ID A0A0C2GQ92_9BILA Unreviewed; 717 AA.
AC A0A0C2GQ92;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=ATP-dependent metallopeptidase HflB {ECO:0000313|EMBL:KIH61264.1};
GN ORFNames=ANCDUO_08470 {ECO:0000313|EMBL:KIH61264.1};
OS Ancylostoma duodenale.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=51022 {ECO:0000313|EMBL:KIH61264.1, ECO:0000313|Proteomes:UP000054047};
RN [1] {ECO:0000313|EMBL:KIH61264.1, ECO:0000313|Proteomes:UP000054047}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Zhejiang {ECO:0000313|EMBL:KIH61264.1,
RC ECO:0000313|Proteomes:UP000054047};
RA Mitreva M.;
RT "Draft genome of the parsitic nematode Ancylostoma duodenale.";
RL Submitted (DEC-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; KN730269; KIH61264.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C2GQ92; -.
DR MEROPS; M41.A11; -.
DR Proteomes; UP000054047; 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; 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 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 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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 Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000054047};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 200..219
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 279..416
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 717 AA; 78901 MW; 943885342BC3A079 CRC64;
MIIAVFKMQV ANGLGAWSSC GYSLQLGPTH RRTVVRRATN DLCRSASYPA VLREIGKDHL
KRALEDGQPL PFITRRAVRR DRFHIRLNGQ LSVCIVPSTG AVMVQERGFR TRRVGNVGIG
GVGSKGDREK NKWSMFADIF GTSKKGKDDP VDGWNQYDSE LKKLPEAQQK TYTEGFVKGL
LASKGSSSSA PKKSSTLTRF YIFLAACIFI GYLTGAIRVR IGDRQFGSLF FSNTQEVKPE
DVQVTFDDVR GMDEAKQEVE EIVSYLRDPE KYSRLGGRLP KGVLLVGPPG TGKTLLARAI
AGEAQVPFFH TSGSEFDEVL VGQGARRVRD LFDKAKARAP CIIFIDEIDS VGSKRVSNSI
HPYANQTINQ LLSEMDGFNR NEGVIVIAAT NRVDDLDKAL LRPGRFDVRV TVPKPDLAGR
TDIFNFYLQR IVHSPGVDPR TLAKGSTGFT GADIENMVNQ AALKAATESA PEVTMQHLDE
ARDRVLMGPA RTGGRIPDEE ANRNTAYHEA GHTLVSLYTK HATPLHKVTI IPRGQSLGHT
AMLPEKDEYQ MTKGQLLAAL DVMMGGRVAE ELVFGDDMVT TGAADDLKKA SQLAVQMVKV
FGMSDKVGLR DFTAEDSSST SLVKISDLSP QTAEAIDKEI NQVLQDSYQR AKDILTKHKK
EHQLLAEALL EYETLSADEV RQVISGKKIK VHVLSGMYIN AELFKLTLCS LIVTRAV
//
