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Conserved domains on  [gi|446382473|ref|WP_000460328|]
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M23 family metallopeptidase [Leptospira interrogans]

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 ...
 181-357 3.71e-28

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: 109.29  E-value: 3.71e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382473 181 LLNGIEPRLRGYSFPVPDGLISSFDSQLpnAPRTYRNGVHKGIDIYKKKeldgqirnlnfQDEIISPADGIVIRADHSys 260
Cdd:COG0739   60 AAAAAAIALGSGAWPVKGRITSGFGYRR--HPVTGRRRFHKGIDIAAPT-----------GTPVYAAADGTVVFAGWN-- 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382473 261 pmtlSDYeyhttqsqkgtvtyvekdfgGRQVWIDHGHGVMTSFNHLSSIhkNIKVGEKVKQGESIGTVGNSGLleeakni 340
Cdd:COG0739  125 ----GGY--------------------GNLVIIDHGNGYTTLYAHLSSI--LVKVGQRVKAGQVIGYVGNTGR------- 171

                        170
                 ....*....|....*..
gi 446382473 341 SDNIHLHFEIWVDGEFL 357
Cdd:COG0739  172 STGPHLHFEVRVNGKPV 188
F5_F8_type_C pfam00754
F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.
 65-166 1.94e-11

F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.


:

Pssm-ID: 459925 [Multi-domain]  Cd Length: 127  Bit Score: 60.92  E-value: 1.94e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382473   65 AEYGGFNLFDSDPNTHWYSVNRSDSEWVIVDFGSKRLINGLEITVPIFKKERAVKKYEIQVliRDD---WRTILTNQ--- 138
Cdd:pfam00754  10 GEGPAAAALDGDPNTAWSAWSGDDPQWIQVDLGKPKKITGVVTQGRQDGSNGYVTSYKIEY--SLDgenWTTVKDEKipg 87

                          90       100       110
                  ....*....|....*....|....*....|...
gi 446382473  139 -----NVELHNFHKlgNIDASVLRIYFPDSTNR 166
Cdd:pfam00754  88 nndnnTPVTNTFDP--PIKARYVRIVPTSWNGG 118
 
Name Accession Description Interval E-value
NlpD COG0739
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell ...
 181-357 3.71e-28

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: 109.29  E-value: 3.71e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382473 181 LLNGIEPRLRGYSFPVPDGLISSFDSQLpnAPRTYRNGVHKGIDIYKKKeldgqirnlnfQDEIISPADGIVIRADHSys 260
Cdd:COG0739   60 AAAAAAIALGSGAWPVKGRITSGFGYRR--HPVTGRRRFHKGIDIAAPT-----------GTPVYAAADGTVVFAGWN-- 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382473 261 pmtlSDYeyhttqsqkgtvtyvekdfgGRQVWIDHGHGVMTSFNHLSSIhkNIKVGEKVKQGESIGTVGNSGLleeakni 340
Cdd:COG0739  125 ----GGY--------------------GNLVIIDHGNGYTTLYAHLSSI--LVKVGQRVKAGQVIGYVGNTGR------- 171

                        170
                 ....*....|....*..
gi 446382473 341 SDNIHLHFEIWVDGEFL 357
Cdd:COG0739  172 STGPHLHFEVRVNGKPV 188
Peptidase_M23 pfam01551
Peptidase family M23; Members of this family are zinc metallopeptidases with a range of ...
 277-355 4.30e-19

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: 81.44  E-value: 4.30e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382473  277 GTVTYVEKDFG-GRQVWIDHGHGVMTSFNHLSSIhkNIKVGEKVKQGESIGTVGNSGLleeakniSDNIHLHFEIWVDGE 355
Cdd:pfam01551  22 GVVVFAGWLGGyGNLVIIDHGNGYSTLYAHLSSI--LVKVGQRVKAGQVIGTVGSTGR-------STGPHLHFEIRKNGK 92
M23_peptidase cd12797
M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; ...
 220-350 1.48e-18

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: 79.56  E-value: 1.48e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382473 220 HKGIDIYKKKEldgqirnlnfqDEIISPADGIVIRADhsyspmtlsdyeyhttqsqkgtvtyvEKDFGGRQVWIDHGHGV 299
Cdd:cd12797    1 HNGIDIAAPEG-----------TPVYAAADGTVVFAG--------------------------WDGGYGNYVIIDHGNGY 43

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446382473 300 MTSFNHLSSIhkNIKVGEKVKQGESIGTVGNSGLleeakniSDNIHLHFEI 350
Cdd:cd12797   44 YTLYAHLSSI--LVKVGQRVKKGQVIGTVGNTGR-------STGPHLHFEI 85
F5_F8_type_C pfam00754
F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.
 65-166 1.94e-11

F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.


