ID F0VQ55_NEOCL Unreviewed; 1803 AA.
AC F0VQ55;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Putative dipeptidyl peptidase IV domain-containing protein {ECO:0000313|EMBL:CBZ55852.1};
GN ORFNames=NCLIV_062780 {ECO:0000313|EMBL:CBZ55852.1};
OS Neospora caninum (strain Liverpool).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Neospora.
OX NCBI_TaxID=572307 {ECO:0000313|EMBL:CBZ55852.1, 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).
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DR EMBL; FR823393; CBZ55852.1; -; Genomic_DNA.
DR RefSeq; XP_003885878.1; XM_003885829.1.
DR ESTHER; neocl-f0vq55; DPP4N_Peptidase_S9.
DR GeneID; 13441283; -.
DR VEuPathDB; ToxoDB:NCLIV_062780; -.
DR eggNOG; KOG2281; Eukaryota.
DR InParanoid; F0VQ55; -.
DR OrthoDB; 170111at2759; -.
DR Proteomes; UP000007494; Chromosome XII.
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; 2.
DR Gene3D; 2.140.10.30; Dipeptidylpeptidase IV, N-terminal domain; 2.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001375; Peptidase_S9.
DR InterPro; IPR002469; Peptidase_S9B_N.
DR PANTHER; PTHR11731:SF193; DIPEPTIDYL PEPTIDASE 9; 1.
DR PANTHER; PTHR11731; PROTEASE FAMILY S9B,C DIPEPTIDYL-PEPTIDASE IV-RELATED; 1.
DR Pfam; PF00930; DPPIV_N; 1.
DR Pfam; PF00326; Peptidase_S9; 2.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 2.
DR SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000007494}.
FT DOMAIN 595..653
FT /note="Dipeptidylpeptidase IV N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00930"
FT DOMAIN 1457..1510
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
FT DOMAIN 1682..1791
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
FT REGION 219..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 432..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 478..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 557..588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 664..818
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 943..967
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1031..1053
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1185..1209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1549..1618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1638..1665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..451
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..498
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..583
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 682..711
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 790..818
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 949..966
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1185..1207
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1604..1618
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1640..1665
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1803 AA; 195436 MW; 9C1291D8ECB4CA7C CRC64;
MDDRQTDSFW AFTGEGGCSS AIDSFAFGVN GADIDRLESL SEGVSAPGLS QNCDKFPSDS
ALCVWISWLD CAERGYKRLY GAPVRIPCAN LISRFAKHVS STTVTKDAGI LATADAASLP
SPSHSMRLPL DLQWKAKSPI FPLPIEYTQA DAPPAYPCSR PVSALALSTT PPRFEPASPD
VFYFNNGGCL LVHPDDLHPH SMELYRQAEI AWSSAQRMNA EGGAGGCSSP TGSGNEADSH
TNSAESSVPG RQSQQSRSRE DQFTSEARSG PVPGECKGNA KHSAASGRAD VCGTGGGVTA
PTAGGSQREK RPPKQSLEEE LLNERQRRRC LGISRYVWSK QGKMIMLSNS SGVWIYDGCS
AIESLLAKEA PRTLPLPYPC SASSSLDVGT KPGAVSATGH TGKKSAPASS NVATFFATNR
LSPAAYMVPA TDSGSGRSGG VSGPSPAKTE TSLVETTFRE LDGRLDAEAM VSALDEHFSN
RNPPSFARNQ SSSTDPASRP RVAIHPSGRS HAFGTARLLV PRKKEGGRSI LDCTFSPDAT
RVAFVHESDI HVVALPQTSE NKRLPEGDTV QTGPATSDEV SGAKGSRGQA LNDGLCMLTT
SGRSGKVVNG LAEYVAQEEM YRTRGYWWSP CGDFIAFCRF TEDHIKPLCL QRVRLPQYQA
CEASDRGTVP AGVAAEARKE QTEASPGQSA GRKQVPSSEN EQGSAETQLS HAETAEDAEM
AGEGVQGENA LKKGTERVGD RRRGGAAGVG SALGEEANGG VRQSEEEEWS EDELSSRGCE
APGAVGEERN GHSRPGEKAK AQDKTSIRDG KQKHSEEPED LLVQEEHHFP FAGMENVRIR
VGILQVPSAS ELRRAAACAV SGEAQESSSQ TSLASCDERV ANGDSSTLSV CRLSSASLPG
YSLDHPLEAC ERCTACCACV SATGNPASSQ LCSSPSLPAA RAEDHASAGS LQRRSNASSS
PCPSLACSHR RGTRERFIDL PVHDWNKDFY VARAQWISIA EWSDLVALKL LTREEVEIMQ
AGIRRRERER NEAANAAGYD EARGRGPSGE DAAGLDCSQV SPPPVLLLQL QDRLQQELRI
CAALPWLPSD FLETPRAKPE DEKLRCVVCF TERSHYWINL HDDLHQLGKS LWYLWTAERK
TMNELYLQSE ASPASASVCL ARLPKDSELR ALQLWCRKCG HESEGQAEKR SGDGAMEPED
HGKAGRKRGK FWGQRGTWKI EIRDLLQPWA FVTNPTVEGT HSFVVSEKAP LVVHQHHARL
SPRQIWIRYI PDWDAVLRHA HVSPASPGAQ LHYSLAAAVS RGRAVFGEQL ELFPDKTEKS
GRAQAEQSCA ETGTGEKTKE TCAKEGHERE QRLSPQEADL QLLKGCEHLS YAYGDTAAAG
QVLYEFQQVQ RVYLRVVRSL VPPVPFELEN EGEKLFGCYY RPNVEVHGPG PYRAVVSLYG
GPTLQFVPDA FDLLTDMRAQ ALAKLGLIVV KVDNRGSYGR SIAFEKAAIH RRLGVAELSD
QRAAVMHLYR VGLVALHADE AARVSHVSPS GLASEPCAVP GCALDTAAEP KETQQARAHA
LRQKRGREAA APQGNAGARG KAGEAEERDA SQCTVAASER GGVERASPRG RKRAKTEGIL
GLDCNAERTP AEVPFDEVAE TGQENERDGR SEKAAEGLER EARKRSADIG AIGGDSLVKY
GVGIYGISYG GYLAAMAHFT HPDFFTCCWS AAPVTAWELY STHYTERYLS LPRLNSEGYK
QSSVLNHVKF LEPQTNRLKL LHGYLDENVH MQHSLILLDK MIRHQVRSQV HACLHLKNVR
PYK
//
