ID A0A397T7F7_9GLOM Unreviewed; 740 AA.
AC A0A397T7F7;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Peptidase family M41-domain-containing protein {ECO:0000313|EMBL:RIA93239.1};
GN ORFNames=C1645_796644 {ECO:0000313|EMBL:RIA93239.1};
OS Glomus cerebriforme.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Glomerales; Glomeraceae; Glomus.
OX NCBI_TaxID=658196 {ECO:0000313|EMBL:RIA93239.1, ECO:0000313|Proteomes:UP000265703};
RN [1] {ECO:0000313|EMBL:RIA93239.1, ECO:0000313|Proteomes:UP000265703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAOM 227022 {ECO:0000313|EMBL:RIA93239.1,
RC ECO:0000313|Proteomes:UP000265703};
RA Morin E., San Clemente H., Chen E.C.H., De La Providencia I., Hainaut M.,
RA Kuo A., Kohler A., Murat C., Tang N., Roy S., Loubradou J., Henrissat B.,
RA Grigoriev I.V., Corradi N., Roux C., Martin F.M.;
RT "Comparative genomics reveals the genomic features of Rhizophagus
RT irregularis, R. cerebriforme, R. diaphanum and Gigaspora rosea, and their
RT symbiotic lifestyle signature.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RIA93239.1}.
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DR EMBL; QKYT01000108; RIA93239.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A397T7F7; -.
DR STRING; 658196.A0A397T7F7; -.
DR Proteomes; UP000265703; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
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:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; 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; 3.40.1690.20; -; 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; IPR011546; Pept_M41_FtsH_extracell.
DR InterPro; IPR000642; Peptidase_M41.
DR InterPro; IPR037219; Peptidase_M41-like.
DR NCBIfam; TIGR01241; FtsH_fam; 1.
DR PANTHER; PTHR43655; ATP-DEPENDENT PROTEASE; 1.
DR PANTHER; PTHR43655:SF2; SD01613P; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF06480; FtsH_ext; 1.
DR Pfam; PF01434; Peptidase_M41; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000265703}.
FT DOMAIN 297..437
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 1..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 713..740
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 740 AA; 82357 MW; 7A875F81CFC8EEDD CRC64;
MYATETNQPF NKENEKESEN KEGNKDSDKE KKSDNKNEIK IPKGFENFFN KNSQRMKQNI
KEQAPKSTQS NHKSEQQKQP PKQPPNVKDF NMQLNLNTLL PLLFSAYILY KITSGVDNSR
EITWQEFRTA FLDKGLVDKL VVINRKKVRV YLHSNATGQM YPNAPSLPGT TYYFSIGSVE
AFERKLDAAQ KELGIPSTER IPVAYHDEIS LMNTLLHFAP TLLLAGALFY ITRRAGGAAG
SQIFGIGKSK AKLFNQETEV KVKFKDVAGM DEAKEEIMEF VKFLKDPTAY ERLGAKIPKG
AILSGPPGTG KTLLAKATAG EAGVPFLSVS GSEFVEMFVG VGPSRVRDLF ANAKKHAPCI
IFVDEIDAIG KSRGKIGQFG GNDERESTLN QLLVEMDGFG SSEHVVVLAG TNRPDVLDPA
LMRPGRFDRH IAIDKPDIKG RSAIFKVHLK PIKTKENIDN LSNKLAALTP GFSGADIANV
CNEAALIAAR FHNDSVTKEH FEQAIDRVIA GLERKSRVLS PEEKKTVAYH EAGHAVAGWF
LEHADPLLKV TIIPRGVAAL GYAQYLPKDQ YLYSTAQLLD RMCMTLGGRV SEQIFFNMIT
TGAHDDLQRV TKLAYAQVTT YGMNPNVGPL SFNNPNDNEP QFQKPYSEET ARMIDEEVRK
LVAVAYERTV KLLTDKKNDV EKVAQLLLSK EVLNREDMIS LLGKRPFVEK NPFEEYITPK
ENTPSPPPPL TEQSQSSSNI
//
