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Conserved domains on  [gi|9950636|gb|AAG07792|]
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hypothetical protein PA4404 [Pseudomonas aeruginosa PAO1]

Protein Classification

M23 family metallopeptidase( domain architecture ID 11432770)

M23 family metallopeptidase lyses bacterial cell wall peptidoglycans

EC:  3.4.24.-
Gene Ontology:  GO:0046872|GO:0008237
MEROPS:  M23
PubMed:  36386627

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 ...
 141-301 4.64e-49

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: 162.06  E-value: 4.64e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9950636  141 ATLDELAARLDTREQQLEVLEQLLADKHISQSTYLAGQPVrQGYISSPFGRRVNPVSGRLSMHKGIDFAAPAGSDVVAVA 220
Cdd:COG0739  36 AAAALAAAALAAAVSAAASAAAAAAAAAAAIALGSGAWPV-KGRITSGFGYRRHPVTGRRRFHKGIDIAAPTGTPVYAAA 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9950636  221 AGVVTWSGRKNGYGNVVEVGHADGYTTLYAHNQKNLVEVGDLVKRGQVLAKVGSTGRSTGYHVHFEVMKDGRVMNPQSFI 300
Cdd:COG0739 115 DGTVVFAGWNGGYGNLVIIDHGNGYTTLYAHLSSILVKVGQRVKAGQVIGYVGNTGRSTGPHLHFEVRVNGKPVDPLPFL 194


                .
gi 9950636  301 A 301
Cdd:COG0739 195 P 195
 
Name Accession Description Interval E-value
NlpD COG0739
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell ...
 141-301 4.64e-49

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: 162.06  E-value: 4.64e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9950636  141 ATLDELAARLDTREQQLEVLEQLLADKHISQSTYLAGQPVrQGYISSPFGRRVNPVSGRLSMHKGIDFAAPAGSDVVAVA 220
Cdd:COG0739  36 AAAALAAAALAAAVSAAASAAAAAAAAAAAIALGSGAWPV-KGRITSGFGYRRHPVTGRRRFHKGIDIAAPTGTPVYAAA 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9950636  221 AGVVTWSGRKNGYGNVVEVGHADGYTTLYAHNQKNLVEVGDLVKRGQVLAKVGSTGRSTGYHVHFEVMKDGRVMNPQSFI 300
Cdd:COG0739 115 DGTVVFAGWNGGYGNLVIIDHGNGYTTLYAHLSSILVKVGQRVKAGQVIGYVGNTGRSTGPHLHFEVRVNGKPVDPLPFL 194


                .
gi 9950636  301 A 301
Cdd:COG0739 195 P 195
Peptidase_M23 pfam01551
Peptidase family M23; Members of this family are zinc metallopeptidases with a range of ...
 201-296 2.13e-36

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: 125.74  E-value: 2.13e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9950636    201 SMHKGIDFAAPAGSDVVAVAAGVVTWSGRKNGYGNVVEVGHADGYTTLYAHNQKNLVEVGDLVKRGQVLAKVGSTGRSTG 280
Cdd:pfam01551   1 RFHKGIDIAAPTGTPVYAAADGVVVFAGWLGGYGNLVIIDHGNGYSTLYAHLSSILVKVGQRVKAGQVIGTVGSTGRSTG 80

                          90
                  ....*....|....*.
gi 9950636    281 YHVHFEVMKDGRVMNP 296
Cdd:pfam01551  81 PHLHFEIRKNGKPVDP 96
M23_peptidase cd12797
M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; ...
 203-287 1.20e-30

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: 110.37  E-value: 1.20e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9950636  203 HKGIDFAAPAGSDVVAVAAGVVTWSGRKNGYGNVVEVGHADGYTTLYAHNQKNLVEVGDLVKRGQVLAKVGSTGRSTGYH 282
Cdd:cd12797   1 HNGIDIAAPEGTPVYAAADGTVVFAGWDGGYGNYVIIDHGNGYYTLYAHLSSILVKVGQRVKKGQVIGTVGNTGRSTGPH 80


