ID D2V1X7_NAEGR Unreviewed; 310 AA.
AC D2V1X7;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Predicted protein {ECO:0000313|EMBL:EFC49237.1};
GN ORFNames=NAEGRDRAFT_30261 {ECO:0000313|EMBL:EFC49237.1};
OS Naegleria gruberi (Amoeba).
OC Eukaryota; Discoba; Heterolobosea; Tetramitia; Eutetramitia;
OC Vahlkampfiidae; Naegleria.
OX NCBI_TaxID=5762 {ECO:0000313|Proteomes:UP000006671};
RN [1] {ECO:0000313|EMBL:EFC49237.1, ECO:0000313|Proteomes:UP000006671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEG-M {ECO:0000313|EMBL:EFC49237.1,
RC ECO:0000313|Proteomes:UP000006671};
RX PubMed=20211133; DOI=10.1016/j.cell.2010.01.032;
RA Fritz-Laylin L.K., Prochnik S.E., Ginger M.L., Dacks J.B., Carpenter M.L.,
RA Field M.C., Kuo A., Paredez A., Chapman J., Pham J., Shu S., Neupane R.,
RA Cipriano M., Mancuso J., Tu H., Salamov A., Lindquist E., Shapiro H.,
RA Lucas S., Grigoriev I.V., Cande W.Z., Fulton C., Rokhsar D.S., Dawson S.C.;
RT "The genome of Naegleria gruberi illuminates early eukaryotic
RT versatility.";
RL Cell 140:631-642(2010).
CC -!- SIMILARITY: Belongs to the peptidase C1 family.
CC {ECO:0000256|ARBA:ARBA00008455}.
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DR EMBL; GG738848; EFC49237.1; -; Genomic_DNA.
DR RefSeq; XP_002681981.1; XM_002681935.1.
DR AlphaFoldDB; D2V1X7; -.
DR STRING; 5762.D2V1X7; -.
DR EnsemblProtists; EFC49237; EFC49237; NAEGRDRAFT_30261.
DR GeneID; 8862556; -.
DR VEuPathDB; AmoebaDB:NAEGRDRAFT_71406; -.
DR eggNOG; KOG1543; Eukaryota.
DR InParanoid; D2V1X7; -.
DR OMA; NRTSTDY; -.
DR OrthoDB; 5471028at2759; -.
DR Proteomes; UP000006671; Unassembled WGS sequence.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd02620; Peptidase_C1A_CathepsinB; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR025661; Pept_asp_AS.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR025660; Pept_his_AS.
DR InterPro; IPR013128; Peptidase_C1A.
DR InterPro; IPR000668; Peptidase_C1A_C.
DR PANTHER; PTHR12411:SF895; CATHEPSIN B; 1.
DR PANTHER; PTHR12411; CYSTEINE PROTEASE FAMILY C1-RELATED; 1.
DR Pfam; PF00112; Peptidase_C1; 1.
DR PRINTS; PR00705; PAPAIN.
DR SMART; SM00645; Pept_C1; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Reference proteome {ECO:0000313|Proteomes:UP000006671}.
FT DOMAIN 88..307
FT /note="Peptidase C1A papain C-terminal"
FT /evidence="ECO:0000259|SMART:SM00645"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 310 AA; 33997 MW; 6F2EA32EE70A28EE CRC64;
MPPKHNNTHP VHPTHPIANH THANTPVNDK SLIDRINSNH THGWKATEYS RFDNMTISQL
RDNLFGLSLM SSDEDTPRMA SIETRVDIPM NFDARTQWKG CVPAIRDQQT CGACWAFSAN
YVLAHRLCIA TNGKTNVVLS PEYQVQCDTM NKACQGGYLK YSWTFLENTG TPLDTCIPYA
SGRGTFSSGT CPTQCKIASM SMSKYKAKNT VYISGINNIK TAIMTYGSVQ AGFTVYRDLT
GYKSGVYKHV VSTVLGGHAV ALIGFGVEGG SNYWLAANSW GPNWGMSGYF KIAQGEGGIE
NQVYAGEAVY
//
