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Conserved domains on  [gi|1907153912|ref|XP_036019498|]
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agrin isoform X11 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Laminin_G_1 pfam00054
Laminin G domain;
627-758 1.98e-51

Laminin G domain;


:

Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 177.12  E-value: 1.98e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153912  627 FRALETEGLLLYNGNARGKDFLALALLDGHVQFRFDTGSGPAVLTSLVPVEPGRWHRLELSRHWRQGTLSVDGEAPVVGE 706
Cdd:pfam00054    1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGE 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907153912  707 SPSGTDG-LNLDTKLYVGGLPEEqvATVLDRTSVGIGLKGCIRMLDINNQQLE 758
Cdd:pfam00054   81 SPLGATTdLDVDGPLYVGGLPSL--GVKKRRLAISPSFDGCIRDVIVNGKPLD 131
Laminin_G_1 pfam00054
Laminin G domain;
895-1030 3.65e-46

Laminin G domain;


:

Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 162.10  E-value: 3.65e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153912  895 FLARGPSGLLLYNGQKTDGkgDFVSLALHNRHLEFRYDLGKGAAIIRSKEPIALGTWVRVFLERNGRKGALQVGDGPRVL 974
Cdd:pfam00054    1 FRTTEPSGLLLYNGTQTER--DFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPT 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907153912  975 GESPKSRKvphTMLNLKEPLYVGGAPDFSKLARGAAVASGFDGAIQLVSLRGHQLL 1030
Cdd:pfam00054   79 GESPLGAT---TDLDVDGPLYVGGLPSLGVKKRRLAISPSFDGCIRDVIVNGKPLD 131
Laminin_G_1 pfam00054
Laminin G domain;
1148-1278 1.21e-45

Laminin G domain;


:

Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 160.56  E-value: 1.21e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153912 1148 RTEATQGLVLWIGKVGERaDYMALAIVDGHLQLSYDLGSQPVVLRSTVKVNTNRWLRVRAHREHREGSLQVGNEAPVTGS 1227
Cdd:pfam00054    2 RTTEPSGLLLYNGTQTER-DFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGE 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907153912 1228 SPLGATQ-LDTDGALWLGGLQKLPVgQALPKAYGTGFVGCLRDVVVGHRQLH 1278
Cdd:pfam00054   81 SPLGATTdLDVDGPLYVGGLPSLGV-KKRRLAISPSFDGCIRDVIVNGKPLD 131
SEA smart00200
Domain found in sea urchin sperm protein, enterokinase, agrin; Proposed function of regulating ...
 359-483 2.78e-31

Domain found in sea urchin sperm protein, enterokinase, agrin; Proposed function of regulating or binding carbohydrate sidechains.


:

Pssm-ID: 214554  Cd Length: 121  Bit Score: 119.05  E-value: 2.78e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153912   359 ATKAFQGVLELEGVEGQELFYTPEMADPKSELFGETARSIESTLDDLFRNSDVKKDFWSIRLRELGPGKLVRAIVDVHFD 438
Cdd:smart00200    1 PTQSFGVSLSVLSVEGENLQYSPSLEDPSSEEYQELVRDVEKLLEQIYGKTDLKPDFVGTEVIEFRNGSVVVDLGLLFNE 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*
gi 1907153912   439 PTTAfqAPDVGQALLQQIQVSRpWALAVRRPlrEHVRFLDFDWFP 483
Cdd:smart00200   81 GVTN--GQDVEEDLLQVIKQAA-YSLKITNV--NVVDVLDPDSAD 120
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 33-84 1.92e-17

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.


:

Pssm-ID: 395007  Cd Length: 49  Bit Score: 77.01  E-value: 1.92e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907153912   33 CHCNPHGSYSGTCDPVTGQCSCRPGVGGLRCDRCEPGFWNFRGivtDGHSGC 84
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPS---DPPQGC 49
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 162-209 1.17e-11

Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains.


:

Pssm-ID: 197624  Cd Length: 46  Bit Score: 60.39  E-value: 1.17e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1907153912   162 VCPTlTCPEaNSTKVCGSDGVTYGNECQLKTIACRQRLDISIQSLGPC 209
Cdd:smart00280    1 DCPE-ACPR-EYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 87-123 3.15e-11

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.


:

Pssm-ID: 395007  Cd Length: 49  Bit Score: 59.29  E-value: 3.15e-11
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1907153912   87 CSCDPRGAVRDDCEQMTGLCSCRPGVAGPKCGQCPDG 123
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPG 37
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 1052-1084 1.84e-07

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


:

Pssm-ID: 238011  Cd Length: 38  Bit Score: 48.40  E-value: 1.84e-07
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1907153912 1052 AVDNPCLNGGSCIPREATYECLCPGGFSGLHCE 1084
Cdd:cd00054      6 ASGNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 560-590 4.44e-04

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


:

Pssm-ID: 394967  Cd Length: 31  Bit Score: 38.90  E-value: 4.44e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1907153912  560 CDSQPCLHGGTCqdLDSGKGFSCSCTAGRAG 590
Cdd:pfam00008    1 CAPNPCSNGGTC--VDTPGGYTCICPEGYTG 29
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 781-812 9.09e-03

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


:

Pssm-ID: 238011  Cd Length: 38  Bit Score: 35.31  E-value: 9.09e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1907153912  781 SPNPCHGGALCQALEAGvFLCQCPPGRFGPTC 812
Cdd:cd00054      7 SGNPCQNGGTCVNTVGS-YRCSCPPGYTGRNC 37
 
