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Conserved domains on  [gi|239787919|ref|NP_116221|]
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low-density lipoprotein receptor-related protein 11 isoform 1 precursor [Homo sapiens]

Protein Classification

MANEC and LDLa domain-containing protein( domain architecture ID 11275462)

protein containing domains MANEC, PKD, and LDLa

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MANEC smart00765
The MANEC domain, formerly called MANSC; This domain, comprising 8 conserved cysteines, is ...
 84-184 4.19e-38

The MANEC domain, formerly called MANSC; This domain, comprising 8 conserved cysteines, is found in the N terminus of higher multicellular animal membrane and extracellular proteins. It is postulated that this domain may play a role in the formation of protein complexes involving various protease activators and inhibitors. It is possible that some of the cysteine residues in the MANSC domain form structurally important disulfide bridges. All of the MANSC-containing proteins contain predicted transmembrane regions and signal peptides. It has been proposed that the MANSC domain in HAI-1 might function through binding with hepatocyte growth factor activator and matriptase.


:

Pssm-ID: 129004  Cd Length: 93  Bit Score: 134.50  E-value: 4.19e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239787919    84 GPQEDCPGpgsgGYSAMPDAIIRTKDSLAAGASFLRAPAAVRGWRQCVAACCSEPRCSVAVVELPRRPAPPAavlgCYLF 163
Cdd:smart00765   1 SPGEDCLG----RFRVLENAIIRTEESLSAGARFLKSPIAVNTWEDCVRACCSTPNCNLAVFELRREDAEGN----CYLF 72

                           90       100
                   ....*....|....*....|.
gi 239787919   164 NCTARGRNVCKFALHSGYSSY 184
Cdd:smart00765  73 NCTYPGKEVCKFKPHEGYTSY 93
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 310-344 2.52e-10

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


:

Pssm-ID: 238060  Cd Length: 35  Bit Score: 55.29  E-value: 2.52e-10
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 239787919 310 CSRYHFFCDDGCCIDITLACDGVQQCPDGSDEDFC 344
Cdd:cd00112    1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
PKD cd00146
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ...
 208-296 9.16e-07

polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an IG-like fold; domain probably functions as a ligand binding site in protein-protein or protein-carbohydrate interactions; a single instance of the repeat is presented here. The domain is also found in microbial collagenases and chitinases.


:

Pssm-ID: 238084 [Multi-domain]  Cd Length: 81  Bit Score: 46.72  E-value: 9.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239787919 208 APPLSKAGQDVVLHLPtdgvvldgreSTDDHAIVQYEWALlqGDPSVDMkvpqSGTLKLSH--LQEGTYTFQLTVTDTAG 285
Cdd:cd00146    7 APPVAELGASVTFSAS----------DSSGGSIVSYKWDF--GDGEVSS----SGEPTVTHtyTKPGTYTVTLTVTNAVG 70

                         90
                 ....*....|.
gi 239787919 286 QRSSDNVSVTV 296
Cdd:cd00146   71 SSSTKTTTVVV 81
 
Name Accession Description Interval E-value
MANEC smart00765
The MANEC domain, formerly called MANSC; This domain, comprising 8 conserved cysteines, is ...
 84-184 4.19e-38

The MANEC domain, formerly called MANSC; This domain, comprising 8 conserved cysteines, is found in the N terminus of higher multicellular animal membrane and extracellular proteins. It is postulated that this domain may play a role in the formation of protein complexes involving various protease activators and inhibitors. It is possible that some of the cysteine residues in the MANSC domain form structurally important disulfide bridges. All of the MANSC-containing proteins contain predicted transmembrane regions and signal peptides. It has been proposed that the MANSC domain in HAI-1 might function through binding with hepatocyte growth factor activator and matriptase.


