ID A0A016WA02_9BILA Unreviewed; 1223 AA.
AC A0A016WA02;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Peptidase family M1 {ECO:0008006|Google:ProtNLM};
GN Name=Acey_s0937.g3120 {ECO:0000313|EMBL:EYC36072.1};
GN ORFNames=Y032_0937g3120 {ECO:0000313|EMBL:EYC36072.1};
OS Ancylostoma ceylanicum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=53326 {ECO:0000313|EMBL:EYC36072.1, ECO:0000313|Proteomes:UP000024635};
RN [1] {ECO:0000313|Proteomes:UP000024635}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX PubMed=25730766; DOI=10.1038/ng.3237;
RA Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA Aroian R.V.;
RT "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT ceylanicum identify infection-specific gene families.";
RL Nat. Genet. 47:416-422(2015).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR634016-3};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634016-3};
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136}.
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:EYC36072.1}.
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DR EMBL; JARK01000537; EYC36072.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A016WA02; -.
DR MEROPS; M01.A21; -.
DR Proteomes; UP000024635; Unassembled WGS sequence.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09601; M1_APN-Q_like; 1.
DR Gene3D; 1.25.50.20; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 2.
DR InterPro; IPR045357; Aminopeptidase_N-like_N.
DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR InterPro; IPR024571; ERAP1-like_C_dom.
DR InterPro; IPR034016; M1_APN-typ.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR11533:SF293; AMINOPEPTIDASE-2-RELATED; 1.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR Pfam; PF11838; ERAP1_C; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 2.
DR PRINTS; PR00756; ALADIPTASE.
DR SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 2.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR634016-3};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000024635};
KW Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1223
FT /note="Peptidase family M1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001494304"
FT DOMAIN 87..270
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 305..528
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 611..912
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT DOMAIN 979..1178
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT ACT_SITE 378
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 377
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 381
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 400
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 459
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 1223 AA; 138955 MW; B4C40C447199C0D0 CRC64;
MVDVLARLLL SLTLFGYVTS AQNATLPPPL GKFFDGGYFA HPVYIPPEEV TLDSVLHDIA
RAYDTRTRLP DVMVVSEYFL KIKPYYPAPG IEYNPEKNMT FEGFVSMPAT IKKPTSVLTL
NALNIVAQKV EVTNFMQQQL KVKETKYDKE KQQFAIVMDK ALAPGAVILI SITYTGLINH
FSQAGFFYTY YIDEKHKTNW MVATKLEAFH ARKVFPCMDE PIYKAVFHIE LTYPTAHVAL
SNMLEPESTV LGKGWSHIAF PPTQAMSTYL MVFTIGPYVM HSIRNKDGTL VRSVGWTGQE
PYLEFAAETA GECLYQMGKF SKIKFSMEKC DHLGLPEFPA GAMENYGLVI YKYQSIAINY
KTMTTTDIVE AARVLCHEVA HMWFGNLVTA RWWDNLFVNE GFATYLMRFI GGRVFPQHAA
LEDSLMIRAD LEPALEYDAS PNTHPLIAPD GPYFDRITYK KGASLIRMLN DVLGEDVLWD
GLSSYLTRYS NGNADHKDLW KCLTDASMKA NVPGWCGPLN VTEMMDPYSH KTGFPVVNVH
MSKEGRLTLT QEPFQASSTQ WAIPVRTASY DSPEPRIIWV VPDDADCARK EMRSDASSKR
WEVVSYASAM YGRVHYDDDS FEALLKKIET DDVPVGVKVM LIGDEVALIG RAKKANEPYS
YNRLLDILNT VFHTPNIQND PRYTLIDIAI PQLEFFANVL RDSIDAPLID ALYKNALEVA
YNPKLWEAST SWDINAFAFA YLPVAVRYNI GDSVKKALKL FEEIMADCRV AQSSNGTSWC
TKVPTDLHRA IYCAAAKYDN KIGSNFNSLM YYYNREVQTN PYFYQEYRSL LYGLTCTEGS
QQLRTLVRDF LSSPLQPSLL FGWLKSNPKA SDALLQQIRT RPDSVLSYPG LSTYLDVMTY
NWRSQRRLNQ FLALHEQLRN RLDPEQEKLF VKYEQRIKDN KEWSAEFTPS IVKWMYDNLV
VVEKVPWTKR LPGNLIVSRY DVEITPYIPG SAQYKHSRNL TFDGKITITF GMKSQSNEIV
LDAHRLVIDT DTIKLIDDQN KNIGLNSQLI TKDYDNGMIT MTVDEMLVPR KLYKLTIEYN
GFIFDGPHRG GVVSNHNYYE FNGKKGWIFS TDFEAGPGAR TLMPCADEPA YKAIVKMSVR
HPADLTALSN MMDSGTDIKE NGWAITTYEE SPPMSAYLIA ISVGHFSALT TVSKTGVLTR
AYSWTGMEKY LDYTLMVGFW NLS
//
