YME1_SCHMA
ID YME1_SCHMA Reviewed; 662 AA.
AC P46508;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=ATP-dependent zinc metalloprotease YME1 homolog;
DE EC=3.4.24.-;
OS Schistosoma mansoni (Blood fluke).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6183;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Liberian;
RA Menrath M.;
RL Thesis (1994), Heinrich-Heine University / Duesseldorf, Germany.
CC -!- FUNCTION: Putative ATP-dependent protease.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000305};
CC -!- SIMILARITY: In the N-terminal section; belongs to the AAA ATPase
CC family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the peptidase M41
CC family. {ECO:0000305}.
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DR EMBL; Z29947; CAA82844.1; -; mRNA.
DR PIR; S42826; S42826.
DR AlphaFoldDB; P46508; -.
DR SMR; P46508; -.
DR MEROPS; M41.A11; -.
DR eggNOG; KOG0734; Eukaryota.
DR Proteomes; UP000008854; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.20.58.760; -; 1.
DR Gene3D; 3.40.50.300; -; 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 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; SSF140990; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01241; FtsH_fam; 1.
DR PROSITE; PS00674; AAA; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Hydrolase; Metal-binding; Metalloprotease; Nucleotide-binding;
KW Protease; Reference proteome; Zinc.
FT CHAIN 1..662
FT /note="ATP-dependent zinc metalloprotease YME1 homolog"
FT /id="PRO_0000084666"
FT ACT_SITE 426
FT /evidence="ECO:0000250"
FT BINDING 206..213
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 425
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 429
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 503
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 662 AA; 72940 MW; 8D36F28A9ACBBB75 CRC64;
MIVSPCCRII RTCCVSNRGT FHSRLAALYP SYIKIPNNHA RIFVTKSRKI NRPSSSFIID
TKEARQRNSD SSTVSSDLDE ILKDQTPSAQ LRLVDAYRRG FQSSTDSGKS SNKMQMWRTI
IIKTILFGVV SCFTIVFLKK TLVGTFPKFL DQNIGSFAEN TDVSFSDVQG CDEVKKELVD
VVEFLRNPEK FNQIGAKLPK GVLLVGPPGV GKTLLAKAVS GEAQVPFLYA SGSSFDEVLV
GLGASRIRQL FTTAKQNSPC LVFIDEIDSV GGNRTFSPHH PFANQTINQL LAEMDGFQSK
EGIIVLGATN QAEVLDKALL RPGRFDVQIH VSPPTYEGRI ALLNLYLKKV KTGSNIDIEK
LAHGTVGYTG ADIQNLVNQA AIAAALRNDP FVEMHHLWDA RDRLIMGPAK RRPLDDQTNR
VSAFHEAGHA LVALLTADSI PLHKVTIIPR GEAGGLTSFL QEKDISFMTR AQLLAQLDVL
MGGRVGEELV FGADKVTNGA ADDFRKATIL AQNMVKRFGF SSKIGPRVIP DTQDEQLGEA
TRDLIDKEVD QLLNDSLTRV RTLLSSQSKQ HKLLAEALLH FETLTKDEVL AVLAGKMKPP
KTQSVTSKST TLLPQLGPST STEIPRMIVS LIIVHVVDFI SFFCPFKDTL HTYTHTHKLL
FS