Pssm-ID: 129004  Cd Length: 93  Bit Score: 134.50  E-value: 4.19e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239787919    84 GPQEDCPGpgsgGYSAMPDAIIRTKDSLAAGASFLRAPAAVRGWRQCVAACCSEPRCSVAVVELPRRPAPPAavlgCYLF 163
Cdd:smart00765   1 SPGEDCLG----RFRVLENAIIRTEESLSAGARFLKSPIAVNTWEDCVRACCSTPNCNLAVFELRREDAEGN----CYLF 72

                           90       100
                   ....*....|....*....|.
gi 239787919   164 NCTARGRNVCKFALHSGYSSY 184
Cdd:smart00765  73 NCTYPGKEVCKFKPHEGYTSY 93
MANEC pfam07502
MANEC domain; This region of similarity, comprising 8 conserved cysteines, is found in the ...
 87-183 8.07e-35

MANEC domain; This region of similarity, comprising 8 conserved cysteines, is found in the N-terminal region of several membrane-associated and extracellular proteins. Although formerly called MANSC (for motif at N terminus with seven cysteines) it has now been renamed by MANEC (motif at N terminus with eight cysteines) by Richard Mitter and Stephen Fitzgerald after the discovery of an eighth conserved cysteine. It is postulated that this domain may play a role in the formation of protein complexes involving various protease activators and inhibitors.


Pssm-ID: 462186  Cd Length: 90  Bit Score: 125.50  E-value: 8.07e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239787919   87 EDCPGpgsgGYSAMPDAIIRTKDSLAAGASFLRaPAAVRGWRQCVAACCSEPRCSVAVVElpRRPAPPAAVLGCYLFNCT 166
Cdd:pfam07502   1 ESCLE----DFTGVEDFIIDTEDSVKNGATFLS-SPEVSSARDCVRACCSTPRCNLAVFE--ERPGGEDAIPSCYLFNCL 73

                          90
                  ....*....|....*..
gi 239787919  167 ARGRNVCKFALHSGYSS 183
Cdd:pfam07502  74 YPSRFVCKFAPHKGYTS 90
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 310-344 2.52e-10

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 55.29  E-value: 2.52e-10
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 239787919 310 CSRYHFFCDDGCCIDITLACDGVQQCPDGSDEDFC 344
Cdd:cd00112    1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 309-341 4.12e-10

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 54.56  E-value: 4.12e-10
                           10        20        30
                   ....*....|....*....|....*....|...
gi 239787919   309 TCSRYHFFCDDGCCIDITLACDGVQQCPDGSDE 341
Cdd:smart00192   1 TCPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
309-344 4.53e-07

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 46.09  E-value: 4.53e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 239787919  309 TCSRYHFFCDDGCCIDITLACDGVQQCPDGSDEDFC 344
Cdd:pfam00057   2 TCSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
PKD cd00146
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ...
 208-296 9.16e-07

polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an IG-like fold; domain probably functions as a ligand binding site in protein-protein or protein-carbohydrate interactions; a single instance of the repeat is presented here. The domain is also found in microbial collagenases and chitinases.


Pssm-ID: 238084 [Multi-domain]  Cd Length: 81  Bit Score: 46.72  E-value: 9.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239787919 208 APPLSKAGQDVVLHLPtdgvvldgreSTDDHAIVQYEWALlqGDPSVDMkvpqSGTLKLSH--LQEGTYTFQLTVTDTAG 285
Cdd:cd00146    7 APPVAELGASVTFSAS----------DSSGGSIVSYKWDF--GDGEVSS----SGEPTVTHtyTKPGTYTVTLTVTNAVG 70

                         90
                 ....*....|.
gi 239787919 286 QRSSDNVSVTV 296
Cdd:cd00146   71 SSSTKTTTVVV 81
PKD smart00089
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ...
 208-296 3.98e-06

Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 protein contains 14 repeats, present elsewhere such as in microbial collagenases.


Pssm-ID: 214510 [Multi-domain]  Cd Length: 79  Bit Score: 44.75  E-value: 3.98e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239787919   208 APPLSKAGQDVVLHLPtdgvvldgreSTDDHAIVQYEWALlqGDPSVDMkvpqSGTLKLSHLQEGTYTFQLTVTDTAGqr 287
Cdd:smart00089   7 SPTVGVAGESVTFTAT----------SSDDGSIVSYTWDF--GDGTSST----GPTVTHTYTKPGTYTVTLTVTNAVG-- 68


                   ....*....
gi 239787919   288 sSDNVSVTV 296
Cdd:smart00089  69 -SASATVTV 76
PKD_4 pfam18911
PKD domain; This entry is composed of PKD domains found in bacterial surface proteins.
 208-296 2.20e-05

PKD domain; This entry is composed of PKD domains found in bacterial surface proteins.


