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Conserved domains on  [gi|15598982|ref|NP_252476|]
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hypothetical protein PA3787 [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 ...
 119-279 8.93e-53

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: 170.54  E-value: 8.93e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598982 119 QVNPLPEDLKRIERELAEQTAAYRRFSPGLPSNLMLDKPVDGPLSSPFGLRRFFNGEERNPHSGLDFAVPAGTPIKAPAA 198
Cdd:COG0739  36 AAAALAAAALAAAVSAAASAAAAAAAAAAAIALGSGAWPVKGRITSGFGYRRHPVTGRRRFHKGIDIAAPTGTPVYAAAD 115

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598982 199 GKVILIGDYFFNGKTVFVDHGQGFISMFCHLSKIDVKLGQQVPRGGVLGKVGATGRATGPHMHWNVSLNDARVDPAIFIG 278
Cdd:COG0739 116 GTVVFAGWNGGYGNLVIIDHGNGYTTLYAHLSSILVKVGQRVKAGQVIGYVGNTGRSTGPHLHFEVRVNGKPVDPLPFLP 195


                .
gi 15598982 279 A 279
Cdd:COG0739 196 A 196
Peptidase_M23_N pfam18421
Peptidase family M23 N-terminal domain; This is the N-terminal domain of Peptidase M23 ...
 32-105 2.09e-33

Peptidase family M23 N-terminal domain; This is the N-terminal domain of Peptidase M23 pfam01551 mostly found in proteobacteria.


:

Pssm-ID: 436488  Cd Length: 73  Bit Score: 116.53  E-value: 2.09e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598982    32 NKPVPGGVAVVDLGEEGPPPRAFYQGKPVLVVREEGRRWIAVVGIPLSTKPGPQKLEVRAAtGNHEERFSVGSK 105
Cdd:pfam18421   1 NHPVPGGVAVIPLGIKGQAPEAYYQGKRVLVVPSDGNQWLAIVGIPLKTKPGIQQLTVTKP-GKRTIPFHVSSK 73
 
Name Accession Description Interval E-value
NlpD COG0739
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell ...
 119-279 8.93e-53

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: 170.54  E-value: 8.93e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598982 119 QVNPLPEDLKRIERELAEQTAAYRRFSPGLPSNLMLDKPVDGPLSSPFGLRRFFNGEERNPHSGLDFAVPAGTPIKAPAA 198
Cdd:COG0739  36 AAAALAAAALAAAVSAAASAAAAAAAAAAAIALGSGAWPVKGRITSGFGYRRHPVTGRRRFHKGIDIAAPTGTPVYAAAD 115

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598982 199 GKVILIGDYFFNGKTVFVDHGQGFISMFCHLSKIDVKLGQQVPRGGVLGKVGATGRATGPHMHWNVSLNDARVDPAIFIG 278
Cdd:COG0739 116 GTVVFAGWNGGYGNLVIIDHGNGYTTLYAHLSSILVKVGQRVKAGQVIGYVGNTGRSTGPHLHFEVRVNGKPVDPLPFLP 195


                .
gi 15598982 279 A 279
Cdd:COG0739 196 A 196
Peptidase_M23 pfam01551
Peptidase family M23; Members of this family are zinc metallopeptidases with a range of ...
 179-273 7.01e-40

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: 134.21  E-value: 7.01e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598982   179 PHSGLDFAVPAGTPIKAPAAGKVILIGDYFFNGKTVFVDHGQGFISMFCHLSKIDVKLGQQVPRGGVLGKVGATGRATGP 258
Cdd:pfam01551   2 FHKGIDIAAPTGTPVYAAADGVVVFAGWLGGYGNLVIIDHGNGYSTLYAHLSSILVKVGQRVKAGQVIGTVGSTGRSTGP 81

                          90
                  ....*....|....*
gi 15598982   259 HMHWNVSLNDARVDP 273
Cdd:pfam01551  82 HLHFEIRKNGKPVDP 96
M23_peptidase cd12797
M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; ...
 180-264 1.65e-38