Name Accession Description Interval E-value
Laminin_G_1 pfam00054
Laminin G domain;
627-758 1.98e-51

Laminin G domain;


Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 177.12  E-value: 1.98e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153912  627 FRALETEGLLLYNGNARGKDFLALALLDGHVQFRFDTGSGPAVLTSLVPVEPGRWHRLELSRHWRQGTLSVDGEAPVVGE 706
Cdd:pfam00054    1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGE 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907153912  707 SPSGTDG-LNLDTKLYVGGLPEEqvATVLDRTSVGIGLKGCIRMLDINNQQLE 758
Cdd:pfam00054   81 SPLGATTdLDVDGPLYVGGLPSL--GVKKRRLAISPSFDGCIRDVIVNGKPLD 131
Laminin_G_1 pfam00054
Laminin G domain;
895-1030 3.65e-46

Laminin G domain;


Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 162.10  E-value: 3.65e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153912  895 FLARGPSGLLLYNGQKTDGkgDFVSLALHNRHLEFRYDLGKGAAIIRSKEPIALGTWVRVFLERNGRKGALQVGDGPRVL 974
Cdd:pfam00054    1 FRTTEPSGLLLYNGTQTER--DFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPT 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907153912  975 GESPKSRKvphTMLNLKEPLYVGGAPDFSKLARGAAVASGFDGAIQLVSLRGHQLL 1030
Cdd:pfam00054   79 GESPLGAT---TDLDVDGPLYVGGLPSLGVKKRRLAISPSFDGCIRDVIVNGKPLD 131
Laminin_G_1 pfam00054
Laminin G domain;
1148-1278 1.21e-45

Laminin G domain;


Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 160.56  E-value: 1.21e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153912 1148 RTEATQGLVLWIGKVGERaDYMALAIVDGHLQLSYDLGSQPVVLRSTVKVNTNRWLRVRAHREHREGSLQVGNEAPVTGS 1227
Cdd:pfam00054    2 RTTEPSGLLLYNGTQTER-DFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGE 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907153912 1228 SPLGATQ-LDTDGALWLGGLQKLPVgQALPKAYGTGFVGCLRDVVVGHRQLH 1278
Cdd:pfam00054   81 SPLGATTdLDVDGPLYVGGLPSLGV-KKRRLAISPSFDGCIRDVIVNGKPLD 131
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
 604-753 1.36e-45

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.


Pssm-ID: 238058 [Multi-domain]  Cd Length: 151  Bit Score: 161.05  E-value: 1.36e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153912  604 FKGHSFLAFPTLRA-YHTLRLALEFRALETEGLLLYNGNARGKDFLALALLDGHVQFRFDTGSGPAVLTSLVPVEPGRWH 682
Cdd:cd00110      4 FSGSSYVRLPTLPApRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDGQWH 83

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907153912  683 RLELSRHWRQGTLSVDGEAPVVGESPSGTDGLNLDTKLYVGGLPEEQVATvldRTSVGIGLKGCIRMLDIN 753
Cdd:cd00110     84 SVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSP---GLPVSPGFVGCIRDLKVN 151
LamG smart00282
Laminin G domain;
622-755 8.73e-43

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 152.49  E-value: 8.73e-43
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153912   622 RLALEFRALETEGLLLYNGNARGKDFLALALLDGHVQFRFDTGSGPAVLTS-LVPVEPGRWHRLELSRHWRQGTLSVDGE 700
Cdd:smart00282    1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSdPTPLNDGQWHRVAVERNGRSVTLSVDGG 80

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 1907153912   701 APVVGESPSGTDGLNLDTKLYVGGLPEEQVATvldRTSVGIGLKGCIRMLDINNQ 755
Cdd:smart00282   81 NRVSGESPGGLTILNLDGPLYLGGLPEDLKLP---PLPVTPGFRGCIRNLKVNGK 132
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
 867-1024 5.25e-35

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.


Pssm-ID: 238058 [Multi-domain]  Cd Length: 151  Bit Score: 131.00  E-value: 5.25e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153912  867 FNGFSYLELKGLHTFERDlgekMALEMVFLARGPSGLLLYNGQKTdgKGDFVSLALHNRHLEFRYDLGKGAAIIRSKEPI 946
Cdd:cd00110      4 FSGSSYVRLPTLPAPRTR----LSISFSFRTTSPNGLLLYAGSQN--GGDFLALELEDGRLVLRYDLGSGSLVLSSKTPL 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907153912  947 ALGTWVRVFLERNGRKGALQVgDGPRVLgESPKSRKvpHTMLNLKEPLYVGGAPDFSKLaRGAAVASGFDGAIQLVSL 1024
Cdd:cd00110     78 NDGQWHSVSVERNGRSVTLSV-DGERVV-ESGSPGG--SALLNLDGPLYLGGLPEDLKS-PGLPVSPGFVGCIRDLKV 150
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
 1128-1272 6.46e-33

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.


