ID M7BWV7_CHEMY Unreviewed; 1052 AA.
AC M7BWV7;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Mitotic checkpoint serine/threonine-protein kinase BUB1 {ECO:0000313|EMBL:EMP36563.1};
DE Flags: Fragment;
GN ORFNames=UY3_06252 {ECO:0000313|EMBL:EMP36563.1};
OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP36563.1, ECO:0000313|Proteomes:UP000031443};
RN [1] {ECO:0000313|Proteomes:UP000031443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
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DR EMBL; KB524693; EMP36563.1; -; Genomic_DNA.
DR AlphaFoldDB; M7BWV7; -.
DR STRING; 8469.M7BWV7; -.
DR Proteomes; UP000031443; Unassembled WGS sequence.
DR GO; GO:0000776; C:kinetochore; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.430; -; 1.
DR Gene3D; 6.10.130.20; -; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR015661; Bub1/Mad3.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR013212; Mad3/Bub1_I.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR14030; MITOTIC CHECKPOINT SERINE/THREONINE-PROTEIN KINASE BUB1; 1.
DR PANTHER; PTHR14030:SF26; MITOTIC CHECKPOINT SERINE_THREONINE-PROTEIN KINASE BUB1; 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}; Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000313|EMBL:EMP36563.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000031443};
KW Transferase {ECO:0000313|EMBL:EMP36563.1}.
FT DOMAIN 3..162
FT /note="BUB1 N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51489"
FT DOMAIN 753..1052
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 356..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 271..301
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 787
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EMP36563.1"
FT NON_TER 1052
FT /evidence="ECO:0000313|EMBL:EMP36563.1"
SQ SEQUENCE 1052 AA; 119065 MW; CB1AD1B98BCECE2C CRC64;
RVFEAQIQRY QGDDPLDPWD RYLQWVEGAF PLQGGQQRYS ASLEQLVKVF ISEERYHQDP
RFVKYCIKLV EFISAPSQFF DYIYSQGVGT RTSALYIAWA QQLETEGNIQ HAGAVLQKGI
HNQAEPMENL QEQYSLYTCL VCKNLWIPAS LGGSDPSSPS SSMSWDLRRC VPLGVSEPLS
LPPQCVLESG GSVHLWREYL TYISKSAVLP KLSSTSNEFE QVAMYNKSML ICEGSELSFE
EVRAKIVYRK QERLRRQKEW EKEERDYAKR KESAILEMQF LQQKLEQLSQ LTKDYPEAKL
EEASMLPSVP DRMVVSMYCD QHQHFFPALQ QDWTAPSQVT NLQTLWSLGP DQLQSRAAAS
TSTADTSVSQ PVEAASHQSV SESLSMVTYE KVTGEAKLDL GELQNTLLQL ELKSRDAVSQ
PIQEHSAFSH GHSVGQHFGN ASQATPNSSL GGVMQATPFK VQPSPTVHTK EALGFLMDMF
QTPILPEMSS LQENEEKFEA YCRKSEPGKS MKANATAPVV SAFSVFEDEN EKENNRFPQQ
KNKLARVRAF GEHPLLRCAE QSKEGTRTTE FLMDDSTVWA LHCNNKTLAP SPNSTRDFAR
ATQLASTPFG YLSAHSWQAM EDKVLEQSPE QGYLSGNAPS AAASLVLNQQ LATEKPVLET
LQAARGYSDE EMVLTACKES VSTPQVPVCA EDRTYQNVKA PVIVENPWDE GLIRKLLSRL
PKPLSTYSNT FEWKSSLPTV KLKTELTLGS KSFHVDCLLG EGAFAHVYQA SVLDTNNPKN
NQKVILKVQK PANPWEFYIA CQLMERLKPS VRHLYIQFYS AHFFQNGSIL VGELYNYGTL
LNTINIYKKL PEKVMPQALV IYFAVKILYM VEELHNCGII HGDIKPDNFI LGERQLLDND
TCDIDSLSHG LTVIDLGQTL TLFPEGTAFT GKCETSGFQC IEMLTQKPWN YQTDYFGIAG
TIYCMLFGTY MRVRNEEGIW KTEGVFRRIP NAELWNELFC SLLNIPDCHH LPSLGALRKK
LRDLFQKSYA KEIKFLRNRL VVLLIENKRS RK
//
