ID F8Q4F4_SERL3 Unreviewed; 816 AA.
AC F8Q4F4;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EGN97009.1};
GN ORFNames=SERLA73DRAFT_111807 {ECO:0000313|EMBL:EGN97009.1};
OS Serpula lacrymans var. lacrymans (strain S7.3) (Dry rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Coniophorineae; Serpulaceae; Serpula.
OX NCBI_TaxID=936435 {ECO:0000313|Proteomes:UP000008063};
RN [1] {ECO:0000313|Proteomes:UP000008063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=strain S7.3 {ECO:0000313|Proteomes:UP000008063};
RX PubMed=21764756; DOI=10.1126/science.1205411;
RA Eastwood D.C., Floudas D., Binder M., Majcherczyk A., Schneider P.,
RA Aerts A., Asiegbu F.O., Baker S.E., Barry K., Bendiksby M., Blumentritt M.,
RA Coutinho P.M., Cullen D., de Vries R.P., Gathman A., Goodell B.,
RA Henrissat B., Ihrmark K., Kauserud H., Kohler A., LaButti K., Lapidus A.,
RA Lavin J.L., Lee Y.-H., Lindquist E., Lilly W., Lucas S., Morin E.,
RA Murat C., Oguiza J.A., Park J., Pisabarro A.G., Riley R., Rosling A.,
RA Salamov A., Schmidt O., Schmutz J., Skrede I., Stenlid J., Wiebenga A.,
RA Xie X., Kuees U., Hibbett D.S., Hoffmeister D., Hoegberg N., Martin F.,
RA Grigoriev I.V., Watkinson S.C.;
RT "The plant cell wall-decomposing machinery underlies the functional
RT diversity of forest fungi.";
RL Science 333:762-765(2011).
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DR EMBL; GL945483; EGN97009.1; -; Genomic_DNA.
DR AlphaFoldDB; F8Q4F4; -.
DR STRING; 936435.F8Q4F4; -.
DR eggNOG; KOG0730; Eukaryota.
DR HOGENOM; CLU_000688_12_0_1; -.
DR InParanoid; F8Q4F4; -.
DR OMA; HACHDIK; -.
DR OrthoDB; 168438at2759; -.
DR Proteomes; UP000008063; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0043170; P:macromolecule metabolic process; IEA:UniProt.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:UniProt.
DR GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProt.
DR CDD; cd19519; RecA-like_CDC48_r1-like; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.10.330.10; -; 1.
DR Gene3D; 6.10.20.150; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR005938; AAA_ATPase_CDC48.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR004201; Cdc48_dom2.
DR InterPro; IPR029067; CDC48_domain_2-like_sf.
DR InterPro; IPR003338; CDC4_N-term_subdom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR015415; Spast_Vps4_C.
DR NCBIfam; TIGR01243; CDC48; 1.
DR PANTHER; PTHR23077; AAA-FAMILY ATPASE; 1.
DR PANTHER; PTHR23077:SF171; ATPASE FAMILY PROTEIN 2 HOMOLOG; 1.
DR Pfam; PF00004; AAA; 2.
DR Pfam; PF17862; AAA_lid_3; 2.
DR Pfam; PF02933; CDC48_2; 1.
DR Pfam; PF02359; CDC48_N; 1.
DR Pfam; PF09336; Vps4_C; 1.
DR PRINTS; PR00830; ENDOLAPTASE.
DR SMART; SM00382; AAA; 2.
DR SMART; SM01072; CDC48_2; 1.
DR SMART; SM01073; CDC48_N; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF54585; Cdc48 domain 2-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00674; AAA; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000008063}.
FT DOMAIN 29..112
FT /note="CDC48 N-terminal subdomain"
FT /evidence="ECO:0000259|SMART:SM01073"
FT DOMAIN 129..195
FT /note="CDC48"
FT /evidence="ECO:0000259|SMART:SM01072"
FT DOMAIN 241..377
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 514..653
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 711..750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 766..816
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..725
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 766..782
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 816 AA; 89915 MW; 0BBC70ACA5FAFC96 CRC64;
MADPSGAPPQ PGPNDTSTAI LRPKKSPNRL IVDEATSDDN SVATLNPATM ETLQLFRGDT
IIVRGKKRRD TVLICLSSDD VEEGRVQMNK VARNNLRVKL GDLVNVHSCL DIKYGKRVHV
LPFDDSIEGL SGNIFDVYLK PYFLEAYRPV RKGDTFLVRG GMRTVEFKVI ETDPAEFCIV
AQDTVIHTEG DPVKREDEEA NLADVGYDDI GGCRKQMAQI RELVELPLRH PQLFKSIGIK
PPRGILMFGP PGTGKTLMAR AVANETGAFF FLINGPEIMS KMAGESESNL RKAFEEAEKN
SPAIIFIDEI DSIAPKREKT NGEVERRVVS QLLTLMDGLK ARSNVVVMAA TNRPNSIDPA
LRRFGRFDRE VDIGIPDPTG RLEILRIHTK NMKLADDVDL EQIAADTHGY VGSDVASLCS
EAAMQQIREK MDLIDLDEDT IDAEVLDSLG VTMENFRFAL GTSNPSALRE TVVEVPTVTW
DDVGGLDKVK LELQETVQYP VDHPEKFLKY GMSPSKGVLF YGPPGTGKTL LAKAIANECN
ANFISIKGPE LLTMWFGESE ANVRDVFDKA RAAAPCVMFF DELDSIAKAR GGSSGDGGGA
GDRVLNQILT EMDGMNAKKN VFIIGATNRP DQIDSALLRP GRLDQLIYIP LPDEPSRLSI
LTAALKKSPI APDVNLSFLA NRTHGFSGAD LTEICQRAAK LAIRESIESD IRKQREKREK
EEAAGDDAKM EEDEEDDPVP QITKEHFEEA MKYARRSVSD QDIRRYEMFS QNLQQSRGFG
NNFRFPEGQD PSGSAPSAPA GNAGFADDSQ DDDLYA
//
