ID A0A0C9Y697_9AGAR Unreviewed; 1191 AA.
AC A0A0C9Y697;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=CAP-Gly domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=K443DRAFT_131357 {ECO:0000313|EMBL:KIK03533.1};
OS Laccaria amethystina LaAM-08-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Hydnangiaceae; Laccaria.
OX NCBI_TaxID=1095629 {ECO:0000313|EMBL:KIK03533.1, ECO:0000313|Proteomes:UP000054477};
RN [1] {ECO:0000313|EMBL:KIK03533.1, ECO:0000313|Proteomes:UP000054477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LaAM-08-1 {ECO:0000313|EMBL:KIK03533.1,
RC ECO:0000313|Proteomes:UP000054477};
RG DOE Joint Genome Institute;
RA Kuo A., Kohler A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000054477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LaAM-08-1 {ECO:0000313|Proteomes:UP000054477};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KN838579; KIK03533.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C9Y697; -.
DR STRING; 1095629.A0A0C9Y697; -.
DR HOGENOM; CLU_008637_0_0_1; -.
DR OrthoDB; 1709743at2759; -.
DR Proteomes; UP000054477; Unassembled WGS sequence.
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 PANTHER; PTHR18916; DYNACTIN 1-RELATED MICROTUBULE-BINDING; 1.
DR PANTHER; PTHR18916:SF6; DYNACTIN SUBUNIT 1; 1.
DR Pfam; PF01302; CAP_GLY; 1.
DR SMART; SM01052; CAP_GLY; 1.
DR SUPFAM; SSF74924; Cap-Gly domain; 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:UP000054477};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT DOMAIN 162..207
FT /note="CAP-Gly"
FT /evidence="ECO:0000259|PROSITE:PS50245"
FT DOMAIN 1171..1185
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 52..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 215..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 767..786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1002..1026
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1090..1126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 500..581
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 635..666
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 892..919
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 64..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..233
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..342
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..360
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1004..1026
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1099..1126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1191 AA; 130114 MW; 5B35C553496B0BAE CRC64;
MTTPGKSRQS GIPGPGRISS IPTPGRSRSS SNVYQNATDS FDDISRAFAD AIKANDPAQH
RTIPQPRAAS TSSLAPQFAP QTTQSGHRSV GRPSSAASTS SAIGASTRTT ERAKTPTSAK
PPSRPPSRHS EAFARSVSRS FEIGDNVRIE SLGFEGLLKY VGEIEGKPGL WAGVELGGGF
AGKGKNNGTV NGKKYFSCPQ NCGVFVATTK LSPPTVGPGT IQRPSSVASS RGRITPALSG
RVTPSFPSAT RTPSASFANG RATPSASGRL TPSNTNGRGT SATTPAASDR TRNVLKAVTS
KGIDVSLTDK ITAGSRASKY MSMTAQQLSS RGSRNMESPT GRNRESPGPA LPPPSPSSFP
SSSPSRGSRM LSSPTRPSGS PFTPKPSLGG RTSTAGNTGL PSSPSRNRPS VSTPRARVSS
AVAMPPPASP IFSSSYSYHA RCLDSEASSA TCSDYLEAQG KALQDNIPLV ISKDTSFNLS
SRPESSASFR STTMDEQSLV EQLQSRIDAL EYENERLRLA SGNEFASALP EQLESLERER
DEAIAKIFYL EEKQAASNSN VEAHTHRITL LEQDLKRITS ERDTQQLKDQ SCVANLQKKV
EEDVLVIQEL QASLTVRSNL VDQQHENLEV KETEIALLNL KLQSMFKELE EEKRELGAQI
DELRIAGQET IALYEERLSS ADTQRYELEL RITSLEAVHS AGREPSTTAS HFASSATQID
NETLRDQVHH LQRKISTMED VIEDARAASE KEEAAFRERM RRLKEKEDGM KKELSEGRKE
VERMTTSELT ARNRVEEIEE ALRESTVALE NARAEVEALR AEMANVDSLV GDISEGDLSS
RVAELAHRAS IDRTRSEQEI SRLTDMLQEL RPGVNRRDVD LESQVFTLQQ QKATLEAKVL
DLTRALDDST NELEATRKKI NRDVFVTDDI HDGLKSSSSL PSKFDSAVAK EEVTGLKHII
QELQKESIMA AQRIKLLESE NQLFSCEAEQ LRQEVQLLED SLHNSSSMED KDLDKSTTSL
DSKDVDSLEQ RLKEQSLRHD AEIEQLKKRL SESEIKHART IHDLNKEISE LEALVEAKDE
LEQEVERLKD KAARAKKSSK NSTETNGMRH RLSSASSNTM SSGGTGQDVC EICERPGHDI
FNCDLLKEDG ASKETIPATT WPPRTVVDLF CEDCESHGHV AADCPHSLDV F
//
