ID A9UZI6_MONBE Unreviewed; 1083 AA.
AC A9UZI6;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 24-JAN-2024, entry version 82.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=MONBRDRAFT_25473 {ECO:0000313|EMBL:EDQ89237.1};
OS Monosiga brevicollis (Choanoflagellate).
OC Eukaryota; Choanoflagellata; Craspedida; Salpingoecidae; Monosiga.
OX NCBI_TaxID=81824 {ECO:0000313|EMBL:EDQ89237.1, ECO:0000313|Proteomes:UP000001357};
RN [1] {ECO:0000313|EMBL:EDQ89237.1, ECO:0000313|Proteomes:UP000001357}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MX1 / ATCC 50154 {ECO:0000313|Proteomes:UP000001357};
RX PubMed=18273011; DOI=10.1038/nature06617;
RG JGI Sequencing;
RA King N., Westbrook M.J., Young S.L., Kuo A., Abedin M., Chapman J.,
RA Fairclough S., Hellsten U., Isogai Y., Letunic I., Marr M., Pincus D.,
RA Putnam N., Rokas A., Wright K.J., Zuzow R., Dirks W., Good M.,
RA Goodstein D., Lemons D., Li W., Lyons J.B., Morris A., Nichols S.,
RA Richter D.J., Salamov A., Bork P., Lim W.A., Manning G., Miller W.T.,
RA McGinnis W., Shapiro H., Tjian R., Grigoriev I.V., Rokhsar D.;
RT "The genome of the choanoflagellate Monosiga brevicollis and the origin of
RT metazoans.";
RL Nature 451:783-788(2008).
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DR EMBL; CH991551; EDQ89237.1; -; Genomic_DNA.
DR RefSeq; XP_001745813.1; XM_001745761.1.
DR AlphaFoldDB; A9UZI6; -.
DR STRING; 81824.A9UZI6; -.
DR EnsemblProtists; EDQ89237; EDQ89237; MONBRDRAFT_25473.
DR GeneID; 5891255; -.
DR KEGG; mbr:MONBRDRAFT_25473; -.
DR eggNOG; KOG0596; Eukaryota.
DR InParanoid; A9UZI6; -.
DR Proteomes; UP000001357; Unassembled WGS sequence.
DR GO; GO:0000776; C:kinetochore; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0007059; P:chromosome segregation; IBA:GO_Central.
DR GO; GO:0033316; P:meiotic spindle assembly checkpoint signaling; IBA:GO_Central.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IBA:GO_Central.
DR GO; GO:0006996; P:organelle organization; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0034501; P:protein localization to kinetochore; IBA:GO_Central.
DR CDD; cd14131; PKc_Mps1; 1.
DR Gene3D; 1.25.40.430; -; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR013212; Mad3/Bub1_I.
DR InterPro; IPR027084; Mps1_cat.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR22974:SF21; DUAL SPECIFICITY PROTEIN KINASE TTK; 1.
DR PANTHER; PTHR22974; MIXED LINEAGE PROTEIN KINASE; 1.
DR Pfam; PF08311; Mad3_BUB1_I; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00777; Mad3_BUB1_I; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51489; BUB1_N; 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:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000001357};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 47..227
FT /note="BUB1 N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51489"
FT DOMAIN 567..841
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 207..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 926..958
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..288
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..463
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 595
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1083 AA; 118221 MW; 1297368CDE3CAB29 CRC64;
MESRAATMRA LQATIEATLE SFEVRYSAKN DQAAIPNLRP ARPRAGLGSA LRIKSASQRM
TELQTDGNPL EGWWSFLNLQ LDSLKGPCQH LLRFYKTGIE RIDQERYRDQ ELYVQLWLEY
ARLAMACGDA EEAGFTFQQM QQDSIGRGFR HFHTIWAEFE ESQGHTGRSL EILRKGRTAR
KPSSEIVARE SRFKCLLETP TSCIRCGGRS KRYNNDQSTD PTPMKRPAPT RQATRRQAAS
RAAAFGPPQR VPLSTSIVEE EDDDEDKANA KEQARPHNHS RSSKESEALM NDDLGLPSVD
PVKARLAQAL SANTSAANLS SDSNLPHLTT SSLGSNGSRL SISSVGSADD ATNNGSGSDN
SFSDIQPGRH ARDPERRTGA NRPSGLQHCD APVDRPHSSP RAPLEAPMPA PAPHSAAAGA
PKRQHATLTV RPDVDEDPLP PPLPMASTSK QATAVSSPGK GQAHGPTTAA PGPTGDTVKF
SLKSRVHEVQ ARDELPIATP MGVPRPKSRH QTALPAPSTV EAAPPVARRM ASAAATPSAA
PASMRHQPVS DEFVRNMETV SVAQRPYIKL EQLGKGGSSR VYRVLDAEHA MLALKEVDLR
DVDAATVASF KNEIHLLERL QGEPNIICLV DWEHDEVAKV LRIVMECGDV DLARMLQTQR
AARASSRGAE LPVIDENHIR LYFQQMLEAV GAVHRQQIVH SDLKPANFLC VKGALKLIDF
GIATGIQEDH TSVMRDAQIG TVNYMSPEAI AGTMGDGACL KVGPASDVWS LGCILYLMVY
GKTPFQHMPV LQKLQRIPDA KHAIEFEPLA NRDLLAALQA CLQRNPKKRP TIEQLLAHPF
LHPGTAAGPA LQTPRRDRSH SRLGGAVPYA ELDGESTATV TQAQLMQLLS QVRQLDVQCS
PGRLSRRIFR QLQQGVTMES LNVAATPARP RAGPTGAAPL RTPLGKLDGN SMRPNTGMKR
GKVKLQTASP LVLGAYTTTL GQSGLREQTK TRPIEKDYAL CLHLEPTNRF TYRYPNCRPN
CSNDPTILVC STVPHPTFSS SRALALSTLH TLALALYLSR SLSLSLNNNN KNNENTIMHT
TLY
//
