ID A0A150VCP5_9PEZI Unreviewed; 1280 AA.
AC A0A150VCP5;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 22-FEB-2023, entry version 14.
DE RecName: Full=Spc7 kinetochore protein domain-containing protein {ECO:0000259|SMART:SM00787};
GN ORFNames=M433DRAFT_132285 {ECO:0000313|EMBL:KYG48255.1};
OS Acidomyces richmondensis BFW.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Acidomyces.
OX NCBI_TaxID=766039 {ECO:0000313|EMBL:KYG48255.1, ECO:0000313|Proteomes:UP000075602};
RN [1] {ECO:0000313|EMBL:KYG48255.1, ECO:0000313|Proteomes:UP000075602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BFW {ECO:0000313|EMBL:KYG48255.1,
RC ECO:0000313|Proteomes:UP000075602};
RX PubMed=26973616; DOI=10.3389/fmicb.2016.00238;
RA Mosier A.C., Miller C.S., Frischkorn K.R., Ohm R.A., Li Z., LaButti K.,
RA Lapidus A., Lipzen A., Chen C., Johnson J., Lindquist E.A., Pan C.,
RA Hettich R.L., Grigoriev I.V., Singer S.W., Banfield J.F.;
RT "Fungi Contribute Critical but Spatially Varying Roles in Nitrogen and
RT Carbon Cycling in Acid Mine Drainage.";
RL Front. Microbiol. 7:238-238(2016).
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:KYG48255.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JPDO01000053; KYG48255.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A150VCP5; -.
DR STRING; 766039.A0A150VCP5; -.
DR Proteomes; UP000075602; Unassembled WGS sequence.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000075602}.
FT DOMAIN 772..1092
FT /note="Spc7 kinetochore protein"
FT /evidence="ECO:0000259|SMART:SM00787"
FT REGION 1..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 296..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 354..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 513..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 594..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 626..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 688..708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 804..826
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 952..1039
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 47..61
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..247
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..537
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 689..708
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1280 AA; 140324 MW; 07A7D2554F4B7FFC CRC64;
MADMLDKENI APIMPSDPLQ VKSPSQKGGR KGRSKSIGPG ELSSDGTKQD TKQDTKNRRK
STYVPATKSI IPNDSQKAER QAARRKTLAN RRVSFAPEAT LHTWDVIEFM RDPTTSTDSS
DQTRRASNVT QGTNCSPFKS PASGSDPPST PADQEDELIQ LPRSPAHQRA MHKKQRRRSS
GIPPMNFNNP DDFGSSDSIS GSSDVSGSED EGEMEDTTGT AMSLDMGDDT SRSSESFSST
SSSARLEAAL RQAAEAAGTR GIEYDEFGDD DMSMELASEE VTNAFKPWVQ RTASAPRGSA
DLDQENVNPF SPAFKAQTVS GTVRWPERVE EEDTGDLSMD VTRAVGGIVN ANQKGQVRSS
LPLEDGTMDC EQAVSNIQDN GLSSSPARGG QKRRRSTTDA GSPGVGASPA LPKRRRSSIA
RSSMGDDTMD LTVAVGGIQS SVSPTKSERK KSLAKRRSSG ISSEVEEVPM DLTQVVGGIK
DAVVTVTEHT SSSFDENEEL TMELTTVLGG IKEKDSPAAE VRPTTPLNQS PKSAANMTPK
DQERFRDAPN SGPKKLLTPL FQKHVTYSAE KGSASVEKRR KSISPAKVSW TGAVFDETRG
PEISTAEASQ PTQKFASAMQ NSFLNSGVSY PHLPSTGNNA SPRRVTPTTT PPSQHGQETS
ISSSLRQELD PQLHVLEPSP LAQKVLRSSP LKEASTPERQ IFPQESRKLT ESIKLMSTPR
KETLKHATPK KGLMTQISPA KVLTPRLGPT LGAQADPKAT PARQLRDDLF KIQSSGQSMQ
KLHLQTFLEQ ANIRFMDLTA TKRRLTTAPT PSKARKDNGA GEPDSDLNLG NAVVAAACTQ
PEHDMFQHAC HELKHYISEG KKVIKQIEVQ TYRDTPPLIA AYMAASAYRR GELDVQMRDM
KTHARFRSKE VWYAWRSQLL DDLVKALSGI GEGMIKDDAV LGRTERILDQ CLPLLLEQHK
NLQLEAARLQ EAAASTSEED KERLDAARDR IVEIDAEMEE KRRILAEVQS EAQELERAIE
KMRDNKAECV SAIQDAERLL ESCRGFSLNE VNVLKSSIKQ LEDVHGWSII SATPSPPALT
MTYKSQLQLF FHPNAFHTPS QPKKTRPNAP ISLSYIARDR NEQPKELSTI LRFFLQLLRA
SLHSLPQCTT RVVELLALVS QGWTIALTVA QAESKLAVEG VTNARIVSDE RLAIDSTLLL
PRVRTKVCVT FDLLVMMADE IELNTTVEAS AKLIYGEQYD EKKMTNLIVK AIGDGYGEWA
TAVQDLKGRL VGQGTKWIKK
//
