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Conserved domains on  [gi|2462508931|ref|XP_054192450|]
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agrin isoform X4 [Homo sapiens]

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;
1324-1454 9.99e-48

Laminin G domain;


:

Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 166.72  E-value: 9.99e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508931 1324 RTEATQGLVLWSGKATERaDYVALAIVDGHLQLSYNLGSQPVVLRSTVPVNTNRWLRVVAHREQREGSLQVGNEAPVTGS 1403
Cdd:pfam00054    2 RTTEPSGLLLYNGTQTER-DFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGE 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462508931 1404 SPLGATQ-LDTDGALWLGGLPELPVgPALPKAYGTGFVGCLRDVVVGRHPLH 1454
Cdd:pfam00054   81 SPLGATTdLDVDGPLYVGGLPSLGV-KKRRLAISPSFDGCIRDVIVNGKPLD 131
Laminin_G_1 pfam00054
Laminin G domain;
822-953 9.02e-47

Laminin G domain;


:

Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 164.03  E-value: 9.02e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508931  822 FRALEPQGLLLYNGNARGKDFLALALLDGRVQLRFDTGSGPAVLTSAVPVEPGQWHRLELSRHWRRGTLSVDGETPVLGE 901
Cdd:pfam00054    1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGE 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462508931  902 SPSGTDG-LNLDTDLFVGGVPEDqaAVALERTFVGAGLRGCIRLLDVNNQRLE 953
Cdd:pfam00054   81 SPLGATTdLDVDGPLYVGGLPSL--GVKKRRLAISPSFDGCIRDVIVNGKPLD 131
Laminin_G_1 pfam00054
Laminin G domain;
1090-1225 3.86e-44

Laminin G domain;


:

Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 156.32  E-value: 3.86e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508931 1090 FLARGPSGLLLYNGQKTDGkgDFVSLALRDRRLEFRYDLGKGAAVIRSREPVTLGAWTRVSLERNGRKGALRVGDGPRVL 1169
Cdd:pfam00054    1 FRTTEPSGLLLYNGTQTER--DFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPT 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462508931 1170 GESPKSRKvphTVLNLKEPLYVGGAPDFSKLARAAAVSSGFDGAIQLVSLGGRQLL 1225
Cdd:pfam00054   79 GESPLGAT---TDLDVDGPLYVGGLPSLGVKKRRLAISPSFDGCIRDVIVNGKPLD 131
SEA smart00200
Domain found in sea urchin sperm protein, enterokinase, agrin; Proposed function of regulating ...
 552-676 1.05e-28

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: 111.73  E-value: 1.05e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508931   552 ATKVFQGVLELEGVEGQELFYTPEMADPKSELFGETARSIESTLDDLFRNSDVKKDFRSVRLRDLGPGKSVRAIVDVHFD 631
Cdd:smart00200    1 PTQSFGVSLSVLSVEGENLQYSPSLEDPSSEEYQELVRDVEKLLEQIYGKTDLKPDFVGTEVIEFRNGSVVVDLGLLFNE 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*
gi 2462508931   632 PTTAfrAPDVARALLRQIQVSrRRSLGVRRplQEHVRFMDFDWFP 676
Cdd:smart00200   81 GVTN--GQDVEEDLLQVIKQA-AYSLKITN--VNVVDVLDPDSAD 120
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 215-257 5.68e-16

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


:

Pssm-ID: 395007  Cd Length: 49  Bit Score: 73.16  E-value: 5.68e-16
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 2462508931  215 CQCNPHGSYGGTCDPATGQCSCRPGVGGLRCDRCEPGFWNFRG 257
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPS 43
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 126-172 2.98e-13

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


:

Pssm-ID: 197624  Cd Length: 46  Bit Score: 65.39  E-value: 2.98e-13
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 2462508931   126 VCDFSCQSVPgSPVCGSDGVTYSTECELKKARCESQRGLYVAAQGAC 172
Cdd:smart00280    1 DCPEACPREY-DPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 34-86 1.37e-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: 1.37e-11
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 2462508931    34 VCSagqCVCPRCEHPppgpVCGSDGVTYGSACELREAACLQQTQIEEARAGPC 86
Cdd:smart00280    1 DCP---EACPREYDP----VCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 344-391 7.37e-11

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


:

Pssm-ID: 197624  Cd Length: 46  Bit Score: 58.46  E-value: 7.37e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 2462508931   344 VCPMlTCPEANAtKVCGSDGVTYGNECQLKTIACRQGLQISIQSLGPC 391
Cdd:smart00280    1 DCPE-ACPREYD-PVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 269-305 2.90e-10

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


:

Pssm-ID: 395007  Cd Length: 49  Bit Score: 56.98  E-value: 2.90e-10
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 2462508931  269 CSCDPQGAVRDDCEQMTGLCSCKPGVAGPKCGQCPDG 305
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPG 37
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 1247-1279 3.48e-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: 48.02  E-value: 3.48e-07
                           10        20        30
                   ....*....|....*....|....*....|...
gi 2462508931 1247 ASGHPCLNGASCVPREAAYVCLCPGGFSGPHCE 1279
Cdd:cd00054      6 ASGNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 755-785 3.54e-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: 39.29  E-value: 3.54e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 2462508931  755 CDSQPCFHGGTCQDwaLGGGFTCSCPAGRGG 785
Cdd:pfam00008    1 CAPNPCSNGGTCVD--TPGGYTCICPEGYTG 29
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 977-1007 3.89e-04

