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Conserved domains on  [gi|2494281|sp|Q90404|]
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RecName: Full=Agrin

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;
1179-1310 1.29e-38

Laminin G domain;


:

Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 140.53  E-value: 1.29e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494281    1179 IKTEATKGLILWSGKIAEKsDYIALAVVDGFVQMTYDLGSKPVTLRSTIPVNTNQWVRIKANRIHGYGTLQVGNEAPVTG 1258
Cdd:pfam00054    1 FRTTEPSGLLLYNGTQTER-DFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTG 79
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2494281    1259 SSPFAATQ-LDTDGALWLGGIEKLAPGNRlPKAYSTGFIGCIKDVVIDRQELQ 1310
Cdd:pfam00054   80 ESPLGATTdLDVDGPLYVGGLPSLGVKKR-RLAISPSFDGCIRDVIVNGKPLD 131
Laminin_G_1 pfam00054
Laminin G domain;
947-1082 3.42e-38

Laminin G domain;


:

Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 139.37  E-value: 3.42e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494281     947 FLAKDPNGMIFYNGQKTDGrgDFVSLNLRDGYLEFKYDLGKGAAVLRSKAPIPLNVWNVVTVERNGRKGLMKINKDELVS 1026
Cdd:pfam00054    1 FRTTEPSGLLLYNGTQTER--DFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPT 78
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2494281    1027 GESPKSRKaphTALNLKEAFYVGGAPDFNKFARAAGIISGFTGAIQKLSLKSIPLL 1082
Cdd:pfam00054   79 GESPLGAT---TDLDVDGPLYVGGLPSLGVKKRRLAISPSFDGCIRDVIVNGKPLD 131
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
654-803 1.34e-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: 126.76  E-value: 1.34e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494281   654 FGGRSYLAFKTMKAYYT-VRISMEFRASNLDGLPLVQWTEKGKGLHFYRPSEGYVELRFNHGVWDGVITSKTLIKPGNWH 732
Cdd:cd00110    4 FSGSSYVRLPTLPAPRTrLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDGQWH 83
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2494281   733 HVVGNRNRRSGMLSVDGEPHLIGESPPGTDGLNLDTDLFLGGTPEDEMTLvteRTTATKGLQGCIRLLDVN 803
Cdd:cd00110   84 SVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSP---GLPVSPGFVGCIRDLKVN 151
SEA smart00200
Domain found in sea urchin sperm protein, enterokinase, agrin; Proposed function of regulating ...
411-535 4.01e-24

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: 98.64  E-value: 4.01e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494281      411 PTKLFQGVLIVEEVEGQELFYTPEMDDPKSELFGETARSIENALNELFGNSNVKKDFKSVRVHGLGPSDPVRIIVEVHFD 490
Cdd:smart00200    1 PTQSFGVSLSVLSVEGENLQYSPSLEDPSSEEYQELVRDVEKLLEQIYGKTDLKPDFVGTEVIEFRNGSVVVDLGLLFNE 80
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*
gi 2494281      491 PRTsyNSHDVQRALLQQVKQSRRkSIVVKKPEqdNVKIVDFDWAP 535
Cdd:smart00200   81 GVT--NGQDVEEDLLQVIKQAAY-SLKITNVN--VVDVLDPDSAD 120
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
79-119 5.90e-14

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: 67.38  E-value: 5.90e-14
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 2494281    79 CECNRYGSYSKTCSPSSGQCSCKPGVGGLKCDRCEPGFWNF 119
Cdd:cd00055    2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGL 42
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
208-255 1.16e-13

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


:

Pssm-ID: 197624  Cd Length: 46  Bit Score: 66.16  E-value: 1.16e-13
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 2494281      208 ECPpSICPKNKQfKVCGSDGVTYANECQLKTIACRQGSVINILHQGPC 255
Cdd:smart00280    1 DCP-EACPREYD-PVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
133-180 6.00e-09

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


:

Pssm-ID: 395007  Cd Length: 49  Bit Score: 53.13  E-value: 6.00e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 2494281     133 CNCYPLGAVRDDCEQMSGLCSCKAGISGMKCNQCPNGSKLGPSGCDQD 180
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQG 48
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
3-39 1.69e-08

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


:

