ID A0A1E3NMQ8_9ASCO Unreviewed; 693 AA.
AC A0A1E3NMQ8;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=AAA+ ATPase domain-containing protein {ECO:0000259|SMART:SM00382};
GN ORFNames=PICMEDRAFT_15366 {ECO:0000313|EMBL:ODQ47415.1};
OS Pichia membranifaciens NRRL Y-2026.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Pichia.
OX NCBI_TaxID=763406 {ECO:0000313|EMBL:ODQ47415.1, ECO:0000313|Proteomes:UP000094455};
RN [1] {ECO:0000313|EMBL:ODQ47415.1, ECO:0000313|Proteomes:UP000094455}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-2026 {ECO:0000313|EMBL:ODQ47415.1,
RC ECO:0000313|Proteomes:UP000094455};
RX PubMed=27535936; DOI=10.1073/pnas.1603941113;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goeker M.,
RA Salamov A.A., Wisecaver J.H., Long T.M., Calvey C.H., Aerts A.L.,
RA Barry K.W., Choi C., Clum A., Coughlan A.Y., Deshpande S., Douglass A.P.,
RA Hanson S.J., Klenk H.-P., LaButti K.M., Lapidus A., Lindquist E.A.,
RA Lipzen A.M., Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J.L.,
RA Peng Y., Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C.,
RA Stielow J.B., Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V.,
RA Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:9882-9887(2016).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
CC {ECO:0000256|RuleBase:RU003651}.
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; KV454002; ODQ47415.1; -; Genomic_DNA.
DR RefSeq; XP_019018528.1; XM_019160794.1.
DR AlphaFoldDB; A0A1E3NMQ8; -.
DR STRING; 763406.A0A1E3NMQ8; -.
DR GeneID; 30177481; -.
DR OrthoDB; 9585at2759; -.
DR Proteomes; UP000094455; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 InterPro; IPR048438; Yme1-like_N.
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 Pfam; PF21232; Yme1-like_N; 1.
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 ATP-binding {ECO:0000256|RuleBase:RU003651};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000094455}.
FT DOMAIN 257..393
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 130..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 672..693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 693 AA; 75833 MW; 63A11FD192ACEE01 CRC64;
MLKNGSFLLS SSHMLRPTRC SRAVQAALLH KRLSLVKRFA STVPSTQDLA ALEKEANNEI
ANPSIQAAFY RSLLDASYPH IVVSRYETPG ISTDNDCAKL YLEALLKMGN KEKAETLSKS
LNVPLPALDP SAVSPNATSG NSGNNNNNNN NTNHSGSKQD PIHVVVTETF WMSLSRWIKW
LVPLGLLSYA AYYGFNVLVE NGSIVKGASA DDKSIEVTDS DVRFSDCKGV DEAKAELEEV
VDFLKDPSKY VSLGAELPKG VLLTGPPGTG KTLLARATAG EAGVPFFFMS GSEFDELYVG
VGAKRVRELF SKARARAPAI VFIDELDAIG GKRKSRDQAY AKQTLNQLLV ELDGFSQSEG
IIILGATNFP DSLDKALTRP GRFDKIVPVD LPDVRGRIEI LKQHLKKVSV SKDVDPSVIA
RSTTGLSGAA LKNLVNQAAL YAAQNNALSV NMSDLEWAKD KVLMGGERKT MVMTEETRRN
TAYHEAGHAI AAMFTNGATP LYKATILPRG RALGVTFQLP EMDKHDITKQ ECFARLDVCM
GGKIAEEMLY GPNNVTSGCS SDLSSATGMA RAMVTSYGMS DKVGPVKLSD KWETWSPKLR
DLADQETRDY LIEAEKRCRE LLNDRRIELK RLAEGLLEYE TLSKDEIEKV VRGEKLDKLK
VMTNKVIKGP NTRKEFDVAP EDPQPLGSIG KSF
//
