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Database: UniProt
Entry: A0A3M0J9Y5_HIRRU
LinkDB: A0A3M0J9Y5_HIRRU
Original site: A0A3M0J9Y5_HIRRU 
ID   A0A3M0J9Y5_HIRRU        Unreviewed;      1752 AA.
AC   A0A3M0J9Y5;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   18-JUN-2025, entry version 29.
DE   RecName: Full=Non-specific serine/threonine protein kinase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=DUI87_25465 {ECO:0000313|EMBL:RMB97987.1};
OS   Hirundo rustica rustica.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC   Passeriformes; Sylvioidea; Hirundinidae; Hirundo.
OX   NCBI_TaxID=333673 {ECO:0000313|EMBL:RMB97987.1, ECO:0000313|Proteomes:UP000269221};
RN   [1] {ECO:0000313|EMBL:RMB97987.1, ECO:0000313|Proteomes:UP000269221}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Chelidonia {ECO:0000313|EMBL:RMB97987.1};
RC   TISSUE=Blood {ECO:0000313|EMBL:RMB97987.1};
RA   Formenti G., Chiara M., Poveda L., Francoijs K.-J., Bonisoli-Alquati A.,
RA   Canova L., Gianfranceschi L., Horner D.S., Saino N.;
RT   "A high quality draft genome assembly of the barn swallow (H. rustica
RT   rustica).";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SUBCELLULAR LOCATION: Chromosome, centromere, kinetochore
CC       {ECO:0000256|ARBA:ARBA00004629}.
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:RMB97987.1}.
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DR   EMBL; QRBI01000154; RMB97987.1; -; Genomic_DNA.
DR   STRING; 333673.A0A3M0J9Y5; -.
DR   OrthoDB; 248495at2759; -.
DR   Proteomes; UP000269221; Unassembled WGS sequence.
DR   GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:TreeGrafter.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051754; P:meiotic sister chromatid cohesion, centromeric; IEA:TreeGrafter.
DR   GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IEA:InterPro.
DR   CDD; cd01093; CRIB_PAK_like; 1.
DR   FunFam; 1.25.40.430:FF:000002; mitotic checkpoint serine/threonine-protein kinase BUB1 beta; 1.
DR   FunFam; 1.10.510.10:FF:000768; Non-specific serine/threonine protein kinase; 1.
DR   FunFam; 3.30.200.20:FF:000141; Non-specific serine/threonine protein kinase; 1.
DR   Gene3D; 1.25.40.430; -; 1.
DR   Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR   InterPro; IPR015661; Bub1/Mad3.
DR   InterPro; IPR000095; CRIB_dom.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR013212; Mad3/Bub1_I.
DR   InterPro; IPR033923; PAK_BD.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   PANTHER; PTHR14030; MITOTIC CHECKPOINT SERINE/THREONINE-PROTEIN KINASE BUB1; 1.
DR   PANTHER; PTHR14030:SF25; MITOTIC CHECKPOINT SERINE_THREONINE-PROTEIN KINASE BUB1 BETA; 1.
DR   Pfam; PF08311; Mad3_BUB1_I; 1.
DR   Pfam; PF00786; PBD; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00777; Mad3_BUB1_I; 1.
DR   SMART; SM00285; PBD; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR   PROSITE; PS51489; BUB1_N; 1.
