ID A0A4U0U684_9PEZI Unreviewed; 1249 AA.
AC A0A4U0U684;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 02-APR-2025, entry version 20.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:TKA30474.1};
GN ORFNames=B0A50_02702 {ECO:0000313|EMBL:TKA30474.1};
OS Salinomyces thailandicus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Salinomyces.
OX NCBI_TaxID=706561 {ECO:0000313|EMBL:TKA30474.1, ECO:0000313|Proteomes:UP000308549};
RN [1] {ECO:0000313|EMBL:TKA30474.1, ECO:0000313|Proteomes:UP000308549}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCFEE 6315 {ECO:0000313|EMBL:TKA30474.1,
RC ECO:0000313|Proteomes:UP000308549};
RA Coleine C., Masonjones S., Stajich J.E.;
RT "Genomes of endolithic fungi from Antarctica.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
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:TKA30474.1}.
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DR EMBL; NAJL01000011; TKA30474.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4U0U684; -.
DR OrthoDB; 248495at2759; -.
DR Proteomes; UP000308549; Unassembled WGS sequence.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:TreeGrafter.
DR GO; GO:0032991; C:protein-containing complex; IEA:UniProtKB-ARBA.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
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; cd13981; STKc_Bub1_BubR1; 1.
DR FunFam; 1.25.40.430:FF:000003; Checkpoint serine/threonine-protein kinase BUB1; 1.
DR Gene3D; 1.25.40.430; -; 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; IPR012572; Mad3/Bub1_II.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR14030:SF4; BUB1 KINASE, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR14030; MITOTIC CHECKPOINT SERINE/THREONINE-PROTEIN KINASE BUB1; 1.
DR Pfam; PF08311; Mad3_BUB1_I; 1.
DR Pfam; PF08171; Mad3_BUB1_II; 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; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW Centromere {ECO:0000256|ARBA:ARBA00023328};
KW Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW Kinetochore {ECO:0000256|ARBA:ARBA00022838};
KW Reference proteome {ECO:0000313|Proteomes:UP000308549}.
FT DOMAIN 59..218
FT /note="BUB1 N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51489"
FT DOMAIN 896..1203
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 232..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 363..704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 716..754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 918..939
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..275
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..293
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..398
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..457
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..496
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..579
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..593
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..628
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..675
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1249 AA; 140757 MW; 5F2EC844C383FD36 CRC64;
MSGDLIDFNV IEGHKENIQA LPSGRSAKAL HQLYSPPILG AQASPADTQD ANTKAREPFE
KELQYIDEAD DPLDVYDRYV KWTLDAYPSA QATPQSRLLP LLERATKAFQ SEAHYKNDPR
YLKLWLHYIR LFSDAPREVF VFLARQNIGE SLALYYEEFA AWLENAGRWN QAEEIYKMGL
ERGARPAERL LRKFGEFERR KEARSQDAPE PTSPALPMAR PALAAKIDPF EASAPAEGQQ
QQARSTAPKK SKSSKMAVFS DSGEDTRPNS DRSSKGWDNI GTLADRKKEN SVEVKPMAGE
KLKGGKTNGG MQKLMIFKDQ TGRMECVFVN LEAVYPDSGR RNEEYCFEEL RARRRGWLGK
DWRRPESKAK HAPRPAQHMS QPVPEPEAKF KSAEKTTPED EESPSGTLDI HVDEPVQPQP
QQPKTKQRGF KIFEDTSSEP LPASKQTRQK ENDEKVLVES FSKTLALNDE NDENAPPSKQ
QGAELAKRLR REERANRTRK IQVMDVKHIS NETKTIQLNM DSPTGPKLKR KKSGERAEPT
MTINTKEAMD EIYGIFNQPL PSQEEQSEEE DSDDDDYTTG DESTATGKLS GTGSEYGDET
RNELLGTSKQ AGEGDDGPSE NTGWSDFTMS KDVPKEADES GPTSAQSTAW DIYQDPSQPA
HVDEDIHSPQ EDPHRTQYVP VAPEDYEPPR GQFREMNPLP NHRLPFMTPI IEQTESSLGT
ATARTEKEDF NAKTPSRKAG AAAPLPEDDE PCSSPFQEVI EDMAEEKRKV LQPIRTKSTK
GTISLGQGSA KSQIAAKTKV PSAPEPQQKG PIVKEQQCNP MDPYLRQTIL SQMKPSLTSY
DGYHQHLDTT SSRTAEIKKY IKTLQKASRN SVNLEKTAST LSLPPMLSFK GAEGTYTIKR
ELGAGTFAPV YLVENSAAMP TDEQENDENR PPSRVGKQAH RKQLEAVKME EPPSTWEFYI
LRQSHRRLGV SRAAESIVRA HEMHLFRDEC FLIEEYRDQG TLLDLVNIAR LDSSSGGGME
EVLAMWTTVE LLRTVEAMHS KQLIHGDLKG DNVLVRFDDP DQETDWSPTY FPSGAHGWAS
KGICLIDFGR GIDMKQFVPN VAFIADWKTT EADCAEMREL RPWTYQIDYH GLAGIVHSLL
FGKYMETIAE KGAALGQGAT KTYRIRESFK RYWQTEIWSE VFHLLLNPLQ HLDGEEGRKM
PVMKGMRGCR ERMEGWLEEN CERGVGLKGM ISRMEAAVRE RKRKSARGI
//
