ID A0A5C6CIR0_9BACT Unreviewed; 561 AA.
AC A0A5C6CIR0;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 02-APR-2025, entry version 17.
DE SubName: Full=Matrixin {ECO:0000313|EMBL:TWU23261.1};
GN ORFNames=Pla52o_27970 {ECO:0000313|EMBL:TWU23261.1};
OS Novipirellula galeiformis.
OC Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia; Pirellulales;
OC Pirellulaceae; Novipirellula.
OX NCBI_TaxID=2528004 {ECO:0000313|EMBL:TWU23261.1, ECO:0000313|Proteomes:UP000316304};
RN [1] {ECO:0000313|EMBL:TWU23261.1, ECO:0000313|Proteomes:UP000316304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pla52o {ECO:0000313|EMBL:TWU23261.1,
RC ECO:0000313|Proteomes:UP000316304};
RA Wiegand S., Jogler M., Boedeker C., Pinto D., Vollmers J., Rivas-Marin E.,
RA Kohn T., Peeters S.H., Heuer A., Rast P., Oberbeckmann S., Bunk B.,
RA Jeske O., Meyerdierks A., Storesund J.E., Kallscheuer N., Luecker S.,
RA Lage O.M., Pohl T., Merkel B.J., Hornburger P., Mueller R.-W., Bruemmer F.,
RA Labrenz M., Spormann A.M., Op Den Camp H., Overmann J., Amann R.,
RA Jetten M.S.M., Mascher T., Medema M.H., Devos D.P., Kaster A.-K.,
RA Ovreas L., Rohde M., Galperin M.Y., Jogler C.;
RT "Deep-cultivation of Planctomycetes and their phenomic and genomic
RT characterization uncovers novel biology.";
RL Submitted (FEB-2019) 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:TWU23261.1}.
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DR EMBL; SJPT01000004; TWU23261.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5C6CIR0; -.
DR Proteomes; UP000316304; Unassembled WGS sequence.
DR GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 1.10.1330.10; Dockerin domain; 1.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR InterPro; IPR002105; Dockerin_1_rpt.
DR InterPro; IPR036439; Dockerin_dom_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001818; Pept_M10_metallopeptidase.
DR InterPro; IPR021190; Pept_M10A.
DR InterPro; IPR006026; Peptidase_Metallo.
DR PANTHER; PTHR10201; MATRIX METALLOPROTEINASE; 1.
DR PANTHER; PTHR10201:SF323; MATRIX METALLOPROTEINASE-21; 1.
DR Pfam; PF00404; Dockerin_1; 1.
DR Pfam; PF00413; Peptidase_M10; 1.
DR PRINTS; PR00138; MATRIXIN.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF63446; Type I dockerin domain; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000316304};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 24..189
FT /note="Peptidase metallopeptidase"
FT /evidence="ECO:0000259|SMART:SM00235"
FT REGION 197..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 330..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..235
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..343
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..377
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..415
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 561 AA; 60345 MW; 93B736F294AC7061 CRC64;
MKFMQRKTRR LSLQPLETRR VLAASLGWDG PGLGSVELTY TINGSPNSLS QAQTNAAIET
ALAAWSSAAD IEFTPTNQVG LSDSIDISFV NIDGASRTLA QAYFPDDVNP TRIAGDIQFD
LSESWEVGNS LGDRAFDLVW VAVHEIGHSL GLDHQEGGDT VLAPSVSPNQ FFTSLSGVDA
DAVQQLYAAA ESNVVIQPDD VPTLNDPVDD VPSDSPTNET PSGDGDDDPG DSDDDPFPRN
RWRHGGRWHR FGGRLEADLG DFNYLNPTDV NGDNATSAID ALMIINQLNR ASSADSSDVE
MEGLCDVNGD GGVSALDALT VINSLHRGDS SVSATVDSTT VDSTEIEVTE TLEDSNDLEN
SNDSEDSDDS VQSEGGDDLG NPIDDGGRID DTDDDGVESD AAHHHHGHQH GHHRTGNFIL
FGNDPESFIT RLDTDEEGSL SEDEVSERLW TQLIDKGIDT DADGLVTLAE LETAIAAARD
EVFNSNDADG DGLISESEVS TRYWAKVSAA DVDRDRGVSR DEFDGYVSEP VDWELPSRPH
RPHHVADAVF GAIGRRASRW G
//
