ID W0I0A9_9EURY Unreviewed; 2314 AA.
AC W0I0A9;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AHF79466.1};
GN ORFNames=TES1_0069 {ECO:0000313|EMBL:AHF79466.1};
OS Thermococcus paralvinellae.
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=582419 {ECO:0000313|EMBL:AHF79466.1, ECO:0000313|Proteomes:UP000019027};
RN [1] {ECO:0000313|EMBL:AHF79466.1, ECO:0000313|Proteomes:UP000019027}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ES1 {ECO:0000313|EMBL:AHF79466.1,
RC ECO:0000313|Proteomes:UP000019027};
RX PubMed=25082851; DOI=10.1099/ijs.0.066100-0;
RA Hensley S.A., Jung J.H., Park C.S., Holden J.F.;
RT "Thermococcus paralvinellae sp. nov. and Thermococcus cleftensis sp. nov.
RT of hyperthermophilic heterotrophs from deep-sea hydrothermal vents.";
RL Int. J. Syst. Evol. Microbiol. 64:3655-3659(2014).
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01240}.
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DR EMBL; CP006965; AHF79466.1; -; Genomic_DNA.
DR RefSeq; WP_051408149.1; NZ_CP006965.1.
DR STRING; 582419.TES1_0069; -.
DR GeneID; 24906763; -.
DR KEGG; ths:TES1_0069; -.
DR HOGENOM; CLU_001115_0_0_2; -.
DR OrthoDB; 27270at2157; -.
DR Proteomes; UP000019027; Chromosome.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.380; -; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 2.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR007280; Peptidase_C_arc/bac.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR PANTHER; PTHR43399; SUBTILISIN-RELATED; 1.
DR PANTHER; PTHR43399:SF4; TK-SUBTILISIN; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR Pfam; PF04151; PPC; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Protease {ECO:0000256|PROSITE-ProRule:PRU01240};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01240}.
FT DOMAIN 702..970
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 1411..1487
FT /note="Peptidase C-terminal archaeal/bacterial"
FT /evidence="ECO:0000259|Pfam:PF04151"
FT ACT_SITE 678
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 706
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 919
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 2314 AA; 258856 MW; 8F84D8E922C8E5DC CRC64;
MNKKILGILI VVLMVLSVVP MVTVGAMNTT NGNENLLVPK VTHTIEKVQI NTKQHPLLPQ
EDIKPENKID QKFLEMLTNK SKQETLAEIG GKKVIPSLII SKEEVELPFK VIGSRNIAGY
TVYWVLVPVE QNTIMLLNKV ASNDAVLQIL PASVAEPVGL FKEPDEKPQK IENFIPLPNI
