(data stored in ACNUC16935 zone)

SWISSPROT: C8VMZ9_EMENI

ID   C8VMZ9_EMENI            Unreviewed;      1133 AA.
AC   C8VMZ9;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   05-JUL-2017, entry version 53.
DE   RecName: Full=Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU361162};
DE            EC=2.7.11.21 {ECO:0000256|RuleBase:RU361162};
GN   Name=plkA {ECO:0000313|EMBL:CBF85111.1};
GN   ORFNames=ANIA_01560 {ECO:0000313|EMBL:CBF85111.1};
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL
OS   194 / M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=227321 {ECO:0000313|EMBL:CBF85111.1, ECO:0000313|Proteomes:UP000000560};
RN   [1] {ECO:0000313|Proteomes:UP000000560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC   {ECO:0000313|Proteomes:UP000000560};
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.J., Wortman J.R.,
RA   Batzoglou S., Lee S.I., Basturkmen M., Spevak C.C., Clutterbuck J.,
RA   Kapitonov V., Jurka J., Scazzocchio C., Farman M., Butler J.,
RA   Purcell S., Harris S., Braus G.H., Draht O., Busch S., D'Enfert C.,
RA   Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S.,
RA   Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U.,
RA   Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T.,
RA   Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W.,
RA   Caddick M., Hynes M., Paoletti M., Fischer R., Miller B., Dyer P.,
RA   Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2] {ECO:0000313|Proteomes:UP000000560}
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC   {ECO:0000313|Proteomes:UP000000560};
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P.,
RA   von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E.,
RA   Fekete E., Flipphi M., Estrada C.G., Geysens S., Goldman G.,
RA   de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K.,
RA   Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S.,
RA   Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E.,
RA   Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A.,
RA   Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P.,
RA   Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R.,
RA   Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I.,
RA   Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B.,
RA   van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N.,
RA   Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J.,
RA   de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W.,
RA   Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a
RT   community effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC       {ECO:0000256|RuleBase:RU361162}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
CC       protein kinase family. CDC5/Polo subfamily.
CC       {ECO:0000256|RuleBase:RU361162}.
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DR   EMBL; BN001307; CBF85111.1; -; Genomic_DNA.
DR   ProteinModelPortal; C8VMZ9; -.
DR   STRING; 162425.CADANIAP00008189; -.
DR   EnsemblFungi; CADANIAT00008189; CADANIAP00008189; CADANIAG00008189.
DR   HOGENOM; HOG000158494; -.
DR   InParanoid; C8VMZ9; -.
DR   OMA; KMGNIFL; -.
DR   OrthoDB; EOG092C0QJU; -.
DR   Proteomes; UP000000560; Chromosome VII.
DR   GO; GO:0005634; C:nucleus; IDA:AspGD.
DR   GO; GO:0005816; C:spindle pole body; IDA:AspGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004672; F:protein kinase activity; ISS:AspGD.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0043936; P:asexual sporulation resulting in formation of a cellular spore; IMP:AspGD.
DR   GO; GO:0007059; P:chromosome segregation; IMP:AspGD.
DR   GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IMP:AspGD.
DR   GO; GO:0030448; P:hyphal growth; IMP:AspGD.
DR   GO; GO:0000022; P:mitotic spindle elongation; IMP:AspGD.
DR   GO; GO:0006468; P:protein phosphorylation; ISS:AspGD.
DR   CDD; cd13118; POLO_box_1; 1.
DR   CDD; cd13117; POLO_box_2; 1.
DR   Gene3D; 3.30.1120.30; -; 2.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR033701; POLO_box_1.
DR   InterPro; IPR033695; POLO_box_2.
DR   InterPro; IPR000959; POLO_box_dom.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 2.
DR   PROSITE; PS50078; POLO_BOX; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
DR   PRODOM; C8VMZ9.
DR   SWISS-2DPAGE; C8VMZ9.
KW   ATP-binding {ECO:0000256|RuleBase:RU361162};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000560};
KW   Kinase {ECO:0000256|RuleBase:RU361162, ECO:0000313|EMBL:CBF85111.1};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU361162};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000560};
KW   Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU361162};
KW   Transferase {ECO:0000256|RuleBase:RU361162}.
FT   DOMAIN       66    327       Protein kinase. {ECO:0000259|PROSITE:
FT                                PS50011}.
FT   DOMAIN      945    964       POLO box. {ECO:0000259|PROSITE:PS50078}.
SQ   SEQUENCE   1133 AA;  124772 MW;  948E5E9B41024B13 CRC64;
     MERHLQPTME ALSPRSTNQM IKPKASMERK VLDKNAAAAQ KASSAKNHAP PPPALVVEPG
     DDGEQYSTGA FLGKGGFAIC YEGTLLRNGR VFAMKVVKSD MGQKKMQEKF RTELQIHSKM
     RHPHIVGFHR AFVYDQCIYV ILELCPNGSV MDMVRKRKCL SLPEVRRFMV QLCGAVKYLH
     KRNVAHRDLK MGNLFLDRNM DIKVGDFGLA AMIMSEKDEK RRKTLCGTPN YIAPEVLDRS
     KGGHTQKVDI WSLGVICFAM LTGYPPFQSK TQEEIYKKVR NLTYVWPKDS ECANHIPDEA
     KSLVSCCLNL DEQKRPEPDD IVEHAFFNMY NGCIPKRLDP KCSVQKPTWL RGAEPQGDAM
     AFGHGLDFDE KFSSYIRDVD DPILRYRTCK AAFYSSCGVG RKPDGTARKS VGHNASKSGF
     AECLAEEEKG LQPLMPLPED MVYKYPHDLI GDWSVPESLP LRRQDALADT SVLSSRSSST
     SLRTNTVSQS RTQAALAAAQ QRRNGSQSHA ASLRQQALTG RGTIRKIPSL CDPPQPTMKA
     MPDVRDAGLN PDPVPPVPTG GLAERPIRTR RGIAASYSGT TSVRGMDTNA VPSVSQASND
     LGMLTVGKTR SQSRKLEAAN QVAVEPLRVL KDRSTSTGPE NLAAVSRQKS ARTVHKDLGG
     VAARKPDSEA ARREEPVTRQ RTEAQPQPMS SSGSKASLSS TNKPRSSLGL HALLHSDDPC
     ELLPGSSIDD VKIDLRNMLS NLVPGSAARR RVVSQRPPHA YVIKWVDYTN RYGIGYVLDD
     GSVGCVFKAE NGQPASGVVL RDGEKHIRRK ARSQENSDSQ SWSYSEADQL VPRHGKPVEF
     YENCSDDLLE CRGGICRALI PPSLFEVKDS SGGVKVRMDS GISRARADAE KIKRVKLVDQ
     FGKYMIGSLG RHGDETLLDD AATDGAPGQF IKFYQRLGNV GVWGFGDGAF QFNFPDHTKL
     VLAPGRTRNS SPWMDFYHLS PTAARYLAAK GKMHPSGFDT RAVVSDEIAT FLSIAYGTST
     SAMDDKIREV LDANSFLQKI AFIKDVLKSW IRQGRLGGRP SSDKPGTEMF WEGSQERPQA
     SGGGSSKFVW VTVGAPGGDG EYRSVSLRDK KGNSVGENDE MEALRERLRL AGL
//

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