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: 39.16  E-value: 3.89e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 2462508931  977 PNPCHGGAPCQNLEaGRFHCQCPPGRVGPTC 1007
Cdd:cd00054      8 GNPCQNGGTCVNTV-GSYRCSCPPGYTGRNC 37
 
Name Accession Description Interval E-value
Laminin_G_1 pfam00054
Laminin G domain;
1324-1454 9.99e-48

Laminin G domain;


Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 166.72  E-value: 9.99e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508931 1324 RTEATQGLVLWSGKATERaDYVALAIVDGHLQLSYNLGSQPVVLRSTVPVNTNRWLRVVAHREQREGSLQVGNEAPVTGS 1403
Cdd:pfam00054    2 RTTEPSGLLLYNGTQTER-DFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGE 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462508931 1404 SPLGATQ-LDTDGALWLGGLPELPVgPALPKAYGTGFVGCLRDVVVGRHPLH 1454
Cdd:pfam00054   81 SPLGATTdLDVDGPLYVGGLPSLGV-KKRRLAISPSFDGCIRDVIVNGKPLD 131
Laminin_G_1 pfam00054
Laminin G domain;
822-953 9.02e-47

Laminin G domain;


Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 164.03  E-value: 9.02e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508931  822 FRALEPQGLLLYNGNARGKDFLALALLDGRVQLRFDTGSGPAVLTSAVPVEPGQWHRLELSRHWRRGTLSVDGETPVLGE 901
Cdd:pfam00054    1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGE 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462508931  902 SPSGTDG-LNLDTDLFVGGVPEDqaAVALERTFVGAGLRGCIRLLDVNNQRLE 953
Cdd:pfam00054   81 SPLGATTdLDVDGPLYVGGLPSL--GVKKRRLAISPSFDGCIRDVIVNGKPLD 131
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
 799-948 1.98e-46

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: 163.74  E-value: 1.98e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508931  799 FEGRSFLAFPTLRA-YHTLRLALEFRALEPQGLLLYNGNARGKDFLALALLDGRVQLRFDTGSGPAVLTSAVPVEPGQWH 877
Cdd:cd00110      4 FSGSSYVRLPTLPApRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDGQWH 83

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462508931  878 RLELSRHWRRGTLSVDGETPVLGESPSGTDGLNLDTDLFVGGVPEDQaavALERTFVGAGLRGCIRLLDVN 948
Cdd:cd00110     84 SVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDL---KSPGLPVSPGFVGCIRDLKVN 151
Laminin_G_1 pfam00054
Laminin G domain;
1090-1225 3.86e-44

Laminin G domain;


Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 156.32  E-value: 3.86e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508931 1090 FLARGPSGLLLYNGQKTDGkgDFVSLALRDRRLEFRYDLGKGAAVIRSREPVTLGAWTRVSLERNGRKGALRVGDGPRVL 1169
Cdd:pfam00054    1 FRTTEPSGLLLYNGTQTER--DFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPT 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462508931 1170 GESPKSRKvphTVLNLKEPLYVGGAPDFSKLARAAAVSSGFDGAIQLVSLGGRQLL 1225
Cdd:pfam00054   79 GESPLGAT---TDLDVDGPLYVGGLPSLGVKKRRLAISPSFDGCIRDVIVNGKPLD 131
LamG smart00282
Laminin G domain;
817-950 5.61e-44

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 155.96  E-value: 5.61e-44
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508931   817 RLALEFRALEPQGLLLYNGNARGKDFLALALLDGRVQLRFDTGSGPAVLTS-AVPVEPGQWHRLELSRHWRRGTLSVDGE 895
Cdd:smart00282    1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSdPTPLNDGQWHRVAVERNGRSVTLSVDGG 80

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 2462508931   896 TPVLGESPSGTDGLNLDTDLFVGGVPEDQaavALERTFVGAGLRGCIRLLDVNNQ 950
Cdd:smart00282   81 NRVSGESPGGLTILNLDGPLYLGGLPEDL---KLPPLPVTPGFRGCIRNLKVNGK 132
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
 1292-1448 2.11e-36

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: 135.24  E-value: 2.11e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508931 1292 TLAFDGRTFVEYLNavteSEKALQSNHFELSLRTEATQGLVLWSGKATeRADYVALAIVDGHLQLSYNLGSQPVVLRSTV 1371
Cdd:cd00110      1 GVSFSGSSYVRLPT----LPAPRTRLSISFSFRTTSPNGLLLYAGSQN-GGDFLALELEDGRLVLRYDLGSGSLVLSSKT 75

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462508931 1372 PVNTNRWLRVVAHREQREGSLQVGNEAPVTGSSPLGATQLDTDGALWLGGLPELPVGPALPkaYGTGFVGCLRDVVV 1448
Cdd:cd00110     76 PLNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLP--VSPGFVGCIRDLKV 150
LamG smart00282
Laminin G domain;
1318-1451 1.01e-33

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 126.69  E-value: 1.01e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508931  1318 HFELSLRTEATQGLVLWSGKAtERADYVALAIVDGHLQLSYNLGSQPVVLRST-VPVNTNRWLRVVAHREQREGSLQVGN 1396
Cdd:smart00282    1 SISFSFRTTSPNGLLLYAGSK-GGGDYLALELRDGRLVLRYDLGSGPARLTSDpTPLNDGQWHRVAVERNGRSVTLSVDG 79

