ID A0A176U378_9FIRM Unreviewed; 587 AA.
AC A0A176U378;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=SH3 domain protein {ECO:0000313|EMBL:OAD87247.1};
GN ORFNames=HMPREF2738_02749 {ECO:0000313|EMBL:OAD87247.1};
OS Clostridiales bacterium KLE1615.
OC Bacteria; Bacillota; Clostridia; Eubacteriales.
OX NCBI_TaxID=1715004 {ECO:0000313|EMBL:OAD87247.1, ECO:0000313|Proteomes:UP000077212};
RN [1] {ECO:0000313|EMBL:OAD87247.1, ECO:0000313|Proteomes:UP000077212}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KLE1615 {ECO:0000313|EMBL:OAD87247.1,
RC ECO:0000313|Proteomes:UP000077212};
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:OAD87247.1}.
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DR EMBL; LXPQ01000204; OAD87247.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A176U378; -.
DR PATRIC; fig|1715004.3.peg.2734; -.
DR Proteomes; UP000077212; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008235; F:metalloexopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR045175; M28_fam.
DR InterPro; IPR007484; Peptidase_M28.
DR InterPro; IPR003646; SH3-like_bac-type.
DR PANTHER; PTHR12147:SF26; ENDOPLASMIC RETICULUM METALLOPEPTIDASE 1; 1.
DR PANTHER; PTHR12147; METALLOPEPTIDASE M28 FAMILY MEMBER; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR Pfam; PF08239; SH3_3; 1.
DR SMART; SM00287; SH3b; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS51781; SH3B; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000077212};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..587
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008050455"
FT TRANSMEM 513..536
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 340..404
FT /note="SH3b"
FT /evidence="ECO:0000259|PROSITE:PS51781"
FT REGION 406..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 542..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..468
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..498
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..587
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 587 AA; 64340 MW; 426BCE58372380D5 CRC64;
MKICKRIKAT VLALCLVIGM CAVSLPQTVH AEYGDNAYAF MKQLQSNYPY RQVNSSNGML
SGAEEWLKAQ IVTMGYEYMA QPFTMTSADG VTPCYGENLI FSKQGASDRV ILVGAHYDCV
EQTFGTDDNA SGVGVLLELA SIYSTKESPY TIRFVLFSAE EPGCLGSQYY VDNLSQEERD
RIACMINIDT IAAGDNMYLY GGTVDDSGSI VQDWAVYQAQ SAADLLGLDM SFHPDVNDSF
PTPTKATASD QMPFANVGIP YIYCEASNWN GEPYTNFYQT SNSAVNGGTI MHKAEYDNLT
FIENTFGARA YEHLQAYAKL LDYLLENMKE GEYATGYTFE DTNTKAATTS SVYLRERPTQ
YSPSVTLLDA DTEVTVTGYH ASWCRVEVDG QEGYIKTDYL TMEDEIASKE DESSEEESEN
ASKEAESSMS EESSSEAAEN ESGEAVSEGE SVESESLSNE ASKNEAVSEA ASSEKETDVA
LSQSASSQNA SVPEADSQNT VEKIIDQLKN DPYTLRIVLI AAIVIIGIWL CVFIALRRKK
NAQKNEDSNG ASNSSEETLK KAKRADMSDS KDSDNGFADP DKNKDEK
//
