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Database: UniProt
Entry: A0A4D9E053_9SAUR
LinkDB: A0A4D9E053_9SAUR
Original site: A0A4D9E053_9SAUR 
ID   A0A4D9E053_9SAUR        Unreviewed;      1110 AA.
AC   A0A4D9E053;
DT   03-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   03-JUL-2019, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Rhomboid domain-containing protein 3 {ECO:0000313|EMBL:TFK02487.1};
GN   ORFNames=DR999_PMT15164 {ECO:0000313|EMBL:TFK02487.1};
OS   Platysternon megacephalum (big-headed turtle).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC   Testudinoidea; Platysternidae; Platysternon.
OX   NCBI_TaxID=55544 {ECO:0000313|EMBL:TFK02487.1, ECO:0000313|Proteomes:UP000297703};
RN   [1] {ECO:0000313|EMBL:TFK02487.1, ECO:0000313|Proteomes:UP000297703}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DO16091913 {ECO:0000313|EMBL:TFK02487.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:TFK02487.1};
RA   Gong S.;
RT   "Draft genome of the big-headed turtle Platysternon megacephalum.";
RL   Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:TFK02487.1, ECO:0000313|Proteomes:UP000297703}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DO16091913 {ECO:0000313|EMBL:TFK02487.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:TFK02487.1};
RA   Gong S.;
RT   "The genome sequence of big-headed turtle.";
RL   Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
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:TFK02487.1}.
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DR   EMBL; QXTE01000187; TFK02487.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4D9E053; -.
DR   STRING; 55544.A0A4D9E053; -.
DR   Proteomes; UP000297703; 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   CDD; cd14028; STKc_Bub1_vert; 1.
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   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000297703}.
FT   DOMAIN          1..164
FT                   /note="BUB1 N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51489"
FT   DOMAIN          810..1110
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          149..192
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          354..373
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          272..302
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        149..165
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        174..192
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         844
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1110 AA;  123887 MW;  F1FBCD1504F408B2 CRC64;
     MENPPSEVDT LWDARSGKGP AVLQVAAEGA QEIPAMGGKC LPASGRTGTL VRFIRAACES
     VHQSGEAEFI SAPSQFFDYI YSQGVGTRTS ALYIAWAQQL ETEGNIQHAG AVLQKGIHNQ
     AEPMENLQEQ YRLFQSRIPR SHPLTQVAAS KQLHNSQTPN QMAPRKDVSE SGDPACLSKS
     QDPTLSAAQS SQDGAGKVEY LTYISKSAVL PKLSSTSNEF EQVAMYNKSM LICEGSELSF
     EEVRAKIVYR KQERLRRQKE WEEEERNYAK RKESAILEMQ CLQQKLEQLS QLTKDYPEAK
     LEEGSMLQSV PDRMVVDPCV KPSPALQHDW TAPSQMTNLQ TSWCLGPDQL QSRAAASTST
     ADTSVPKPVE AASHQSVSAS LSMVTYEKVT GEAKLDLGEL RNTLSQLELK SGDAVSQPIQ
     EHSTFSHGHS AGQQHSNVST PGLKLDHCTA MKEAPRMGNA SVSFGNASQA TPNTSLGGVM
     QATPFKVQPS PTVHTKEALG FLMDMFQTPI LPEMPSLQEN EEKFEAYCRK SEPGKSMKAN
     DTAPVVSAFS IFEDENEKEN NRFPQQKNKL AQARAFGEHP LLRCAEQSKE GTRTTEFLMD
     DSTVWALQCN NKTLAPSPNS TRDFARATQL ASTPFNYLSA HSWQPMEDKE NAVHNNDGKM
     VLDSSEEQYM EVSKTRKLSP VLEQSPEQGS LPGNAHSAAA SLVLNQQLAT EKAVLETLQA
     ARGYSHEETV LTACKESVST PQILVCTEDR TYQNVKTPVI VENPWDEGLI RTLLSRLPKP
     LSTYSNTFEW KSSLPTIKLK TELTLGPKSF HVDCLLGEGA FAHVYQASVL DTNNPKNNQK
     VILKVQKPAS PWEFYIASQL MERLKPSVRH LYIQFYSAHF FQNGSILVGE LYNYGTLLNT
     INIYKKLPEK VMPQALVIYF AVKILYMVEE LHNCGIIHGD IKPDNFILGE RLLDNDTCDI
     DSLSHGLTVI DLGQSIDLKL FPEGTAFIGK CETSGFQCIE MLTRKPWNYQ TDYFGIAGTI
     YCMLFGTYMR VRNEEGIWKT KGVFRRIPNA ELWNEFFCSL LNIPDCHHLP SLGALRKKLR
     DLFQKSYAKE IKFLRNRLVV LLIENKRSRK
//
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