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 2462508931  1397 EAPVTGSSPLGATQLDTDGALWLGGLPELPVGPALPkaYGTGFVGCLRDVVVGRH 1451
Cdd:smart00282   80 GNRVSGESPGGLTILNLDGPLYLGGLPEDLKLPPLP--VTPGFRGCIRNLKVNGK 132
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
 1062-1219 6.65e-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: 125.22  E-value: 6.65e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508931 1062 FNGFSHLELRGLHTFARDlgekMALEVVFLARGPSGLLLYNGQKTdgKGDFVSLALRDRRLEFRYDLGKGAAVIRSREPV 1141
Cdd:cd00110      4 FSGSSYVRLPTLPAPRTR----LSISFSFRTTSPNGLLLYAGSQN--GGDFLALELEDGRLVLRYDLGSGSLVLSSKTPL 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462508931 1142 TLGAWTRVSLERNGRKGALRVgDGPRVLgESPKSRKVPHtvLNLKEPLYVGGAPDFSKLaRAAAVSSGFDGAIQLVSL 1219
Cdd:cd00110     78 NDGQWHSVSVERNGRSVTLSV-DGERVV-ESGSPGGSAL--LNLDGPLYLGGLPEDLKS-PGLPVSPGFVGCIRDLKV 150
LamG smart00282
Laminin G domain;
1086-1222 1.48e-31

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 120.52  E-value: 1.48e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508931  1086 LEVVFLARGPSGLLLYNGQKtdGKGDFVSLALRDRRLEFRYDLGKGAAVIRS-REPVTLGAWTRVSLERNGRKGALRVGD 1164
Cdd:smart00282    2 ISFSFRTTSPNGLLLYAGSK--GGGDYLALELRDGRLVLRYDLGSGPARLTSdPTPLNDGQWHRVAVERNGRSVTLSVDG 79

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462508931  1165 GPRVLGESPKSrkvpHTVLNLKEPLYVGGAPDFSKLaRAAAVSSGFDGAIQLVSLGGR 1222
Cdd:smart00282   80 GNRVSGESPGG----LTILNLDGPLYLGGLPEDLKL-PPLPVTPGFRGCIRNLKVNGK 132
SEA smart00200
Domain found in sea urchin sperm protein, enterokinase, agrin; Proposed function of regulating ...
 552-676 1.05e-28

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: 111.73  E-value: 1.05e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508931   552 ATKVFQGVLELEGVEGQELFYTPEMADPKSELFGETARSIESTLDDLFRNSDVKKDFRSVRLRDLGPGKSVRAIVDVHFD 631
Cdd:smart00200    1 PTQSFGVSLSVLSVEGENLQYSPSLEDPSSEEYQELVRDVEKLLEQIYGKTDLKPDFVGTEVIEFRNGSVVVDLGLLFNE 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*
gi 2462508931   632 PTTAfrAPDVARALLRQIQVSrRRSLGVRRplQEHVRFMDFDWFP 676
Cdd:smart00200   81 GVTN--GQDVEEDLLQVIKQA-AYSLKITN--VNVVDVLDPDSAD 120
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 215-257 5.68e-16

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 73.16  E-value: 5.68e-16
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 2462508931  215 CQCNPHGSYGGTCDPATGQCSCRPGVGGLRCDRCEPGFWNFRG 257
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPS 43
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 214-255 1.32e-15

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: 72.00  E-value: 1.32e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 2462508931  214 ACQCNPHGSYGGTCDPATGQCSCRPGVGGLRCDRCEPGFWNF 255
Cdd:cd00055      1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGL 42
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
215-257 1.02e-14

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 69.26  E-value: 1.02e-14
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 2462508931   215 CQCNPHGSYGGTCDPATGQCSCRPGVGGLRCDRCEPGFWNFRG 257
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
SEA pfam01390
SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed ...
 570-648 2.89e-14

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: 69.96  E-value: 2.89e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508931  570 LFYTPEMADPKSELFGETARSIESTLDDLFRNSDVKKDFRSVRLRDLGPGK-SVRAIVDVHFDPTTAFRAPDVAR---AL 645
Cdd:pfam01390   12 LQYTPDLGNPSSQEFKSLSRRIESLLNELFRNSSLRKQYIKSHVLRLRPDGgSVVVDVVLVFRFPSTEPALDREKlieEI 91


                   ...
gi 2462508931  646 LRQ 648
Cdd:pfam01390   92 LRQ 94
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 126-172 2.98e-13

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


Pssm-ID: 197624  Cd Length: 46  Bit Score: 65.39  E-value: 2.98e-13
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 2462508931   126 VCDFSCQSVPgSPVCGSDGVTYSTECELKKARCESQRGLYVAAQGAC 172
Cdd:smart00280    1 DCPEACPREY-DPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 34-86 1.37e-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: 1.37e-11
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 2462508931    34 VCSagqCVCPRCEHPppgpVCGSDGVTYGSACELREAACLQQTQIEEARAGPC 86
Cdd:smart00280    1 DCP---EACPREYDP----VCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 344-391 7.37e-11