Pssm-ID: 197624  Cd Length: 46  Bit Score: 51.53  E-value: 1.69e-08
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 2494281        3 LSPVCGSDGVTYDSECALKLMRCMIQKDLHVVMLSPC 39
Cdd:smart00280   10 YDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
612-640 5.29e-06

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: 44.30  E-value: 5.29e-06
                           10        20
                   ....*....|....*....|....*....
gi 2494281     612 CDSQPCLHGGTCEDDGVSYTCSCPAGRGG 640
Cdd:pfam00008    1 CAPNPCSNGGTCVDTPGGYTCICPEGYTG 29
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
1104-1135 1.70e-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: 39.93  E-value: 1.70e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 2494281  1104 TRNPCQNGGVCSPRLREYDCMCQRGFSGPQCE 1135
Cdd:cd00054    7 SGNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
 
Name Accession Description Interval E-value
Laminin_G_1 pfam00054
Laminin G domain;
1179-1310 1.29e-38

Laminin G domain;


Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 140.53  E-value: 1.29e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494281    1179 IKTEATKGLILWSGKIAEKsDYIALAVVDGFVQMTYDLGSKPVTLRSTIPVNTNQWVRIKANRIHGYGTLQVGNEAPVTG 1258
Cdd:pfam00054    1 FRTTEPSGLLLYNGTQTER-DFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTG 79
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2494281    1259 SSPFAATQ-LDTDGALWLGGIEKLAPGNRlPKAYSTGFIGCIKDVVIDRQELQ 1310
Cdd:pfam00054   80 ESPLGATTdLDVDGPLYVGGLPSLGVKKR-RLAISPSFDGCIRDVIVNGKPLD 131
Laminin_G_1 pfam00054
Laminin G domain;
947-1082 3.42e-38

Laminin G domain;


Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 139.37  E-value: 3.42e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494281     947 FLAKDPNGMIFYNGQKTDGrgDFVSLNLRDGYLEFKYDLGKGAAVLRSKAPIPLNVWNVVTVERNGRKGLMKINKDELVS 1026
Cdd:pfam00054    1 FRTTEPSGLLLYNGTQTER--DFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPT 78
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2494281    1027 GESPKSRKaphTALNLKEAFYVGGAPDFNKFARAAGIISGFTGAIQKLSLKSIPLL 1082
Cdd:pfam00054   79 GESPLGAT---TDLDVDGPLYVGGLPSLGVKKRRLAISPSFDGCIRDVIVNGKPLD 131
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
654-803 1.34e-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: 126.76  E-value: 1.34e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494281   654 FGGRSYLAFKTMKAYYT-VRISMEFRASNLDGLPLVQWTEKGKGLHFYRPSEGYVELRFNHGVWDGVITSKTLIKPGNWH 732
Cdd:cd00110    4 FSGSSYVRLPTLPAPRTrLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDGQWH 83
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2494281   733 HVVGNRNRRSGMLSVDGEPHLIGESPPGTDGLNLDTDLFLGGTPEDEMTLvteRTTATKGLQGCIRLLDVN 803
Cdd:cd00110   84 SVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSP---GLPVSPGFVGCIRDLKVN 151
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
1148-1305 9.42e-32

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: 121.76  E-value: 9.42e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494281  1148 SVAFNGRTFIEYHNTVTRSEKavqvNYFEMSIKTEATKGLILWSGKiAEKSDYIALAVVDGFVQMTYDLGSKPVTLRSTI 1227
Cdd:cd00110    1 GVSFSGSSYVRLPTLPAPRTR----LSISFSFRTTSPNGLLLYAGS-QNGGDFLALELEDGRLVLRYDLGSGSLVLSSKT 75
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2494281  1228 PVNTNQWVRIKANRIHGYGTLQVGNEAPVTGSSPFAATQLDTDGALWLGGIEklAPGNRLPKAYSTGFIGCIKDVVID 1305
Cdd:cd00110   76 PLNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLP--EDLKSPGLPVSPGFVGCIRDLKVN 151
LamG smart00282
Laminin G domain;
1174-1307 1.59e-30

