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Database: UniProt
Entry: A0A136Q5W4_9FIRM
LinkDB: A0A136Q5W4_9FIRM
Original site: A0A136Q5W4_9FIRM 
ID   A0A136Q5W4_9FIRM        Unreviewed;       439 AA.
AC   A0A136Q5W4;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=FHA domain protein {ECO:0000313|EMBL:KXK66057.1};
GN   ORFNames=HMPREF3293_01085 {ECO:0000313|EMBL:KXK66057.1};
OS   Christensenella minuta.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Christensenellaceae;
OC   Christensenella.
OX   NCBI_TaxID=626937 {ECO:0000313|EMBL:KXK66057.1, ECO:0000313|Proteomes:UP000070366};
RN   [1] {ECO:0000313|EMBL:KXK66057.1, ECO:0000313|Proteomes:UP000070366}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22607 {ECO:0000313|EMBL:KXK66057.1,
RC   ECO:0000313|Proteomes:UP000070366};
RA   Wen L., He K., Yang H.;
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KXK66057.1}.
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DR   EMBL; LSZW01000049; KXK66057.1; -; Genomic_DNA.
DR   RefSeq; WP_066523560.1; NZ_MAIR01000022.1.
DR   AlphaFoldDB; A0A136Q5W4; -.
DR   STRING; 626937.HMPREF3293_01085; -.
DR   KEGG; cmiu:B1H56_09170; -.
DR   OrthoDB; 9783862at2; -.
DR   Proteomes; UP000070366; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd00060; FHA; 1.
DR   Gene3D; 2.40.10.120; -; 1.
DR   Gene3D; 2.60.200.20; -; 1.
DR   InterPro; IPR000253; FHA_dom.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR001940; Peptidase_S1C.
DR   InterPro; IPR008984; SMAD_FHA_dom_sf.
DR   PANTHER; PTHR43019:SF23; PROTEASE DO-LIKE 5, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR43019; SERINE ENDOPROTEASE DEGS; 1.
DR   Pfam; PF00498; FHA; 1.
DR   Pfam; PF13365; Trypsin_2; 1.
DR   PRINTS; PR00834; PROTEASES2C.
DR   SMART; SM00240; FHA; 1.
DR   SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS50006; FHA_DOMAIN; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070366};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..43
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           44..439
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007478628"
FT   TRANSMEM        281..302
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          356..410
FT                   /note="FHA"
FT                   /evidence="ECO:0000259|PROSITE:PS50006"
SQ   SEQUENCE   439 AA;  46637 MW;  1F7AE51072A0D84F CRC64;
     METKKKISTK KIMAIALFCV FAISCVLCGI SAASSMGMTP AQARNGVAYV QQVLYDVSGS
     PVAAGSGTCW AVGKPGEPVE YFVTNGHVVQ YAYIVPKQDP SYSGKVTVVY SGAENDFVDA
     QVLYYSGPEE KDIAILKVPS PTDKRIPLPI RPSDTVQPGE TAYALGFPGV SDTLAENIRY
     DIDDVTITDG VISKRASVSG TGYEAFQMNV DINPGNSGGP LVDADGNVIG VNTSGLVTQI
     GTEEQSVNIN TSVNYASVAD QLIRILDEER IEYTLMGEKN WMLYTFVVIG GVTLILGIVF
     LVMDRKKTSV LSAADTEGSF VAGKPAKNSP SGKKPLLRGV TGKYAGQSFD LSKGKVTLGR
     DPNLCNIVFD KSTPGISGNH CQVSYDAAGD YFLLMDNGSS YGTFLGNGKK LPASVAEKLA
     TGDTFYLCNN ANKFIVAKE
//
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