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


Pssm-ID: 197624  Cd Length: 46  Bit Score: 58.46  E-value: 7.37e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 2462508931   344 VCPMlTCPEANAtKVCGSDGVTYGNECQLKTIACRQGLQISIQSLGPC 391
Cdd:smart00280    1 DCPE-ACPREYD-PVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
 42-86 7.44e-11

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: 58.44  E-value: 7.44e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2462508931   42 CPRCEHPppgpVCGSDGVTYGSACELREAACLQQTQIEEARAGPC 86
Cdd:cd00104      1 CPKEYDP----VCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 269-305 2.90e-10

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 56.98  E-value: 2.90e-10
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 2462508931  269 CSCDPQGAVRDDCEQMTGLCSCKPGVAGPKCGQCPDG 305
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPG 37
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
 137-172 1.22e-09

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: 54.97  E-value: 1.22e-09
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 2462508931  137 SPVCGSDGVTYSTECELKKARCESQRGLYVAAQGAC 172
Cdd:cd00104      6 DPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
 350-391 1.45e-09

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: 54.58  E-value: 1.45e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 2462508931  350 CPEaNATKVCGSDGVTYGNECQLKTIACRQGLQISIQSLGPC 391
Cdd:cd00104      1 CPK-EYDPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 268-314 1.54e-09

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: 54.67  E-value: 1.54e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2462508931  268 PCSCDPQGAVRDDCEQMTGLCSCKPGVAGPKCGQCPDG---RALGPAGCE 314
Cdd:cd00055      1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGyygLPSQGGGCQ 50
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
269-305 2.10e-08

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 51.54  E-value: 2.10e-08
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 2462508931   269 CSCDPQGAVRDDCEQMTGLCSCKPGVAGPKCGQCPDG 305
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPG 37
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 127-164 2.77e-08

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: 51.34  E-value: 2.77e-08
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 2462508931  127 CDFSCQSVPGSPVCGSDGVTYSTECELKKARCESQRGL 164
Cdd:pfam07648    2 CNCQCPKTEYEPVCGSDGVTYPSPCALCAAGCKLGKEV 39
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 1247-1279 3.48e-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: 48.02  E-value: 3.48e-07
                           10        20        30
                   ....*....|....*....|....*....|...
gi 2462508931 1247 ASGHPCLNGASCVPREAAYVCLCPGGFSGPHCE 1279
Cdd:cd00054      6 ASGNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 40-86 5.19e-07

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: 47.87  E-value: 5.19e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2462508931   40 CVCPRCEHPPPGPVCGSDGVTYGSACELREAACLQQTQIEEARA---GPC 86
Cdd:pfam07648    1 NCNCQCPKTEYEPVCGSDGVTYPSPCALCAAGCKLGKEVKEEKVkydGSC 50
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 349-391 9.76e-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: 44.02  E-value: 9.76e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2462508931  349 TCPEANATKVCGSDGVTYGNECQLKTIACRQGLQIS---IQSLGPC 391
Cdd:pfam07648    5 QCPKTEYEPVCGSDGVTYPSPCALCAAGCKLGKEVKeekVKYDGSC 50
EGF_CA smart00179
Calcium-binding EGF-like domain;
1247-1279 1.05e-05

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 43.77  E-value: 1.05e-05
                            10        20        30
                    ....*....|....*....|....*....|....
gi 2462508931  1247 ASGHPCLNGASCVPREAAYVCLCPGGFS-GPHCE 1279
Cdd:smart00179    6 ASGNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 755-785 3.54e-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: 39.29  E-value: 3.54e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 2462508931  755 CDSQPCFHGGTCQDwaLGGGFTCSCPAGRGG 785
Cdd:pfam00008    1 CAPNPCSNGGTCVD--TPGGYTCICPEGYTG 29
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 977-1007 3.89e-04

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: 39.16  E-value: 3.89e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 2462508931  977 PNPCHGGAPCQNLEaGRFHCQCPPGRVGPTC 1007
Cdd:cd00054      8 GNPCQNGGTCVNTV-GSYRCSCPPGYTGRNC 37
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 975-1006 8.40e-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: 38.13  E-value: 8.40e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 2462508931  975 CLPNPCHGGAPCQNLEaGRFHCQCPPGRVGPT 1006
Cdd:pfam00008    1 CAPNPCSNGGTCVDTP-GGYTCICPEGYTGKR 31
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 755-789 1.04e-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: 38.00  E-value: 1.04e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 2462508931  755 CDSQ-PCFHGGTCQDwaLGGGFTCSCPAGRGGAVCE 789
Cdd:cd00054      5 CASGnPCQNGGTCVN--TVGSYRCSCPPGYTGRNCE 38
EGF_CA smart00179
Calcium-binding EGF-like domain;
755-789 2.51e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 36.84  E-value: 2.51e-03
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 2462508931   755 CDS-QPCFHGGTCQDwaLGGGFTCSCPAG-RGGAVCE 789
Cdd:smart00179    5 CASgNPCQNGGTCVN--TVGSYRCECPPGyTDGRNCE 39
EGF_CA smart00179
Calcium-binding EGF-like domain;
977-1007 2.89e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 36.84  E-value: 2.89e-03
                            10        20        30
                    ....*....|....*....|....*....|..
gi 2462508931   977 PNPCHGGAPCQNLEaGRFHCQCPPG-RVGPTC 1007
Cdd:smart00179    8 GNPCQNGGTCVNTV-GSYRCECPPGyTDGRNC 38
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 1250-1277 9.45e-03

