ID F0VQD4_NEOCL Unreviewed; 892 AA.
AC F0VQD4;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=acylaminoacyl-peptidase {ECO:0000256|ARBA:ARBA00012917};
DE EC=3.4.19.1 {ECO:0000256|ARBA:ARBA00012917};
GN ORFNames=NCLIV_063570 {ECO:0000313|EMBL:CBZ55931.1};
OS Neospora caninum (strain Liverpool).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Neospora.
OX NCBI_TaxID=572307 {ECO:0000313|EMBL:CBZ55931.1, ECO:0000313|Proteomes:UP000007494};
RN [1] {ECO:0000313|Proteomes:UP000007494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Liverpool {ECO:0000313|Proteomes:UP000007494};
RX PubMed=22457617; DOI=10.1371/journal.ppat.1002567;
RA Reid A.J., Vermont S.J., Cotton J.A., Harris D., Hill-Cawthorne G.A.,
RA Konen-Waisman S., Latham S.M., Mourier T., Norton R., Quail M.A.,
RA Sanders M., Shanmugam D., Sohal A., Wasmuth J.D., Brunk B., Grigg M.E.,
RA Howard J.C., Parkinson J., Roos D.S., Trees A.J., Berriman M., Pain A.,
RA Wastling J.M.;
RT "Comparative genomics of the apicomplexan parasites Toxoplasma gondii and
RT Neospora caninum: Coccidia differing in host range and transmission
RT strategy.";
RL PLoS Pathog. 8:e1002567-e1002567(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of an N-acetyl or N-formyl amino acid from the N-
CC terminus of a polypeptide.; EC=3.4.19.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000721};
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; FR823393; CBZ55931.1; -; Genomic_DNA.
DR RefSeq; XP_003885957.1; XM_003885908.1.
DR AlphaFoldDB; F0VQD4; -.
DR GeneID; 13445154; -.
DR VEuPathDB; ToxoDB:NCLIV_063570; -.
DR eggNOG; KOG2100; Eukaryota.
DR InParanoid; F0VQD4; -.
DR OrthoDB; 2877590at2759; -.
DR Proteomes; UP000007494; Chromosome XII.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR045550; AARE_N.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001375; Peptidase_S9.
DR PANTHER; PTHR42776:SF4; ACYLAMINO-ACID-RELEASING ENZYME; 1.
DR PANTHER; PTHR42776; SERINE PEPTIDASE S9 FAMILY MEMBER; 1.
DR Pfam; PF19283; APEH_N; 1.
DR Pfam; PF00326; Peptidase_S9; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000007494}.
FT DOMAIN 168..291
FT /note="Acylamino-acid-releasing enzyme N-terminal"
FT /evidence="ECO:0000259|Pfam:PF19283"
FT DOMAIN 661..873
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
FT REGION 183..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 892 AA; 96960 MW; D7A507A59E85F8B6 CRC64;
MHCTMGGSGC PQPAAGDQTK RLREAFSVCS ESVIQCLSAR IAATKSSDPS QDAIVVLGQQ
KVLNERRVVG MTARVPNCDL LTAWPLGLPS ALTVLSPSAH FFASVVEATP PNAKKKPRPS
FPQASAADYR IELFGRGPVH TGPVVTVSAP RDTKPWNSSV GGGVFCPERE ELFVYVAEAS
KRDDNDASSG STSDGTGETS DGDSLDTYEF KTHWGEQLVG HRRGRLVLTD FKRRTAQLLK
PPKKETACGQ PRFLSDGSGV VCSNWELDPY CLGLIYCMNR ASKVLLAQLP SSTSEEGKAG
EKADEETKES TVECEWIQIS GDEDFAAWSP TVLHTRDGSD PNTQRIAFLC LEKDKVCPAS
VCARFPLSTR IPAGLEGGEA GKTDRVFHLS CEEPSVRRRM ALQRTSRVPS LLAFQPETLP
HMCAPRIKAV TLRRKNACSS WEVVERQTLA QAVSVPPQSE SLFSRQSVPY TGIYTDRLGP
WVHNDFLFLN TFVGARRTVV VVDAHGGGCV GELCLEEEAL RAKPCAASKV EASCPPGSIL
LHDVTSDWLL LESSSARHIP RLMLAKLLLS PSGAQSPQSG RGFHIRVAGS VSLGGPSDPQ
RLLPWSPFAR LTTHLERLEV RYLSDNRHIL LRWKESPRRD GKRALAVVLH GGPHSVWANI
FSAEAVYLTF LGFDVLAVNY RGSLGFGQAE LLSLLGNVGR QDVDDVKQAV TDFIDSDPEA
YSPARAVVVG GSHGGFLTCH LIGQFPDMFA AASTRNPVTN LASMVVESDI PDWCAAEALR
ERLNPSFVLS ETDVVALYKA SPVAYARHVK TPLLLGIGGA DLRVPACQGI AFHKMLLGQG
SPTRLLFYPE EDHRIDRPSC SEDYWVNTAL WFAGYTGTLE ALKEDVLPAA PH
//