Pssm-ID: 238058 [Multi-domain]  Cd Length: 151  Bit Score: 124.84  E-value: 6.46e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153912 1128 DSRALFSEKALQSNHFELSL--RTEATQGLVLWIGkVGERADYMALAIVDGHLQLSYDLGSQPVVLRSTVKVNTNRWLRV 1205
Cdd:cd00110      7 SSYVRLPTLPAPRTRLSISFsfRTTSPNGLLLYAG-SQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDGQWHSV 85

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907153912 1206 RAHREHREGSLQVGNEAPVTGSSPLGATQLDTDGALWLGGLQklPVGQALPKAYGTGFVGCLRDVVV 1272
Cdd:cd00110     86 SVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLP--EDLKSPGLPVSPGFVGCIRDLKV 150
LamG smart00282
Laminin G domain;
1142-1275 2.87e-32

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 122.45  E-value: 2.87e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153912  1142 HFELSLRTEATQGLVLWIGkVGERADYMALAIVDGHLQLSYDLGSQPVVLRST-VKVNTNRWLRVRAHREHREGSLQVGN 1220
Cdd:smart00282    1 SISFSFRTTSPNGLLLYAG-SKGGGDYLALELRDGRLVLRYDLGSGPARLTSDpTPLNDGQWHRVAVERNGRSVTLSVDG 79

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907153912  1221 EAPVTGSSPLGATQLDTDGALWLGGlqkLPVGQALPK-AYGTGFVGCLRDVVVGHR 1275
Cdd:smart00282   80 GNRVSGESPGGLTILNLDGPLYLGG---LPEDLKLPPlPVTPGFRGCIRNLKVNGK 132
LamG smart00282
Laminin G domain;
891-1027 7.42e-32

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 121.29  E-value: 7.42e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153912   891 LEMVFLARGPSGLLLYNGQKtdGKGDFVSLALHNRHLEFRYDLGKGAAIIRSK-EPIALGTWVRVFLERNGRKGALQVGD 969
Cdd:smart00282    2 ISFSFRTTSPNGLLLYAGSK--GGGDYLALELRDGRLVLRYDLGSGPARLTSDpTPLNDGQWHRVAVERNGRSVTLSVDG 79

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907153912   970 GPRVLGESPKSrkvpHTMLNLKEPLYVGGAPDFSKLARGaAVASGFDGAIQLVSLRGH 1027
Cdd:smart00282   80 GNRVSGESPGG----LTILNLDGPLYLGGLPEDLKLPPL-PVTPGFRGCIRNLKVNGK 132
SEA smart00200
Domain found in sea urchin sperm protein, enterokinase, agrin; Proposed function of regulating ...
 359-483 2.78e-31

Domain found in sea urchin sperm protein, enterokinase, agrin; Proposed function of regulating or binding carbohydrate sidechains.


Pssm-ID: 214554  Cd Length: 121  Bit Score: 119.05  E-value: 2.78e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153912   359 ATKAFQGVLELEGVEGQELFYTPEMADPKSELFGETARSIESTLDDLFRNSDVKKDFWSIRLRELGPGKLVRAIVDVHFD 438
Cdd:smart00200    1 PTQSFGVSLSVLSVEGENLQYSPSLEDPSSEEYQELVRDVEKLLEQIYGKTDLKPDFVGTEVIEFRNGSVVVDLGLLFNE 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*
gi 1907153912   439 PTTAfqAPDVGQALLQQIQVSRpWALAVRRPlrEHVRFLDFDWFP 483
Cdd:smart00200   81 GVTN--GQDVEEDLLQVIKQAA-YSLKITNV--NVVDVLDPDSAD 120
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 33-84 1.92e-17

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.


Pssm-ID: 395007  Cd Length: 49  Bit Score: 77.01  E-value: 1.92e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907153912   33 CHCNPHGSYSGTCDPVTGQCSCRPGVGGLRCDRCEPGFWNFRGivtDGHSGC 84
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPS---DPPQGC 49
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 33-73 3.44e-17

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


Pssm-ID: 238012  Cd Length: 50  Bit Score: 76.24  E-value: 3.44e-17
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1907153912   33 CHCNPHGSYSGTCDPVTGQCSCRPGVGGLRCDRCEPGFWNF 73
Cdd:cd00055      2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGL 42
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
33-75 4.52e-16

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 73.11  E-value: 4.52e-16
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 1907153912    33 CHCNPHGSYSGTCDPVTGQCSCRPGVGGLRCDRCEPGFWNFRG 75
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 162-209 1.17e-11

Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains.


Pssm-ID: 197624  Cd Length: 46  Bit Score: 60.39  E-value: 1.17e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1907153912   162 VCPTlTCPEaNSTKVCGSDGVTYGNECQLKTIACRQRLDISIQSLGPC 209
Cdd:smart00280    1 DCPE-ACPR-EYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
SEA pfam01390
SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed ...
 377-455 1.43e-11

SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed function of regulating or binding carbohydrate side chains. Recently a proteolytic activity has been shown for a SEA domain.


Pssm-ID: 460188  Cd Length: 100  Bit Score: 62.26  E-value: 1.43e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153912  377 LFYTPEMADPKSELFGETARSIESTLDDLFRNSDVKKDFWS---IRLRELGPGklVRAIVDVHFDPTTAFQAPDVGQ--- 450
Cdd:pfam01390   12 LQYTPDLGNPSSQEFKSLSRRIESLLNELFRNSSLRKQYIKshvLRLRPDGGS--VVVDVVLVFRFPSTEPALDREKlie 89


                   ....*
gi 1907153912  451 ALLQQ 455
Cdd:pfam01390   90 EILRQ 94
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 87-123 3.15e-11

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.