                ....*
gi 9950636  283 VHFEV 287
Cdd:cd12797  81 LHFEI 85
PRK11649 PRK11649
putative peptidase; Provisional
 180-296 1.61e-25

putative peptidase; Provisional


Pssm-ID: 236946 [Multi-domain]  Cd Length: 439  Bit Score: 105.13  E-value: 1.61e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9950636   180 VRQGYISSPFG-RRVNPVSGRLSMHKGIDFAAPAGSDVVAVAAGVVTWSGRKNGYGNVVEVGHADGYTTLYAHNQKNLVE 258
Cdd:PRK11649 289 AKQFRISSNFNpRRLNPVTGRVAPHRGVDFAMPVGTPVLAVGDGEVVVAKRSGAAGNYVAIRHGRQYTTRYMHLRKLLVK 368

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 9950636   259 VGDLVKRGQVLAKVGSTGRSTGYHVHFEVMKDGRVMNP 296
Cdd:PRK11649 369 PGQKVKRGDRIALSGNTGRSTGPHLHYEVWINQQAVNP 406
 
Name Accession Description Interval E-value
NlpD COG0739
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell ...
 141-301 4.64e-49

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: 162.06  E-value: 4.64e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9950636  141 ATLDELAARLDTREQQLEVLEQLLADKHISQSTYLAGQPVrQGYISSPFGRRVNPVSGRLSMHKGIDFAAPAGSDVVAVA 220
Cdd:COG0739  36 AAAALAAAALAAAVSAAASAAAAAAAAAAAIALGSGAWPV-KGRITSGFGYRRHPVTGRRRFHKGIDIAAPTGTPVYAAA 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9950636  221 AGVVTWSGRKNGYGNVVEVGHADGYTTLYAHNQKNLVEVGDLVKRGQVLAKVGSTGRSTGYHVHFEVMKDGRVMNPQSFI 300
Cdd:COG0739 115 DGTVVFAGWNGGYGNLVIIDHGNGYTTLYAHLSSILVKVGQRVKAGQVIGYVGNTGRSTGPHLHFEVRVNGKPVDPLPFL 194


                .
gi 9950636  301 A 301
Cdd:COG0739 195 P 195
Peptidase_M23 pfam01551
Peptidase family M23; Members of this family are zinc metallopeptidases with a range of ...
 201-296 2.13e-36

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: 125.74  E-value: 2.13e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9950636    201 SMHKGIDFAAPAGSDVVAVAAGVVTWSGRKNGYGNVVEVGHADGYTTLYAHNQKNLVEVGDLVKRGQVLAKVGSTGRSTG 280
Cdd:pfam01551   1 RFHKGIDIAAPTGTPVYAAADGVVVFAGWLGGYGNLVIIDHGNGYSTLYAHLSSILVKVGQRVKAGQVIGTVGSTGRSTG 80

                          90
                  ....*....|....*.
gi 9950636    281 YHVHFEVMKDGRVMNP 296
Cdd:pfam01551  81 PHLHFEIRKNGKPVDP 96
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 59-302 3.33e-34

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: 127.96  E-value: 3.33e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9950636   59 AALQAQSAEISSAREDAQRQMDALSVHLGELQARLVRLDALGERLTELADVdpdefdfslsvgqggvdepLEGSAYAPPS 138
Cdd:COG4942 153 EELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLAR-------------------LEKELAELAA 213

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9950636  139 FMATLDELAARLDTREQQLEVLEQLLADKHISQS-TYLAGQ---PVRqGYISSPFGRRVNPVSGrlsmHKGIDFAAPAGS 214
Cdd:COG4942 214 ELAELQQEAEELEALIARLEAEAAAAAERTPAAGfAALKGKlpwPVS-GRVVRRFGERDGGGGR----NKGIDIAAPPGA 288

