ID U5H2Z6_USTV1 Unreviewed; 851 AA.
AC U5H2Z6;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=AAA+ ATPase domain-containing protein {ECO:0000259|SMART:SM00382};
GN ORFNames=MVLG_01724 {ECO:0000313|EMBL:KDE08022.1};
OS Microbotryum lychnidis-dioicae (strain p1A1 Lamole / MvSl-1064) (Anther
OS smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Microbotryales; Microbotryaceae; Microbotryum.
OX NCBI_TaxID=683840 {ECO:0000313|EMBL:KDE08022.1};
RN [1] {ECO:0000313|Proteomes:UP000017200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=p1A1 Lamole {ECO:0000313|Proteomes:UP000017200};
RA Cuomo C., Perlin M., Young S.K., Zeng Q., Gargeya S., Alvarado L.,
RA Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heilman E., Heiman D., Howarth C., Mehta T.,
RA Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C., Birren B.;
RT "The genome sequence of Microbotryum violaceum strain p1A1 Lamole.";
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KDE08022.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=P1A1 Lamole {ECO:0000313|EMBL:KDE08022.1};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Butler R., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heilman E., Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P.,
RA Mehta T., Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M.,
RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S.,
RA White J., Yandava C., Wortman J., Nusbaum C., Birren B.;
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KDE08022.1, ECO:0000313|Proteomes:UP000017200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=p1A1 Lamole {ECO:0000313|Proteomes:UP000017200}, and P1A1
RC Lamole {ECO:0000313|EMBL:KDE08022.1};
RX PubMed=26076695; DOI=10.1186/s12864-015-1660-8;
RA Perlin M.H., Amselem J., Fontanillas E., Toh S.S., Chen Z., Goldberg J.,
RA Duplessis S., Henrissat B., Young S., Zeng Q., Aguileta G., Petit E.,
RA Badouin H., Andrews J., Razeeq D., Gabaldon T., Quesneville H., Giraud T.,
RA Hood M.E., Schultz D.J., Cuomo C.A.;
RT "Sex and parasites: genomic and transcriptomic analysis of Microbotryum
RT lychnidis-dioicae, the biotrophic and plant-castrating anther smut
RT fungus.";
RL BMC Genomics 16:461-461(2015).
RN [4] {ECO:0000313|EnsemblFungi:MVLG_01724T0}
RP IDENTIFICATION.
RG EnsemblFungi;
RL Submitted (JUN-2015) to UniProtKB.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: In the C-terminal section; belongs to the peptidase M41
CC family. {ECO:0000256|ARBA:ARBA00010044}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the AAA ATPase
CC family. {ECO:0000256|ARBA:ARBA00010550}.
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DR EMBL; AEIJ01000165; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; GL541653; KDE08022.1; -; Genomic_DNA.
DR AlphaFoldDB; U5H2Z6; -.
DR STRING; 683840.U5H2Z6; -.
DR EnsemblFungi; MVLG_01724T0; MVLG_01724T0; MVLG_01724.
DR HOGENOM; CLU_000688_9_2_1; -.
DR InParanoid; U5H2Z6; -.
DR OrthoDB; 9585at2759; -.
DR Proteomes; UP000017200; Unassembled WGS sequence.
DR GO; GO:0031942; C:i-AAA complex; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:EnsemblFungi.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; IEA:EnsemblFungi.
DR GO; GO:0045041; P:protein import into mitochondrial intermembrane space; IEA:EnsemblFungi.
DR GO; GO:0030150; P:protein import into mitochondrial matrix; IEA:EnsemblFungi.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IEA:EnsemblFungi.
DR CDD; cd19501; RecA-like_FtsH; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.20.58.760; Peptidase M41; 1.
DR HAMAP; MF_01458; FtsH; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR005936; FtsH.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000642; Peptidase_M41.
DR InterPro; IPR037219; Peptidase_M41-like.
DR PANTHER; PTHR23076:SF37; ATP-DEPENDENT ZINC METALLOPROTEASE YME1L1; 1.
DR PANTHER; PTHR23076; METALLOPROTEASE M41 FTSH; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF01434; Peptidase_M41; 1.
DR PRINTS; PR00830; ENDOLAPTASE.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF140990; FtsH protease domain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00674; AAA; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000017200};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 356..375
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 442..578
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 42..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 251..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 387..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 791..818
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 264..283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 851 AA; 91025 MW; 7F248446BE4C8114 CRC64;
MSTSIAMTMQ RQRHTLRSVL TTAIASTRLT RPLPAAAFGE RTSIVPSSQG GSSRFASTLS
STSSAVRRNS SSSSSPSPSW QRAVSNSTNQ TFARTFSAVP TTATSTTRHP FSTSALARAQ
PTSSAAAWSS PFGRFNTLSS LRTKASNDPS NLPLQRQLFT KLLHSPKPQD QEELIGRYEE
LSGLWMVEPA PSTTAVTTEQ QVTLLNDDEL FAAYLRALAA RAAVESDPSS YFAKLNTAWP
IRQGKLAPST TAIPAAPSTA EAEATAAAAS TSTPSSTSST ASAPFTTPAL TPAALVTALF
SGAGGRGKGG DARVVSGGSS WPFSSGSSST SSGGPEPIRV VVEEVKSPLA LRMLRFILVT
VLYSFLLLSL LSLLLDSSGI LRAGAAQTTP FQTTPPPDPH DPSGRGTTFK DVHGVEEAKE
ELYEIVEFLK DPERFSKLGG RLPRGVLLTG PPGTGKTLLA RAVAGEAGVS FFSASGSEFD
EMYVGVGARR IRELFATARK NAPSIIFIDE IDAIGGKRSP RDQHYIKQTL NQLLTELDGF
SPGEGVILIG ATNFPESLDK ALVRAGRFDR IVAVPLPDVR GRAEILKHHM RNIQFDRAQV
DITTLARGTI GFSGADLQAL VNQAAVKASS DHASAVRSSH FEWAKERIMM GAARKSAFIS
ETDKLATAYH EGGHALVALY TKGAYPLQSI TVVPRGNALG YTLMLPEADK NSHSLSEYRA
KLDVAMGGRV AEELIYGKDH VTDGASSDIS NATSMASNMV RRFGFSDLIG PVAHSNDPDS
QTSPDTQAKI EQEVRGMIEE AQNRARDLLL ERKEELDRLA KALVRYETLT LKEVEKVVKG
EEIEKDPLDL V
//