Pssm-ID: 395007  Cd Length: 49  Bit Score: 59.29  E-value: 3.15e-11
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1907153912   87 CSCDPRGAVRDDCEQMTGLCSCRPGVAGPKCGQCPDG 123
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPG 37
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
 168-209 5.36e-10

Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit serine proteases, such as, trypsin, chyomotrypsin, avian ovomucoids, and elastases. The inhibitory domain has one reactive site peptide bond, which serves the cognate enzyme as substrate. The reactive site peptide bond is a combining loop which has an identical conformation in all Kazal inhibitors and in all enzyme/inhibitor complexes. These Kazal domains (small hydrophobic core of alpha/beta structure with 3 to 4 disulfide bonds) often occur in tandem arrays. Similar domains are also present in follistatin (FS) and follistatin-like family members, which play an important role in tissue specific regulation. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a Kazal-like domain and has five disulfide bonds. Although the Kazal-like FS substructure is similar to Kazal proteinase inhibitors, no FS domain has yet been shown to be a proteinase inhibitor. Follistatin-like family members include SPARC, also known as, BM-40 or osteonectin, the Gallus gallus Flik protein, as well as, agrin which has a long array of FS domains. The kazal-type inhibitor domain has also been detected in an extracellular loop region of solute carrier 21 (SLC21) family members (organic anion transporters) , which may regulate the specificity of anion uptake. The distant homolog, Ascidian trypsin inhibitor, is included in this CD.


Pssm-ID: 238052 [Multi-domain]  Cd Length: 41  Bit Score: 55.74  E-value: 5.36e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1907153912  168 CPEaNSTKVCGSDGVTYGNECQLKTIACRQRLDISIQSLGPC 209
Cdd:cd00104      1 CPK-EYDPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 86-132 6.63e-10

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


Pssm-ID: 238012  Cd Length: 50  Bit Score: 55.82  E-value: 6.63e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907153912   86 PCSCDPRGAVRDDCEQMTGLCSCRPGVAGPKCGQCPDG---QALGHLGCE 132
Cdd:cd00055      1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGyygLPSQGGGCQ 50
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
87-123 3.61e-09

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 53.47  E-value: 3.61e-09
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 1907153912    87 CSCDPRGAVRDDCEQMTGLCSCRPGVAGPKCGQCPDG 123
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPG 37
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 1052-1084 1.84e-07

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 48.40  E-value: 1.84e-07
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1907153912 1052 AVDNPCLNGGSCIPREATYECLCPGGFSGLHCE 1084
Cdd:cd00054      6 ASGNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
EGF_CA smart00179
Calcium-binding EGF-like domain;
1052-1084 7.55e-06

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 43.77  E-value: 7.55e-06
                            10        20        30
                    ....*....|....*....|....*....|....
gi 1907153912  1052 AVDNPCLNGGSCIPREATYECLCPGGFS-GLHCE 1084
Cdd:smart00179    6 ASGNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 167-209 7.78e-06

Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. However, kazal-like domains are also seen in the extracellular part of agrins, which are not known to be protease inhibitors. Kazal domains often occur in tandem arrays. Small alpha+beta fold containing three disulphides.


Pssm-ID: 400135  Cd Length: 50  Bit Score: 44.41  E-value: 7.78e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1907153912  167 TCPEANSTKVCGSDGVTYGNECQLKTIACRQRLDIS---IQSLGPC 209
Cdd:pfam07648    5 QCPKTEYEPVCGSDGVTYPSPCALCAAGCKLGKEVKeekVKYDGSC 50
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 1054-1082 1.30e-04

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 394967  Cd Length: 31  Bit Score: 40.44  E-value: 1.30e-04
                           10        20
                   ....*....|....*....|....*....
gi 1907153912 1054 DNPCLNGGSCIPREATYECLCPGGFSGLH 1082
Cdd:pfam00008    3 PNPCSNGGTCVDTPGGYTCICPEGYTGKR 31
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 560-590 4.44e-04

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 394967  Cd Length: 31  Bit Score: 38.90  E-value: 4.44e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1907153912  560 CDSQPCLHGGTCqdLDSGKGFSCSCTAGRAG 590
Cdd:pfam00008    1 CAPNPCSNGGTC--VDTPGGYTCICPEGYTG 29
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 560-594 2.76e-03

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 36.85  E-value: 2.76e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1907153912  560 CDSQ-PCLHGGTCQDLDSgkGFSCSCTAGRAGTVCE 594
Cdd:cd00054      5 CASGnPCQNGGTCVNTVG--SYRCSCPPGYTGRNCE 38
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 781-812 9.09e-03

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 35.31  E-value: 9.09e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1907153912  781 SPNPCHGGALCQALEAGvFLCQCPPGRFGPTC 812
Cdd:cd00054      7 SGNPCQNGGTCVNTVGS-YRCSCPPGYTGRNC 37
 
Name Accession Description Interval E-value
Laminin_G_1 pfam00054
Laminin G domain;
627-758 1.98e-51

Laminin G domain;


Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 177.12  E-value: 1.98e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153912  627 FRALETEGLLLYNGNARGKDFLALALLDGHVQFRFDTGSGPAVLTSLVPVEPGRWHRLELSRHWRQGTLSVDGEAPVVGE 706
Cdd:pfam00054    1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGE 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907153912  707 SPSGTDG-LNLDTKLYVGGLPEEqvATVLDRTSVGIGLKGCIRMLDINNQQLE 758
Cdd:pfam00054   81 SPLGATTdLDVDGPLYVGGLPSL--GVKKRRLAISPSFDGCIRDVIVNGKPLD 131
Laminin_G_1 pfam00054
Laminin G domain;
895-1030 3.65e-46

Laminin G domain;


Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 162.10  E-value: 3.65e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153912  895 FLARGPSGLLLYNGQKTDGkgDFVSLALHNRHLEFRYDLGKGAAIIRSKEPIALGTWVRVFLERNGRKGALQVGDGPRVL 974
Cdd:pfam00054    1 FRTTEPSGLLLYNGTQTER--DFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPT 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907153912  975 GESPKSRKvphTMLNLKEPLYVGGAPDFSKLARGAAVASGFDGAIQLVSLRGHQLL 1030
Cdd:pfam00054   79 GESPLGAT---TDLDVDGPLYVGGLPSLGVKKRRLAISPSFDGCIRDVIVNGKPLD 131
Laminin_G_1 pfam00054
Laminin G domain;
1148-1278 1.21e-45

Laminin G domain;


Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 160.56  E-value: 1.21e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153912 1148 RTEATQGLVLWIGKVGERaDYMALAIVDGHLQLSYDLGSQPVVLRSTVKVNTNRWLRVRAHREHREGSLQVGNEAPVTGS 1227
Cdd:pfam00054    2 RTTEPSGLLLYNGTQTER-DFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGE 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907153912 1228 SPLGATQ-LDTDGALWLGGLQKLPVgQALPKAYGTGFVGCLRDVVVGHRQLH 1278
Cdd:pfam00054   81 SPLGATTdLDVDGPLYVGGLPSLGV-KKRRLAISPSFDGCIRDVIVNGKPLD 131
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
 604-753 1.36e-45

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.


Pssm-ID: 238058 [Multi-domain]  Cd Length: 151  Bit Score: 161.05  E-value: 1.36e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153912  604 FKGHSFLAFPTLRA-YHTLRLALEFRALETEGLLLYNGNARGKDFLALALLDGHVQFRFDTGSGPAVLTSLVPVEPGRWH 682
Cdd:cd00110      4 FSGSSYVRLPTLPApRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDGQWH 83

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907153912  683 RLELSRHWRQGTLSVDGEAPVVGESPSGTDGLNLDTKLYVGGLPEEQVATvldRTSVGIGLKGCIRMLDIN 753
Cdd:cd00110     84 SVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSP---GLPVSPGFVGCIRDLKVN 151
LamG smart00282
Laminin G domain;
622-755 8.73e-43

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 152.49  E-value: 8.73e-43
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153912   622 RLALEFRALETEGLLLYNGNARGKDFLALALLDGHVQFRFDTGSGPAVLTS-LVPVEPGRWHRLELSRHWRQGTLSVDGE 700
Cdd:smart00282    1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSdPTPLNDGQWHRVAVERNGRSVTLSVDGG 80

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 1907153912   701 APVVGESPSGTDGLNLDTKLYVGGLPEEQVATvldRTSVGIGLKGCIRMLDINNQ 755
Cdd:smart00282   81 NRVSGESPGGLTILNLDGPLYLGGLPEDLKLP---PLPVTPGFRGCIRNLKVNGK 132
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
 867-1024 5.25e-35

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.


Pssm-ID: 238058 [Multi-domain]  Cd Length: 151  Bit Score: 131.00  E-value: 5.25e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153912  867 FNGFSYLELKGLHTFERDlgekMALEMVFLARGPSGLLLYNGQKTdgKGDFVSLALHNRHLEFRYDLGKGAAIIRSKEPI 946
Cdd:cd00110      4 FSGSSYVRLPTLPAPRTR----LSISFSFRTTSPNGLLLYAGSQN--GGDFLALELEDGRLVLRYDLGSGSLVLSSKTPL 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907153912  947 ALGTWVRVFLERNGRKGALQVgDGPRVLgESPKSRKvpHTMLNLKEPLYVGGAPDFSKLaRGAAVASGFDGAIQLVSL 1024
Cdd:cd00110     78 NDGQWHSVSVERNGRSVTLSV-DGERVV-ESGSPGG--SALLNLDGPLYLGGLPEDLKS-PGLPVSPGFVGCIRDLKV 150
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
 1128-1272 6.46e-33

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.


Pssm-ID: 238058 [Multi-domain]  Cd Length: 151  Bit Score: 124.84  E-value: 6.46e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153912 1128 DSRALFSEKALQSNHFELSL--RTEATQGLVLWIGkVGERADYMALAIVDGHLQLSYDLGSQPVVLRSTVKVNTNRWLRV 1205
Cdd:cd00110      7 SSYVRLPTLPAPRTRLSISFsfRTTSPNGLLLYAG-SQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDGQWHSV 85

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907153912 1206 RAHREHREGSLQVGNEAPVTGSSPLGATQLDTDGALWLGGLQklPVGQALPKAYGTGFVGCLRDVVV 1272
Cdd:cd00110     86 SVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLP--EDLKSPGLPVSPGFVGCIRDLKV 150
LamG smart00282
Laminin G domain;
1142-1275 2.87e-32