Pssm-ID: 459925 [Multi-domain]  Cd Length: 127  Bit Score: 60.92  E-value: 1.94e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382473   65 AEYGGFNLFDSDPNTHWYSVNRSDSEWVIVDFGSKRLINGLEITVPIFKKERAVKKYEIQVliRDD---WRTILTNQ--- 138
Cdd:pfam00754  10 GEGPAAAALDGDPNTAWSAWSGDDPQWIQVDLGKPKKITGVVTQGRQDGSNGYVTSYKIEY--SLDgenWTTVKDEKipg 87

                          90       100       110
                  ....*....|....*....|....*....|...
gi 446382473  139 -----NVELHNFHKlgNIDASVLRIYFPDSTNR 166
Cdd:pfam00754  88 nndnnTPVTNTFDP--PIKARYVRIVPTSWNGG 118
PRK11649 PRK11649
putative peptidase; Provisional
 277-353 3.72e-08

putative peptidase; Provisional


Pssm-ID: 236946 [Multi-domain]  Cd Length: 439  Bit Score: 55.06  E-value: 3.72e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446382473 277 GTVTYVEKD-FGGRQVWIDHGHGVMTSFNHLSSIHknIKVGEKVKQGESIGTVGNSGLleeakniSDNIHLHFEIWVD 353
Cdd:PRK11649 332 GEVVVAKRSgAAGNYVAIRHGRQYTTRYMHLRKLL--VKPGQKVKRGDRIALSGNTGR-------STGPHLHYEVWIN 400
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 66-154 2.02e-03

Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached carbohydrate-binding domain, present in eukaryotes and assumed to have horizontally transferred to eubacterial genomes.


Pssm-ID: 238014 [Multi-domain]  Cd Length: 143  Bit Score: 38.10  E-value: 2.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382473  66 EYGGFNLFDSDPNTHWYSVNRSDSEWVIVDFGSKRLINGLEITVP--IFKKERaVKKYEIQV-LIRDDWRTILTNQNVEL 142
Cdd:cd00057   22 SGWEASRARLNSDNAWTPAVNDPPQWLQVDLGKTRRVTGIQTQGRkgGGSSEW-VTSYKVQYsLDGETWTTYKDKGEEKV 100

                         90
                 ....*....|..
gi 446382473 143 HNfhklGNIDAS 154
Cdd:cd00057  101 FT----GNSDGS 108
 
Name Accession Description Interval E-value
NlpD COG0739
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell ...
 181-357 3.71e-28

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: 109.29  E-value: 3.71e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382473 181 LLNGIEPRLRGYSFPVPDGLISSFDSQLpnAPRTYRNGVHKGIDIYKKKeldgqirnlnfQDEIISPADGIVIRADHSys 260
Cdd:COG0739   60 AAAAAAIALGSGAWPVKGRITSGFGYRR--HPVTGRRRFHKGIDIAAPT-----------GTPVYAAADGTVVFAGWN-- 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382473 261 pmtlSDYeyhttqsqkgtvtyvekdfgGRQVWIDHGHGVMTSFNHLSSIhkNIKVGEKVKQGESIGTVGNSGLleeakni 340
Cdd:COG0739  125 ----GGY--------------------GNLVIIDHGNGYTTLYAHLSSI--LVKVGQRVKAGQVIGYVGNTGR------- 171

                        170
                 ....*....|....*..
gi 446382473 341 SDNIHLHFEIWVDGEFL 357
Cdd:COG0739  172 STGPHLHFEVRVNGKPV 188
SpoIIQ2 COG5821
Stage II sporulation protein SpoIIQ, clostridial version, metallopeptidase M23 family [Cell ...
 245-355 9.64e-21

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: 88.93  E-value: 9.64e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382473 245 ISPADGIVIRA---DHSYSPmTLSDYEYHT---------TQ---SQKGTVTYVEKDFG-GRQVWIDHGHGVMTSFNHLSS 308
Cdd:COG5821   70 LKPVSGKITREfgeDLVYSK-TLNEWRTHTgidiaakegTPvkaAADGVVVEVGKDPKyGITVVIDHGNGIKTVYANLDS 148

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 446382473 309 iHKNIKVGEKVKQGESIGTVGNSGLLEeaknISDNIHLHFEIWVDGE 355
Cdd:COG5821  149 -KIKVKVGQKVKKGQVIGKVGSTALFE----SSEGPHLHFEVLKNGK 190
Peptidase_M23 pfam01551
Peptidase family M23; Members of this family are zinc metallopeptidases with a range of ...
 277-355 4.30e-19

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: 81.44  E-value: 4.30e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382473  277 GTVTYVEKDFG-GRQVWIDHGHGVMTSFNHLSSIhkNIKVGEKVKQGESIGTVGNSGLleeakniSDNIHLHFEIWVDGE 355
Cdd:pfam01551  22 GVVVFAGWLGGyGNLVIIDHGNGYSTLYAHLSSI--LVKVGQRVKAGQVIGTVGSTGR-------STGPHLHFEIRKNGK 92
M23_peptidase cd12797
M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; ...
 220-350 1.48e-18

