,
RA Sacco F.;
RT "Next Generation Sequencing and Analysis of the Genome of Puccinia sorghi L
RT Schw, the Causal Agent of Maize Common Rust.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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:KNZ59631.1}.
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DR EMBL; LAVV01006493; KNZ59631.1; -; Genomic_DNA.
DR STRING; 27349.A0A0L6VFR5; -.
DR VEuPathDB; FungiDB:VP01_1690g2; -.
DR OrthoDB; 1630at2759; -.
DR Proteomes; UP000037035; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004521; F:RNA endonuclease activity; IEA:InterPro.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IEA:InterPro.
DR GO; GO:0006397; P:mRNA processing; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd10422; RNase_Ire1; 1.
DR Gene3D; 1.20.1440.180; KEN domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR045133; IRE1/2-like.
DR InterPro; IPR010513; KEN_dom.
DR InterPro; IPR038357; KEN_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR018391; PQQ_beta_propeller_repeat.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR13954; IRE1-RELATED; 1.
DR PANTHER; PTHR13954:SF6; NON-SPECIFIC SERINE_THREONINE PROTEIN KINASE; 1.
DR Pfam; PF00069; Pkinase; 2.
DR Pfam; PF06479; Ribonuc_2-5A; 1.
DR SMART; SM00564; PQQ; 2.
DR SMART; SM00580; PUG; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
DR PROSITE; PS51392; KEN; 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};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KNZ59631.1};
KW Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000037035};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 869..1195
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1198..1354
FT /note="KEN"
FT /evidence="ECO:0000259|PROSITE:PS51392"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 181..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 350..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 506..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 652..798
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1089..1108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..99
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 533..571
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 652..681
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..721
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 752..767
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1357 AA; 150828 MW; 18C624BD0400AE9B CRC64;
MNYGFALLTT PNPRNSKMHS LPSTSTSTIS NPSSKQSTSS TDQSFQLSPI LLVSTLDGQL
HALDRQTGTW NWTLNDPHLT PNTLLHRTGL VNSPSPSSDH THPDQDHHEL YAIEPHNDGD
LYVFIKSSNQ PSRLEKLPLS VSQLVNLSPF TFPGDSSKMF IGKKESHLIA IDLTTGSVVN
SLHSHPKQTS LKGKEKTSSG NQCHPQHSFH SSESQVPQLT CPLEPPTTNP SFDHLENPGS
VNQSPRDLLY IGRTDYQVSI YSKPHTLIQS LSYSTYTPSN LPHSLQTMWT RTPDDLYLEP
THDGNLVCFQ APSTSNSTTP PIRSEHTKIK WQNSFDHPVT SIFDVVFPNV PNETPPSSSS
STDQSYPPLG SNNTPSDYSA SKATNLQQPI IFVQPKFLPH KDDQSHPKFS PDDDQFNLFK
HLHSQNSFST PFQPSHPSGQ QSAFVGKYQD SFYVMSQQIY PLVVFAPSAY QTVGHVPSIG
THRLLNSQAL NGFLDFSYSN RLLDPATRQN HHTSGHSPLA LDPAPKPLTL PPSQKDVESN
KPSDTAVPST HNKNVITGSE KLTSESSPVQ LHQRAAKISS LLVRTFKQQM LPSEGKSLPS
NGRSEDRFPD LNPLLTLFLV LVIMSWWASR KVGSPSTARW DHLHRIVNQA LGSHDDSSKM
KQAPNLKSLG TTDSQDVTAI AEVPTTIPIK EPECPTGVDG SSDTAGLDAA KDDDSLLPAS
KQKPKRRRGK RPGQKAAAAA ARAEAEAAKD FVSSTPSDSS LPQPGSMEIT SLPPRAPLEP
KTPQKSKPNV KKSKLPTSVN GVDVIQPLNH STRITAPVEH SNLTETAPNP AAIPLKVNGE
NVEQPINSPT GFSMNGYGGL EPQKVGSLIV TNETIGYGSH GTVVLKGTFQ GRQVAVKRLL
KDFVTLARHE VSLLQESDDH PNVVRYFVKE SLDSFLYIAL ELCHATLFDL VEKRQFKEYE
ELDRIFNAKK ALKQITSGLR YLHKLKIVHR DIKPQNILIS LTKSLPISSK ATKTNKAAAG
KSFRMLISDF GLCKKLELDE SSFAQTANHA AGSFGYRAPE ILKGQVNLSE QSNSTASSSI
MNSTVQNVIP GTAHGGESNG SSSISNPEAS HHRLTRSIDI FSLGCIYYYV LTKGDHPFGS
RYEREMNILK DEVCLEQLDG LDEEAFEAQQ LIRSMIRSNP KERPTAEEVL QNPYFWEPTK
RLNFLCDCSD RFEIMERDPP EESLLRLEDQ EQFFRFVNHH RLPTKSLHHH PHIHDHDHNR
LDWYKVIDRA LVDNLGKYRK YDGGSIRDLL RVMRNKKHHF QDLPDGIKKA LGDIPEGFLN
YFSRKFPSLL VHVYSVILDS NLKSENLFAT YFQVDDI
//