DR   PROSITE; PS50108; CRIB; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Centromere {ECO:0000256|ARBA:ARBA00023328};
KW   Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW   Kinetochore {ECO:0000256|ARBA:ARBA00022838};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000269221};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          197..364
FT                   /note="BUB1 N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51489"
FT   DOMAIN          673..1075
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          1075..1088
FT                   /note="CRIB"
FT                   /evidence="ECO:0000259|PROSITE:PS50108"
FT   DOMAIN          1508..1752
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          430..466
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          584..606
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1226..1252
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1287..1483
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        584..599
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1294..1318
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1441..1455
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1456..1467
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         1537
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1752 AA;  195562 MW;  4987AD4A158990DF CRC64;
     MSVSPVKRQK MESALDQLKH HTTVVADTGD FNELIKENIL HLAEEDELTG IERLSEDAIV
     SGSYKNKSLC ANPEDTCDFN RAAHLASTPF HGVVAQRVPA PAFCPSELKE DSPESKSAPL
     SQETPVCEGA FTESLSVKKL RIKGEVVMSE EDGHEWELSK ENVQPLRHGR VMSSLQEALA
     QQDCSSHTAV QLKKQEFEAE IRFYSGDDPL DVWERYIKWT EQAFPGGGKD GNLAAVLERA
     VRALHGQQRY YKDPRYLNLW LKFGDCCNEP LDLYSYLCSQ EIGTTLALLY ITWAEALEAR
     GSFRKADLIF QEGLQRKAEP LDKLQAHHKQ FQARVSRQTL LALEENSDGD NMGLLEIAEP
     QRSSLADLKG RGKKKVRAPI SRVGDAVKVM NPNRSCQPQT SQQLPNAPSF AVFDENSVSG
     PEIATLTAQS WPAPPVPKAK ENELSAGPWN SGRRPRSTVS SGVEVPQPLP SFTPYVEESA
     QPQMMTPCKI EPSINSVLST RKPGEREDPL QRVQHQQQDA QAKKEMVMYC KEKVYAGVDE
     FSFEEIRAEI YRKKAKKKDE DEIQAIERKK EEIQRKIEEL EKKLKKKEDD KQQQPHEQDE
     LTGIERLSED AIVSGSYKNK SLCANPEDTC DFNRAAHLAS TPFHGVVAQR VPAPAFCPSE
     LKEDSPESKS APLSQETPVC EGAFTESLSV KKLSPIMEAS LEDTRSSGSS VSGGSLSSVT
     QMSAIKYLHI SDKLELAHSL PAEVGIDSGG GNVSEDDVTQ FPWSPEQRKK LLDPMLSSLV
     ASPDFHLETG ALPHMEVEKD VELGNETYCI KMEYWNNEEY KMFFAIPTGC IFQWDAKGYA
     VKVYSQPVPW DFYITLELQK RLDSDFDQSF SENCSCYLYQ DGCAIVHKDT NCFTLRDVLC
     DRKFITKEIL FLVVHDLLHM VEKLHKAEIV HGDLRPEVLF LGDRICDAFS DEEVPNALKM
     VDFSHSLDLR VLPRVSLPYN FPTAQTPHGQ QLLAESSLPY QVDLVGIADI VHLMLFGDHI
     QVYQENSIWK ISQNLSMTPD SDFWSKLFER ILNADGSKRG DGIMFRKKKK KRPEISAPQN
     FEHRVHTSFD PKEGKFVGLP PQWQNILDTL RRPKPVVDPS RITRMQLQPM KALSKPGARL
     CTVVVFSVEI AGATVLHQLS IRLSVINSTC LEDPWSSVSK QEIAVTPGKD FPQAKTVVRG
     STVEVEGYIS GLLNDIQKLS AISSNTLRGR SPTSRRRAQS LGLLGDERPP DMYLQSPEGD
     WADKYGNYLN CNGGSKVARR QTMWPDYKSR SEGQSHPNGM VTKAQSLGPS EFQGTDGSCL
     QRASGLNESE TAMKSPEEGW HQRQPNARPS GEGSPGSKSR ENSLKRRLLR SVFPSSSTSN
     KPGPPVQVKP NAFFKPQQWG SPHSPAAKAQ SLPPDQPASE FPRMISEAGT PQKSPTAEKA
     VAVPPGRPSP AGSPRNRQTQ TSSSNLHLPQ DSAGKGQPTS EDPVVVTHEQ FKAALRMVVD
     QGDPRTLLEN YIKIGEGSTG IVCIAREKHS GRQVAVKMMD LRKQQRRELL FNEVVIMRDY
     QHVNVVEMYK SYLVGEELWV LMEFLQGGAL TDIVSQIRLN EEQIATVCES VLQALSYLHS
     QGVIHRDIKS DSILLTLDGR VKLSDFGFCA QISKDVPKRK SLVGTPYWMA PEVIARIPYT
     TEVDIWSLGI MVIEMVDGEP PYFSDSPVQA MKRLRDSPPP KLKNFHRGET LGYGPQSGLC
     EDQVILPPES YG
//
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