ID S2KE31_MUCC1 Unreviewed; 683 AA.
AC S2KE31;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=ATP-dependent metalloprotease {ECO:0000313|EMBL:EPB90620.1};
GN ORFNames=HMPREF1544_02530 {ECO:0000313|EMBL:EPB90620.1};
OS Mucor circinelloides f. circinelloides (strain 1006PhL) (Mucormycosis
OS agent) (Calyptromyces circinelloides).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX NCBI_TaxID=1220926 {ECO:0000313|EMBL:EPB90620.1, ECO:0000313|Proteomes:UP000014254};
RN [1] {ECO:0000313|Proteomes:UP000014254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1006PhL {ECO:0000313|Proteomes:UP000014254};
RG The Broad Institute Genomics Platform;
RA Cuomo C., Earl A., Findley K., Lee S.C., Walker B., Young S., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome sequence of Mucor circinelloides f. circinelloides 1006PhL.";
RL Submitted (MAY-2013) 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}.
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DR EMBL; KE123918; EPB90620.1; -; Genomic_DNA.
DR AlphaFoldDB; S2KE31; -.
DR STRING; 1220926.S2KE31; -.
DR MEROPS; M41.004; -.
DR VEuPathDB; FungiDB:HMPREF1544_02530; -.
DR eggNOG; KOG0734; Eukaryota.
DR InParanoid; S2KE31; -.
DR OMA; RCWPVYV; -.
DR OrthoDB; 9585at2759; -.
DR Proteomes; UP000014254; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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: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; 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 NCBIfam; TIGR01241; FtsH_fam; 1.
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.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000313|EMBL:EPB90620.1};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:EPB90620.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000014254};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 202..221
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 279..415
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 683 AA; 75753 MW; B9816A34912FDD9A CRC64;
MLKANPSIAL NMARFIPKEN FKTKAFQPIQ QQQHRTLFSS SGGSNRIINY RRLNKLEQEA
NASPTDAFKQ ATLYKEWLRS NNPQAVITRF ERGNFTHNEE CWQYYIAALA QTGKSEAVLP
RILQKLEESG SHKLSEAAGG NNQNTLTKEI IQQVIASRQG GRAVNIEGAG GAIASGSGNK
SNPIYVVVEE ARKYMFWKAL RWVGVTLTYA FCILTILSLA LENSGLLKAA NSQTEYEPVT
QTTVRFEDVQ GVDEAKQELE EIVEFLKNPH RFTELGGKLP KGVLLTGPPG TGKTMLARAV
AGEANVPFFF MSGSEFDEMY VGVGARRVRE LFAAARAKAP SIVFIDEIDA IGSKRNPKDQ
SYMKQTLNQL LVDLDGFSQT EGVIFIAATN FPELLDKALV RPGRFDRTVN VPLPDVRGRI
EILKHHMKKI HVASEVDVSV VARGTPGFSG ADLANLVNQA AIQASRENCK EVNLRHLEYS
KDKIIMGAER KSAVITEENK RLTAYHEGGH ALVAYYTPGA MPLHKATIMP RGSALGMTVQ
LPEMDKDSFT KKEFLAQIDV CMGGRVAEEL IFGQDNVTSG ASSDIMKATD VAKRMVRYYG
MSEKVGPVNH DDDDMQLLST QTKQLIESEI LNLIESSEKR AKHILVEHRE ELDRLANALV
EYETLDYQEI IDALAGKPIS RSK
//