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 117.44  E-value: 1.59e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494281     1174 YFEMSIKTEATKGLILWSGKiAEKSDYIALAVVDGFVQMTYDLGSKPVTLRST-IPVNTNQWVRIKANRIHGYGTLQVGN 1252
Cdd:smart00282    1 SISFSFRTTSPNGLLLYAGS-KGGGDYLALELRDGRLVLRYDLGSGPARLTSDpTPLNDGQWHRVAVERNGRSVTLSVDG 79
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 2494281     1253 EAPVTGSSPFAATQLDTDGALWLGGIekLAPGNRLPKAYSTGFIGCIKDVVIDRQ 1307
Cdd:smart00282   80 GNRVSGESPGGLTILNLDGPLYLGGL--PEDLKLPPLPVTPGFRGCIRNLKVNGK 132
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
919-1076 9.01e-30

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: 115.98  E-value: 9.01e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494281   919 FNGLSYLEMNGIHTFvsdlLQKLSMEVIFLAKDPNGMIFYNGQKTdgRGDFVSLNLRDGYLEFKYDLGKGAAVLRSKAPI 998
Cdd:cd00110    4 FSGSSYVRLPTLPAP----RTRLSISFSFRTTSPNGLLLYAGSQN--GGDFLALELEDGRLVLRYDLGSGSLVLSSKTPL 77
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2494281   999 PLNVWNVVTVERNGRKGLMKInkDELVSGESPKSRKAPHtaLNLKEAFYVGGAPDFNKFARAAgIISGFTGAIQKLSL 1076
Cdd:cd00110   78 NDGQWHSVSVERNGRSVTLSV--DGERVVESGSPGGSAL--LNLDGPLYLGGLPEDLKSPGLP-VSPGFVGCIRDLKV 150
LamG smart00282
Laminin G domain;
672-804 2.35e-29

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 113.97  E-value: 2.35e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494281      672 RISMEFRASNLDGLpLVQWTEKGKGLHFY-RPSEGYVELRFNHGVWDGVITSKTL-IKPGNWHHVVGNRNRRSGMLSVDG 749
Cdd:smart00282    1 SISFSFRTTSPNGL-LLYAGSKGGGDYLAlELRDGRLVLRYDLGSGPARLTSDPTpLNDGQWHRVAVERNGRSVTLSVDG 79
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 2494281      750 EPHLIGESPPGTDGLNLDTDLFLGGTPEDemtLVTERTTATKGLQGCIRLLDVNN 804
Cdd:smart00282   80 GNRVSGESPGGLTILNLDGPLYLGGLPED---LKLPPLPVTPGFRGCIRNLKVNG 131
LamG smart00282
Laminin G domain;
942-1076 5.93e-28

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 110.12  E-value: 5.93e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494281      942 SMEVIFLAKDPNGMIFYNGQKtdGRGDFVSLNLRDGYLEFKYDLGKGAAVLRSKA-PIPLNVWNVVTVERNGRKGLMKIN 1020
Cdd:smart00282    1 SISFSFRTTSPNGLLLYAGSK--GGGDYLALELRDGRLVLRYDLGSGPARLTSDPtPLNDGQWHRVAVERNGRSVTLSVD 78
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 2494281     1021 KDELVSGESPksrkAPHTALNLKEAFYVGGAPDFNKfARAAGIISGFTGAIQKLSL 1076
Cdd:smart00282   79 GGNRVSGESP----GGLTILNLDGPLYLGGLPEDLK-LPPLPVTPGFRGCIRNLKV 129
SEA smart00200
Domain found in sea urchin sperm protein, enterokinase, agrin; Proposed function of regulating ...
411-535 4.01e-24

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: 98.64  E-value: 4.01e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494281      411 PTKLFQGVLIVEEVEGQELFYTPEMDDPKSELFGETARSIENALNELFGNSNVKKDFKSVRVHGLGPSDPVRIIVEVHFD 490
Cdd:smart00200    1 PTQSFGVSLSVLSVEGENLQYSPSLEDPSSEEYQELVRDVEKLLEQIYGKTDLKPDFVGTEVIEFRNGSVVVDLGLLFNE 80
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*
gi 2494281      491 PRTsyNSHDVQRALLQQVKQSRRkSIVVKKPEqdNVKIVDFDWAP 535
Cdd:smart00200   81 GVT--NGQDVEEDLLQVIKQAAY-SLKITNVN--VVDVLDPDSAD 120
Laminin_G_1 pfam00054
Laminin G domain;
677-804 6.08e-24