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: 35.05  E-value: 9.45e-03
                           10        20
                   ....*....|....*....|....*...
gi 2462508931 1250 HPCLNGASCVPREAAYVCLCPGGFSGPH 1277
Cdd:pfam00008    4 NPCSNGGTCVDTPGGYTCICPEGYTGKR 31
 
Name Accession Description Interval E-value
Laminin_G_1 pfam00054
Laminin G domain;
1324-1454 9.99e-48

Laminin G domain;


Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 166.72  E-value: 9.99e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508931 1324 RTEATQGLVLWSGKATERaDYVALAIVDGHLQLSYNLGSQPVVLRSTVPVNTNRWLRVVAHREQREGSLQVGNEAPVTGS 1403
Cdd:pfam00054    2 RTTEPSGLLLYNGTQTER-DFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGE 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462508931 1404 SPLGATQ-LDTDGALWLGGLPELPVgPALPKAYGTGFVGCLRDVVVGRHPLH 1454
Cdd:pfam00054   81 SPLGATTdLDVDGPLYVGGLPSLGV-KKRRLAISPSFDGCIRDVIVNGKPLD 131
Laminin_G_1 pfam00054
Laminin G domain;
822-953 9.02e-47

Laminin G domain;


Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 164.03  E-value: 9.02e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508931  822 FRALEPQGLLLYNGNARGKDFLALALLDGRVQLRFDTGSGPAVLTSAVPVEPGQWHRLELSRHWRRGTLSVDGETPVLGE 901
Cdd:pfam00054    1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGE 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462508931  902 SPSGTDG-LNLDTDLFVGGVPEDqaAVALERTFVGAGLRGCIRLLDVNNQRLE 953
Cdd:pfam00054   81 SPLGATTdLDVDGPLYVGGLPSL--GVKKRRLAISPSFDGCIRDVIVNGKPLD 131
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
 799-948 1.98e-46

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: 163.74  E-value: 1.98e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508931  799 FEGRSFLAFPTLRA-YHTLRLALEFRALEPQGLLLYNGNARGKDFLALALLDGRVQLRFDTGSGPAVLTSAVPVEPGQWH 877
Cdd:cd00110      4 FSGSSYVRLPTLPApRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDGQWH 83

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462508931  878 RLELSRHWRRGTLSVDGETPVLGESPSGTDGLNLDTDLFVGGVPEDQaavALERTFVGAGLRGCIRLLDVN 948
Cdd:cd00110     84 SVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDL---KSPGLPVSPGFVGCIRDLKVN 151
Laminin_G_1 pfam00054
Laminin G domain;
1090-1225 3.86e-44

Laminin G domain;


Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 156.32  E-value: 3.86e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508931 1090 FLARGPSGLLLYNGQKTDGkgDFVSLALRDRRLEFRYDLGKGAAVIRSREPVTLGAWTRVSLERNGRKGALRVGDGPRVL 1169
Cdd:pfam00054    1 FRTTEPSGLLLYNGTQTER--DFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPT 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462508931 1170 GESPKSRKvphTVLNLKEPLYVGGAPDFSKLARAAAVSSGFDGAIQLVSLGGRQLL 1225
Cdd:pfam00054   79 GESPLGAT---TDLDVDGPLYVGGLPSLGVKKRRLAISPSFDGCIRDVIVNGKPLD 131
LamG smart00282
Laminin G domain;
817-950 5.61e-44

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 155.96  E-value: 5.61e-44
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508931   817 RLALEFRALEPQGLLLYNGNARGKDFLALALLDGRVQLRFDTGSGPAVLTS-AVPVEPGQWHRLELSRHWRRGTLSVDGE 895
Cdd:smart00282    1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSdPTPLNDGQWHRVAVERNGRSVTLSVDGG 80

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 2462508931   896 TPVLGESPSGTDGLNLDTDLFVGGVPEDQaavALERTFVGAGLRGCIRLLDVNNQ 950
Cdd:smart00282   81 NRVSGESPGGLTILNLDGPLYLGGLPEDL---KLPPLPVTPGFRGCIRNLKVNGK 132
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
 1292-1448 2.11e-36

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: 135.24  E-value: 2.11e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508931 1292 TLAFDGRTFVEYLNavteSEKALQSNHFELSLRTEATQGLVLWSGKATeRADYVALAIVDGHLQLSYNLGSQPVVLRSTV 1371
Cdd:cd00110      1 GVSFSGSSYVRLPT----LPAPRTRLSISFSFRTTSPNGLLLYAGSQN-GGDFLALELEDGRLVLRYDLGSGSLVLSSKT 75

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462508931 1372 PVNTNRWLRVVAHREQREGSLQVGNEAPVTGSSPLGATQLDTDGALWLGGLPELPVGPALPkaYGTGFVGCLRDVVV 1448
Cdd:cd00110     76 PLNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLP--VSPGFVGCIRDLKV 150
LamG smart00282
Laminin G domain;
1318-1451 1.01e-33

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 126.69  E-value: 1.01e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508931  1318 HFELSLRTEATQGLVLWSGKAtERADYVALAIVDGHLQLSYNLGSQPVVLRST-VPVNTNRWLRVVAHREQREGSLQVGN 1396
Cdd:smart00282    1 SISFSFRTTSPNGLLLYAGSK-GGGDYLALELRDGRLVLRYDLGSGPARLTSDpTPLNDGQWHRVAVERNGRSVTLSVDG 79

