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Database: UniProt
Entry: A0A423XF95_9PEZI
LinkDB: A0A423XF95_9PEZI
Original site: A0A423XF95_9PEZI 
ID   A0A423XF95_9PEZI        Unreviewed;      1877 AA.
AC   A0A423XF95;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   28-JUN-2023, entry version 11.
DE   RecName: Full=Spc7 kinetochore protein domain-containing protein {ECO:0000259|SMART:SM00787};
GN   ORFNames=VPNG_03690 {ECO:0000313|EMBL:ROW14817.1};
OS   Cytospora leucostoma.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Diaporthales; Valsaceae; Cytospora.
OX   NCBI_TaxID=1230097 {ECO:0000313|EMBL:ROW14817.1, ECO:0000313|Proteomes:UP000285146};
RN   [1] {ECO:0000313|EMBL:ROW14817.1, ECO:0000313|Proteomes:UP000285146}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SXYLt {ECO:0000313|EMBL:ROW14817.1,
RC   ECO:0000313|Proteomes:UP000285146};
RA   Yin Z., Huang L.;
RT   "Host preference determinants of Valsa canker pathogens revealed by
RT   comparative genomics.";
RL   Submitted (SEP-2015) 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:ROW14817.1}.
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DR   EMBL; LKEB01000012; ROW14817.1; -; Genomic_DNA.
DR   STRING; 1230097.A0A423XF95; -.
DR   InParanoid; A0A423XF95; -.
DR   Proteomes; UP000285146; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR040850; Knl1_RWD_C.
DR   InterPro; IPR033338; Spc105/Spc7.
DR   InterPro; IPR013253; Spc7_domain.
DR   PANTHER; PTHR28260; SPINDLE POLE BODY COMPONENT SPC105; 1.
DR   PANTHER; PTHR28260:SF1; SPINDLE POLE BODY COMPONENT SPC105; 1.
DR   Pfam; PF18210; Knl1_RWD_C; 1.
DR   Pfam; PF15402; MELT_2; 5.
DR   Pfam; PF08317; Spc7; 1.
DR   SMART; SM00787; Spc7; 1.
DR   SMART; SM01315; Spc7_N; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000285146};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        1444..1465
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1471..1497
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          905..1222
FT                   /note="Spc7 kinetochore protein"
FT                   /evidence="ECO:0000259|SMART:SM00787"
FT   REGION          1..143
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          148..167
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          179..505
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          594..677
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          707..895
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1769..1806
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1084..1157
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..23
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        100..127
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        148..165
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        181..202
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        286..335
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        344..368
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        370..395
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        421..440
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        599..629
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        642..670
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        732..781
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        801..826
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        831..876
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1780..1803
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1877 AA;  206880 MW;  39F0ABE037107FD0 CRC64;
     MAGNTTLPAT RRTRKSTSAM DMDNATIDLG AGATLAESRK KSKSRSKSLG PGGVDALKAG
     SGNRRVSLAG PPRAIPRSIL KPTVPLPEIP GYKPRHSYAA GTSGTENLPS PFHGDDSSSS
     GTKVALRTEE EQQAAARERE EQERLALEKE IKDRREARRK SLANRRVSFA AEATLHTFHE
     VEYMQDSTTS TDNTQRRASS AAAQPQAPPE EEHLAPDAAD TASTPPEQVE ETIADSPENQ
     HHLHHRQQRR ISGLPAHDNF DDQGDITMAS TIYDSDSDEG DDVAEVQTEA SNSDSDSDND
     GTMMTVEAEE LTSASLASTR YGDEANTTTS SLDGALREAA QRAVNQSREP DEDEEVIAGF
     KGWSRKAREQ RQAIASSQEQ PASEDDVQSS PLKPSPGKHN VDDGTEMTMD MDMDITNVVG
     GIIRTTPSSS PRQAEQEDMS MDVTNVYGGI LSPQAQPEDD RSDHEEQAME LTTTVGGIQG
     GPPSDNDSGH ASDEEMSMEL TTVMGRLLAA KNNQLRKSIL PSSSPVKDPV DDAPLDITMD
     LAQGIGRILP ADGEDNERDS ADDEATVGMD ITTAVGGIIK PVSSVERTAA KKLMEQEADQ
     PEVTTTTDPV SLKSPPKQPT LQTIQGDSPG LSAFREKNAF PRTRLATSQP NTERQPHAVS
     TATSVASQGR ITARKDDAIL QRPKLSGIGV DRSGIGSPRV TEILDRRSSI GDTAANFSPV
     PLPQYRKAVT FGDPRVMEEE VDRDRRADQE RESSRSNLEK EADDATSSLK EMIEGLSPKK
     KPFKGRKSLH VGSARGLLGK RPPELDNDSD AEEQDGVKRL KGREGSPVKN IKLQQPPSKA
     ETTGSRPTLQ SSQVLNDAEI STVTPTATQS PPKATTPKDQ GRFRDVDNDQ PTATFTLNVT
     PSMNIADLQP PDDNEERIHL QDFLNLTSIR FMELTTTKRR HTIAPSARKD SLSSGEENIS
     LEKCVVAGAC TVPMLELYQH SCRELKKYIS EGRRIVREIE TETFMENPPL FREYITASPE
     FKLLMDNQFK NVKTHARLQS KAMWYEWRTK LQEGLREGLV KTAEGMVADA ELLDQQQKLL
     LSVLPALIKQ VEALDRECEN LEAVATELKD CDPEELGSAR ADLTAVDEDM EAKAREIAQL
     REQLQATEES VGKLVEQKQQ CSTDIKEAEK MREECRGWSS PEISALKARV DAIEKEHGWA
     ITGIAGTSVS MTYRKEIELV FDIAGLRAGQ QASRIDIWYI AATREHKPLP STTEKNFCLQ
     CIRDHVRSVA QLKTEPKRIL SLVSAAWDHA NALANQVYQL NLTFPTAVQR ISDSAISIRS
     SLQLVPLKTK VEVVLRVQSA AGANGLQFIL SSQAAVVYGE QFNAGKMEEF LSSRIGDHIN
     LDNQVEDWCD VVSELHMPIM LDYALAMLWR IIALIAALIN ALLEAAHKWG KQSFPTMLDG
     ALAMFWRITA FIIALFGAAY TIFYYTISIS VLAAGVCFGF LALCIMPAVF QSVVELLPLK
     QYFDRRLQKD YINKIKKMEY QEKKTRARLI QLMGDVKLQN EANNKVLKEI RTNEAIIKRK
     VRGFASCVVD RYQIQPTIIG IIVPPHQEPE EPSRRPIIRW LFAQSLQLYQ HERSIAKYEA
     QISGELIKLQ QLDEEHICLS NILDDINSKR SRVMLLNDLP KPYRVSASTR KYCSQFDHTR
     MKPSPYPNFE RPSDWESRLN RLAGLTSREP EIYQVRLDFP PMTKHFTFPT RLAVGTDTSF
     GASFGAPIFS APAQAPPLFA APVTTTAPGS FSTSLYDPPP SAAPFQPTFG PPAAAPTTPA
     AAPTLAPPAE NRLSLAERMT DPTGLRAPLP ASILATPAPI QSDEEIQAER KAARLAEIEL
     AQELKAARAK WPRRFKG
//
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