ID A0A0C3MVP5_PISTI Unreviewed; 844 AA.
AC A0A0C3MVP5;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=CCHC-type domain-containing protein {ECO:0000259|PROSITE:PS50158};
GN ORFNames=M404DRAFT_36508 {ECO:0000313|EMBL:KIN92989.1};
OS Pisolithus tinctorius Marx 270.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Sclerodermatineae; Pisolithaceae; Pisolithus.
OX NCBI_TaxID=870435 {ECO:0000313|EMBL:KIN92989.1, ECO:0000313|Proteomes:UP000054217};
RN [1] {ECO:0000313|EMBL:KIN92989.1, ECO:0000313|Proteomes:UP000054217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Marx 270 {ECO:0000313|EMBL:KIN92989.1,
RC ECO:0000313|Proteomes:UP000054217};
RG DOE Joint Genome Institute;
RA Kuo A., Kohler A., Costa M.D., Nagy L.G., Floudas D., Copeland A.,
RA Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA Lipzen A., 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:UP000054217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Marx 270 {ECO:0000313|Proteomes:UP000054217};
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; KN832264; KIN92989.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C3MVP5; -.
DR STRING; 870435.A0A0C3MVP5; -.
DR HOGENOM; CLU_012455_0_0_1; -.
DR InParanoid; A0A0C3MVP5; -.
DR OrthoDB; 1657587at2759; -.
DR Proteomes; UP000054217; Unassembled WGS sequence.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd00303; retropepsin_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 1.
DR Gene3D; 4.10.60.10; Zinc finger, CCHC-type; 1.
DR InterPro; IPR032567; LDOC1-rel.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR PANTHER; PTHR15503:SF22; CCHC-TYPE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR15503; LDOC1 RELATED; 1.
DR Pfam; PF08284; RVP_2; 1.
DR SMART; SM00343; ZnF_C2HC; 1.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Reference proteome {ECO:0000313|Proteomes:UP000054217};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT DOMAIN 303..316
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..291
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 844 AA; 96018 MW; 63A382AC410A3315 CRC64;
MSDTSSSSDD TSSPESEDSS DTHSMSGSSP SDDSSSSLNS DDGTTGEGDP ESYDGSDDTH
SYHRFVTEGT AYIEDGRVAP KKCAFVLSHY LTGKAYEFYV REVSGDPYKW RLSDFFMELF
NYCFPINFRL WQREKLQACY QNSKTVKNYV YELNELWNMI GETDERAKVH KLWSGLRKEL
QQDLWREKLN LEISSLKRVI ASAEVLEIAQ SITGDYIPKS QRRRSKKRAV ASAATSPEGP
ESSKHERRCH RRKRRDYEPR KEAASTDAHQ SKGKHDGRSD KHKCDTPKLS KDEQEWHKAE
GLCYICHKPG HFSRNCLTRH TVSSLSKPPR VASFGIDVNF GDVECQRQLA KSSNDDTEVT
ANFIHPIGPT ISDEDDDVPD LESIWSDDNS EDAGNRVTTD DDDLPEGMRV YVYSRSQFLG
HRSTGPTFGY PLEEHAIEWL SGICYPGDDQ NSLSMFMDTR FLVYEIGDGL HMIIDSERDV
LGPADAITIE TRLLGNPAFQ LDSWYWFRKG EKAGMTKFDL CQMDRARTWR AAPMGRPIEE
AIETRLKMYS FPVLEGENQD RFACIAKDES TYEVYDYHMA LCFERPAYKL GSQEFDVMHW
HARRLFDACA DLTRSDPTED CDLGLAHLFE RDDDDLKGEW CEPGNDFTHK VPKPLVVVVH
VNGQPAHALI DTGSLADFMS VMLAEQPNVK KIPLEKPLTI QLAVQGSRSR VNFGTKVRFQ
YQGIDCERHF DVMNIQNYDL ILGTPFLYQH QVLVGLHSPR VVIGSKTPME MRGPQVSVLE
SRATEVYQDS IERAQRYLQE LSKPLCSLVG STALPPFCAI NHEVPLIDEK KIYPWRPSKC
PDAL
//