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 122.45  E-value: 2.87e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153912  1142 HFELSLRTEATQGLVLWIGkVGERADYMALAIVDGHLQLSYDLGSQPVVLRST-VKVNTNRWLRVRAHREHREGSLQVGN 1220
Cdd:smart00282    1 SISFSFRTTSPNGLLLYAG-SKGGGDYLALELRDGRLVLRYDLGSGPARLTSDpTPLNDGQWHRVAVERNGRSVTLSVDG 79

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907153912  1221 EAPVTGSSPLGATQLDTDGALWLGGlqkLPVGQALPK-AYGTGFVGCLRDVVVGHR 1275
Cdd:smart00282   80 GNRVSGESPGGLTILNLDGPLYLGG---LPEDLKLPPlPVTPGFRGCIRNLKVNGK 132
LamG smart00282
Laminin G domain;
891-1027 7.42e-32

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 121.29  E-value: 7.42e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153912   891 LEMVFLARGPSGLLLYNGQKtdGKGDFVSLALHNRHLEFRYDLGKGAAIIRSK-EPIALGTWVRVFLERNGRKGALQVGD 969
Cdd:smart00282    2 ISFSFRTTSPNGLLLYAGSK--GGGDYLALELRDGRLVLRYDLGSGPARLTSDpTPLNDGQWHRVAVERNGRSVTLSVDG 79

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907153912   970 GPRVLGESPKSrkvpHTMLNLKEPLYVGGAPDFSKLARGaAVASGFDGAIQLVSLRGH 1027
Cdd:smart00282   80 GNRVSGESPGG----LTILNLDGPLYLGGLPEDLKLPPL-PVTPGFRGCIRNLKVNGK 132
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
 627-755 2.19e-31

Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.


Pssm-ID: 460494 [Multi-domain]  Cd Length: 126  Bit Score: 119.45  E-value: 2.19e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153912  627 FRALETEGLLLYNGNARGkDFLALALLDGHVQFRFDTGSGPAVLTSL-VPVEPGRWHRLELSRHWRQGTLSVDGEAPVVG 705
Cdd:pfam02210    1 FRTRQPNGLLLYAGGGGS-DFLALELVNGRLVLRYDLGSGPESLLSSgKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSS 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907153912  706 ESPSGTDGLNLDTKLYVGGLPEEqvaTVLDRTSVGIGLKGCIRMLDINNQ 755
Cdd:pfam02210   80 LPPGESLLLNLNGPLYLGGLPPL---LLLPALPVRAGFVGCIRDVRVNGE 126
SEA smart00200
Domain found in sea urchin sperm protein, enterokinase, agrin; Proposed function of regulating ...
 359-483 2.78e-31

Domain found in sea urchin sperm protein, enterokinase, agrin; Proposed function of regulating or binding carbohydrate sidechains.


Pssm-ID: 214554  Cd Length: 121  Bit Score: 119.05  E-value: 2.78e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153912   359 ATKAFQGVLELEGVEGQELFYTPEMADPKSELFGETARSIESTLDDLFRNSDVKKDFWSIRLRELGPGKLVRAIVDVHFD 438
Cdd:smart00200    1 PTQSFGVSLSVLSVEGENLQYSPSLEDPSSEEYQELVRDVEKLLEQIYGKTDLKPDFVGTEVIEFRNGSVVVDLGLLFNE 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*
gi 1907153912   439 PTTAfqAPDVGQALLQQIQVSRpWALAVRRPlrEHVRFLDFDWFP 483
Cdd:smart00200   81 GVTN--GQDVEEDLLQVIKQAA-YSLKITNV--NVVDVLDPDSAD 120
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
 1147-1275 2.15e-27

Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.


Pssm-ID: 460494 [Multi-domain]  Cd Length: 126  Bit Score: 108.28  E-value: 2.15e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153912 1147 LRTEATQGLVLWIGkvGERADYMALAIVDGHLQLSYDLGSQPVVLRST-VKVNTNRWLRVRAHREHREGSLQVGNEAPVT 1225
Cdd:pfam02210    1 FRTRQPNGLLLYAG--GGGSDFLALELVNGRLVLRYDLGSGPESLLSSgKNLNDGQWHSVRVERNGNTLTLSVDGQTVVS 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907153912 1226 GSSPLGATQLDTDGALWLGGLQKLPVGQALPkaYGTGFVGCLRDVVVGHR 1275
Cdd:pfam02210   79 SLPPGESLLLNLNGPLYLGGLPPLLLLPALP--VRAGFVGCIRDVRVNGE 126
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
 895-1027 1.03e-20

Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.


Pssm-ID: 460494 [Multi-domain]  Cd Length: 126  Bit Score: 89.02  E-value: 1.03e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153912  895 FLARGPSGLLLYNGqktDGKGDFVSLALHNRHLEFRYDLGKGAAIIRS-KEPIALGTWVRVFLERNGRKGALQVGDGPRV 973
Cdd:pfam02210    1 FRTRQPNGLLLYAG---GGGSDFLALELVNGRLVLRYDLGSGPESLLSsGKNLNDGQWHSVRVERNGNTLTLSVDGQTVV 77

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907153912  974 LGESPKsrkvPHTMLNLKEPLYVGGAPDFSKLaRGAAVASGFDGAIQLVSLRGH 1027
Cdd:pfam02210   78 SSLPPG----ESLLLNLNGPLYLGGLPPLLLL-PALPVRAGFVGCIRDVRVNGE 126
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 33-84 1.92e-17

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.


