(data stored in ACNUC7421 zone)

SWISSPROT: Q4WNS1_ASPFU

ID   Q4WNS1_ASPFU            Unreviewed;      1367 AA.
AC   Q4WNS1;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   11-DEC-2019, entry version 92.
DE   SubName: Full=Serine-threonine kinase SepH {ECO:0000313|EMBL:EAL90113.1};
DE            EC=2.7.1.- {ECO:0000313|EMBL:EAL90113.1};
GN   ORFNames=AFUA_4G06750 {ECO:0000313|EMBL:EAL90113.1};
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=330879 {ECO:0000313|EMBL:EAL90113.1, ECO:0000313|Proteomes:UP000002530};
RN   [1] {ECO:0000313|EMBL:EAL90113.1, ECO:0000313|Proteomes:UP000002530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100
RC   {ECO:0000313|Proteomes:UP000002530};
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.,
RA   Fedorova N., Fedorova N., Feldblyum T.V., Fischer R., Fosker N., Fraser A.,
RA   Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B., Haas H., Harris D., Horiuchi H.,
RA   Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K.,
RA   Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafon A., Latge J.P.,
RA   Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y.,
RA   Molina M., Monod M., Mouyna I., Mulligan S., Murphy L., O'Neil S.,
RA   Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
RA   Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H.,
RA   Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M.,
RA   Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D.,
RA   Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G.,
RA   Vazquez de Aldana C.R., Weidman J., White O., Woodward J., Yu J.H.,
RA   Fraser C., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.,
RA   Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
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:EAL90113.1}.
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DR   EMBL; AAHF01000005; EAL90113.1; -; Genomic_DNA.
DR   RefSeq; XP_752151.1; XM_747058.1.
DR   STRING; 746128.CADAFUBP00006208; -.
DR   EnsemblFungi; EAL90113; EAL90113; AFUA_4G06750.
DR   GeneID; 3509307; -.
DR   KEGG; afm:AFUA_4G06750; -.
DR   EuPathDB; FungiDB:Afu4g06750; -.
DR   HOGENOM; HOG000188178; -.
DR   InParanoid; Q4WNS1; -.
DR   OMA; KLLRHPW; -.
DR   OrthoDB; 1290401at2759; -.
DR   Proteomes; UP000002530; Chromosome 4.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0032147; P:activation of protein kinase activity; IBA:GO_Central.
DR   GO; GO:0023014; P:signal transduction by protein phosphorylation; IBA:GO_Central.
DR   Gene3D; 1.25.10.10; -; 2.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF48371; SSF48371; 2.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
DR   PRODOM; Q4WNS1.
DR   SWISS-2DPAGE; Q4WNS1.
KW   Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:EAL90113.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002530};
KW   Transferase {ECO:0000313|EMBL:EAL90113.1}.
FT   DOMAIN          32..323
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          351..401
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          611..632
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          659..696
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1242..1293
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          698..725
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..30
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..47
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        671..686
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1260..1287
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1367 AA;  153004 MW;  D5984484605F428B CRC64;
     MVSRSSEGNE GPHPSSRTPG TPAKTRVSKL GSSPSKRDEK SGEGRVVKSS AKDVAELKDY
     TVAVKQIKLA DLPKSELRVI MLEIDLLKNL DVRLRYNKHS RPTELTEWLQ HPNIVKYHGF
     VKSAETLNII LEYVSSSTDR LSIGGANKRR YCENGSLHSI SKNFGRFPEN LVGLYMSQVL
     HGLLYLHEQG VIHRDIKGAN ILTTKEGLVK LADFGVASRT TGLSESSVVG TPYWMAPEVI
     ELSGATTASD IWSLGCTVIE LLEGKPPYYN LQPMPALFRI VNDDHPPLPQ GASPAVKDFL
     MQCFQKDPNL RVSARKLLKH PWIVNARRSD SVVPKKSTEY EEAVRSVQEW NEALRSPGAG
     TLRKPFRHDR QSPSPLRRNQ LPSRNTPTKD ALPAPVVSNA KDQSLLSNAT AEDNWDDDFA
     TAISPSALQL PHLRPHDNFG GMLSSEKLKA FASLDGTVIK SENSFGDFND SFRTTLHCGE
     SDPLQTIRPF PFKQTGTDDG FAQKSPLQME PKRSTPFVHN VPILTQNPVP PSRQARPASF
     YKENSVEDYS DIIITDEDVL GRKLNGVKVR MEANIYPNVD DCLSDLFQET DEERYISNSA
     DLPPSKEIVR YHTPSRDDEQ EPHLRRQLST KRHRSAVEIH RFAENERDED FSDILGPEEV
     ALDKPDSDGS SDRSTLMLNS RHSNNSWLGD QDDEDDPFAQ LEEGLDEMDL EANIARDKYA
     RLRGQVEGLV SSLKTSQDED VLEDISEQLL TIFCDLPETK NIIMSAHGML PILEILDTCR
     RRNVVSCLLK IVNAIIYEDY EIQENLCFVG GIPIINEFAS KKYPREIRLE AAAFVQQMYQ
     TSTLTLQMFV SAGGLNVLVE FLEDDYEDER DLVLIGVNGI WSVFELQGST PKNDFCRILS
     RSSVLDPLSL VLSRVLDEGG ELAEIVEGRI ASIFFVFSQA ENHVKEMVAE RTVLHRVLKE
     LKRMTPAHQI TMLKFIKNLS MLSTTLDSLQ NSNAIDVLTD LLRSTIKRPH FREVSNQILN
     TIYNMCRLNK SRQEDAALNG IVPLLQKIVK TERPLKEFAL PILCDMAHSG KVGRRELWRN
     RGLPFYISLL SDPYWQVTAL DAIFTWLQEE TAKVEEHLLS YHPDQPSFTE SIIRCLTVSK
     ANAFENLLEP LQKLLRLSPP IALTFAREDM FVRIRQKLHH NKAAVRLNLL RIISSICEAS
     EDHGGLLAEY GLLEAIRELE HDPAILVRDM AGKLIQANER SESYGLGKRR PGVRRGSTAT
     TPPGLLTNQS APSTPSVPRT NQSKSYFDGR EVQRHPRNAL SGSALALRPA SRDGASPALA
     VGGSKGSNAS SASRNRLPRV ILLALVELLN NTKMVFLSFG VCISGYP
//

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