Laminin G domain;


Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 98.54  E-value: 6.08e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494281     677 FRASNLDGLPLvqWTEKGKGLHFY----RpsEGYVELRFNHGVWDGVITSKTLIKPGNWHHVVGNRNRRSGMLSVDGEPH 752
Cdd:pfam00054    1 FRTTEPSGLLL--YNGTQTERDFLalelR--DGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEAR 76
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2494281     753 LIGESPPGTDG-LNLDTDLFLGGTPEDEMTLvtERTTATKGLQGCIRLLDVNN 804
Cdd:pfam00054   77 PTGESPLGATTdLDVDGPLYVGGLPSLGVKK--RRLAISPSFDGCIRDVIVNG 127
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
79-119 5.90e-14

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: 67.38  E-value: 5.90e-14
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 2494281    79 CECNRYGSYSKTCSPSSGQCSCKPGVGGLKCDRCEPGFWNF 119
Cdd:cd00055    2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGL 42
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
79-130 8.19e-14

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 66.99  E-value: 8.19e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2494281      79 CECNRYGSYSKTCSPSSGQCSCKPGVGGLKCDRCEPGFWNFRGivtDEKSGC 130
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPS---DPPQGC 49
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
208-255 1.16e-13

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


Pssm-ID: 197624  Cd Length: 46  Bit Score: 66.16  E-value: 1.16e-13
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 2494281      208 ECPpSICPKNKQfKVCGSDGVTYANECQLKTIACRQGSVINILHQGPC 255
Cdd:smart00280    1 DCP-EACPREYD-PVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
79-121 1.65e-13

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 65.80  E-value: 1.65e-13
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 2494281       79 CECNRYGSYSKTCSPSSGQCSCKPGVGGLKCDRCEPGFWNFRG 121
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
SEA pfam01390
SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed ...
429-511 1.93e-13

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: 67.65  E-value: 1.93e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494281     429 LFYTPEMDDPKSELFGETARSIENALNELFGNSNVKKDFKSVRVHGLGPSDP-VRIIVEVHFDPRTSYNSHDVQR---AL 504
Cdd:pfam01390   12 LQYTPDLGNPSSQEFKSLSRRIESLLNELFRNSSLRKQYIKSHVLRLRPDGGsVVVDVVLVFRFPSTEPALDREKlieEI 91

                   ....*..
gi 2494281     505 LQQVKQS 511
Cdd:pfam01390   92 LRQTLNN 98
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
214-255 2.25e-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: 59.59  E-value: 2.25e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 2494281   214 CPKNkQFKVCGSDGVTYANECQLKTIACRQGSVINILHQGPC 255
Cdd:cd00104    1 CPKE-YDPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
133-180 6.00e-09

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 53.13  E-value: 6.00e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 2494281     133 CNCYPLGAVRDDCEQMSGLCSCKAGISGMKCNQCPNGSKLGPSGCDQD 180
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQG 48
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
3-39 1.69e-08

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


Pssm-ID: 197624  Cd Length: 46  Bit Score: 51.53  E-value: 1.69e-08
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 2494281        3 LSPVCGSDGVTYDSECALKLMRCMIQKDLHVVMLSPC 39
Cdd:smart00280   10 YDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
132-169 1.26e-07

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: 49.27  E-value: 1.26e-07
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 2494281   132 PCNCYPLGAVRDDCEQMSGLCSCKAGISGMKCNQCPNG 169
Cdd:cd00055    1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPG 38
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
209-255 1.59e-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: 49.03  E-value: 1.59e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2494281     209 CPPSICPKNKQFKVCGSDGVTYANECQLKTIACRQGSVIN---ILHQGPC 255
Cdd:pfam07648    1 NCNCQCPKTEYEPVCGSDGVTYPSPCALCAAGCKLGKEVKeekVKYDGSC 50
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
133-169 2.75e-07

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 48.08  E-value: 2.75e-07
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 2494281      133 CNCYPLGAVRDDCEQMSGLCSCKAGISGMKCNQCPNG 169
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPG 37
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
4-39 2.95e-07

