ID A0A0R3SCF7_HYMDI Unreviewed; 984 AA.
AC A0A0R3SCF7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 22-FEB-2023, entry version 28.
DE RecName: Full=Aspartyl aminopeptidase {ECO:0000256|ARBA:ARBA00015118};
DE EC=3.4.11.21 {ECO:0000256|ARBA:ARBA00011965};
GN ORFNames=HDID_LOCUS2263 {ECO:0000313|EMBL:VDL19724.1};
OS Hymenolepis diminuta (Rat tapeworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Hymenolepididae; Hymenolepis.
OX NCBI_TaxID=6216 {ECO:0000313|Proteomes:UP000046397, ECO:0000313|WBParaSite:HDID_0000226201-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:HDID_0000226201-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDL19724.1, ECO:0000313|Proteomes:UP000274504}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal aspartate or glutamate from a
CC peptide, with a preference for aspartate.; EC=3.4.11.21;
CC Evidence={ECO:0000256|ARBA:ARBA00001335};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBUNIT: Tetrahedron-shaped homododecamer built from six homodimers.
CC {ECO:0000256|ARBA:ARBA00011395}.
CC -!- SIMILARITY: Belongs to the peptidase M18 family.
CC {ECO:0000256|ARBA:ARBA00008290}.
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DR EMBL; UYSG01000534; VDL19724.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R3SCF7; -.
DR STRING; 6216.A0A0R3SCF7; -.
DR WBParaSite; HDID_0000226201-mRNA-1; HDID_0000226201-mRNA-1; HDID_0000226201.
DR Proteomes; UP000046397; Unplaced.
DR Proteomes; UP000274504; Unassembled WGS sequence.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
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; cd05658; M18_DAP; 1.
DR Gene3D; 2.30.250.10; Aminopeptidase i, Domain 2; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR007889; HTH_Psq.
DR InterPro; IPR001948; Peptidase_M18.
DR InterPro; IPR023358; Peptidase_M18_dom2.
DR PANTHER; PTHR28570; ASPARTYL AMINOPEPTIDASE; 1.
DR PANTHER; PTHR28570:SF3; ASPARTYL AMINOPEPTIDASE; 1.
DR Pfam; PF05225; HTH_psq; 1.
DR Pfam; PF02127; Peptidase_M18; 1.
DR PRINTS; PR00932; AMINO1PTASE.
DR SUPFAM; SSF101821; Aminopeptidase/glucanase lid domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000274504};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 113..149
FT /note="HTH psq-type"
FT /evidence="ECO:0000259|Pfam:PF05225"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 74..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 264..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..99
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 984 AA; 104379 MW; 6C79D193CB5D3E80 CRC64;
MANIDPNASS NGGMNTTPPI DVTSSSITAP SSTVVSMESS NFSADISLPL TLPSSNSTPT
TTSSSTDVVV KTESLSNAPT STPVITSTTT ATTTTTRSPP LKRPRHKPGE RKELLERAVR
DVREENISMR KAASRYNLAK SSLCDYVRKN HIVLPNNRCR PSAAASAAAA AAAANNSNST
NHQNHLGGGS LLSGMQQQHQ QSLNHAGGGG GGLFNLSAES MRNNHPTTTK LESPWSNVSG
LPTQVPMQNW SSFPLTSLKT LSGLTHISST PSPKQQHNEI SNSDVHSPLE DNLNGNTAVN
TSSSTSFICT PITSETIEGQ SITTTAPFFN STPAAAAQLL NPTGVDAARS LATIYAASTQ
QQNNSNNNNA NSQLTPNLLP TVTQSTPTLP NAAAASVPLV FPNPDTSVLN DSLQRILLAA
RGQPNFGDLF LPPPAPSPVI NCFSSIPPEM KNKLTLPNIL SSLISANTVN TNSATNTTTN
SNACSGAAAV VTDNAIARMP HSQKVVNDLI RFINMSPTPF HVVRSAVEML KKAGFRQLLE
RDAWKLQPND CVFVTKNQST LFAVAVGGAY KPGEGLSMIG AHTDSPCLRL KPISERVKEG
FVQLGVQTYG GGLWYTWFDR ELSLAGRVII RNSSTGALEE HLIHINRPLA CIPSLAIHLN
RNANKSFAPD PETHLAPIIS TTIMEQLSGG EDGEISIGGH PAGLMRLIAA ELQCAPSDIV
DLELYLTDTQ PACIGGLHGE FVHAPRLDNQ FGAFTSLSAL VNSLPSLEDD SNIRVVCLYD
HEEIGSRSCQ GAASVLTEHF LRRIIQALAD GAAVETVDNN GGGSNAMDST TSIPSAEGCI
FERSLARSFF LSADQAHAVH PSWSEKHEPA HKPAFHQGLV IKHNVAQSYA TNSQTSAIVK
EIAKRSNVPL QEFVVRQDVP SGSTIGPIVA SHLGVMTADV GGAQLAMHSC REITCTSSVD
HAVALFTGYF EQLANIMTNF GHAK
//
