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Conserved domains on  [gi|2789528272|ref|WP_370847409|]
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peptidoglycan DD-metalloendopeptidase family protein [Phascolarctobacterium faecium]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NlpD COG0739
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell ...
 57-250 4.46e-62

Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 440502 [Multi-domain]  Cd Length: 196  Bit Score: 193.27  E-value: 4.46e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789528272  57 AVQPSRSGIDRSQYLGQGGPQAAKVEAVDIYAAQNKVLQEKVKDRKATLNDLLGRLRELNQRKAALPTLWPTNGgTITSY 136
Cdd:COG0739     4 ALALAAALLALALLASAAGAAAAVAAAAAAAAAAAALAAAALAAAVSAAASAAAAAAAAAAAIALGSGAWPVKG-RITSG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789528272 137 FGGRSDPFGNRsYDWHPGVDIANEYGAPVYASASGTIEEAGWVSGYGRYVRIQHGYGYETAYGHMSKLAVQAGQSVSKGD 216
Cdd:COG0739    83 FGYRRHPVTGR-RRFHKGIDIAAPTGTPVYAAADGTVVFAGWNGGYGNLVIIDHGNGYTTLYAHLSSILVKVGQRVKAGQ 161

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2789528272 217 VIGYVGSSGYSTGPHVHFEVLVNGQTTDPLELVR 250
Cdd:COG0739   162 VIGYVGNTGRSTGPHLHFEVRVNGKPVDPLPFLP 195
FtsB super family cl42746
Cell division protein FtsB [Cell cycle control, cell division, chromosome partitioning];
9-54 1.04e-03

Cell division protein FtsB [Cell cycle control, cell division, chromosome partitioning];


The actual alignment was detected with superfamily member COG2919:

Pssm-ID: 442163 [Multi-domain]  Cd Length: 96  Bit Score: 37.55  E-value: 1.04e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2789528272   9 QELLTYRSEKAVQEQKIGQLLQENEAIEKEMAELSK----LEEAVRRELG 54
Cdd:COG2919    29 LAYRELRQEIAELEAENAKLKARNAELEAEVADLKDgpdyIEERAREELG 78
 
Name Accession Description Interval E-value
NlpD COG0739
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell ...
 57-250 4.46e-62

Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440502 [Multi-domain]  Cd Length: 196  Bit Score: 193.27  E-value: 4.46e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789528272  57 AVQPSRSGIDRSQYLGQGGPQAAKVEAVDIYAAQNKVLQEKVKDRKATLNDLLGRLRELNQRKAALPTLWPTNGgTITSY 136
Cdd:COG0739     4 ALALAAALLALALLASAAGAAAAVAAAAAAAAAAAALAAAALAAAVSAAASAAAAAAAAAAAIALGSGAWPVKG-RITSG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789528272 137 FGGRSDPFGNRsYDWHPGVDIANEYGAPVYASASGTIEEAGWVSGYGRYVRIQHGYGYETAYGHMSKLAVQAGQSVSKGD 216
Cdd:COG0739    83 FGYRRHPVTGR-RRFHKGIDIAAPTGTPVYAAADGTVVFAGWNGGYGNLVIIDHGNGYTTLYAHLSSILVKVGQRVKAGQ 161

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2789528272 217 VIGYVGSSGYSTGPHVHFEVLVNGQTTDPLELVR 250
Cdd:COG0739   162 VIGYVGNTGRSTGPHLHFEVRVNGKPVDPLPFLP 195
Peptidase_M23 pfam01551
Peptidase family M23; Members of this family are zinc metallopeptidases with a range of ...
 152-245 2.78e-47

Peptidase family M23; Members of this family are zinc metallopeptidases with a range of specificities. The peptidase family M23 is included in this family, these are Gly-Gly endopeptidases. Peptidase family M23 are also endopeptidases. This family also includes some bacterial lipoproteins such as Swiss:P33648 for which no proteolytic activity has been demonstrated. This family also includes leukocyte cell-derived chemotaxin 2 (LECT2) proteins. LECT2 is a liver-specific protein which is thought to be linked to hepatocyte growth although the exact function of this protein is unknown.