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: 130.02  E-value: 1.65e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598982 180 HSGLDFAVPAGTPIKAPAAGKVILIGDYFFNGKTVFVDHGQGFISMFCHLSKIDVKLGQQVPRGGVLGKVGATGRATGPH 259
Cdd:cd12797   1 HNGIDIAAPEGTPVYAAADGTVVFAGWDGGYGNYVIIDHGNGYYTLYAHLSSILVKVGQRVKKGQVIGTVGNTGRSTGPH 80


                ....*
gi 15598982 260 MHWNV 264
Cdd:cd12797  81 LHFEI 85
Peptidase_M23_N pfam18421
Peptidase family M23 N-terminal domain; This is the N-terminal domain of Peptidase M23 ...
 32-105 2.09e-33

Peptidase family M23 N-terminal domain; This is the N-terminal domain of Peptidase M23 pfam01551 mostly found in proteobacteria.


Pssm-ID: 436488  Cd Length: 73  Bit Score: 116.53  E-value: 2.09e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598982    32 NKPVPGGVAVVDLGEEGPPPRAFYQGKPVLVVREEGRRWIAVVGIPLSTKPGPQKLEVRAAtGNHEERFSVGSK 105
Cdd:pfam18421   1 NHPVPGGVAVIPLGIKGQAPEAYYQGKRVLVVPSDGNQWLAIVGIPLKTKPGIQQLTVTKP-GKRTIPFHVSSK 73
PRK11649 PRK11649
putative peptidase; Provisional
 162-273 6.23e-21

putative peptidase; Provisional


Pssm-ID: 236946 [Multi-domain]  Cd Length: 439  Bit Score: 91.65  E-value: 6.23e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598982  162 LSSPFGLRRFFNGEER-NPHSGLDFAVPAGTPIKAPAAGKVILIGDYFFNGKTVFVDHGQGFISMFCHLSKIDVKLGQQV 240
Cdd:PRK11649 294 ISSNFNPRRLNPVTGRvAPHRGVDFAMPVGTPVLAVGDGEVVVAKRSGAAGNYVAIRHGRQYTTRYMHLRKLLVKPGQKV 373

                         90       100       110
                 ....*....|....*....|....*....|...
gi 15598982  241 PRGGVLGKVGATGRATGPHMHWNVSLNDARVDP 273
Cdd:PRK11649 374 KRGDRIALSGNTGRSTGPHLHYEVWINQQAVNP 406
 
Name Accession Description Interval E-value
NlpD COG0739
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell ...
 119-279 8.93e-53

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: 170.54  E-value: 8.93e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598982 119 QVNPLPEDLKRIERELAEQTAAYRRFSPGLPSNLMLDKPVDGPLSSPFGLRRFFNGEERNPHSGLDFAVPAGTPIKAPAA 198
Cdd:COG0739  36 AAAALAAAALAAAVSAAASAAAAAAAAAAAIALGSGAWPVKGRITSGFGYRRHPVTGRRRFHKGIDIAAPTGTPVYAAAD 115

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598982 199 GKVILIGDYFFNGKTVFVDHGQGFISMFCHLSKIDVKLGQQVPRGGVLGKVGATGRATGPHMHWNVSLNDARVDPAIFIG 278
Cdd:COG0739 116 GTVVFAGWNGGYGNLVIIDHGNGYTTLYAHLSSILVKVGQRVKAGQVIGYVGNTGRSTGPHLHFEVRVNGKPVDPLPFLP 195


                .
gi 15598982 279 A 279
Cdd:COG0739 196 A 196
Peptidase_M23 pfam01551
Peptidase family M23; Members of this family are zinc metallopeptidases with a range of ...
 179-273 7.01e-40

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: 134.21  E-value: 7.01e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598982   179 PHSGLDFAVPAGTPIKAPAAGKVILIGDYFFNGKTVFVDHGQGFISMFCHLSKIDVKLGQQVPRGGVLGKVGATGRATGP 258
Cdd:pfam01551   2 FHKGIDIAAPTGTPVYAAADGVVVFAGWLGGYGNLVIIDHGNGYSTLYAHLSSILVKVGQRVKAGQVIGTVGSTGRSTGP 81

