ID D2V753_NAEGR Unreviewed; 1498 AA.
AC D2V753;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Subtilisin-like serine peptidase {ECO:0000313|EMBL:EFC47310.1};
GN ORFNames=NAEGRDRAFT_64673 {ECO:0000313|EMBL:EFC47310.1};
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:EFC47310.1, ECO:0000313|Proteomes:UP000006671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEG-M {ECO:0000313|EMBL:EFC47310.1,
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 S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR EMBL; GG738855; EFC47310.1; -; Genomic_DNA.
DR RefSeq; XP_002680054.1; XM_002680008.1.
DR STRING; 5762.D2V753; -.
DR EnsemblProtists; EFC47310; EFC47310; NAEGRDRAFT_64673.
DR GeneID; 8860427; -.
DR VEuPathDB; AmoebaDB:NAEGRDRAFT_64673; -.
DR eggNOG; KOG4266; Eukaryota.
DR InParanoid; D2V753; -.
DR OrthoDB; 5606at2759; -.
DR Proteomes; UP000006671; Unassembled WGS sequence.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR PANTHER; PTHR43806:SF7; MEMBRANE-BOUND TRANSCRIPTION FACTOR SITE-1 PROTEASE; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000006671};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 696..1012
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT REGION 95..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 209..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 359..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 509..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..297
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 705
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 738
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 934
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1498 AA; 169468 MW; 0E0F5BEFA5CFDAA6 CRC64;
MPTIVTVGAD EDDEYFDEEE KAKILQEEKA FSTSMNSSTF NENLQASELI GSKVDEIEEG
MDAEQFMPEV RDIELKNIVE EHVLDRVDNN FSPMMTDTYD IDSRASSSMS SDSNGSPQLQ
EQDPEALAKT IEDETFRRYL KIPPEERERL KNREAELPIK FDDFIAIHGF SAENQKVKND
KRNDHISDSI AYIDSQHFSY HYEKYSGSSE EKASIPSKND MEKSSNVKKN KKRRKKQTEE
VVDMDHANKT LSQEQIAEQR KVNKQLREER KKRQSNREKK VSNLEKQSKK SQEMYEKAER
RSKIFSEWMD QQGIITEDVA NLIPRLSEKD FYEEEEASST KSFFITDMND SQNYIEKRKQ
KEKQKSLLSM PQTFDTSNYD RKSKLSDLGS VLDHKYGSNN KDGSTSSRMP SISRGSNKSV
GFLTFWNKSS VPKRPAVREI TTLTNLSKLL KGYEFDTNIE SGGFYVMAAH SSTSNQCSVR
KMYERFFQPI PFVKSKNLHR MCKKFNTSSI GSNSSGQNME GATASNNNNN NTTPTSRERY
IVMFKEYMKA FKHDEYISTL LGGTHRGYKI IERDNAATRM FDTDFALVEF ENITLKSELE
SRTQFVRYVV RQHEYHNMMN NERKLLNHDI ETLPDDEQDH SILNSIGKLF TQWSTEDKYS
DHHHHRRKLC NHPSHSYVDV SEKLNAHKLW EQGIYGQNIR VAVFDTGLSS TKHEESFSHI
EDMINYTTED SVNDELGHGT FISGVIGSKH LTPYTPKSNT TQPFNEKKER GSGCRGLAPE
ASVFIFKVFT SKQVSYTSWF LDAFNYAMKS GIQILNLSIG GPDYLDIPFI DKVKELTANG
IIIISAIGND GPLYGTLNNP ADLVNVIGVG GIDDNDNIAK FSSRGVTTYE LRFNNGYGRV
KPDIVTMSVK LRGLGLNKAG DNVGYCHSIL SGTSVASPVI AGAITLLASS TLKNKDTSTQ
NSDDISIRAK MDDYPNTHNS LLPLINPASI KQILLESAQR VHHANIFEQG AGKLNLEKAY
ELLQDYMEKA KPRATFYPSE LDLTSCPYMW PYCSQPIYHT AMPIVFNVTV LNAMSASGRV
VGEPVFVPGK YGDFLDVTFT HPRVMWPYSG WLGVQISVNS GGRFFNGYCE GTIKMKIMSP
PLGVGKDGNE MQVSEMELKL KVKVIQPPLR QQRILWDQYH NIQYPPGYIP RDNLGNKDEI
LDWNGDHIHT NFRDLYIFLR NKGYYVEILT GDLTTFDASK YSTLMIVDSE EEFTEKEREK
LKEDVQVYGL SVAVFADWYS VPIMKHIKFF DDNTYTVWTP ITGGCNLPAL NALLDPFNIV
FGTRVYTGEI TIGKEKASFL SGTSIIKFPE EGMLASFHLK DQGIEILSGK QNSKPILGTD
SSSTIHKVPV LGFSKSGKGR IAVFGDSNCL DAVGNPTHNC FWLLDQILQY TSQHKMSEEF
IKDANIKTLS HLFISQSSSV VGASGLVAVS TNNSFLTVSD FFFLPLLACV VVVEGEAV
//