Pssm-ID: 460250 [Multi-domain]  Cd Length: 96  Bit Score: 151.93  E-value: 2.78e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789528272 152 HPGVDIANEYGAPVYASASGTIEEAGWVSGYGRYVRIQHGYGYETAYGHMSKLAVQAGQSVSKGDVIGYVGSSGYSTGPH 231
Cdd:pfam01551   3 HKGIDIAAPTGTPVYAAADGVVVFAGWLGGYGNLVIIDHGNGYSTLYAHLSSILVKVGQRVKAGQVIGTVGSTGRSTGPH 82

                          90
                  ....*....|....
gi 2789528272 232 VHFEVLVNGQTTDP 245
Cdd:pfam01551  83 LHFEIRKNGKPVDP 96
M23_peptidase cd12797
M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; ...
 152-236 5.13e-44

M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; This model describes the metallopeptidase M23 family, which includes beta-lytic metallopeptidase and lysostaphin. Members of this family are zinc endopeptidases that lyse bacterial cell wall peptidoglycans; they cleave either the N-acylmuramoyl-Ala bond between the cell wall peptidoglycan and the cross-linking peptide (e.g. beta-lytic endopeptidase) or a bond within the cross-linking peptide (e.g. stapholysin, and lysostaphin). Beta-lytic metallopeptidase, formerly known as beta-lytic protease, has a preference for cleavage of Gly-X bonds and favors hydrophobic or apolar residues on either side. It inhibits growth of sensitive organisms and may potentially serve as an antimicrobial agent. Lysostaphin, produced by Staphylococcus genus, cleaves pentaglycine cross-bridges of cell wall peptidoglycan, acting as autolysins to maintain cell wall metabolism or as toxins and weapons against competing strains. Staphylolysin (also known as LasA) is implicated in a range of processes related to Pseudomonas virulence, including stimulating shedding of the ectodomain of cell surface heparan sulphate proteoglycan syndecan-1, and elastin degradation in connective tissue. Its active site is less constricted and contains a five-coordinate zinc ion with trigonal bipyramidal geometry and two metal-bound water molecules, possibly contributing to its activity against a wider range of substrates than those used by related lytic enzymes, consistent with its multiple roles in Pseudomonas virulence. The family includes members that do not appear to have the conserved zinc-binding site and might be lipoproteins lacking proteolytic activity.


Pssm-ID: 410984 [Multi-domain]  Cd Length: 85  Bit Score: 143.12  E-value: 5.13e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789528272 152 HPGVDIANEYGAPVYASASGTIEEAGWVSGYGRYVRIQHGYGYETAYGHMSKLAVQAGQSVSKGDVIGYVGSSGYSTGPH 231
Cdd:cd12797     1 HNGIDIAAPEGTPVYAAADGTVVFAGWDGGYGNYVIIDHGNGYYTLYAHLSSILVKVGQRVKKGQVIGTVGNTGRSTGPH 80


                  ....*
gi 2789528272 232 VHFEV 236
Cdd:cd12797    81 LHFEI 85
PRK11649 PRK11649
putative peptidase; Provisional
 152-246 9.90e-24

putative peptidase; Provisional


Pssm-ID: 236946 [Multi-domain]  Cd Length: 439  Bit Score: 98.58  E-value: 9.90e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789528272 152 HPGVDIANEYGAPVYASASGTIEEAGWVSGYGRYVRIQHGYGYETAYGHMSKLAVQAGQSVSKGDVIGYVGSSGYSTGPH 231
Cdd:PRK11649  313 HRGVDFAMPVGTPVLAVGDGEVVVAKRSGAAGNYVAIRHGRQYTTRYMHLRKLLVKPGQKVKRGDRIALSGNTGRSTGPH 392

                          90
                  ....*....|....*
gi 2789528272 232 VHFEVLVNGQTTDPL 246
Cdd:PRK11649  393 LHYEVWINQQAVNPL 407
FtsB COG2919
Cell division protein FtsB [Cell cycle control, cell division, chromosome partitioning];
9-54 1.04e-03

Cell division protein FtsB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442163 [Multi-domain]  Cd Length: 96  Bit Score: 37.55  E-value: 1.04e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2789528272   9 QELLTYRSEKAVQEQKIGQLLQENEAIEKEMAELSK----LEEAVRRELG 54
Cdd:COG2919    29 LAYRELRQEIAELEAENAKLKARNAELEAEVADLKDgpdyIEERAREELG 78
Med21 pfam11221
Subunit 21 of Mediator complex; Med21 has been known as Srb7 in yeasts, hSrb7 in humans and ...
 16-55 4.91e-03

Subunit 21 of Mediator complex; Med21 has been known as Srb7 in yeasts, hSrb7 in humans and Trap 19 in Drosophila. The heterodimer of the two subunits Med7 and Med21 appears to act as a hinge between the middle and the tail regions of Mediator.