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 2462508931  1397 EAPVTGSSPLGATQLDTDGALWLGGLPELPVGPALPkaYGTGFVGCLRDVVVGRH 1451
Cdd:smart00282   80 GNRVSGESPGGLTILNLDGPLYLGGLPEDLKLPPLP--VTPGFRGCIRNLKVNGK 132
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
 822-950 1.17e-33

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: 126.38  E-value: 1.17e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508931  822 FRALEPQGLLLYNGNARGkDFLALALLDGRVQLRFDTGSGPAVLTSA-VPVEPGQWHRLELSRHWRRGTLSVDGETPVLG 900
Cdd:pfam02210    1 FRTRQPNGLLLYAGGGGS-DFLALELVNGRLVLRYDLGSGPESLLSSgKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSS 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2462508931  901 ESPSGTDGLNLDTDLFVGGVPEDQAAVALErtfVGAGLRGCIRLLDVNNQ 950
Cdd:pfam02210   80 LPPGESLLLNLNGPLYLGGLPPLLLLPALP---VRAGFVGCIRDVRVNGE 126
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
 1062-1219 6.65e-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: 125.22  E-value: 6.65e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508931 1062 FNGFSHLELRGLHTFARDlgekMALEVVFLARGPSGLLLYNGQKTdgKGDFVSLALRDRRLEFRYDLGKGAAVIRSREPV 1141
Cdd:cd00110      4 FSGSSYVRLPTLPAPRTR----LSISFSFRTTSPNGLLLYAGSQN--GGDFLALELEDGRLVLRYDLGSGSLVLSSKTPL 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462508931 1142 TLGAWTRVSLERNGRKGALRVgDGPRVLgESPKSRKVPHtvLNLKEPLYVGGAPDFSKLaRAAAVSSGFDGAIQLVSL 1219
Cdd:cd00110     78 NDGQWHSVSVERNGRSVTLSV-DGERVV-ESGSPGGSAL--LNLDGPLYLGGLPEDLKS-PGLPVSPGFVGCIRDLKV 150
LamG smart00282
Laminin G domain;
1086-1222 1.48e-31

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 120.52  E-value: 1.48e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508931  1086 LEVVFLARGPSGLLLYNGQKtdGKGDFVSLALRDRRLEFRYDLGKGAAVIRS-REPVTLGAWTRVSLERNGRKGALRVGD 1164
Cdd:smart00282    2 ISFSFRTTSPNGLLLYAGSK--GGGDYLALELRDGRLVLRYDLGSGPARLTSdPTPLNDGQWHRVAVERNGRSVTLSVDG 79

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462508931  1165 GPRVLGESPKSrkvpHTVLNLKEPLYVGGAPDFSKLaRAAAVSSGFDGAIQLVSLGGR 1222
Cdd:smart00282   80 GNRVSGESPGG----LTILNLDGPLYLGGLPEDLKL-PPLPVTPGFRGCIRNLKVNGK 132
SEA smart00200
Domain found in sea urchin sperm protein, enterokinase, agrin; Proposed function of regulating ...
 552-676 1.05e-28

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: 111.73  E-value: 1.05e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508931   552 ATKVFQGVLELEGVEGQELFYTPEMADPKSELFGETARSIESTLDDLFRNSDVKKDFRSVRLRDLGPGKSVRAIVDVHFD 631
Cdd:smart00200    1 PTQSFGVSLSVLSVEGENLQYSPSLEDPSSEEYQELVRDVEKLLEQIYGKTDLKPDFVGTEVIEFRNGSVVVDLGLLFNE 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*
gi 2462508931   632 PTTAfrAPDVARALLRQIQVSrRRSLGVRRplQEHVRFMDFDWFP 676
Cdd:smart00200   81 GVTN--GQDVEEDLLQVIKQA-AYSLKITN--VNVVDVLDPDSAD 120
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
 1323-1449 8.36e-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: 106.74  E-value: 8.36e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508931 1323 LRTEATQGLVLWSGkaTERADYVALAIVDGHLQLSYNLGSQPVVLRST-VPVNTNRWLRVVAHREQREGSLQVGNEAPVT 1401
Cdd:pfam02210    1 FRTRQPNGLLLYAG--GGGSDFLALELVNGRLVLRYDLGSGPESLLSSgKNLNDGQWHSVRVERNGNTLTLSVDGQTVVS 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 2462508931 1402 GSSPLGATQLDTDGALWLGGLPELPVGPALPkaYGTGFVGCLRDVVVG 1449
Cdd:pfam02210   79 SLPPGESLLLNLNGPLYLGGLPPLLLLPALP--VRAGFVGCIRDVRVN 124
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
 1090-1222 5.85e-22

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: 92.87  E-value: 5.85e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508931 1090 FLARGPSGLLLYNGqktDGKGDFVSLALRDRRLEFRYDLGKGAAVIRS-REPVTLGAWTRVSLERNGRKGALRVGDGPRV 1168
Cdd:pfam02210    1 FRTRQPNGLLLYAG---GGGSDFLALELVNGRLVLRYDLGSGPESLLSsGKNLNDGQWHSVRVERNGNTLTLSVDGQTVV 77

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462508931 1169 LGESPKsrkvPHTVLNLKEPLYVGGAPDFSKLaRAAAVSSGFDGAIQLVSLGGR 1222
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.
 215-257 5.68e-16

