ID A0A317XNG8_9BASI Unreviewed; 1323 AA.
AC A0A317XNG8;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=CAP-Gly domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=BCV70DRAFT_162362 {ECO:0000313|EMBL:PWY99816.1};
OS Testicularia cyperi.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Anthracoideaceae; Testicularia.
OX NCBI_TaxID=1882483 {ECO:0000313|EMBL:PWY99816.1, ECO:0000313|Proteomes:UP000246740};
RN [1] {ECO:0000313|EMBL:PWY99816.1, ECO:0000313|Proteomes:UP000246740}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 3645 {ECO:0000313|EMBL:PWY99816.1,
RC ECO:0000313|Proteomes:UP000246740};
RX PubMed=29771364; DOI=10.1093/molbev/msy072;
RA Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA Spatafora J.W., Aime M.C.;
RT "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT clade Ustilaginomycotina.";
RL Mol. Biol. Evol. 0:0-0(2018).
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DR EMBL; KZ819194; PWY99816.1; -; Genomic_DNA.
DR STRING; 1882483.A0A317XNG8; -.
DR InParanoid; A0A317XNG8; -.
DR Proteomes; UP000246740; Unassembled WGS sequence.
DR GO; GO:0030286; C:dynein complex; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR Gene3D; 2.30.30.190; CAP Gly-rich-like domain; 1.
DR Gene3D; 4.10.60.10; Zinc finger, CCHC-type; 1.
DR InterPro; IPR036859; CAP-Gly_dom_sf.
DR InterPro; IPR000938; CAP-Gly_domain.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR PANTHER; PTHR18916; DYNACTIN 1-RELATED MICROTUBULE-BINDING; 1.
DR PANTHER; PTHR18916:SF94; RESTIN HOMOLOG; 1.
DR Pfam; PF01302; CAP_GLY; 1.
DR SMART; SM01052; CAP_GLY; 1.
DR SUPFAM; SSF74924; Cap-Gly domain; 1.
DR SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 1.
DR PROSITE; PS00845; CAP_GLY_1; 1.
DR PROSITE; PS50245; CAP_GLY_2; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Reference proteome {ECO:0000313|Proteomes:UP000246740};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT DOMAIN 243..288
FT /note="CAP-Gly"
FT /evidence="ECO:0000259|PROSITE:PS50245"
FT DOMAIN 1303..1317
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT REGION 1..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 190..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 443..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 651..722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 961..995
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1009..1050
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1224..1251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1078..1123
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..531
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1009..1026
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1027..1050
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1226..1246
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1323 AA; 142521 MW; 66EC2CC5A9836F5F CRC64;
MSFSSGLPTT PNSSHMRSGL PTPSGSLRRT SLATSAVSPV DSPDIVFKKQ TLAEAISRND
PAKYRLSGTS PSAAAVPTSP QKGGNGTDSE SPLLTAGKLP RTSLLSRKSN IALRSHTPSG
RLTPASYTPP SSHGRLDVSP NSYPDTARSK SPLVPSGAFA SVSSSSSAAA AARAFSTPKR
LSDLHSRASL VSTVGRTPSH SSTTVASRAR QASTTTRRGR ELEIGDVVSM EGSDLVGVLR
HLGPVTFKPG FYAGLELTGD SVGKGKNDGS VQGTQYFACA PGNGVFCPAS KVVAINDQPP
CDAVARPASS LSSRPGSRAS ELSDRHSAIT PARRRASTIS RPPSTTPSRA SSRASSRVAS
GTDGGRPASA LSSSRPTSRL AARKSLASTA TRGTDHEDGA QCRADPVKSS LYSASASVSR
TPRSSTAPTS SAAAAAAAAS QATPMLAKKR QSLGGIPTPR ATKGRASMFA RPTGLGTIDS
SMPPPPSPTK DGRVGERSVS SLSFRSSSRL GREQGDIESS PVTSAPNNNV STDVIMERNM
LLLEQMDLTP KKAAAQALRA ESRASAAGTV AAGVVTGDDE LTRDSVAEAV VPLSLYEEQV
AEFDRLRTQL DALEKQNLEL QRAQEARKAR TSEVRSNQAI LEEERVKMRA EARERQSEME
EERRLEREDE VRRRKEIEER ERELKEKLHE SQTLLSRAND EQDKLRSDFD SQKRGLQAKV
DESERLIAEM KKRIEEHAED RQSSEMDLKD AEIESLRSSV TRLEEESQKE RLVLSQQIDE
LKEAGRETIS LYEQRIEEID REKAGLLDDM ELLAAKAQEA IRTAESKYED LLQQQEQRGG
TGGGATAGLG GAAEIDNEAL REQVAHLQDK LGKYEDQIAE ATMVLEKEKD YSQKRREKSL
EVEASLKNEI KRLRAEVERL TRLDRENRQS LDELQRALKE SQSALEQERA ELEGLRADVE
NIESLEGGSG GGVGGSRTAA TASRKQWQSE KAEMQSEIDA LRAALRLRES DSGDKAPVEV
HADSTLEKPS VEQQQQQQNR TPRRTSQRLS VNSIGALSEA SADSTSSANQ VSGLSYLVRQ
LTDDNNDTKA RYKLLESEMK ERLQEAETKA RTLEITVESL RAQLGASSSE SGGAAAAAGE
TSDQSALAAK LADSEARLRL ADEQVATLQL SLAEAGREQR KVASSLQKEV SELEALVEAR
IFREDELMTE IDRLKRKLDR HDVSRPAISS NGTSETSASA SVPASHESQA GLAEDDEELN
FCGLCSNSGH SLEECTVPHE SQPLSKAASK TAISGITDGR EPCDDCGEVG HRFEDCPYAA
EMF
//