Pssm-ID: 395007  Cd Length: 49  Bit Score: 77.01  E-value: 1.92e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907153912   33 CHCNPHGSYSGTCDPVTGQCSCRPGVGGLRCDRCEPGFWNFRGivtDGHSGC 84
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPS---DPPQGC 49
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 33-73 3.44e-17

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


Pssm-ID: 238012  Cd Length: 50  Bit Score: 76.24  E-value: 3.44e-17
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1907153912   33 CHCNPHGSYSGTCDPVTGQCSCRPGVGGLRCDRCEPGFWNF 73
Cdd:cd00055      2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGL 42
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
33-75 4.52e-16

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 73.11  E-value: 4.52e-16
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 1907153912    33 CHCNPHGSYSGTCDPVTGQCSCRPGVGGLRCDRCEPGFWNFRG 75
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 162-209 1.17e-11

Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains.


Pssm-ID: 197624  Cd Length: 46  Bit Score: 60.39  E-value: 1.17e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1907153912   162 VCPTlTCPEaNSTKVCGSDGVTYGNECQLKTIACRQRLDISIQSLGPC 209
Cdd:smart00280    1 DCPE-ACPR-EYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
SEA pfam01390
SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed ...
 377-455 1.43e-11

SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed function of regulating or binding carbohydrate side chains. Recently a proteolytic activity has been shown for a SEA domain.


Pssm-ID: 460188  Cd Length: 100  Bit Score: 62.26  E-value: 1.43e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153912  377 LFYTPEMADPKSELFGETARSIESTLDDLFRNSDVKKDFWS---IRLRELGPGklVRAIVDVHFDPTTAFQAPDVGQ--- 450
Cdd:pfam01390   12 LQYTPDLGNPSSQEFKSLSRRIESLLNELFRNSSLRKQYIKshvLRLRPDGGS--VVVDVVLVFRFPSTEPALDREKlie 89


                   ....*
gi 1907153912  451 ALLQQ 455
Cdd:pfam01390   90 EILRQ 94
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 87-123 3.15e-11

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.


Pssm-ID: 395007  Cd Length: 49  Bit Score: 59.29  E-value: 3.15e-11
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1907153912   87 CSCDPRGAVRDDCEQMTGLCSCRPGVAGPKCGQCPDG 123
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPG 37
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
 168-209 5.36e-10

Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit serine proteases, such as, trypsin, chyomotrypsin, avian ovomucoids, and elastases. The inhibitory domain has one reactive site peptide bond, which serves the cognate enzyme as substrate. The reactive site peptide bond is a combining loop which has an identical conformation in all Kazal inhibitors and in all enzyme/inhibitor complexes. These Kazal domains (small hydrophobic core of alpha/beta structure with 3 to 4 disulfide bonds) often occur in tandem arrays. Similar domains are also present in follistatin (FS) and follistatin-like family members, which play an important role in tissue specific regulation. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a Kazal-like domain and has five disulfide bonds. Although the Kazal-like FS substructure is similar to Kazal proteinase inhibitors, no FS domain has yet been shown to be a proteinase inhibitor. Follistatin-like family members include SPARC, also known as, BM-40 or osteonectin, the Gallus gallus Flik protein, as well as, agrin which has a long array of FS domains. The kazal-type inhibitor domain has also been detected in an extracellular loop region of solute carrier 21 (SLC21) family members (organic anion transporters) , which may regulate the specificity of anion uptake. The distant homolog, Ascidian trypsin inhibitor, is included in this CD.


Pssm-ID: 238052 [Multi-domain]  Cd Length: 41  Bit Score: 55.74  E-value: 5.36e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1907153912  168 CPEaNSTKVCGSDGVTYGNECQLKTIACRQRLDISIQSLGPC 209
Cdd:cd00104      1 CPK-EYDPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 86-132 6.63e-10

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


Pssm-ID: 238012  Cd Length: 50  Bit Score: 55.82  E-value: 6.63e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907153912   86 PCSCDPRGAVRDDCEQMTGLCSCRPGVAGPKCGQCPDG---QALGHLGCE 132
Cdd:cd00055      1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGyygLPSQGGGCQ 50
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
87-123 3.61e-09

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 53.47  E-value: 3.61e-09
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 1907153912    87 CSCDPRGAVRDDCEQMTGLCSCRPGVAGPKCGQCPDG 123
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPG 37
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 1052-1084 1.84e-07

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 48.40  E-value: 1.84e-07
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1907153912 1052 AVDNPCLNGGSCIPREATYECLCPGGFSGLHCE 1084
Cdd:cd00054      6 ASGNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
EGF_CA smart00179
Calcium-binding EGF-like domain;
1052-1084 7.55e-06

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 43.77  E-value: 7.55e-06
                            10        20        30
                    ....*....|....*....|....*....|....
gi 1907153912  1052 AVDNPCLNGGSCIPREATYECLCPGGFS-GLHCE 1084
Cdd:smart00179    6 ASGNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 167-209 7.78e-06

Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. However, kazal-like domains are also seen in the extracellular part of agrins, which are not known to be protease inhibitors. Kazal domains often occur in tandem arrays. Small alpha+beta fold containing three disulphides.


