ID I3TCZ3_THEC1 Unreviewed; 356 AA.
AC I3TCZ3;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Peptidase M50 {ECO:0000313|EMBL:AFK50631.1};
GN OrderedLocusNames=TCELL_0206 {ECO:0000313|EMBL:AFK50631.1};
OS Thermogladius calderae (strain DSM 22663 / VKM B-2946 / 1633).
OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Thermogladius.
OX NCBI_TaxID=1184251 {ECO:0000313|EMBL:AFK50631.1, ECO:0000313|Proteomes:UP000005270};
RN [1] {ECO:0000313|EMBL:AFK50631.1, ECO:0000313|Proteomes:UP000005270}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22663 / VKM B-2946 / 1633
RC {ECO:0000313|Proteomes:UP000005270};
RX PubMed=22843584; DOI=10.1128/JB.00894-12;
RA Mardanov A.V., Kochetkova T.V., Beletsky A.V., Bonch-Osmolovskaya E.A.,
RA Ravin N.V., Skryabin K.G.;
RT "Complete genome sequence of the hyperthermophilic cellulolytic
RT Crenarchaeon 'Thermogladius cellulolyticus' 1633.";
RL J. Bacteriol. 194:4446-4447(2012).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP003531; AFK50631.1; -; Genomic_DNA.
DR RefSeq; WP_014736882.1; NC_017954.1.
DR AlphaFoldDB; I3TCZ3; -.
DR STRING; 1184251.TCELL_0206; -.
DR GeneID; 13012486; -.
DR KEGG; thg:TCELL_0206; -.
DR eggNOG; arCOG04064; Archaea.
DR HOGENOM; CLU_042134_0_0_2; -.
DR InParanoid; I3TCZ3; -.
DR OrthoDB; 15212at2157; -.
DR Proteomes; UP000005270; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd00987; PDZ_serine_protease; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR001193; MBTPS2.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR008915; Peptidase_M50.
DR PANTHER; PTHR13325:SF3; MEMBRANE-BOUND TRANSCRIPTION FACTOR SITE-2 PROTEASE; 1.
DR PANTHER; PTHR13325; PROTEASE M50 MEMBRANE-BOUND TRANSCRIPTION FACTOR SITE 2 PROTEASE; 1.
DR Pfam; PF17820; PDZ_6; 1.
DR Pfam; PF02163; Peptidase_M50; 1.
DR PRINTS; PR01000; SREBPS2PTASE.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000005270};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..23
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 60..82
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 94..119
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 131..150
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 170..188
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 299..318
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 338..355
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 181..230
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 356 AA; 37853 MW; 7113B215FE9CDFCE CRC64;
MNTALTVLGG LLAAWSTLNL LYYRKREFFE SRRIRLMYGG VLVYRAGRVR GASGAWRRAS
VLLVASYAVS VAWFFLVVYS GIDAKLNGTG ALRVLVPGVD ITGLDLVYFV VAVGVAVVLH
ELFHGKTAVS HNVGVKSFGL AVAVIVPLAF TEIEESDFNK SSRFVKTSIL AAGVAANLAL
GLLGLALFNI AASPSGVLVT GVVPGSLASR AGIEPYSILL SVNGVSLRGV EDLRSLLSNT
TTTVLNITLL TPRGVVETIS IVRNATERAL GVYVTTPPAS WLIDAVGVYP AVQFMRAFFW
LYLVNFNLAI LNAAPLFITD GGRIVFEVLG ERFKKAALLV NAASLLALVL SLAPVP
//