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Conserved domains on  [gi|58613865|gb|AAW79534|]
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SR-CIV [Drosophila melanogaster]

Protein Classification

PHA02927 and MAM domain-containing protein( domain architecture ID 13332460)

PHA02927 and MAM domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 132-237 6.05e-30

MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain along with the associated Ig domain in type IIB receptor protein tyrosine phosphatases forms a structural unit (termed MIg) with a seamless interdomain interface. It plays a major role in homodimerization of the phosphatase ectoprotein and in cell adhesion. MAM is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets rotated away from each other by approx 25 degrees, and plays a similar role in meprin metalloproteinases.


:

Pssm-ID: 459878 [Multi-domain]  Cd Length: 159  Bit Score: 110.91  E-value: 6.05e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58613865   132 CDFESEDMCGWTAELSFLGTWKRVSTvadfHSEKTGPQKDHTfQNQSVGHYVRMETESDAFG-TYHFLSPLYPkeLSLSG 210
Cdd:pfam00629   1 CDFEDGNLCGWTQDSSDDFDWERVSG----PSVKTGPSSDHT-QGTGSGHFMYVDTSSGAPGqTARLLSPLLP--PSRSP 73

                          90       100
                  ....*....|....*....|....*..
gi 58613865   211 ACFQFHYFMFGSGVGSLLVSIKPVSLT 237
Cdd:pfam00629  74 QCLRFWYHMSGSGVGTLRVYVRENGGT 100
PHA02927 super family cl33700
secreted complement-binding protein; Provisional
 19-115 6.65e-04

secreted complement-binding protein; Provisional


The actual alignment was detected with superfamily member PHA02927:

Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 40.41  E-value: 6.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58613865   19 RCLESVHLEHGSTEIvNGSIIFHCDQEYFLQGSKVFTCDRG-----IPRGKKPFCAKSGCQEYEQIQNG-------FVLN 86
Cdd:PHA02927  90 RDIDNGQLDIGGVDF-GSSITYSCNSGYQLIGESKSYCELGstgsmVWNPEAPICESVKCQSPPSISNGrhngyedFYTD 168

                         90       100
                 ....*....|....*....|....*....
gi 58613865   87 APMkAKIICSDGHGLVGNRIAYCDGEKWS 115
Cdd:PHA02927 169 GSV-VTYSCNSGYSLIGNSGVLCSGGEWS 196
 
Name Accession Description Interval E-value
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 132-237 6.05e-30

MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain along with the associated Ig domain in type IIB receptor protein tyrosine phosphatases forms a structural unit (termed MIg) with a seamless interdomain interface. It plays a major role in homodimerization of the phosphatase ectoprotein and in cell adhesion. MAM is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets rotated away from each other by approx 25 degrees, and plays a similar role in meprin metalloproteinases.


Pssm-ID: 459878 [Multi-domain]  Cd Length: 159  Bit Score: 110.91  E-value: 6.05e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58613865   132 CDFESEDMCGWTAELSFLGTWKRVSTvadfHSEKTGPQKDHTfQNQSVGHYVRMETESDAFG-TYHFLSPLYPkeLSLSG 210
Cdd:pfam00629   1 CDFEDGNLCGWTQDSSDDFDWERVSG----PSVKTGPSSDHT-QGTGSGHFMYVDTSSGAPGqTARLLSPLLP--PSRSP 73

                          90       100
                  ....*....|....*....|....*..
gi 58613865   211 ACFQFHYFMFGSGVGSLLVSIKPVSLT 237
Cdd:pfam00629  74 QCLRFWYHMSGSGVGTLRVYVRENGGT 100
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 129-232 1.29e-19

Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions.


Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 83.93  E-value: 1.29e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58613865    129 DASCDFESEDMCGWTAELSFLGTWKRVSTVADfhseKTGPQKDHTFQNqsvGHYVRMETESDAFG-TYHFLSP-LYPKel 206
Cdd:smart00137   3 PGNCDFEEGSTCGWHQDSNDDGHWERVSSATG----IPGPNRDHTTGN---GHFMFFETSSGAEGqTARLLSPpLYEN-- 73

                           90       100
                   ....*....|....*....|....*.
gi 58613865    207 sLSGACFQFHYFMFGSGVGSLLVSIK 232
Cdd:smart00137  74 -RSTHCLTFWYYMYGSGSGTLNVYVR 98
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 132-233 1.30e-18

Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members include: type IIB receptor protein tyrosine phosphatases (such as RPTPmu), meprins (plasma membrane metalloproteases), neuropilins (receptors of secreted semaphorins), and zonadhesins (sperm-specific membrane proteins which bind to the extracellular matrix of the egg). In meprin A and neuropilin-1 and -2, MAM is involved in homo-oligomerization. In RPTPmu, it has been associated with both homophilic adhesive (trans) interactions and lateral (cis) receptor oligomerization. In a GPI-anchored protein that is expressed in cells in the embryonic chicken spinal chord, MDGA1, the MAM domain has been linked to heterophilic interactions with axon-rich region.