QRTRYIKGYN VLSFDKNALL KESRLVNVKR EGVAFPKNFE PADIFAVYHH KALQTWKELN
ITGEGVSVAV LDSGVDFGNP DLLDAYAVDP VSGWPIAFDS SSLNAYMLLN LTFINFATLL
GVDYKPFYIY SWYADTSFEV SPLTISGNIT IGYKGNYTAV FTTFDLANIL DDKERAMFIQ
EVIDWIGGAE RVLLVDDDEG TWGNGNFDYY LPDVEDFYKK ALDSLNITYD TITVPFGSDG
PSLDILRNYD LVIWVTGGSF EPGHVLTDND VNTLEQFLDN GGKLWLISQD YIYSRGIDEF
ASEYLHVTDY YALDIPAPTF IVTNEGMYHA GPIYHGMYLS PTDGFIDMII PDNESEVLAV
GIEALAYSDY GILPFIKLPL NESLEYPTQS GKFYIGPHPD LALWFDWFGA FVLVADPEGK
YDTVYVDFSS PYVIDFTDDD PHTKDNPVIT LDFWDSLNGT FGSDGYPDLS GGMIYYIADG
NSTIPYADVI YNVWNMADYG IQLPVPEEGK LVAFMIGTAY TGGGYHGTLC AAAVAARGRT
LGITYGNAPG SKIIAIGSIY TGMDNWIDEV FFAVEGYDGI PYTGDEALVA SNSYGISSII
NKGTSWNDVF LSFITQYYAP YTTFLFAAGN GGPGYGTVTT PGASPGVITV GAAVEFGYRF
MYGYDEGPYG GPLANYGDVV DFSNRGPNVL GQPKPDVLAV GAFAHGSIPV NWMTWWVYYL
FYGNYFGGYY ASELWAGTSL ATPMAAGVTA LVYQAYTEAH GTYPTNELVK TILKSSADNV
NADVFSQGAG FLNAYRAVKL AMGLDGLMVT PSEEYTVTIP GSEFSWEFTI YNVNASAEKS
ANVSVEVFQK IDEVELDTYA GMITRIDQYI PEDADLMKIT LYYPFDSFDP LMNYWPATYA
WFRVYDWTDV DGDGTVDAYW GLYGNETNLI HQAYTFGTSA SLLLGNPKTK YHDGMFLWVR
EAGAGAKIKI EFYKRVPWNW ATIDKNSVTL APSSSENVTV TISVPADAFG VYEAALYVAY
DNTETVVPLS VIVAASEPNF DYVPSDYTGL YDNGYVYGYF DWFWRYESGD WRLYYVNVPE
VDNGTYLVTS VTWEGYPQDI NVHILGPKDG DFVELARGMD GYMGAGMFKF MTSNGPQGEI
VGTKAYKPGL YAIWLHNVLY DGKEAQRKIK EIKVGTVKVT PEVLTINTSK ALSGELSLSL
ENNIELTPNI NVYGLIMPEI HNATIAPPTG DYDVYEVYVE DSAMLSVVLE SIYDDVGGLD
LDLFVFYDYI DMYSYSSLVA YSAGPTADES VSITFPVPGH YYIVVESYSN PVPGSTYDLK
IYNYEKSDTI KIKDIIVNNT IYNITLEYEL PESGEYSGIV TIGFENNPAV IVVPINVEEV
KPGSTKGYDL VVYPLTLETP YDVPYVNMTY NVSTIFYIEG KWSAERVKAY VYWNGYVVDI
VDIPFVEPNT YYKLTFSIPI MDDSLQRIWV ELKSDNDMAE YNNYAGTFCL LPVTPDKLSD
YGKVIGGYAI GRYARWDVPK TEGDLNTITI YSDGESYPGY VRTVLALSPL IDNESIQVDF
TWLKSIHLIS FKNKKDLIVI DSEGNEVFNP FALREVRYAL NYLINREAMV KEGFGGNATA
LFGPIYPAQI EFHKAQEVYT VLNLTSESSV DLAVQIIDMA MANVAEQYSL NLTKVNGTWY
FNDEPIVIRS AGWEPVDYYV KEALRKAGFE VVDNWSNWDY HIESWGWGLT MPLWITEAVF
YDPSWEDYIP EVTVANVTDL ISKLDLIYYN SSEKLDEIKD FTIEDILELL MYGEIPVNIT
KRDYGHAAIW FTWPYEVTYY TIQNEDQRSD LEKIALLLGI LESPNVFLVQ EFDTPYQSSY
KVVTLEDGVL VSMDYAYWRP VVIRVSFKEK PQEELEQEVV KMINNILEEL QKGVEVSEES
QEDVAVAESE TTGDQVVAKI IQEAGGDANV TVDVDVARET GTKEVKVTAE VNGDHGTVVT
LAIVLPEEVT KYEVHVQDAD LLDEPYAVYD QGKTIVIVTV KLHSPAIIEV TGVTEYPEEI
IGTYVVIWDM LYTRYTHKFD ELYNESIKLG IDNETIQEAL YYKQLAEQYY EQASSFGSPL
SNPIRSLAPI RKAYLNIKKA VEILEKAIEE AESS
//