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: 79.56  E-value: 1.48e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382473 220 HKGIDIYKKKEldgqirnlnfqDEIISPADGIVIRADhsyspmtlsdyeyhttqsqkgtvtyvEKDFGGRQVWIDHGHGV 299
Cdd:cd12797    1 HNGIDIAAPEG-----------TPVYAAADGTVVFAG--------------------------WDGGYGNYVIIDHGNGY 43

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446382473 300 MTSFNHLSSIhkNIKVGEKVKQGESIGTVGNSGLleeakniSDNIHLHFEI 350
Cdd:cd12797   44 YTLYAHLSSI--LVKVGQRVKKGQVIGTVGNTGR-------STGPHLHFEI 85
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 187-357 2.64e-17

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: 82.50  E-value: 2.64e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382473 187 PRLRG-YSFPVPDGLISSFDSQLPNAPRtyrngvHKGIDIYKKKEldgqirnlnfqDEIISPADGIVIRADhsyspmTLS 265
Cdd:COG4942  249 AALKGkLPWPVSGRVVRRFGERDGGGGR------NKGIDIAAPPG-----------APVRAVADGTVVYAG------WLR 305

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382473 266 DYeyhttqsqkgtvtyvekdfgGRQVWIDHGHGVMTSFNHLSSIhkNIKVGEKVKQGESIGTVGNSGLLEEAknisdniH 345
Cdd:COG4942  306 GY--------------------GNLVIIDHGGGYLTLYAHLSSL--LVKVGQRVKAGQPIGTVGSSGGQGGP-------T 356

                        170
                 ....*....|..
gi 446382473 346 LHFEIWVDGEFL 357
Cdd:COG4942  357 LYFELRKNGKPV 368
SpoIIQ COG5820
Stage II sporulation protein SpoIIQ, required for engulfement [Cell cycle control, cell ...
 272-355 1.14e-16

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: 78.04  E-value: 1.14e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382473 272 TQSQKGTVTYVEKD-FGGRQVWIDHGHGVMTSFNHLSSIhkNIKVGEKVKQGESIGTVGNSGLLEEAKNisdniHLHFEI 350
Cdd:COG5820  136 LAALSGTVTEVEEDpLLGYVVEIKHDNGVSTVYQSLSDV--KVKAGDEVKQGQVIGTAGRNLFNKDAGV-----HLHFEV 208


                 ....*
gi 446382473 351 WVDGE 355
Cdd:COG5820  209 RKDGK 213
F5_F8_type_C pfam00754
F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.
 65-166 1.94e-11

F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.


Pssm-ID: 459925 [Multi-domain]  Cd Length: 127  Bit Score: 60.92  E-value: 1.94e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382473   65 AEYGGFNLFDSDPNTHWYSVNRSDSEWVIVDFGSKRLINGLEITVPIFKKERAVKKYEIQVliRDD---WRTILTNQ--- 138
Cdd:pfam00754  10 GEGPAAAALDGDPNTAWSAWSGDDPQWIQVDLGKPKKITGVVTQGRQDGSNGYVTSYKIEY--SLDgenWTTVKDEKipg 87

                          90       100       110
                  ....*....|....*....|....*....|...
gi 446382473  139 -----NVELHNFHKlgNIDASVLRIYFPDSTNR 166
Cdd:pfam00754  88 nndnnTPVTNTFDP--PIKARYVRIVPTSWNGG 118
PRK11649 PRK11649
putative peptidase; Provisional
 277-353 3.72e-08

putative peptidase; Provisional


Pssm-ID: 236946 [Multi-domain]  Cd Length: 439  Bit Score: 55.06  E-value: 3.72e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446382473 277 GTVTYVEKD-FGGRQVWIDHGHGVMTSFNHLSSIHknIKVGEKVKQGESIGTVGNSGLleeakniSDNIHLHFEIWVD 353
Cdd:PRK11649 332 GEVVVAKRSgAAGNYVAIRHGRQYTTRYMHLRKLL--VKPGQKVKRGDRIALSGNTGR-------STGPHLHYEVWIN 400
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 66-154 2.02e-03

Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached carbohydrate-binding domain, present in eukaryotes and assumed to have horizontally transferred to eubacterial genomes.


Pssm-ID: 238014 [Multi-domain]  Cd Length: 143  Bit Score: 38.10  E-value: 2.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382473  66 EYGGFNLFDSDPNTHWYSVNRSDSEWVIVDFGSKRLINGLEITVP--IFKKERaVKKYEIQV-LIRDDWRTILTNQNVEL 142
Cdd:cd00057   22 SGWEASRARLNSDNAWTPAVNDPPQWLQVDLGKTRRVTGIQTQGRkgGGSSEW-VTSYKVQYsLDGETWTTYKDKGEEKV 100

                         90
                 ....*....|..
gi 446382473 143 HNfhklGNIDAS 154
Cdd:cd00057  101 FT----GNSDGS 108
 
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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