Pssm-ID: 463241  Cd Length: 134  Bit Score: 36.41  E-value: 4.91e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2789528272  16 SEKAvQEQKIGQLLQENEAIEKEMAELSKLEEAVRRELGE 55
Cdd:pfam11221  89 SEEE-QLQRIKELEEELREAEEERQEAVKEKEELLKKLDE 127
 
Name Accession Description Interval E-value
NlpD COG0739
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell ...
 57-250 4.46e-62

Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440502 [Multi-domain]  Cd Length: 196  Bit Score: 193.27  E-value: 4.46e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789528272  57 AVQPSRSGIDRSQYLGQGGPQAAKVEAVDIYAAQNKVLQEKVKDRKATLNDLLGRLRELNQRKAALPTLWPTNGgTITSY 136
Cdd:COG0739     4 ALALAAALLALALLASAAGAAAAVAAAAAAAAAAAALAAAALAAAVSAAASAAAAAAAAAAAIALGSGAWPVKG-RITSG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789528272 137 FGGRSDPFGNRsYDWHPGVDIANEYGAPVYASASGTIEEAGWVSGYGRYVRIQHGYGYETAYGHMSKLAVQAGQSVSKGD 216
Cdd:COG0739    83 FGYRRHPVTGR-RRFHKGIDIAAPTGTPVYAAADGTVVFAGWNGGYGNLVIIDHGNGYTTLYAHLSSILVKVGQRVKAGQ 161

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2789528272 217 VIGYVGSSGYSTGPHVHFEVLVNGQTTDPLELVR 250
Cdd:COG0739   162 VIGYVGNTGRSTGPHLHFEVRVNGKPVDPLPFLP 195
Peptidase_M23 pfam01551
Peptidase family M23; Members of this family are zinc metallopeptidases with a range of ...
 152-245 2.78e-47

Peptidase family M23; Members of this family are zinc metallopeptidases with a range of specificities. The peptidase family M23 is included in this family, these are Gly-Gly endopeptidases. Peptidase family M23 are also endopeptidases. This family also includes some bacterial lipoproteins such as Swiss:P33648 for which no proteolytic activity has been demonstrated. This family also includes leukocyte cell-derived chemotaxin 2 (LECT2) proteins. LECT2 is a liver-specific protein which is thought to be linked to hepatocyte growth although the exact function of this protein is unknown.


Pssm-ID: 460250 [Multi-domain]  Cd Length: 96  Bit Score: 151.93  E-value: 2.78e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789528272 152 HPGVDIANEYGAPVYASASGTIEEAGWVSGYGRYVRIQHGYGYETAYGHMSKLAVQAGQSVSKGDVIGYVGSSGYSTGPH 231
Cdd:pfam01551   3 HKGIDIAAPTGTPVYAAADGVVVFAGWLGGYGNLVIIDHGNGYSTLYAHLSSILVKVGQRVKAGQVIGTVGSTGRSTGPH 82

                          90
                  ....*....|....
gi 2789528272 232 VHFEVLVNGQTTDP 245
Cdd:pfam01551  83 LHFEIRKNGKPVDP 96
M23_peptidase cd12797
M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; ...
 152-236 5.13e-44