Pssm-ID: 436824 [Multi-domain]  Cd Length: 85  Bit Score: 42.64  E-value: 2.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239787919  208 APPLSKAGQDVVLHlPTDGVVLDGRESTD-DHAIVQYEWALlqGDPSVdmkvpqSGTLKLSHL--QEGTYTFQLTVTDTA 284
Cdd:pfam18911   2 AAPVADAGGDRIVA-EGETVTFDASASDDpDGDILSYRWDF--GDGTT------ATGANVSHTyaAPGTYTVTLTVTDDS 72

                          90
                  ....*....|...
gi 239787919  285 G-QRSSDNVSVTV 296
Cdd:pfam18911  73 GaSNSTATDTVTV 85
myxo_dep_M36 NF038112
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ...
 183-306 3.26e-04

myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal MYXO-CTERM domain (see TIGR03901), suggesting processing and surface-anchoring by the still-unknown putative transpeptidase, myxosortase. Members of this family include MXAN_3564 (mepA), part of the effector cargo of outer membrane vesicles that the species produces in large numbers during predation on other microbes.


Pssm-ID: 468355 [Multi-domain]  Cd Length: 1597  Bit Score: 43.49  E-value: 3.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239787919  183 SYSLSRAPDGAALATARASPRQEKDAP-PLSKAGQDVVLHlPTDGVVLDGRESTDDHAIVQYEWALLQGdPSVDMKVPQS 261
Cdd:NF038112 1442 TFQLTVSADGQASADVTVTVTVRNVNRaPVAHAGESITVD-EGSTVTLDASATDPDGDTLTYAWTQVAG-PSVTLTGADS 1519

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 239787919  262 GTLKLS--HLQEGT-YTFQLTVTDTAGQRSSDNVSVTVLRA--AYSTGGC 306
Cdd:NF038112 1520 AKLTFTapEVSADTtLTFSLTVTDGSGSSGPVVVTVTVKNVnrAPDGGGC 1569
myxo_dep_M36 NF038112
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ...
 209-296 2.45e-03

myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal MYXO-CTERM domain (see TIGR03901), suggesting processing and surface-anchoring by the still-unknown putative transpeptidase, myxosortase. Members of this family include MXAN_3564 (mepA), part of the effector cargo of outer membrane vesicles that the species produces in large numbers during predation on other microbes.


Pssm-ID: 468355 [Multi-domain]  Cd Length: 1597  Bit Score: 40.80  E-value: 2.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239787919  209 PPLSKAGQDVVLHLPTDgVVLDGRESTD-DHAIVQYEWALLQGDP----SVDMKVPQSGTLKLSHLQegTYTFQLTVTDT 283
Cdd:NF038112 1187 RPVANAGPDQTVLERTT-VTLNGSGSFDpDGDPLTYAWTQVSGPAvtltGADTATPSFTAPEVTADT--VLTFQLVVSDG 1263

                          90
                  ....*....|...
gi 239787919  284 AGQRSSDNVSVTV 296
Cdd:NF038112 1264 TKTSAPDTVTVLV 1276
 
Name Accession Description Interval E-value
MANEC smart00765
The MANEC domain, formerly called MANSC; This domain, comprising 8 conserved cysteines, is ...
 84-184 4.19e-38

The MANEC domain, formerly called MANSC; This domain, comprising 8 conserved cysteines, is found in the N terminus of higher multicellular animal membrane and extracellular proteins. It is postulated that this domain may play a role in the formation of protein complexes involving various protease activators and inhibitors. It is possible that some of the cysteine residues in the MANSC domain form structurally important disulfide bridges. All of the MANSC-containing proteins contain predicted transmembrane regions and signal peptides. It has been proposed that the MANSC domain in HAI-1 might function through binding with hepatocyte growth factor activator and matriptase.


Pssm-ID: 129004  Cd Length: 93  Bit Score: 134.50  E-value: 4.19e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239787919    84 GPQEDCPGpgsgGYSAMPDAIIRTKDSLAAGASFLRAPAAVRGWRQCVAACCSEPRCSVAVVELPRRPAPPAavlgCYLF 163
Cdd:smart00765   1 SPGEDCLG----RFRVLENAIIRTEESLSAGARFLKSPIAVNTWEDCVRACCSTPNCNLAVFELRREDAEGN----CYLF 72

                           90       100
                   ....*....|....*....|.
gi 239787919   164 NCTARGRNVCKFALHSGYSSY 184
Cdd:smart00765  73 NCTYPGKEVCKFKPHEGYTSY 93
MANEC pfam07502
MANEC domain; This region of similarity, comprising 8 conserved cysteines, is found in the ...
 87-183 8.07e-35

MANEC domain; This region of similarity, comprising 8 conserved cysteines, is found in the N-terminal region of several membrane-associated and extracellular proteins. Although formerly called MANSC (for motif at N terminus with seven cysteines) it has now been renamed by MANEC (motif at N terminus with eight cysteines) by Richard Mitter and Stephen Fitzgerald after the discovery of an eighth conserved cysteine. It is postulated that this domain may play a role in the formation of protein complexes involving various protease activators and inhibitors.