                          90
                  ....*....|....*
gi 15598982   259 HMHWNVSLNDARVDP 273
Cdd:pfam01551  82 HLHFEIRKNGKPVDP 96
M23_peptidase cd12797
M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; ...
 180-264 1.65e-38

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: 130.02  E-value: 1.65e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598982 180 HSGLDFAVPAGTPIKAPAAGKVILIGDYFFNGKTVFVDHGQGFISMFCHLSKIDVKLGQQVPRGGVLGKVGATGRATGPH 259
Cdd:cd12797   1 HNGIDIAAPEGTPVYAAADGTVVFAGWDGGYGNYVIIDHGNGYYTLYAHLSSILVKVGQRVKKGQVIGTVGNTGRSTGPH 80


                ....*
gi 15598982 260 MHWNV 264
Cdd:cd12797  81 LHFEI 85
SpoIIQ2 COG5821
Stage II sporulation protein SpoIIQ, clostridial version, metallopeptidase M23 family [Cell ...
 117-277 3.46e-34

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: 122.83  E-value: 3.46e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598982 117 KRQVNPLPEDLKRIERELAEQTAAyrrfSPGLPSNLMLDKPVDGPLSSPFGLRRFFN---GEERNpHSGLDFAVPAGTPI 193
Cdd:COG5821  36 NNNLNKLEEETVKNKSESNEKSKS----KVTASTSNKFLKPVSGKITREFGEDLVYSktlNEWRT-HTGIDIAAKEGTPV 110

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598982 194 KAPAAGKVILIGDYFFNGKTVFVDHGQGFISMFCHL-SKIDVKLGQQVPRGGVLGKVGATGR---ATGPHMHWNVSLNDA 269
Cdd:COG5821 111 KAAADGVVVEVGKDPKYGITVVIDHGNGIKTVYANLdSKIKVKVGQKVKKGQVIGKVGSTALfesSEGPHLHFEVLKNGK 190


                ....*...
gi 15598982 270 RVDPAIFI 277
Cdd:COG5821 191 PVDPMKYL 198
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 85-279 1.94e-33

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: 125.26  E-value: 1.94e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598982  85 QKLEVRAATGNHEERFSVGSKHYREQRITLKN-KRQVNPLPEDLKRIERELAEqtAAYRRFSPGLPSNL-MLDKPVDGPL 162
Cdd:COG4942 186 ERAALEALKAERQKLLARLEKELAELAAELAElQQEAEELEALIARLEAEAAA--AAERTPAAGFAALKgKLPWPVSGRV 263

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598982 163 SSPFGLRRffNGEERNPhsGLDFAVPAGTPIKAPAAGKVILIGDYFFNGKTVFVDHGQGFISMFCHLSKIDVKLGQQVPR 242
Cdd:COG4942 264 VRRFGERD--GGGGRNK--GIDIAAPPGAPVRAVADGTVVYAGWLRGYGNLVIIDHGGGYLTLYAHLSSLLVKVGQRVKA 339

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 15598982 243 GGVLGKVGATGRATGPHMHWNVSLNDARVDPAIFIGA 279
Cdd:COG4942 340 GQPIGTVGSSGGQGGPTLYFELRKNGKPVDPLPWLAK 376
Peptidase_M23_N pfam18421
Peptidase family M23 N-terminal domain; This is the N-terminal domain of Peptidase M23 ...
 32-105 2.09e-33

Peptidase family M23 N-terminal domain; This is the N-terminal domain of Peptidase M23 pfam01551 mostly found in proteobacteria.


Pssm-ID: 436488  Cd Length: 73  Bit Score: 116.53  E-value: 2.09e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598982    32 NKPVPGGVAVVDLGEEGPPPRAFYQGKPVLVVREEGRRWIAVVGIPLSTKPGPQKLEVRAAtGNHEERFSVGSK 105
Cdd:pfam18421   1 NHPVPGGVAVIPLGIKGQAPEAYYQGKRVLVVPSDGNQWLAIVGIPLKTKPGIQQLTVTKP-GKRTIPFHVSSK 73
PRK11649 PRK11649
putative peptidase; Provisional
 162-273 6.23e-21

putative peptidase; Provisional


Pssm-ID: 236946 [Multi-domain]  Cd Length: 439  Bit Score: 91.65  E-value: 6.23e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598982  162 LSSPFGLRRFFNGEER-NPHSGLDFAVPAGTPIKAPAAGKVILIGDYFFNGKTVFVDHGQGFISMFCHLSKIDVKLGQQV 240
Cdd:PRK11649 294 ISSNFNPRRLNPVTGRvAPHRGVDFAMPVGTPVLAVGDGEVVVAKRSGAAGNYVAIRHGRQYTTRYMHLRKLLVKPGQKV 373