M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; This model describes the metallopeptidase M23 family, which includes beta-lytic metallopeptidase and lysostaphin. Members of this family are zinc endopeptidases that lyse bacterial cell wall peptidoglycans; they cleave either the N-acylmuramoyl-Ala bond between the cell wall peptidoglycan and the cross-linking peptide (e.g. beta-lytic endopeptidase) or a bond within the cross-linking peptide (e.g. stapholysin, and lysostaphin). Beta-lytic metallopeptidase, formerly known as beta-lytic protease, has a preference for cleavage of Gly-X bonds and favors hydrophobic or apolar residues on either side. It inhibits growth of sensitive organisms and may potentially serve as an antimicrobial agent. Lysostaphin, produced by Staphylococcus genus, cleaves pentaglycine cross-bridges of cell wall peptidoglycan, acting as autolysins to maintain cell wall metabolism or as toxins and weapons against competing strains. Staphylolysin (also known as LasA) is implicated in a range of processes related to Pseudomonas virulence, including stimulating shedding of the ectodomain of cell surface heparan sulphate proteoglycan syndecan-1, and elastin degradation in connective tissue. Its active site is less constricted and contains a five-coordinate zinc ion with trigonal bipyramidal geometry and two metal-bound water molecules, possibly contributing to its activity against a wider range of substrates than those used by related lytic enzymes, consistent with its multiple roles in Pseudomonas virulence. The family includes members that do not appear to have the conserved zinc-binding site and might be lipoproteins lacking proteolytic activity.


Pssm-ID: 410984 [Multi-domain]  Cd Length: 85  Bit Score: 143.12  E-value: 5.13e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789528272 152 HPGVDIANEYGAPVYASASGTIEEAGWVSGYGRYVRIQHGYGYETAYGHMSKLAVQAGQSVSKGDVIGYVGSSGYSTGPH 231
Cdd:cd12797     1 HNGIDIAAPEGTPVYAAADGTVVFAGWDGGYGNYVIIDHGNGYYTLYAHLSSILVKVGQRVKKGQVIGTVGNTGRSTGPH 80


                  ....*
gi 2789528272 232 VHFEV 236
Cdd:cd12797    81 LHFEI 85
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 9-250 1.41e-43

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 151.07  E-value: 1.41e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789528272   9 QELLTYRSEKAVQ-EQKIGQLLQENEAIEKEMAELSKLEEAVRRELGEGAVQPSRsgidRSQYLGQGGPQAAKveavdiY 87
Cdd:COG4942   142 KYLAPARREQAEElRADLAELAALRAELEAERAELEALLAELEEERAALEALKAE----RQKLLARLEKELAE------L 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789528272  88 AAQNKVLQEKVKDRKATLNDLLGRLRELNQRKAALPT-------LWPTNGgTITSYFGGRSDPFGNrsydwHPGVDIANE 160
Cdd:COG4942   212 AAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFaalkgklPWPVSG-RVVRRFGERDGGGGR-----NKGIDIAAP 285

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789528272 161 YGAPVYASASGTIEEAGWVSGYGRYVRIQHGYGYETAYGHMSKLAVQAGQSVSKGDVIGYVGSSGYSTGPHVHFEVLVNG 240
Cdd:COG4942   286 PGAPVRAVADGTVVYAGWLRGYGNLVIIDHGGGYLTLYAHLSSLLVKVGQRVKAGQPIGTVGSSGGQGGPTLYFELRKNG 365

                         250
                  ....*....|
gi 2789528272 241 QTTDPLELVR 250
Cdd:COG4942   366 KPVDPLPWLA 375
SpoIIQ2 COG5821
Stage II sporulation protein SpoIIQ, clostridial version, metallopeptidase M23 family [Cell ...
 119-249 7.37e-40

Stage II sporulation protein SpoIIQ, clostridial version, metallopeptidase M23 family [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444523 [Multi-domain]  Cd Length: 200  Bit Score: 136.31  E-value: 7.37e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789528272 119 KAALPTLWPTNGgTITSYFGGRS--DPFGNrSYDWHPGVDIANEYGAPVYASASGTIEEAGWVSGYGRYVRIQHGYGYET 196
Cdd:COG5821    64 STSNKFLKPVSG-KITREFGEDLvySKTLN-EWRTHTGIDIAAKEGTPVKAAADGVVVEVGKDPKYGITVVIDHGNGIKT 141

