ID A0A137NRG2_CONC2 Unreviewed; 776 AA.
AC A0A137NRG2;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=ATP-dependent metallopeptidase Hfl {ECO:0000313|EMBL:KXN65325.1};
GN ORFNames=CONCODRAFT_13120 {ECO:0000313|EMBL:KXN65325.1};
OS Conidiobolus coronatus (strain ATCC 28846 / CBS 209.66 / NRRL 28638)
OS (Delacroixia coronata).
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota;
OC Entomophthoromycotina; Entomophthoromycetes; Entomophthorales;
OC Ancylistaceae; Conidiobolus.
OX NCBI_TaxID=796925 {ECO:0000313|EMBL:KXN65325.1, ECO:0000313|Proteomes:UP000070444};
RN [1] {ECO:0000313|EMBL:KXN65325.1, ECO:0000313|Proteomes:UP000070444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 28638 {ECO:0000313|EMBL:KXN65325.1,
RC ECO:0000313|Proteomes:UP000070444};
RX PubMed=25977457; DOI=10.1093/gbe/evv090;
RA Chang Y., Wang S., Sekimoto S., Aerts A.L., Choi C., Clum A., LaButti K.M.,
RA Lindquist E.A., Yee Ngan C., Ohm R.A., Salamov A.A., Grigoriev I.V.,
RA Spatafora J.W., Berbee M.L.;
RT "Phylogenomic Analyses Indicate that Early Fungi Evolved Digesting Cell
RT Walls of Algal Ancestors of Land Plants.";
RL Genome Biol. Evol. 7:1590-1601(2015).
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; KQ964910; KXN65325.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A137NRG2; -.
DR STRING; 796925.A0A137NRG2; -.
DR EnsemblFungi; KXN65325; KXN65325; CONCODRAFT_13120.
DR OMA; TLHTDFS; -.
DR OrthoDB; 9585at2759; -.
DR Proteomes; UP000070444; 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; 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 Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000070444}.
FT DOMAIN 379..515
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 776 AA; 86069 MW; 4F793E605C434FF7 CRC64;
MYIPKHFTLP PLTKTKAYNS NKYLTNKYLP ITINQVKRDF LNKYEFIPTN KHTPKREFAY
FELKQIGGLN KRYFDRKLTL TKWDNQARSY KTLSNSLQYW ALNSSQKLTK ISNVSEFSTK
APNHQYLQSG NRNLSNSSNS GRAMLGKLES EANQDPNDLN KQLKFYRELL TNNYYDLIIN
RFETYQLACN LEILQIYIKC LVTTNQTSNL ANKVVQAIRT KPDLRGYFES ADGDTIINNL
LGSSHGGGPL TNGANGSTVS LGSIGQSGAQ GGASGRKGDK FAPIHVVVEQ PKGAALWKTL
KSFGLTLTYI FCILTFLSLA LDNSGLAKPP STSPEYEAET SNSVKFDDVQ GVDEAKQELV
ELVEFLKDPA KFTSLGGKLP KGVLLTGPPG TGKTLLARAV AGQAGVPFFF MSGSEFDEMY
VGVGARRVRE LFAAARRKAP SIVFIDELDA IGARRNPKDQ SYMKQTLNQL LVDLDGFSQT
EGVIFIAATN FPDLLDKALT RPGRFDRHVH VPNPDVRGRL QILKLHSSKI QLADDVNLER
IARGTIGFSG ADLANLVNLA AIEAAKKSSK NVTTVHFEFA KDRIIMGAER KSAVITEESK
RMTAYHEGGH ALVAYFTEGA MPLHKATVIP RGQSLGMVVQ LPEMDKNSFS KKEYRARLDV
CMGGRVAEEL IYGKDNVSSG AQSDLQQATD IARGMIISFG MSDKVGPVEY SNHLNSLSQH
TKQLIEDETK RMLTESYERA KQLLITKRPE LERLAKALVE KETLNLEEIE SVIASN
//