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: 48.04  E-value: 2.95e-07
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 2494281     4 SPVCGSDGVTYDSECALKLMRCMIQKDLHVVMLSPC 39
Cdd:cd00104    6 DPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
612-640 5.29e-06

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: 44.30  E-value: 5.29e-06
                           10        20
                   ....*....|....*....|....*....
gi 2494281     612 CDSQPCLHGGTCEDDGVSYTCSCPAGRGG 640
Cdd:pfam00008    1 CAPNPCSNGGTCVDTPGGYTCICPEGYTG 29
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
612-644 8.28e-05

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: 41.08  E-value: 8.28e-05
                         10        20        30
                 ....*....|....*....|....*....|....
gi 2494281   612 CDSQ-PCLHGGTCEDDGVSYTCSCPAGRGGAVCE 644
Cdd:cd00054    5 CASGnPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
1104-1135 1.70e-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: 39.93  E-value: 1.70e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 2494281  1104 TRNPCQNGGVCSPRLREYDCMCQRGFSGPQCE 1135
Cdd:cd00054    7 SGNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
3-36 1.97e-04

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: 40.17  E-value: 1.97e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2494281       3 LSPVCGSDGVTYDSECALKLMRCMIQKDLHVVML 36
Cdd:pfam07648   11 YEPVCGSDGVTYPSPCALCAAGCKLGKEVKEEKV 44
EGF_CA smart00179
Calcium-binding EGF-like domain;
612-644 6.13e-04

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 38.38  E-value: 6.13e-04
                            10        20        30
                    ....*....|....*....|....*....|....*
gi 2494281      612 CDS-QPCLHGGTCEDDGVSYTCSCPAG-RGGAVCE 644
Cdd:smart00179    5 CASgNPCQNGGTCVNTVGSYRCECPPGyTDGRNCE 39
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
1106-1133 5.53e-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: 35.82  E-value: 5.53e-03
                           10        20
                   ....*....|....*....|....*...
gi 2494281    1106 NPCQNGGVCSPRLREYDCMCQRGFSGPQ 1133
Cdd:pfam00008    4 NPCSNGGTCVDTPGGYTCICPEGYTGKR 31
EGF_CA smart00179
Calcium-binding EGF-like domain;
1104-1135 8.93e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 35.30  E-value: 8.93e-03
                            10        20        30
                    ....*....|....*....|....*....|...
gi 2494281     1104 TRNPCQNGGVCSPRLREYDCMCQRGFS-GPQCE 1135
Cdd:smart00179    7 SGNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
 
Name Accession Description Interval E-value
Laminin_G_1 pfam00054
Laminin G domain;
1179-1310 1.29e-38

Laminin G domain;


Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 140.53  E-value: 1.29e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494281    1179 IKTEATKGLILWSGKIAEKsDYIALAVVDGFVQMTYDLGSKPVTLRSTIPVNTNQWVRIKANRIHGYGTLQVGNEAPVTG 1258
Cdd:pfam00054    1 FRTTEPSGLLLYNGTQTER-DFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTG 79
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2494281    1259 SSPFAATQ-LDTDGALWLGGIEKLAPGNRlPKAYSTGFIGCIKDVVIDRQELQ 1310
Cdd:pfam00054   80 ESPLGATTdLDVDGPLYVGGLPSLGVKKR-RLAISPSFDGCIRDVIVNGKPLD 131
Laminin_G_1 pfam00054
Laminin G domain;
947-1082 3.42e-38

Laminin G domain;


Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 139.37  E-value: 3.42e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494281     947 FLAKDPNGMIFYNGQKTDGrgDFVSLNLRDGYLEFKYDLGKGAAVLRSKAPIPLNVWNVVTVERNGRKGLMKINKDELVS 1026
Cdd:pfam00054    1 FRTTEPSGLLLYNGTQTER--DFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPT 78
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2494281    1027 GESPKSRKaphTALNLKEAFYVGGAPDFNKFARAAGIISGFTGAIQKLSLKSIPLL 1082
Cdd:pfam00054   79 GESPLGAT---TDLDVDGPLYVGGLPSLGVKKRRLAISPSFDGCIRDVIVNGKPLD 131
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
654-803 1.34e-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: 126.76  E-value: 1.34e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494281   654 FGGRSYLAFKTMKAYYT-VRISMEFRASNLDGLPLVQWTEKGKGLHFYRPSEGYVELRFNHGVWDGVITSKTLIKPGNWH 732
Cdd:cd00110    4 FSGSSYVRLPTLPAPRTrLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDGQWH 83
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2494281   733 HVVGNRNRRSGMLSVDGEPHLIGESPPGTDGLNLDTDLFLGGTPEDEMTLvteRTTATKGLQGCIRLLDVN 803
Cdd:cd00110   84 SVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSP---GLPVSPGFVGCIRDLKVN 151
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
1148-1305 9.42e-32