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 73.16  E-value: 5.68e-16
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 2462508931  215 CQCNPHGSYGGTCDPATGQCSCRPGVGGLRCDRCEPGFWNFRG 257
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPS 43
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 214-255 1.32e-15

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: 72.00  E-value: 1.32e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 2462508931  214 ACQCNPHGSYGGTCDPATGQCSCRPGVGGLRCDRCEPGFWNF 255
Cdd:cd00055      1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGL 42
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
215-257 1.02e-14

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 69.26  E-value: 1.02e-14
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 2462508931   215 CQCNPHGSYGGTCDPATGQCSCRPGVGGLRCDRCEPGFWNFRG 257
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
SEA pfam01390
SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed ...
 570-648 2.89e-14

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: 69.96  E-value: 2.89e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508931  570 LFYTPEMADPKSELFGETARSIESTLDDLFRNSDVKKDFRSVRLRDLGPGK-SVRAIVDVHFDPTTAFRAPDVAR---AL 645
Cdd:pfam01390   12 LQYTPDLGNPSSQEFKSLSRRIESLLNELFRNSSLRKQYIKSHVLRLRPDGgSVVVDVVLVFRFPSTEPALDREKlieEI 91


                   ...
gi 2462508931  646 LRQ 648
Cdd:pfam01390   92 LRQ 94
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 126-172 2.98e-13

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


Pssm-ID: 197624  Cd Length: 46  Bit Score: 65.39  E-value: 2.98e-13
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 2462508931   126 VCDFSCQSVPgSPVCGSDGVTYSTECELKKARCESQRGLYVAAQGAC 172
Cdd:smart00280    1 DCPEACPREY-DPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 34-86 1.37e-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: 1.37e-11
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 2462508931    34 VCSagqCVCPRCEHPppgpVCGSDGVTYGSACELREAACLQQTQIEEARAGPC 86
Cdd:smart00280    1 DCP---EACPREYDP----VCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 344-391 7.37e-11

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


Pssm-ID: 197624  Cd Length: 46  Bit Score: 58.46  E-value: 7.37e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 2462508931   344 VCPMlTCPEANAtKVCGSDGVTYGNECQLKTIACRQGLQISIQSLGPC 391
Cdd:smart00280    1 DCPE-ACPREYD-PVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
 42-86 7.44e-11

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: 58.44  E-value: 7.44e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2462508931   42 CPRCEHPppgpVCGSDGVTYGSACELREAACLQQTQIEEARAGPC 86
Cdd:cd00104      1 CPKEYDP----VCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 269-305 2.90e-10

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 56.98  E-value: 2.90e-10
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 2462508931  269 CSCDPQGAVRDDCEQMTGLCSCKPGVAGPKCGQCPDG 305
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPG 37
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
 137-172 1.22e-09

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: 54.97  E-value: 1.22e-09
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 2462508931  137 SPVCGSDGVTYSTECELKKARCESQRGLYVAAQGAC 172
Cdd:cd00104      6 DPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
 350-391 1.45e-09

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: 54.58  E-value: 1.45e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 2462508931  350 CPEaNATKVCGSDGVTYGNECQLKTIACRQGLQISIQSLGPC 391
Cdd:cd00104      1 CPK-EYDPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 268-314 1.54e-09

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: 54.67  E-value: 1.54e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2462508931  268 PCSCDPQGAVRDDCEQMTGLCSCKPGVAGPKCGQCPDG---RALGPAGCE 314
Cdd:cd00055      1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGyygLPSQGGGCQ 50
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
269-305 2.10e-08

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 51.54  E-value: 2.10e-08
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 2462508931   269 CSCDPQGAVRDDCEQMTGLCSCKPGVAGPKCGQCPDG 305
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPG 37
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 127-164 2.77e-08

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: 51.34  E-value: 2.77e-08
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 2462508931  127 CDFSCQSVPGSPVCGSDGVTYSTECELKKARCESQRGL 164
Cdd:pfam07648    2 CNCQCPKTEYEPVCGSDGVTYPSPCALCAAGCKLGKEV 39
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 1247-1279 3.48e-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: 48.02  E-value: 3.48e-07
                           10        20        30
                   ....*....|....*....|....*....|...
gi 2462508931 1247 ASGHPCLNGASCVPREAAYVCLCPGGFSGPHCE 1279
Cdd:cd00054      6 ASGNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 40-86 5.19e-07

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: 47.87  E-value: 5.19e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2462508931   40 CVCPRCEHPPPGPVCGSDGVTYGSACELREAACLQQTQIEEARA---GPC 86
Cdd:pfam07648    1 NCNCQCPKTEYEPVCGSDGVTYPSPCALCAAGCKLGKEVKEEKVkydGSC 50
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 349-391 9.76e-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: 44.02  E-value: 9.76e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2462508931  349 TCPEANATKVCGSDGVTYGNECQLKTIACRQGLQIS---IQSLGPC 391
Cdd:pfam07648    5 QCPKTEYEPVCGSDGVTYPSPCALCAAGCKLGKEVKeekVKYDGSC 50
EGF_CA smart00179
Calcium-binding EGF-like domain;
1247-1279 1.05e-05

