GenomeNet

Database: UniProt
Entry: F0UTG2_AJEC8
LinkDB: F0UTG2_AJEC8
Original site: F0UTG2_AJEC8 
ID   F0UTG2_AJEC8            Unreviewed;      1157 AA.
AC   F0UTG2;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   Name=IRE1 {ECO:0000313|EMBL:QSS54782.1};
GN   ORFNames=HCEG_08404 {ECO:0000313|EMBL:EGC49189.1}, I7I53_02444
GN   {ECO:0000313|EMBL:QSS54782.1};
OS   Ajellomyces capsulatus (strain H88) (Darling's disease fungus) (Histoplasma
OS   capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX   NCBI_TaxID=544711 {ECO:0000313|Proteomes:UP000008142};
RN   [1] {ECO:0000313|EMBL:EGC49189.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H88 {ECO:0000313|EMBL:EGC49189.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Champion M., Cuomo C., Ma L.-J., Henn M.R., Sil A., Goldman B., Young S.K.,
RA   Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A., Borenstein D.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B.,
RA   Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C., Klein B.,
RA   McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA   San-Blas G., Taylor J., Mendoza L., Galagan J., Nusbaum C., Birren B.;
RT   "Annotation of Ajellomyces capsulatus strain H88.";
RL   Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000008142}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H88 {ECO:0000313|Proteomes:UP000008142};
RA   Champion M., Cuomo C., Ma L.-J., Henn M.R., Sil A., Goldman B., Young S.K.,
RA   Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A., Borenstein D.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B.,
RA   Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C., Klein B.,
RA   McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA   San-Blas G., Taylor J., Mendoza L., Galagan J., Nusbaum C., Birren B.;
RT   "Annotation of Ajellomyces capsulatus strain H88.";
RL   Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:QSS54782.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=H88 {ECO:0000313|EMBL:QSS54782.1};
RA   Voorhies M., Cohen S., Shea T.P., Petrus S., Munoz J.F., Poplawski S.,
RA   Goldman W.E., Michael T., Cuomo C.A., Sil A., Beyhan S.;
RT   "Chromosome-level genome assembly of a human fungal pathogen reveals
RT   clustering of transcriptionally co-regulated genes.";
RL   Submitted (JAN-2021) 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   ---------------------------------------------------------------------------
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; DS990642; EGC49189.1; -; Genomic_DNA.
DR   EMBL; CP069104; QSS54782.1; -; Genomic_DNA.
DR   AlphaFoldDB; F0UTG2; -.
DR   STRING; 544711.F0UTG2; -.
DR   VEuPathDB; FungiDB:I7I53_02444; -.
DR   HOGENOM; CLU_004875_2_0_1; -.
DR   OMA; QCYEKDY; -.
DR   Proteomes; UP000008142; Unassembled WGS sequence.
DR   Proteomes; UP000663419; Chromosome 3.
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-KW.
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; cd09769; Luminal_IRE1; 1.
DR   CDD; cd10422; RNase_Ire1; 1.
DR   CDD; cd13982; STKc_IRE1; 1.
DR   Gene3D; 1.20.1440.180; KEN domain; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 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   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
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; 3.
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:EGC49189.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00022989};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008142};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW   ECO:0000313|EMBL:EGC49189.1}; Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..1157
FT                   /note="non-specific serine/threonine protein kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5033972519"
FT   DOMAIN          721..1018
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          1021..1155
FT                   /note="KEN"
FT                   /evidence="ECO:0000259|PROSITE:PS51392"
FT   REGION          361..384
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          455..493
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          553..700
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          906..929
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        362..377
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        455..471
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        553..571
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        578..592
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        597..643
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        644..662
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        663..695
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1157 AA;  128519 MW;  306F3F220CF7F4EF CRC64;
     MVWRLLPGAR SALPTGIALL LLPLWAAQQQ QPLAHNVEPL QAYIGNNAPL QSHTQAHSLA
     NTNDASAIET VALAAPNPAV RAPPARLNSN AGPGPQLQAR SLQDWEVEDF VLLATVDGTI
     HARDRKTGAP RWALEVPSSP MVETIYHQSN RSGFADAQPE DDFIWIVEPS RDGDLYIYNQ
     APNGGLQKLG LTVKALVDET PYSGTDPPVT YTARKETTLY TVDARTGTIL RVFSSRGSAA
     ATEQSCRRVN DLEALDDEEC ETKNGTLTLG RLEYIVTVQN TETGNLICTI KYSEWGPNNR
     DVDLQSQYFR TMDERHIYSM HDGVIFGFDH SKVDGRRYTQ RFTSPVARVF DVARPARTDS
     PDTSLVLLSQ PRNPPDDSFG VNTPEDRESR VFVNCTENGG WYAMSEASYP LVTGRARQAE
     CYEKDYLMNE KPLMSHSLAQ QRAALAGVHS LNEPSGKYQR TIPSISGPPA DLSNDTPRDV
     ARVSPKSPPQ PTIRPGVLIQ KGWDNVVDVV VTLCLLTFGT FLYLNSHTLQ ELAKQKLDLK
     NVISINGKPL STTPSTPIIA STPTLPSEFG TDGVPSSLGP GVTVNITVPT LDQDGDVTPR
     LKSRNSSEDI ESTPRARIQD PDNNDDKNDD VEELNLLQTP EKTKKKARRG RRGGVAHKRG
     KKNQNQKQSE DADGKISTET PSDNDHTEIA RRPGLERQLS RTISTEMVEI DGSIRIGQLK
     VHTDKVLGHG SHGTVVYKGS FDGRDVAVKR MLVEFYDIAS HEVGLLQESD DHKNVIRYFC
     REQTAGFLYI GLELCPASLQ DVVEKPLDYP SLVNGGLDVP DVLWQITAGV RYLHSLKIVH
     RDLKPQNILV AAPKPRTGSS SLRLLISDFG LCKKLEDNQS SFRATTAHAA GTSGWRAPEL
     LVDDDQTAPS GSTWDNQSVD SSDPAVVDPQ TNRRATRAID IFSLGCVFYY VLTRGGHPFD
     KDGKFMREAN IVKGYHNLDD LQKLGDYAFE ADDLIRQMLS LDPRRRPDAT TIMLHPFFWS
     PADRLNFLCD VSDHFEFEPR DPPSADLLCL ESVAPDVIGL EMDFLKLLPK DFKDSLGKQR
     KYTGSKMLDL LRALRNKRNH YNDMPEHLKA NIGGLPVGYL QFWALRFPSL LINCHWVILQ
     LGLTKVERFK RYFTPPA
//
DBGET integrated database retrieval system