Pssm-ID: 462186  Cd Length: 90  Bit Score: 125.50  E-value: 8.07e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239787919   87 EDCPGpgsgGYSAMPDAIIRTKDSLAAGASFLRaPAAVRGWRQCVAACCSEPRCSVAVVElpRRPAPPAAVLGCYLFNCT 166
Cdd:pfam07502   1 ESCLE----DFTGVEDFIIDTEDSVKNGATFLS-SPEVSSARDCVRACCSTPRCNLAVFE--ERPGGEDAIPSCYLFNCL 73

                          90
                  ....*....|....*..
gi 239787919  167 ARGRNVCKFALHSGYSS 183
Cdd:pfam07502  74 YPSRFVCKFAPHKGYTS 90
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 310-344 2.52e-10

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 55.29  E-value: 2.52e-10
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 239787919 310 CSRYHFFCDDGCCIDITLACDGVQQCPDGSDEDFC 344
Cdd:cd00112    1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 309-341 4.12e-10

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 54.56  E-value: 4.12e-10
                           10        20        30
                   ....*....|....*....|....*....|...
gi 239787919   309 TCSRYHFFCDDGCCIDITLACDGVQQCPDGSDE 341
Cdd:smart00192   1 TCPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
309-344 4.53e-07

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 46.09  E-value: 4.53e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 239787919  309 TCSRYHFFCDDGCCIDITLACDGVQQCPDGSDEDFC 344
Cdd:pfam00057   2 TCSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
PKD cd00146
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ...
 208-296 9.16e-07

polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an IG-like fold; domain probably functions as a ligand binding site in protein-protein or protein-carbohydrate interactions; a single instance of the repeat is presented here. The domain is also found in microbial collagenases and chitinases.


Pssm-ID: 238084 [Multi-domain]  Cd Length: 81  Bit Score: 46.72  E-value: 9.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239787919 208 APPLSKAGQDVVLHLPtdgvvldgreSTDDHAIVQYEWALlqGDPSVDMkvpqSGTLKLSH--LQEGTYTFQLTVTDTAG 285
Cdd:cd00146    7 APPVAELGASVTFSAS----------DSSGGSIVSYKWDF--GDGEVSS----SGEPTVTHtyTKPGTYTVTLTVTNAVG 70

                         90
                 ....*....|.
gi 239787919 286 QRSSDNVSVTV 296
Cdd:cd00146   71 SSSTKTTTVVV 81
PKD smart00089
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ...
 208-296 3.98e-06

Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 protein contains 14 repeats, present elsewhere such as in microbial collagenases.


Pssm-ID: 214510 [Multi-domain]  Cd Length: 79  Bit Score: 44.75  E-value: 3.98e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239787919   208 APPLSKAGQDVVLHLPtdgvvldgreSTDDHAIVQYEWALlqGDPSVDMkvpqSGTLKLSHLQEGTYTFQLTVTDTAGqr 287
Cdd:smart00089   7 SPTVGVAGESVTFTAT----------SSDDGSIVSYTWDF--GDGTSST----GPTVTHTYTKPGTYTVTLTVTNAVG-- 68


                   ....*....
gi 239787919   288 sSDNVSVTV 296
Cdd:smart00089  69 -SASATVTV 76
PKD_4 pfam18911
PKD domain; This entry is composed of PKD domains found in bacterial surface proteins.
 208-296 2.20e-05

PKD domain; This entry is composed of PKD domains found in bacterial surface proteins.