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 43.77  E-value: 1.05e-05
                            10        20        30
                    ....*....|....*....|....*....|....
gi 2462508931  1247 ASGHPCLNGASCVPREAAYVCLCPGGFS-GPHCE 1279
Cdd:smart00179    6 ASGNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
KAZAL_PSTI cd01327
Kazal-type pancreatic secretory trypsin inhibitors (PSTI) and related proteins, including the ...
 345-391 3.37e-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: 42.27  E-value: 3.37e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 2462508931  345 CPMLTCPeanatkVCGSDGVTYGNECQLKTIACRQGLQISIQSLGPC 391
Cdd:cd01327      5 CPKDYDP------VCGTDGVTYSNECLLCAENLKRQTNIRIKHDGEC 45
Kazal_1 pfam00050
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 346-391 3.75e-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: 42.27  E-value: 3.75e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2462508931  346 PMLTCPeANATKVCGSDGVTYGNECQLKTIACRQGLQISIQSLGPC 391
Cdd:pfam00050    5 PSGACP-RIYDPVCGTDGKTYSNECLFCAENGKRGTNLHKVHDGEC 49
FSL_SPARC cd01328
Follistatin-like SPARC (secreted protein, acidic, and rich in cysteines) domain; SPARC/BM-40 ...
 323-377 1.23e-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: 42.08  E-value: 1.23e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462508931  323 CAEMRCEFGARC-VEESGSAHCVCpMLTCPEANAT--KVCGSDGVTYGNECQLKTIAC 377
Cdd:cd01328      2 CENHHCGAGKVCeVDDENTPKCVC-IDPCPEEVDDrrKVCTNDNETFDSDCELYRTRC 58
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 755-785 3.54e-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: 39.29  E-value: 3.54e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 2462508931  755 CDSQPCFHGGTCQDwaLGGGFTCSCPAGRGG 785
Cdd:pfam00008    1 CAPNPCSNGGTCVD--TPGGYTCICPEGYTG 29
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 977-1007 3.89e-04

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: 39.16  E-value: 3.89e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 2462508931  977 PNPCHGGAPCQNLEaGRFHCQCPPGRVGPTC 1007
Cdd:cd00054      8 GNPCQNGGTCVNTV-GSYRCSCPPGYTGRNC 37
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 975-1006 8.40e-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: 38.13  E-value: 8.40e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 2462508931  975 CLPNPCHGGAPCQNLEaGRFHCQCPPGRVGPT 1006
Cdd:pfam00008    1 CAPNPCSNGGTCVDTP-GGYTCICPEGYTGKR 31
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
 1247-1279 8.78e-04

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: 38.23  E-value: 8.78e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2462508931 1247 ASGHPCLNGASCVPREAAYVCLCPGGFSGP-HCE 1279
Cdd:cd00053      3 AASNPCSNGGTCVNTPGSYRCVCPPGYTGDrSCE 36
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 755-789 1.04e-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: 38.00  E-value: 1.04e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 2462508931  755 CDSQ-PCFHGGTCQDwaLGGGFTCSCPAGRGGAVCE 789
Cdd:cd00054      5 CASGnPCQNGGTCVN--TVGSYRCSCPPGYTGRNCE 38
Kazal_1 pfam00050
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 138-172 1.92e-03

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: 37.65  E-value: 1.92e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 2462508931  138 PVCGSDGVTYSTECELKKARCESQRGLYVAAQGAC 172
Cdd:pfam00050   15 PVCGTDGKTYSNECLFCAENGKRGTNLHKVHDGEC 49
EGF_CA smart00179
Calcium-binding EGF-like domain;
755-789 2.51e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 36.84  E-value: 2.51e-03
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 2462508931   755 CDS-QPCFHGGTCQDwaLGGGFTCSCPAG-RGGAVCE 789
Cdd:smart00179    5 CASgNPCQNGGTCVN--TVGSYRCECPPGyTDGRNCE 39
EGF_CA smart00179
Calcium-binding EGF-like domain;
977-1007 2.89e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 36.84  E-value: 2.89e-03
                            10        20        30
                    ....*....|....*....|....*....|..
gi 2462508931   977 PNPCHGGAPCQNLEaGRFHCQCPPG-RVGPTC 1007
Cdd:smart00179    8 GNPCQNGGTCVNTV-GSYRCECPPGyTDGRNC 38
Kazal_1 pfam00050
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 52-86 3.18e-03

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: 36.88  E-value: 3.18e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 2462508931   52 PVCGSDGVTYGSACELREAACLQQTQIEEARAGPC 86
Cdd:pfam00050   15 PVCGTDGKTYSNECLFCAENGKRGTNLHKVHDGEC 49
KAZAL_PSTI cd01327
Kazal-type pancreatic secretory trypsin inhibitors (PSTI) and related proteins, including the ...
 138-172 3.65e-03

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: 36.88  E-value: 3.65e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 2462508931  138 PVCGSDGVTYSTECELKKARCESQRGLYVAAQGAC 172
Cdd:cd01327     11 PVCGTDGVTYSNECLLCAENLKRQTNIRIKHDGEC 45
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 1250-1277 9.45e-03

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: 35.05  E-value: 9.45e-03
                           10        20
                   ....*....|....*....|....*...
gi 2462508931 1250 HPCLNGASCVPREAAYVCLCPGGFSGPH 1277
Cdd:pfam00008    4 NPCSNGGTCVDTPGGYTCICPEGYTGKR 31
 
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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