ID S8AUW5_DACHA Unreviewed; 1669 AA.
AC S8AUW5;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Centrosomin N-terminal motif 1 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=H072_1244 {ECO:0000313|EMBL:EPS44741.1};
OS Dactylellina haptotyla (strain CBS 200.50) (Nematode-trapping fungus)
OS (Monacrosporium haptotylum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Dactylellina.
OX NCBI_TaxID=1284197 {ECO:0000313|EMBL:EPS44741.1, ECO:0000313|Proteomes:UP000015100};
RN [1] {ECO:0000313|EMBL:EPS44741.1, ECO:0000313|Proteomes:UP000015100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 200.50 {ECO:0000313|EMBL:EPS44741.1,
RC ECO:0000313|Proteomes:UP000015100};
RX PubMed=24244185;
RA Meerupati T., Andersson K.M., Friman E., Kumar D., Tunlid A., Ahren D.;
RT "Genomic mechanisms accounting for the adaptation to parasitism in
RT nematode-trapping fungi.";
RL PLoS Genet. 9:E1003909-E1003909(2013).
RN [2] {ECO:0000313|Proteomes:UP000015100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 200.50 {ECO:0000313|Proteomes:UP000015100};
RA Ahren D.G.;
RT "Genomic mechanisms accounting for the adaptation to parasitism in
RT nematode-trapping fungi.";
RL Submitted (APR-2013) 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:EPS44741.1}.
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DR EMBL; AQGS01000035; EPS44741.1; -; Genomic_DNA.
DR RefSeq; XP_011107236.1; XM_011108934.1.
DR STRING; 1284197.S8AUW5; -.
DR eggNOG; ENOG502QU0H; Eukaryota.
DR HOGENOM; CLU_000791_0_0_1; -.
DR OMA; DENERRW; -.
DR OrthoDB; 1384930at2759; -.
DR Proteomes; UP000015100; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005815; C:microtubule organizing center; IEA:InterPro.
DR Gene3D; 1.10.287.1490; -; 2.
DR InterPro; IPR012943; Cnn_1N.
DR InterPro; IPR024545; Mto2p-binding.
DR PANTHER; PTHR23157; GRIP AND COILED-COIL DOMAIN-CONTAINING PROTEIN 1; 1.
DR PANTHER; PTHR23157:SF25; GRIP AND COILED-COIL DOMAIN-CONTAINING PROTEIN 1; 1.
DR Pfam; PF07989; Cnn_1N; 1.
DR Pfam; PF12808; Mto2_bdg; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000015100}.
FT DOMAIN 516..587
FT /note="Centrosomin N-terminal motif 1"
FT /evidence="ECO:0000259|Pfam:PF07989"
FT DOMAIN 1421..1470
FT /note="Mto2p-binding"
FT /evidence="ECO:0000259|Pfam:PF12808"
FT REGION 1..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 496..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 584..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1172..1196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1472..1625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1640..1669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 620..766
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 793..978
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1007..1034
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1064..1105
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1282..1362
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 26..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..131
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..151
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..375
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..412
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..451
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1172..1193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1472..1490
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1526..1604
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1605..1625
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1669 AA; 188489 MW; 25E10605B944312E CRC64;
MLKNTSADDD NDDLPSPISP VYPSSPPVRR NITQQIRTSS SYARNNPNNN KRAGSPDLIS
PAMTKPSPLK SSQLSDSDSE EGDDEQLSAI DPDDDLSDRD DHHYHEDDVD RDDDDGNGRH
NEDRRGDSPV LSEEEEEEEA EDDDDDDDDF SVADHTNLSL PADQQKELAQ VESSFRHSTP
DPFLQPGAGD NDADLSIVGG IRPGDSLKAS KPKPRHQSKL SVDRHHGSST TQRKVSDMGP
PSVPASAYRK DKKTDHKPTT KSKLSRTSLA VSSDKVRSEA SSPMPELPTG DEDESYSSRS
VPASDSLESF SSPSTMAKAR NISRAISSQY MTPKPAKKSG LSNEITSTDT TVRRPRLKTQ
RSRSSISSVG SEQVSDIEDN GDAPSRRNRD SADFDFGFDE RRSSKSNRLS TDRVVRRNVS
SGSVASSVNM NAAVEKVLED LDEEGRSDSG ADSDSAPETP RARVTASDPL PPETQLNAQI
RNIKVPETIA RDFRKREASN GSFSPTKKPG GGRGMTLKEQ SGTIDKLQKE NWDLRIKVFH
LNNRLDKTSE ESVKTLQNEN GILAVENTQL KSHIKTLKKR IKQLEKAGDT SSTRNGSDDA
DDKADITTLE TEVIYWKEQT EKVEVEVETL RSKVKEKESQ CERLSEIVRG MAGGGEETET
LRDFLESETN RRKQAEDDNA SLRREVWDLK AAAQAPPPND MNHRTRSSIS INSDNTLVSQ
LRLENEDLRR EVSAQLSMLT SRNREKERLY QEIEELKLGL PRENNQLVQV SDYDRAISRV
SSNPQNHMTD AEREDYENAN GALRDKISEH KLKIQDLEIE LETKLREMDK VVIQRQEFGD
LAAEYEDELE VLNADLQVVL AERNEQARLR EELEQDFDNL KEEAEEEIQR LEEEIDIRVA
EMEKLEEDLR NKDENFGALQ EEMRTLSTVV VRLEDSAQER LTRVQELEAD LEKSQKMINE
NEAEMTTLEK QIHDLTSKSE RLGVQQESAQ GEIAFLREEQ DSDKIKIGQL ESAMKSLEEG
LKDEKERSRS LSDRLLEERK LMDETRNMNK AEMEKLVGDK NQEILNMKEA ARQLKKSLAR
RETEVKEWKD KLAELEGSIR EAIGDVGSKA DVLKAVVHLQ QELEKRMEEI GRVKTDLADK
DRVLKDRENL LENTALEMRR LQDLLEKERQ ARKSDRAVAD TLQTNHDKSR RQIAQHQSQL
AELEKARSKD SKALSQLEIQ YKEQLAERNS LLVQLWIRLS ALCGTEWADK NKLIGKGGAV
LSADASVNGH LPGFSKSVLA AAKNLETVLT GFKTRIRNIE RDLWKEYAVV ENTLETRTRR
LERLEAMVRD GVGEQSSMRN EITKLKTENR LLKAELNVVR LQPSKLPLRS GVASVASRDS
LTAADNSVVR ASPDPAPDTN TLAINNTIAS LDDVTDENER RWILRLRELE KRLKAEREAR
LLDRTGAKQR LEEARNEREA LKKELERERT ISRIDRHDAE EDDKKGGRMS MIPKPSKAGG
GKSRDLGDEN GVGNSSGLLA PPDDEDVRSL IVRVERERRG EHRAKSRDRR DRKGNRDTPE
VEERSRNRDA GVSRADSRAR EREPGTPRER DPRERLKERS ISERGSSARS SMTKRADTTT
SQNKMVNIIS SIDELNARME RGKSPAKKEN TLSPRKFLGF FGGKTKEEA
//