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: 121.76  E-value: 9.42e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494281  1148 SVAFNGRTFIEYHNTVTRSEKavqvNYFEMSIKTEATKGLILWSGKiAEKSDYIALAVVDGFVQMTYDLGSKPVTLRSTI 1227
Cdd:cd00110    1 GVSFSGSSYVRLPTLPAPRTR----LSISFSFRTTSPNGLLLYAGS-QNGGDFLALELEDGRLVLRYDLGSGSLVLSSKT 75
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2494281  1228 PVNTNQWVRIKANRIHGYGTLQVGNEAPVTGSSPFAATQLDTDGALWLGGIEklAPGNRLPKAYSTGFIGCIKDVVID 1305
Cdd:cd00110   76 PLNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLP--EDLKSPGLPVSPGFVGCIRDLKVN 151
LamG smart00282
Laminin G domain;
1174-1307 1.59e-30

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 117.44  E-value: 1.59e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494281     1174 YFEMSIKTEATKGLILWSGKiAEKSDYIALAVVDGFVQMTYDLGSKPVTLRST-IPVNTNQWVRIKANRIHGYGTLQVGN 1252
Cdd:smart00282    1 SISFSFRTTSPNGLLLYAGS-KGGGDYLALELRDGRLVLRYDLGSGPARLTSDpTPLNDGQWHRVAVERNGRSVTLSVDG 79
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 2494281     1253 EAPVTGSSPFAATQLDTDGALWLGGIekLAPGNRLPKAYSTGFIGCIKDVVIDRQ 1307
Cdd:smart00282   80 GNRVSGESPGGLTILNLDGPLYLGGL--PEDLKLPPLPVTPGFRGCIRNLKVNGK 132
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
919-1076 9.01e-30

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: 115.98  E-value: 9.01e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494281   919 FNGLSYLEMNGIHTFvsdlLQKLSMEVIFLAKDPNGMIFYNGQKTdgRGDFVSLNLRDGYLEFKYDLGKGAAVLRSKAPI 998
Cdd:cd00110    4 FSGSSYVRLPTLPAP----RTRLSISFSFRTTSPNGLLLYAGSQN--GGDFLALELEDGRLVLRYDLGSGSLVLSSKTPL 77
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2494281   999 PLNVWNVVTVERNGRKGLMKInkDELVSGESPKSRKAPHtaLNLKEAFYVGGAPDFNKFARAAgIISGFTGAIQKLSL 1076
Cdd:cd00110   78 NDGQWHSVSVERNGRSVTLSV--DGERVVESGSPGGSAL--LNLDGPLYLGGLPEDLKSPGLP-VSPGFVGCIRDLKV 150
LamG smart00282
Laminin G domain;
672-804 2.35e-29

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 113.97  E-value: 2.35e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494281      672 RISMEFRASNLDGLpLVQWTEKGKGLHFY-RPSEGYVELRFNHGVWDGVITSKTL-IKPGNWHHVVGNRNRRSGMLSVDG 749
Cdd:smart00282    1 SISFSFRTTSPNGL-LLYAGSKGGGDYLAlELRDGRLVLRYDLGSGPARLTSDPTpLNDGQWHRVAVERNGRSVTLSVDG 79
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 2494281      750 EPHLIGESPPGTDGLNLDTDLFLGGTPEDemtLVTERTTATKGLQGCIRLLDVNN 804
Cdd:smart00282   80 GNRVSGESPGGLTILNLDGPLYLGGLPED---LKLPPLPVTPGFRGCIRNLKVNG 131
LamG smart00282
Laminin G domain;
942-1076 5.93e-28

