ID A0A384LFS1_PLAKH Unreviewed; 1506 AA.
AC A0A384LFS1; A0A1A7W1Q3; B3KZP1;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Zinc-carboxypeptidase, putative {ECO:0000313|EMBL:CAA9986367.1};
DE EC=3.4.17.- {ECO:0000313|EMBL:CAA9986367.1};
GN ORFNames=PKNH_0210100 {ECO:0000313|EMBL:CAA9986367.1};
OS Plasmodium knowlesi (strain H).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX NCBI_TaxID=5851 {ECO:0000313|EMBL:CAA9986367.1, ECO:0000313|Proteomes:UP000031513};
RN [1] {ECO:0000313|EMBL:CAA9986367.1, ECO:0000313|Proteomes:UP000031513}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H {ECO:0000313|EMBL:CAA9986367.1,
RC ECO:0000313|Proteomes:UP000031513};
RA Pain A., Boehme U., Berry A.E., Mungall K., Finn R., Jackson A.P.,
RA Mourier T., Mistry J., Pasini E.M., Aslett M., Balasubrammaniam S.,
RA Borgwardt K., Brooks K., Carret C., Carver T.J., Cherevach I.,
RA Chillingworth T., Clarke T.G., Galinski M.R., Hall N., Harper D.,
RA Harris D., Hauser H., Ivens A., Janssen C.S., Keane T., Larke N., Lapp S.,
RA Marti M., Moule S., Meyer I.M., Ormond D., Peters N., Sanders M.,
RA Sanders S., Sergeant T.J., Simmonds M., Smith F., Squares R., Thurston S.,
RA Tivey A.R., Walker D., White B., Zuiderwijk E., Churcher C., Quail M.A.,
RA Cowman A.F., Turner C.M.R., Rajandream M.A., Kocken C.H.M., Thomas A.W.,
RA Newbold C.I., Barrell B.G., Berriman M.;
RT "The genome of Plasmodium knowlesi strain H, a zoonotic malaria parasite
RT with host range from monkey to man.";
RL Nature 455:799-803(2008).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M14 family.
CC {ECO:0000256|ARBA:ARBA00005988}.
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DR EMBL; AM910984; CAA9986367.1; -; Genomic_DNA.
DR RefSeq; XP_002257773.1; XM_002257737.1.
DR STRING; 5851.A0A384LFS1; -.
DR GeneID; 7318645; -.
DR KEGG; pkn:PKNH_0210100; -.
DR VEuPathDB; PlasmoDB:PKNH_0210100; -.
DR InParanoid; A0A384LFS1; -.
DR OMA; ASFAWHD; -.
DR OrthoDB; 168164at2759; -.
DR Proteomes; UP000031513; Chromosome 2.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 2.60.40.3120; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR000834; Peptidase_M14.
DR PANTHER; PTHR12756; CYTOSOLIC CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR12756:SF45; CYTOSOLIC CARBOXYPEPTIDASE NNA1; 1.
DR Pfam; PF00246; Peptidase_M14; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:CAA9986367.1};
KW Hydrolase {ECO:0000313|EMBL:CAA9986367.1};
KW Protease {ECO:0000313|EMBL:CAA9986367.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000031513}.
FT DOMAIN 778..857
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|Pfam:PF00246"
FT REGION 81..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 272..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 702..721
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 739..776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1053..1075
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1169..1261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1363..1387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1466..1506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..97
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..288
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..718
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 752..776
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1177..1192
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1198..1250
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1373..1387
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1506 AA; 170018 MW; 33078335FF61B4C8 CRC64;
MLIEDEDSSS RLHHFDCHSS GPVYLLHYLG VDGECGLRKG VWAEGDVEEA ADKRKRSEEG
ELTICNYKEV VKDALEGNEV KFKSGHPQGE DRNHVDVRGS SGGSGRGRGN TLEANQLDLI
FHESVKAIYE GTNTHVEIPT ITSNGRMYDA PCHLGEEIQT TKVHKNHVYP DRIHMKEMMD
QVNYPHKIEN LKIFLRDRLE NVNEKNRQLF LQSMNTITEI LNYNFLCISR NGSDLDPASF
AWHDSFVSHA MGRAWKHDSL FSPCSVNNAN TGEITGSGKT TNVGKGNWEK GEKTQGKKIP
SVPSSCPSNI YEKLKNVRCL EKPGLTYKYV YPPKYNSDLT REVKVPKGRI LFNAKFESAN
LQYVLKEKNK EVYSIFLNQD MRSNEKKNQW FYFSASYVPE DYYQSDYFEE KKKKKNEQRC
IDEIVNEINR DAHLDNKESL KVSFDFSDMF LVNNLNKLDK PFSVKFKIEN MSRPYFLYKE
GHSPLVFSVC KSVKENIQWE RAAYNVIYTK NENPKYFNIK TNTFEKLSYC TYTLEFSYDF
LYPYDTVYFA SSLPYSYSNL LHYLGLLKSY VHRVQEGEKK INYVQGTLCR TPCGFPCPIL
AITNYDTGEE SSPNGESYDR SAMNNTVQRK LGSSKIEGLY RNSVPKGPYQ EKQVHSVEST
SVPSVENQNL VYVANEAPCQ CSGGNTYIED ARCMYNLCHR KMGSSRKEKE DNPRQRRPRK
YSNSFMRQFE LLLERHSMHP LNHDGGKRPS GSVVSPSLSG SSTHVVSPST VGEPTVQSPR
EEKKIIFLTA RVHPGETNAS YVMHGFLSFI TSDNAYADAL RDNFIFIVIP MLNVDGVVLG
HNRFCSNGFD LNRQWNRPIY YLHQTVHTAK SLIKKIHRNG KIIFFCDFHG HSRKYNCFLF
GNSDSRAHLR GKKLPEVFPH ILGSSLPWFS LEDTKFKGEN MNRGVARHVC GSEFSIDCSY
TFEVSLIGIK MKSNCNGVVP VGGSTNGVGK SNEPIGSIEV TETREGGEGA TCNNTQKYDF
CFYDENILML TGISFGISLF KFFNFLSHHR TAISGGGNQT NKPEMSSPNG NSEMPPSRFK
TNGRVQLGGQ LPCHRNNLKM LGRKKKGEIV MKSNLKEVLP LGSVWVGPTS DGKSALMEPT
TCLKSHLNGG DALEGDSRSS KPYVKVDGEI SFPPGVSTPR SVITSGNGNG NCNKRGGEGE
PNLRKDVAKR DSSVGKGRRE GKEKGLSNRK KEEKEKRRNQ IKESRVQEGT RGTSHNRASV
KNVPTYSMKK KNWLKLLPYK NPFFCSLNGK ISSGGNGRGR LHVKVCRLPG NGDNASKKER
HGNLSSGSNY RTRRRIEHPC LGEDLKANIC EVLQTCGKKP HGYDPQLGGK KRSVGHSHGK
FSRQRKRPLR ITRRKLVIIK KVNSVKGRKA NGTQAKQTKK EEKKNGGLCL NHGELKREYL
ICLKRKKLKR GLGLIKLLRR KVKASGVGRA SDDVVGEAKR KKKKKKKSDP GKGISMNTVV
NGKRES
//