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9950636  215 DVVAVAAGVVTWSGRKNGYGNVVEVGHADGYTTLYAHNQKNLVEVGDLVKRGQVLAKVGSTGRSTGYHVHFEVMKDGRVM 294
Cdd:COG4942 289 PVRAVADGTVVYAGWLRGYGNLVIIDHGGGYLTLYAHLSSLLVKVGQRVKAGQPIGTVGSSGGQGGPTLYFELRKNGKPV 368


                ....*...
gi 9950636  295 NPQSFIAR 302
Cdd:COG4942 369 DPLPWLAK 376
M23_peptidase cd12797
M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; ...
 203-287 1.20e-30

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: 110.37  E-value: 1.20e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9950636  203 HKGIDFAAPAGSDVVAVAAGVVTWSGRKNGYGNVVEVGHADGYTTLYAHNQKNLVEVGDLVKRGQVLAKVGSTGRSTGYH 282
Cdd:cd12797   1 HNGIDIAAPEGTPVYAAADGTVVFAGWDGGYGNYVIIDHGNGYYTLYAHLSSILVKVGQRVKKGQVIGTVGNTGRSTGPH 80


                ....*
gi 9950636  283 VHFEV 287
Cdd:cd12797  81 LHFEI 85
SpoIIQ2 COG5821
Stage II sporulation protein SpoIIQ, clostridial version, metallopeptidase M23 family [Cell ...
 179-300 1.81e-30

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: 113.97  E-value: 1.81e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9950636  179 PVRqGYISSPFGRR--VNPVSGRLSMHKGIDFAAPAGSDVVAVAAGVVTWSGRKNGYGNVVEVGHADGYTTLYAH-NQKN 255
Cdd:COG5821  72 PVS-GKITREFGEDlvYSKTLNEWRTHTGIDIAAKEGTPVKAAADGVVVEVGKDPKYGITVVIDHGNGIKTVYANlDSKI 150

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 9950636  256 LVEVGDLVKRGQVLAKVGSTGR---STGYHVHFEVMKDGRVMNPQSFI 300
Cdd:COG5821 151 KVKVGQKVKKGQVIGKVGSTALfesSEGPHLHFEVLKNGKPVDPMKYL 198
PRK11649 PRK11649
putative peptidase; Provisional
 180-296 1.61e-25

putative peptidase; Provisional


Pssm-ID: 236946 [Multi-domain]  Cd Length: 439  Bit Score: 105.13  E-value: 1.61e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9950636   180 VRQGYISSPFG-RRVNPVSGRLSMHKGIDFAAPAGSDVVAVAAGVVTWSGRKNGYGNVVEVGHADGYTTLYAHNQKNLVE 258
Cdd:PRK11649 289 AKQFRISSNFNpRRLNPVTGRVAPHRGVDFAMPVGTPVLAVGDGEVVVAKRSGAAGNYVAIRHGRQYTTRYMHLRKLLVK 368

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 9950636   259 VGDLVKRGQVLAKVGSTGRSTGYHVHFEVMKDGRVMNP 296
Cdd:PRK11649 369 PGQKVKRGDRIALSGNTGRSTGPHLHYEVWINQQAVNP 406
SpoIIQ COG5820
Stage II sporulation protein SpoIIQ, required for engulfement [Cell cycle control, cell ...
 201-301 5.49e-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: 5.49e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9950636  201 SMHKGIDFAAPAGSDVVAVAAGVVTWSGRKNG--YGNVVEVGHADGYTTLYAHNQKNLVEVGDLVKRGQVLAKvgsTGRS 278
Cdd:COG5820 118 YPSTGIDIAAKDGESFDVLAALSGTVTEVEEDplLGYVVEIKHDNGVSTVYQSLSDVKVKAGDEVKQGQVIGT---AGRN 194

