ID C1G7H5_PARBD Unreviewed; 1032 AA.
AC C1G7H5;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 2.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Cep57 centrosome microtubule-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PADG_03130 {ECO:0000313|EMBL:EEH47032.2};
OS Paracoccidioides brasiliensis (strain Pb18).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502780 {ECO:0000313|EMBL:EEH47032.2, ECO:0000313|Proteomes:UP000001628};
RN [1] {ECO:0000313|EMBL:EEH47032.2, ECO:0000313|Proteomes:UP000001628}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pb18 {ECO:0000313|EMBL:EEH47032.2,
RC ECO:0000313|Proteomes:UP000001628};
RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT "Comparative genomic analysis of human fungal pathogens causing
RT paracoccidioidomycosis.";
RL PLoS Genet. 7:E1002345-E1002345(2011).
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DR EMBL; KN275959; EEH47032.2; -; Genomic_DNA.
DR RefSeq; XP_010758273.1; XM_010759971.1.
DR AlphaFoldDB; C1G7H5; -.
DR GeneID; 22582493; -.
DR KEGG; pbn:PADG_03130; -.
DR VEuPathDB; FungiDB:PADG_03130; -.
DR eggNOG; ENOG502S3TV; Eukaryota.
DR HOGENOM; CLU_004834_0_0_1; -.
DR InParanoid; C1G7H5; -.
DR OMA; MKSDQIY; -.
DR OrthoDB; 2729811at2759; -.
DR Proteomes; UP000001628; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR InterPro; IPR024957; Cep57_MT-bd_dom.
DR InterPro; IPR025925; PPC89_CLD.
DR PANTHER; PTHR19336:SF9; SPINDLE POLE BODY PROTEIN PPC89; 1.
DR PANTHER; PTHR19336; UNCHARACTERIZED DUF1167; 1.
DR Pfam; PF14197; Cep57_CLD_2; 1.
DR Pfam; PF06657; Cep57_MT_bd; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Reference proteome {ECO:0000313|Proteomes:UP000001628}.
FT DOMAIN 427..492
FT /note="PPC89 centrosome localisation"
FT /evidence="ECO:0000259|Pfam:PF14197"
FT DOMAIN 870..946
FT /note="Cep57 centrosome microtubule-binding"
FT /evidence="ECO:0000259|Pfam:PF06657"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 82..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 108..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 220..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 274..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 497..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 746..774
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 973..1032
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 357..398
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 879..906
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..101
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..199
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..247
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..545
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 746..772
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1032 AA; 115055 MW; 7C52256E049002C6 CRC64;
MFPNDHTNTS DVMAHSHASR EPTTSDFDPD HEALVSTRQL DNDHLHPQSK RANWDDAHAE
QEPDPDFVIN TSALHRAFPD FSDASSLEEE EEEDDEDEDD LSVEMGRAAK KTSQQLDDSR
DSVMSVDGSK YSALPAGREG RFGSRSPRAP LRPITNRAST GRDSLRKDAQ IRRASLAMKD
SNQPKDIKLK SGSQRRTLSE IHAKVNETYD GSYISDERPA KVTLTTRNTR FSNRRTNDQS
SRLADAGNKA SGKNYLKHYN AGDVEQAQLR RQLPSKTTDS NGTTDNPTHQ SYALPDIPDL
SELVSGIYED GTPKGRSRTT RFTSPPAMGV STSQPPEHLP LDSIPVPDDE KAIFVSLKLL
QEKVQALQTD KSDMEIRLEE MEEEILILRN ENARLRKQDK KRFSMDGGDE DINNGGVGKL
FIQKNRLEAA NLALQNRLDV SIRKNSSHET TIKHLTQERD SARTQLGVAY LNIEELKLEN
DALAQENDEM RIQIESNAFP EAANDSKPIE MCDSKTKRRE ATAMDPTKAT KPHRIRTKHA
EDPDANGSNE QIGFDTRRRN SNRTQQDRSQ PCVPSAVKVA ASKQQKQAEY DSLFSLDLSH
LSVQQSTQHT KMQANTTQKK LPNTSKLRTK KAVVEYMEDS NLSEEEMGTE TRGFRNRTGP
TNDLTFLSFI DANEIAKLRK TLEEERVARK TCLSRELTEQ TKTGNFGTRL LGNATHSIPF
KSSLKNTSSK ASRPVILEAT DFTGTEHRSV ANTRDLSQHN LTNHSTSTAG PRRRLNKTEE
MTSAFILPDI TLHAISGKSG EPPKLSAAAQ RVLNEVAKHD GKNCSVCKNV IDKNCIHGLS
NREGQVSFKV TKPVPVSARV PEPSPYIEEP TLRPSQQPAL ALATVLKALE DELAHLKMQL
VLQQTALNKH DASLRKKQRK SILRKFEFLL REIDTKSDQI YALYDVLEGQ KEDGHEMTQQ
EVDVTLQSIG LGGKDGSDLT ERLGHDGYEG KGVTGGANSD GDSDYDDPPW EGFESTGHLT
GRNFPKKLAK SS
//
