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Database: UniProt
Entry: A0A0N4X9J0_HAEPC
LinkDB: A0A0N4X9J0_HAEPC
Original site: A0A0N4X9J0_HAEPC 
ID   A0A0N4X9J0_HAEPC        Unreviewed;       642 AA.
AC   A0A0N4X9J0;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Peptidase A2 domain-containing protein {ECO:0000313|WBParaSite:HPLM_0002103201-mRNA-1};
GN   ORFNames=HPLM_LOCUS21024 {ECO:0000313|EMBL:VDO87414.1};
OS   Haemonchus placei (Barber's pole worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Trichostrongylidae; Haemonchus.
OX   NCBI_TaxID=6290 {ECO:0000313|Proteomes:UP000038042, ECO:0000313|WBParaSite:HPLM_0002103201-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:HPLM_0002103201-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDO87414.1, ECO:0000313|Proteomes:UP000268014}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MHpl1 {ECO:0000313|EMBL:VDO87414.1,
RC   ECO:0000313|Proteomes:UP000268014};
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; UZAF01022850; VDO87414.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N4X9J0; -.
DR   STRING; 6290.A0A0N4X9J0; -.
DR   WBParaSite; HPLM_0002103201-mRNA-1; HPLM_0002103201-mRNA-1; HPLM_0002103201.
DR   OMA; ECLSITC; -.
DR   Proteomes; UP000038042; Unplaced.
DR   Proteomes; UP000268014; Unassembled WGS sequence.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 2.40.70.10; Acid Proteases; 1.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR   InterPro; IPR001995; Peptidase_A2_cat.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   PANTHER; PTHR37984; PROTEIN CBG26694; 1.
DR   PANTHER; PTHR37984:SF8; PROTEIN CBG26711; 1.
DR   Pfam; PF13650; Asp_protease_2; 1.
DR   SUPFAM; SSF50630; Acid proteases; 2.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR   PROSITE; PS50175; ASP_PROT_RETROV; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000268014}.
FT   DOMAIN          340..358
FT                   /note="Peptidase A2"
FT                   /evidence="ECO:0000259|PROSITE:PS50175"
FT   REGION          560..642
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        560..577
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        606..620
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        628..642
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   642 AA;  74552 MW;  EF96A5F5A99AC6FE CRC64;
     MAVRAAIINS ETKERLPVII LLDSGAQASF ISKAAVKRHK LNVFEEAPMT ACAFGAALRS
     VIPDVIIGID YLWDILTLQE PVTLPSDNIV IPLNVARYQV NSKSIIRDSR VPEDKKRDLI
     LLKLDDAAYR KYADDILPSQ PHEIDFNTTV RNLQKLFTSK KTLIRRRYEC LSITCPPLTQ
     DNVPFRDYAN TIKRMDEDAA LKEMDYTSMK TLQFVARLQD PSLLKIRLRM LRRLDTQAED
     VPLTIEDLVA ECENITALKV DNANMEASHD VHAVQKKKVK CFECGGPHYK TFCPLLMKQF
     PKKPKRMHHR LKRNKCKDVA TFSAEHARTY INVDVSGHKL RFQLDTGADI TLISRHTWKK
     LGFPALEPYA TPVKTADGSP MKIDGRFHIE FSVKDRPAYK ELQEKYHSRM GIEHIRSPPL
     HPQSNGAFRR HAEESFTQIE GRRELLTEFL KCYRRMPCTT TPKQLSPAEL FLGRQLRTTL
     TLLKEEIRNE KGSRKTRMER QHNLHHEARE RSYDIEDPVY IRNYRSGEQN WIPAHVKNLY
     GRVLYDVSME DGQLWRRHTN QMRTRSQPSA TDQAKKTVGE HSQYENPQEK YNVVHNEEVQ
     PTRDFSDESM DPNATATVLD RMNRQRRPPN RLQVRPRKKT YM
//
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