Pssm-ID: 400135  Cd Length: 50  Bit Score: 44.41  E-value: 7.78e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1907153912  167 TCPEANSTKVCGSDGVTYGNECQLKTIACRQRLDIS---IQSLGPC 209
Cdd:pfam07648    5 QCPKTEYEPVCGSDGVTYPSPCALCAAGCKLGKEVKeekVKYDGSC 50
Kazal_1 pfam00050
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 164-209 1.39e-05

Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. However, kazal-like domains are also seen in the extracellular part of agrins, which are not known to be protease inhibitors. Kazal domains often occur in tandem arrays. Small alpha+beta fold containing three disulphides. Alignment also includes a single domain from transporters in the OATP/PGT family.


Pssm-ID: 395004  Cd Length: 49  Bit Score: 43.43  E-value: 1.39e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1907153912  164 PTLTCPeANSTKVCGSDGVTYGNECQLKTIACRQRLDISIQSLGPC 209
Cdd:pfam00050    5 PSGACP-RIYDPVCGTDGKTYSNECLFCAENGKRGTNLHKVHDGEC 49
KAZAL_PSTI cd01327
Kazal-type pancreatic secretory trypsin inhibitors (PSTI) and related proteins, including the ...
 163-209 2.74e-05

Kazal-type pancreatic secretory trypsin inhibitors (PSTI) and related proteins, including the second domain of the ovomucoid turkey inhibitor and the C-terminal domain of the esophagus cancer-related gene-2 protein (ECRG-2), are members of the superfamily of kazal-type proteinase inhibitors and follistatin-like proteins.


Pssm-ID: 238648  Cd Length: 45  Bit Score: 42.66  E-value: 2.74e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907153912  163 CPTLTCPeanstkVCGSDGVTYGNECQLktiaCRQRL----DISIQSLGPC 209
Cdd:cd01327      5 CPKDYDP------VCGTDGVTYSNECLL----CAENLkrqtNIRIKHDGEC 45
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
 1052-1084 4.52e-05

Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large number of proteins, mostly animal; the list of proteins currently known to contain one or more copies of an EGF-like pattern is large and varied; the functional significance of EGF-like domains in what appear to be unrelated proteins is not yet clear; a common feature is that these repeats are found in the extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandin G/H synthase); the domain includes six cysteine residues which have been shown to be involved in disulfide bonds; the main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet; Subdomains between the conserved cysteines vary in length; the region between the 5th and 6th cysteine contains two conserved glycines of which at least one is present in most EGF-like domains; a subset of these bind calcium.


Pssm-ID: 238010  Cd Length: 36  Bit Score: 41.69  E-value: 4.52e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1907153912 1052 AVDNPCLNGGSCIPREATYECLCPGGFSG-LHCE 1084
Cdd:cd00053      3 AASNPCSNGGTCVNTPGSYRCVCPPGYTGdRSCE 36
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 1054-1082 1.30e-04

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 394967  Cd Length: 31  Bit Score: 40.44  E-value: 1.30e-04
                           10        20
                   ....*....|....*....|....*....
gi 1907153912 1054 DNPCLNGGSCIPREATYECLCPGGFSGLH 1082
Cdd:pfam00008    3 PNPCSNGGTCVDTPGGYTCICPEGYTGKR 31
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 560-590 4.44e-04

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 394967  Cd Length: 31  Bit Score: 38.90  E-value: 4.44e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1907153912  560 CDSQPCLHGGTCqdLDSGKGFSCSCTAGRAG 590
Cdd:pfam00008    1 CAPNPCSNGGTC--VDTPGGYTCICPEGYTG 29
FSL_SPARC cd01328
Follistatin-like SPARC (secreted protein, acidic, and rich in cysteines) domain; SPARC/BM-40 ...
 141-195 6.05e-04

Follistatin-like SPARC (secreted protein, acidic, and rich in cysteines) domain; SPARC/BM-40/osteonectin is a multifunctional glycoprotein which modulates cellular interaction with the extracellular matrix by its binding to structural matrix proteins such as collagen and vitronectin. The protein it composed of an N-terminal acidic region, a follistatin (FS) domain and an EF-hand calcium binding domain. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a small hydrophobic core of alpha/beta structure (Kazal domain) and has five disulfide bonds and a conserved N-glycosylation site. The FSL_SPARC domain is a member of the superfamily of kazal-like proteinase inhibitors and follistatin-like proteins.


Pssm-ID: 238649 [Multi-domain]  Cd Length: 86  Bit Score: 40.15  E-value: 6.05e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907153912  141 CVEMHCEFGASC-VEEAGFAQCVCPTlTCPEANST--KVCGSDGVTYGNECQLKTIAC 195
Cdd:cd01328      2 CENHHCGAGKVCeVDDENTPKCVCID-PCPEEVDDrrKVCTNDNETFDSDCELYRTRC 58
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 560-594 2.76e-03

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 36.85  E-value: 2.76e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1907153912  560 CDSQ-PCLHGGTCQDLDSgkGFSCSCTAGRAGTVCE 594
Cdd:cd00054      5 CASGnPCQNGGTCVNTVG--SYRCSCPPGYTGRNCE 38
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 781-812 9.09e-03

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 35.31  E-value: 9.09e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1907153912  781 SPNPCHGGALCQALEAGvFLCQCPPGRFGPTC 812
Cdd:cd00054      7 SGNPCQNGGTCVNTVGS-YRCSCPPGYTGRNC 37
 
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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