Pssm-ID: 436824 [Multi-domain]  Cd Length: 85  Bit Score: 42.64  E-value: 2.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239787919  208 APPLSKAGQDVVLHlPTDGVVLDGRESTD-DHAIVQYEWALlqGDPSVdmkvpqSGTLKLSHL--QEGTYTFQLTVTDTA 284
Cdd:pfam18911   2 AAPVADAGGDRIVA-EGETVTFDASASDDpDGDILSYRWDF--GDGTT------ATGANVSHTyaAPGTYTVTLTVTDDS 72

                          90
                  ....*....|...
gi 239787919  285 G-QRSSDNVSVTV 296
Cdd:pfam18911  73 GaSNSTATDTVTV 85
myxo_dep_M36 NF038112
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ...
 183-306 3.26e-04

myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal MYXO-CTERM domain (see TIGR03901), suggesting processing and surface-anchoring by the still-unknown putative transpeptidase, myxosortase. Members of this family include MXAN_3564 (mepA), part of the effector cargo of outer membrane vesicles that the species produces in large numbers during predation on other microbes.


Pssm-ID: 468355 [Multi-domain]  Cd Length: 1597  Bit Score: 43.49  E-value: 3.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239787919  183 SYSLSRAPDGAALATARASPRQEKDAP-PLSKAGQDVVLHlPTDGVVLDGRESTDDHAIVQYEWALLQGdPSVDMKVPQS 261
Cdd:NF038112 1442 TFQLTVSADGQASADVTVTVTVRNVNRaPVAHAGESITVD-EGSTVTLDASATDPDGDTLTYAWTQVAG-PSVTLTGADS 1519

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 239787919  262 GTLKLS--HLQEGT-YTFQLTVTDTAGQRSSDNVSVTVLRA--AYSTGGC 306
Cdd:NF038112 1520 AKLTFTapEVSADTtLTFSLTVTDGSGSSGPVVVTVTVKNVnrAPDGGGC 1569
Big_13 pfam19077
Bacterial Ig-like domain; Presumed domain found as tandem repeats of high sequence identity in ...
 269-296 5.57e-04

Bacterial Ig-like domain; Presumed domain found as tandem repeats of high sequence identity in bacterial cell surface proteins.


Pssm-ID: 465968 [Multi-domain]  Cd Length: 102  Bit Score: 39.17  E-value: 5.57e-04
                          10        20
                  ....*....|....*....|....*....
gi 239787919  269 LQEGTYTFQLTVTDTAG-QRSSDNVSVTV 296
Cdd:pfam19077  72 LADGTYTLTVTVTDIAGnTATSSPLSFTI 100
He_PIG pfam05345
Putative Ig domain; This alignment represents the conserved core region of ~90 residue repeat ...
 261-296 1.17e-03

Putative Ig domain; This alignment represents the conserved core region of ~90 residue repeat found in several haemagglutinins and other cell surface proteins. Sequence similarities to (pfam02494) and (pfam00801) suggest an Ig-like fold (personal obs:C. Yeats). So this family may be similar in function to the (pfam02639) and (pfam02638) domains. This domain is also found in the WisP family of proteins of Tropheryma whipplei.


Pssm-ID: 398814 [Multi-domain]  Cd Length: 95  Bit Score: 38.22  E-value: 1.17e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 239787919  261 SGTLKLShlQEGTYTFQLTVTDTAGQRSSDNVSVTV 296
Cdd:pfam05345  61 SGTPTSV--QPGTYTFTVTATDSSGLSSSTTFTLTV 94
myxo_dep_M36 NF038112
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ...
 209-296 2.45e-03

myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal MYXO-CTERM domain (see TIGR03901), suggesting processing and surface-anchoring by the still-unknown putative transpeptidase, myxosortase. Members of this family include MXAN_3564 (mepA), part of the effector cargo of outer membrane vesicles that the species produces in large numbers during predation on other microbes.


Pssm-ID: 468355 [Multi-domain]  Cd Length: 1597  Bit Score: 40.80  E-value: 2.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239787919  209 PPLSKAGQDVVLHLPTDgVVLDGRESTD-DHAIVQYEWALLQGDP----SVDMKVPQSGTLKLSHLQegTYTFQLTVTDT 283
Cdd:NF038112 1187 RPVANAGPDQTVLERTT-VTLNGSGSFDpDGDPLTYAWTQVSGPAvtltGADTATPSFTAPEVTADT--VLTFQLVVSDG 1263

                          90
                  ....*....|...
gi 239787919  284 AGQRSSDNVSVTV 296
Cdd:NF038112 1264 TKTSAPDTVTVLV 1276
 
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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