                         90       100       110
                 ....*....|....*....|....*....|...
gi 15598982  241 PRGGVLGKVGATGRATGPHMHWNVSLNDARVDP 273
Cdd:PRK11649 374 KRGDRIALSGNTGRSTGPHLHYEVWINQQAVNP 406
SpoIVFA COG5833
Stage IV sporulation protein SpoIVFA, regulates SpoIVFB [Cell cycle control, cell division, ...
 157-274 1.43e-11

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


Pssm-ID: 444535 [Multi-domain]  Cd Length: 219  Bit Score: 62.70  E-value: 1.43e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598982 157 PVDGPLSSPFGLRrffngeernpHSGLDFAVPAGTPIKAPAAGKVILIGDYFFNGKTVFVDHGQGFISMFCHLSKIDVKL 236
Cdd:COG5833 107 PVSGKVVESFQEN----------GKGVDIETPGGANVKAVKEGYVIFAGKDEETGKTVIIQHADGSESWYGNLSSIDVKL 176

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 15598982 237 GQQVPRGGVLGKVGATGRATGpHMHWNVSLNDARVDPA 274
Cdd:COG5833 177 YDFVEAGQKIGTVPATEGEEG-TFYFAIKKGGKFIDPI 213
PRK06148 PRK06148
hypothetical protein; Provisional
 170-266 9.00e-07

hypothetical protein; Provisional


Pssm-ID: 180426 [Multi-domain]  Cd Length: 1013  Bit Score: 50.02  E-value: 9.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598982   170 RFFNGEERNPHSGLDFAVPAGTPIKAPAAGKVILIG------DYffnGKTVFVDH----GQGFISMFCHLSKIDV---KL 236
Cdd:PRK06148  431 RFIEGERRTVHLGVDLFAPAGTPVYAPLAGTVRSVEieavplGY---GGLVALEHetpgGDPFYTLYGHLAHEAVsrlKP 507

                          90       100       110
                  ....*....|....*....|....*....|..
gi 15598982   237 GQQVPRGGVLGKVGATGRATG--PHMHWNVSL 266
Cdd:PRK06148  508 GDRLAAGELFGAMGDAHENGGwaPHLHFQLST 539
PRK11637 PRK11637
AmiB activator; Provisional
 157-253 2.80e-05

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 45.07  E-value: 2.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598982  157 PVDGPLSSPFGLRrfFNGEERnpHSGLDFAVPAGTPIKAPAAGKVILiGDYFFN-GKTVFVDHGQGFISMFCHLSKIDVK 235
Cdd:PRK11637 310 PVRGPTLHRFGEQ--LQGELR--WKGMVIGASEGTEVKAIADGRVLL-ADWLQGyGLVVVVEHGKGDMSLYGYNQSALVS 384

                         90
                 ....*....|....*...
gi 15598982  236 LGQQVPRGGVLGKVGATG 253
Cdd:PRK11637 385 VGAQVRAGQPIALVGSSG 402
PRK06149 PRK06149
aminotransferase;
180-254 5.93e-03

aminotransferase;


Pssm-ID: 235716 [Multi-domain]  Cd Length: 972  Bit Score: 38.05  E-value: 5.93e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598982  180 HSGLDFAVPAGTPIKAPAAGKVILIGDyffnGKTVFVDHGqgfisMFCHLSKID--VKLGQQVPRGGVLGKVGATGR 254
Cdd:PRK06149 432 ALGVDLCLPAGTAVAAPFAGTVVRDGQ----GHLTLRGDA-----LELHLDGVEpaVEDGAAVRAGDPLGSVAGEGP 499
 
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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