Pssm-ID: 99706  Cd Length: 157  Bit Score: 80.88  E-value: 1.30e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58613865 132 CDFEsEDMCGWTAELSFLGTWKRVStvadfHSEKTGPQKDHTFQNQSVGHYVRMETESDAFG-TYHFLSPLYPkeLSLSG 210
Cdd:cd06263   1 CDFE-DGLCGWTQDSTDDFDWTRVS-----GSTPSPGTPPDHTHGTGSGHYLYVESSSGREGqKARLLSPLLP--PPRSS 72

                        90       100
                ....*....|....*....|...
gi 58613865 211 ACFQFHYFMFGSGVGSLLVSIKP 233
Cdd:cd06263  73 HCLSFWYHMYGSGVGTLNVYVRE 95
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 19-115 6.65e-04

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 40.41  E-value: 6.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58613865   19 RCLESVHLEHGSTEIvNGSIIFHCDQEYFLQGSKVFTCDRG-----IPRGKKPFCAKSGCQEYEQIQNG-------FVLN 86
Cdd:PHA02927  90 RDIDNGQLDIGGVDF-GSSITYSCNSGYQLIGESKSYCELGstgsmVWNPEAPICESVKCQSPPSISNGrhngyedFYTD 168

                         90       100
                 ....*....|....*....|....*....
gi 58613865   87 APMkAKIICSDGHGLVGNRIAYCDGEKWS 115
Cdd:PHA02927 169 GSV-VTYSCNSGYSLIGNSGVLCSGGEWS 196
 
Name Accession Description Interval E-value
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 132-237 6.05e-30

MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain along with the associated Ig domain in type IIB receptor protein tyrosine phosphatases forms a structural unit (termed MIg) with a seamless interdomain interface. It plays a major role in homodimerization of the phosphatase ectoprotein and in cell adhesion. MAM is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets rotated away from each other by approx 25 degrees, and plays a similar role in meprin metalloproteinases.


Pssm-ID: 459878 [Multi-domain]  Cd Length: 159  Bit Score: 110.91  E-value: 6.05e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58613865   132 CDFESEDMCGWTAELSFLGTWKRVSTvadfHSEKTGPQKDHTfQNQSVGHYVRMETESDAFG-TYHFLSPLYPkeLSLSG 210
Cdd:pfam00629   1 CDFEDGNLCGWTQDSSDDFDWERVSG----PSVKTGPSSDHT-QGTGSGHFMYVDTSSGAPGqTARLLSPLLP--PSRSP 73

                          90       100
                  ....*....|....*....|....*..
gi 58613865   211 ACFQFHYFMFGSGVGSLLVSIKPVSLT 237
Cdd:pfam00629  74 QCLRFWYHMSGSGVGTLRVYVRENGGT 100
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 129-232 1.29e-19

Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions.


Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 83.93  E-value: 1.29e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58613865    129 DASCDFESEDMCGWTAELSFLGTWKRVSTVADfhseKTGPQKDHTFQNqsvGHYVRMETESDAFG-TYHFLSP-LYPKel 206
Cdd:smart00137   3 PGNCDFEEGSTCGWHQDSNDDGHWERVSSATG----IPGPNRDHTTGN---GHFMFFETSSGAEGqTARLLSPpLYEN-- 73

                           90       100
                   ....*....|....*....|....*.
gi 58613865    207 sLSGACFQFHYFMFGSGVGSLLVSIK 232
Cdd:smart00137  74 -RSTHCLTFWYYMYGSGSGTLNVYVR 98
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 132-233 1.30e-18

Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members include: type IIB receptor protein tyrosine phosphatases (such as RPTPmu), meprins (plasma membrane metalloproteases), neuropilins (receptors of secreted semaphorins), and zonadhesins (sperm-specific membrane proteins which bind to the extracellular matrix of the egg). In meprin A and neuropilin-1 and -2, MAM is involved in homo-oligomerization. In RPTPmu, it has been associated with both homophilic adhesive (trans) interactions and lateral (cis) receptor oligomerization. In a GPI-anchored protein that is expressed in cells in the embryonic chicken spinal chord, MDGA1, the MAM domain has been linked to heterophilic interactions with axon-rich region.


Pssm-ID: 99706  Cd Length: 157  Bit Score: 80.88  E-value: 1.30e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58613865 132 CDFEsEDMCGWTAELSFLGTWKRVStvadfHSEKTGPQKDHTFQNQSVGHYVRMETESDAFG-TYHFLSPLYPkeLSLSG 210
Cdd:cd06263   1 CDFE-DGLCGWTQDSTDDFDWTRVS-----GSTPSPGTPPDHTHGTGSGHYLYVESSSGREGqKARLLSPLLP--PPRSS 72

                        90       100
                ....*....|....*....|...
gi 58613865 211 ACFQFHYFMFGSGVGSLLVSIKP 233
Cdd:cd06263  73 HCLSFWYHMYGSGVGTLNVYVRE 95
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 19-115 6.65e-04

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 40.41  E-value: 6.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58613865   19 RCLESVHLEHGSTEIvNGSIIFHCDQEYFLQGSKVFTCDRG-----IPRGKKPFCAKSGCQEYEQIQNG-------FVLN 86
Cdd:PHA02927  90 RDIDNGQLDIGGVDF-GSSITYSCNSGYQLIGESKSYCELGstgsmVWNPEAPICESVKCQSPPSISNGrhngyedFYTD 168

                         90       100
                 ....*....|....*....|....*....
gi 58613865   87 APMkAKIICSDGHGLVGNRIAYCDGEKWS 115
Cdd:PHA02927 169 GSV-VTYSCNSGYSLIGNSGVLCSGGEWS 196
 
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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