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2789528272 197 AYGHM-SKLAVQAGQSVSKGDVIGYVGSSG---YSTGPHVHFEVLVNGQTTDPLELV 249
Cdd:COG5821   142 VYANLdSKIKVKVGQKVKKGQVIGKVGSTAlfeSSEGPHLHFEVLKNGKPVDPMKYL 198
PRK11649 PRK11649
putative peptidase; Provisional
 152-246 9.90e-24

putative peptidase; Provisional


Pssm-ID: 236946 [Multi-domain]  Cd Length: 439  Bit Score: 98.58  E-value: 9.90e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789528272 152 HPGVDIANEYGAPVYASASGTIEEAGWVSGYGRYVRIQHGYGYETAYGHMSKLAVQAGQSVSKGDVIGYVGSSGYSTGPH 231
Cdd:PRK11649  313 HRGVDFAMPVGTPVLAVGDGEVVVAKRSGAAGNYVAIRHGRQYTTRYMHLRKLLVKPGQKVKRGDRIALSGNTGRSTGPH 392

                          90
                  ....*....|....*
gi 2789528272 232 VHFEVLVNGQTTDPL 246
Cdd:PRK11649  393 LHYEVWINQQAVNPL 407
SpoIIQ COG5820
Stage II sporulation protein SpoIIQ, required for engulfement [Cell cycle control, cell ...
 146-248 2.02e-19

Stage II sporulation protein SpoIIQ, required for engulfement [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444522 [Multi-domain]  Cd Length: 224  Bit Score: 83.82  E-value: 2.02e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789528272 146 NRSYDWHPGVDIANEYGAP--VYASASGTIEEAGWVSGYGRYVRIQHGYGYETAYGHMSKLAVQAGQSVSKGDVIGYVGS 223
Cdd:COG5820   114 NNTYYPSTGIDIAAKDGESfdVLAALSGTVTEVEEDPLLGYVVEIKHDNGVSTVYQSLSDVKVKAGDEVKQGQVIGTAGR 193

                          90       100
                  ....*....|....*....|....*..
gi 2789528272 224 SGYST--GPHVHFEVLVNGQTTDPLEL 248
Cdd:COG5820   194 NLFNKdaGVHLHFEVRKDGKAVNPESY 220
SpoIVFA COG5833
Stage IV sporulation protein SpoIVFA, regulates SpoIVFB [Cell cycle control, cell division, ...
 152-250 4.34e-18

Stage IV sporulation protein SpoIVFA, regulates SpoIVFB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444535 [Multi-domain]  Cd Length: 219  Bit Score: 80.04  E-value: 4.34e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789528272 152 HPGVDIANEYGAPVYASASGTIEEAGWVSGYGRYVRIQHGYGYETAYGHMSKLAVQAGQSVSKGDVIGYVGSSGYSTGpH 231
Cdd:COG5833   120 GKGVDIETPGGANVKAVKEGYVIFAGKDEETGKTVIIQHADGSESWYGNLSSIDVKLYDFVEAGQKIGTVPATEGEEG-T 198

                          90
                  ....*....|....*....
gi 2789528272 232 VHFEVLVNGQTTDPLELVR 250
Cdd:COG5833   199 FYFAIKKGGKFIDPIQVIS 217
nlpD PRK10871
murein hydrolase activator NlpD;
126-246 2.34e-14

murein hydrolase activator NlpD;


Pssm-ID: 236782 [Multi-domain]  Cd Length: 319  Bit Score: 71.02  E-value: 2.34e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789528272 126 WPTNGGTITSYFGGRSdpfGNRsydwhpGVDIANEYGAPVYASASGTIEEAG-WVSGYGRYVRIQHGYGYETAYGHMSKL 204
Cdd:PRK10871  202 WPTDGKVIENFSASEG---GNK------GIDIAGSKGQAIIATADGRVVYAGnALRGYGNLIIIKHNDDYLSAYAHNDTM 272

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2789528272 205 AVQAGQSVSKGDVIGYVGSSGYSTgPHVHFEVLVNGQTTDPL 246
Cdd:PRK10871  273 LVREQQEVKAGQKIATMGSTGTSS-TRLHFEIRYKGKSVNPL 313
PRK11637 PRK11637
AmiB activator; Provisional
 125-246 3.44e-10

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 59.32  E-value: 3.44e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789528272 125 LWPTNGGTITSyfggrsdpFGNR---SYDWHpGVDIANEYGAPVYASASGTIEEAGWVSGYGRYVRIQHGYGYETAYGHM 201
Cdd:PRK11637  308 FWPVRGPTLHR--------FGEQlqgELRWK-GMVIGASEGTEVKAIADGRVLLADWLQGYGLVVVVEHGKGDMSLYGYN 378

