ID H5SN78_9ZZZZ Unreviewed; 574 AA.
AC H5SN78;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Peptidase M23 {ECO:0000313|EMBL:BAL57614.1};
GN ORFNames=HGMM_F51E10C26 {ECO:0000313|EMBL:BAL57614.1};
OS uncultured prokaryote.
OC unclassified sequences; environmental samples.
OX NCBI_TaxID=198431 {ECO:0000313|EMBL:BAL57614.1};
RN [1] {ECO:0000313|EMBL:BAL57614.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=16309394; DOI=10.1111/j.1462-2920.2005.00881.x;
RA Nunoura T., Hirayama H., Takami H., Oida H., Nishi S., Shimamura S.,
RA Suzuki Y., Inagaki F., Takai K., Nealson K.H., Horikoshi K.;
RT "Genetic and functional properties of uncultivated thermophilic
RT crenarchaeotes from a subsurface gold mine as revealed by analysis of
RT genome fragments.";
RL Environ. Microbiol. 7:1967-1984(2005).
RN [2] {ECO:0000313|EMBL:BAL57614.1}
RP NUCLEOTIDE SEQUENCE.
RA Takami H., Noguchi H., Takaki Y., Uchiyama I., Toyoda A., Nishi S.,
RA Chee G.-J., Arai W., Nunoura T., Itoh T., Hattori M., Takai K.;
RT "A Deeply Branching Thermophilic Bacterium with an Ancient Acetyl-CoA
RT Pathway Dominates a Subsurface Ecosystem.";
RL PLoS ONE 7:e30559-e30559(2012).
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DR EMBL; AP011780; BAL57614.1; -; Genomic_DNA.
DR AlphaFoldDB; H5SN78; -.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:InterPro.
DR CDD; cd14256; Dockerin_I; 1.
DR CDD; cd12797; M23_peptidase; 1.
DR Gene3D; 1.10.1330.10; Dockerin domain; 1.
DR Gene3D; 2.70.70.10; Glucose Permease (Domain IIA); 1.
DR InterPro; IPR002105; Dockerin_1_rpt.
DR InterPro; IPR036439; Dockerin_dom_sf.
DR InterPro; IPR011055; Dup_hybrid_motif.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR016047; Peptidase_M23.
DR PANTHER; PTHR21666:SF270; OUTER MEMBRANE ANTIGENIC LIPOPROTEIN B; 1.
DR PANTHER; PTHR21666; PEPTIDASE-RELATED; 1.
DR Pfam; PF00404; Dockerin_1; 1.
DR Pfam; PF01551; Peptidase_M23; 1.
DR SUPFAM; SSF51261; Duplicated hybrid motif; 1.
DR SUPFAM; SSF47473; EF-hand; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
PE 4: Predicted;
FT DOMAIN 507..542
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
SQ SEQUENCE 574 AA; 61674 MW; 01B389F04FB40B98 CRC64;
MGMLCAVPSA QMIQRNDRVG ITLLGNRLWV CGRACGSIRE AGPPAGTDGI VLSEADFCDR
TPWWRVGWSN GQRGWSAERR MNRVQLLPLP GEGSYPNISA AGAYPVQVAP DGNPLNVRMG
PGLNYGILTQ KPAGATGWAY QVVIDSTNRL VWWKIRWDDA NGGHVGWSAD SRLFSGVYLT
KIGAVRPINT LTIESSASGV GITVSLRDLQ GNPASGTANT PTTLSYVSGT QITLTAPDTA
PDDSSFLYWE RNGTPYTSSL SITLYLTQSQ TLRAVYRARE EQFLWNLIAP WRQGQYWTPS
TYDGHGGGNM LNAVDLNRAA SSRSTCPYTN GWIQDCDEVL VASHAGRAYT RAQSGCTGYG
NYVVLVSDVL VSGTSNTYLA TIYAHLNYFL VDNGTQVVAG QPIARLGSTG SSTGPHLHYE
IREVTVSGST LTLGARRQVL NNPAIRLSGQ ELRVDLSCTV SGLGYVGSPI LGTASVGSVP
GNRTPPCTPY SCGGFLWSPE TAPERCIEED ELPVLLYLSD VNGDGCVDET DLRRVLMAIG
SDMSDTSSDV NWDGIVDEAD LIAVLLDWGH CAVP
//