                        90       100
                ....*....|....*....|....*...
gi 9950636  279 T-----GYHVHFEVMKDGRVMNPQSFIA 301
Cdd:COG5820 195 LfnkdaGVHLHFEVRKDGKAVNPESYLP 222
SpoIVFA COG5833
Stage IV sporulation protein SpoIVFA, regulates SpoIVFB [Cell cycle control, cell division, ...
 193-300 7.61e-13

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


Pssm-ID: 444535 [Multi-domain]  Cd Length: 219  Bit Score: 66.55  E-value: 7.61e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9950636  193 VNPVSGRLSM-----HKGIDFAAPAGSDVVAVAAGVVTWSGRKNGYGNVVEVGHADGYTTLYAHNQKNLVEVGDLVKRGQ 267
Cdd:COG5833 105 ALPVSGKVVEsfqenGKGVDIETPGGANVKAVKEGYVIFAGKDEETGKTVIIQHADGSESWYGNLSSIDVKLYDFVEAGQ 184

                        90       100       110
                ....*....|....*....|....*....|...
gi 9950636  268 VLAKVGSTGRSTGYhVHFEVMKDGRVMNPQSFI 300
Cdd:COG5833 185 KIGTVPATEGEEGT-FYFAIKKGGKFIDPIQVI 216
PRK11637 PRK11637
AmiB activator; Provisional
 181-302 7.61e-13

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 68.57  E-value: 7.61e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9950636   181 RQGYISSPFGRRVNPVSGRLsMH------------KGIDFAAPAGSDVVAVAAGVVTWSGRKNGYGNVVEVGHADGYTTL 248
Cdd:PRK11637 296 RTGGLGRPRGQAFWPVRGPT-LHrfgeqlqgelrwKGMVIGASEGTEVKAIADGRVLLADWLQGYGLVVVVEHGKGDMSL 374

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 9950636   249 YAHNQKNLVEVGDLVKRGQVLAKVGSTGRSTGYHVHFEVMKDGRVMNPQSFIAR 302
Cdd:PRK11637 375 YGYNQSALVSVGAQVRAGQPIALVGSSGGQGRPSLYFEIRRQGQAVNPQPWLGR 428
nlpD PRK10871
murein hydrolase activator NlpD;
204-296 1.02e-11

murein hydrolase activator NlpD;


Pssm-ID: 236782 [Multi-domain]  Cd Length: 319  Bit Score: 64.47  E-value: 1.02e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9950636   204 KGIDFAAPAGSDVVAVAAGVVTWSGRK-NGYGNVVEVGHADGYTTLYAHNQKNLVEVGDLVKRGQVLAKVGSTGRSTgYH 282
Cdd:PRK10871 220 KGIDIAGSKGQAIIATADGRVVYAGNAlRGYGNLIIIKHNDDYLSAYAHNDTMLVREQQEVKAGQKIATMGSTGTSS-TR 298

                         90
                 ....*....|....
gi 9950636   283 VHFEVMKDGRVMNP 296
Cdd:PRK10871 299 LHFEIRYKGKSVNP 312
PRK06148 PRK06148
hypothetical protein; Provisional
 195-290 3.92e-03

hypothetical protein; Provisional


Pssm-ID: 180426 [Multi-domain]  Cd Length: 1013  Bit Score: 38.85  E-value: 3.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9950636    195 PVSGRLSMHKGIDFAAPAGSDVVAVAAGVVTWSGRKN---GYGNVV----EVGHADGYTTLYAHNQKNLV---EVGDLVK 264
Cdd:PRK06148  433 IEGERRTVHLGVDLFAPAGTPVYAPLAGTVRSVEIEAvplGYGGLValehETPGGDPFYTLYGHLAHEAVsrlKPGDRLA 512

                          90       100
                  ....*....|....*....|....*...
gi 9950636    265 RGQVLAKVGSTGRSTGY--HVHFEVMKD 290
Cdd:PRK06148  513 AGELFGAMGDAHENGGWapHLHFQLSTD 540
 
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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