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2789528272 202 SKLAVQAGQSVSKGDVIGYVGSSGYSTGPHVHFEVLVNGQTTDPL 246
Cdd:PRK11637  379 QSALVSVGAQVRAGQPIALVGSSGGQGRPSLYFEIRRQGQAVNPQ 423
PRK06148 PRK06148
hypothetical protein; Provisional
 152-237 4.34e-08

hypothetical protein; Provisional


Pssm-ID: 180426 [Multi-domain]  Cd Length: 1013  Bit Score: 53.49  E-value: 4.34e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789528272  152 HPGVDIANEYGAPVYASASGTIEEAGWVS---GYGRYVRIQH----GYGYETAYGHMSKLAV---QAGQSVSKGDVIGYV 221
Cdd:PRK06148   441 HLGVDLFAPAGTPVYAPLAGTVRSVEIEAvplGYGGLVALEHetpgGDPFYTLYGHLAHEAVsrlKPGDRLAAGELFGAM 520

                           90
                   ....*....|....*...
gi 2789528272  222 GSSGYSTG--PHVHFEVL 237
Cdd:PRK06148   521 GDAHENGGwaPHLHFQLS 538
FtsB COG2919
Cell division protein FtsB [Cell cycle control, cell division, chromosome partitioning];
9-54 1.04e-03

Cell division protein FtsB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442163 [Multi-domain]  Cd Length: 96  Bit Score: 37.55  E-value: 1.04e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2789528272   9 QELLTYRSEKAVQEQKIGQLLQENEAIEKEMAELSK----LEEAVRRELG 54
Cdd:COG2919    29 LAYRELRQEIAELEAENAKLKARNAELEAEVADLKDgpdyIEERAREELG 78
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 6-234 3.76e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 38.27  E-value: 3.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789528272   6 QDQQELLTYRSEKAVQEQKIGQLLQENEAIEKEMAELSKLEEAVRRELGEGAVQPSRSGIDRSQYLGQggpQAAKVEAVD 85
Cdd:COG3883   130 ADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQ---LAELEAELA 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789528272  86 IYAAQNKVLQEKVKDRKATLNDLLGRLRELNQRKAALPTLWPTNGGTITSYFGGRSDPFGNRSYDWHPGVDIANEYGAPV 165
Cdd:COG3883   207 AAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGA 286

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2789528272 166 YASASGTIEEAGWVSGYGRYVRIQHGYGYETAYGHMSKLAVQAGQSVSKGDVIGYVGSSGYSTGPHVHF 234
Cdd:COG3883   287 GGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAVVGGASAGGGGGSGGGGGSSGGGSGGGGGGGGGG 355
Med21 pfam11221
Subunit 21 of Mediator complex; Med21 has been known as Srb7 in yeasts, hSrb7 in humans and ...
 16-55 4.91e-03

Subunit 21 of Mediator complex; Med21 has been known as Srb7 in yeasts, hSrb7 in humans and Trap 19 in Drosophila. The heterodimer of the two subunits Med7 and Med21 appears to act as a hinge between the middle and the tail regions of Mediator.


Pssm-ID: 463241  Cd Length: 134  Bit Score: 36.41  E-value: 4.91e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2789528272  16 SEKAvQEQKIGQLLQENEAIEKEMAELSKLEEAVRRELGE 55
Cdd:pfam11221  89 SEEE-QLQRIKELEEELREAEEERQEAVKEKEELLKKLDE 127
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
8-122 6.66e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 37.74  E-value: 6.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789528272   8 QQELLTYRSEKAVQEQKIGQLlqeNEAIEKEMAELSKLEEAVRR--ELGEGAVQPSRSGIDRSQYLgqggPQAAKVEA-V 84
Cdd:PRK03918  244 EKELESLEGSKRKLEEKIREL---EERIEELKKEIEELEEKVKElkELKEKAEEYIKLSEFYEEYL----DELREIEKrL 316

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2789528272  85 DIYAAQNKVLQEKVKDR---KATLNDLLGRLRELNQRKAAL 122
Cdd:PRK03918  317 SRLEEEINGIEERIKELeekEERLEELKKKLKELEKRLEEL 357
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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