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 110.12  E-value: 5.93e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494281      942 SMEVIFLAKDPNGMIFYNGQKtdGRGDFVSLNLRDGYLEFKYDLGKGAAVLRSKA-PIPLNVWNVVTVERNGRKGLMKIN 1020
Cdd:smart00282    1 SISFSFRTTSPNGLLLYAGSK--GGGDYLALELRDGRLVLRYDLGSGPARLTSDPtPLNDGQWHRVAVERNGRSVTLSVD 78
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 2494281     1021 KDELVSGESPksrkAPHTALNLKEAFYVGGAPDFNKfARAAGIISGFTGAIQKLSL 1076
Cdd:smart00282   79 GGNRVSGESP----GGLTILNLDGPLYLGGLPEDLK-LPPLPVTPGFRGCIRNLKV 129
SEA smart00200
Domain found in sea urchin sperm protein, enterokinase, agrin; Proposed function of regulating ...
411-535 4.01e-24

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: 98.64  E-value: 4.01e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494281      411 PTKLFQGVLIVEEVEGQELFYTPEMDDPKSELFGETARSIENALNELFGNSNVKKDFKSVRVHGLGPSDPVRIIVEVHFD 490
Cdd:smart00200    1 PTQSFGVSLSVLSVEGENLQYSPSLEDPSSEEYQELVRDVEKLLEQIYGKTDLKPDFVGTEVIEFRNGSVVVDLGLLFNE 80
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*
gi 2494281      491 PRTsyNSHDVQRALLQQVKQSRRkSIVVKKPEqdNVKIVDFDWAP 535
Cdd:smart00200   81 GVT--NGQDVEEDLLQVIKQAAY-SLKITNVN--VVDVLDPDSAD 120
Laminin_G_1 pfam00054
Laminin G domain;
677-804 6.08e-24

Laminin G domain;


Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 98.54  E-value: 6.08e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494281     677 FRASNLDGLPLvqWTEKGKGLHFY----RpsEGYVELRFNHGVWDGVITSKTLIKPGNWHHVVGNRNRRSGMLSVDGEPH 752
Cdd:pfam00054    1 FRTTEPSGLLL--YNGTQTERDFLalelR--DGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEAR 76
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2494281     753 LIGESPPGTDG-LNLDTDLFLGGTPEDEMTLvtERTTATKGLQGCIRLLDVNN 804
Cdd:pfam00054   77 PTGESPLGATTdLDVDGPLYVGGLPSLGVKK--RRLAISPSFDGCIRDVIVNG 127
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
1179-1307 1.82e-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: 94.02  E-value: 1.82e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494281    1179 IKTEATKGLILWSGkiAEKSDYIALAVVDGFVQMTYDLGSKPVTLRST-IPVNTNQWVRIKANRIHGYGTLQVGNEAPVT 1257
Cdd:pfam02210    1 FRTRQPNGLLLYAG--GGGSDFLALELVNGRLVLRYDLGSGPESLLSSgKNLNDGQWHSVRVERNGNTLTLSVDGQTVVS 78
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2494281    1258 GSSPFAATQLDTDGALWLGGIekLAPGNRLPKAYSTGFIGCIKDVVIDRQ 1307
Cdd:pfam02210   79 SLPPGESLLLNLNGPLYLGGL--PPLLLLPALPVRAGFVGCIRDVRVNGE 126
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
951-1076 2.34e-18

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: 82.47  E-value: 2.34e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494281     951 DPNGMIFYNGqktDGRGDFVSLNLRDGYLEFKYDLGKGAAVLRSKaPIPLN--VWNVVTVERNGRKGLMKINKDELVSGE 1028
Cdd:pfam02210    5 QPNGLLLYAG---GGGSDFLALELVNGRLVLRYDLGSGPESLLSS-GKNLNdgQWHSVRVERNGNTLTLSVDGQTVVSSL 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 2494281    1029 SPksrkAPHTALNLKEAFYVGGAPDFNKFARAAgIISGFTGAIQKLSL 1076
Cdd:pfam02210   81 PP----GESLLLNLNGPLYLGGLPPLLLLPALP-VRAGFVGCIRDVRV 123
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
703-804 1.78e-15

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: 73.99  E-value: 1.78e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494281     703 SEGYVELRFNHGvwDGVITSKTLIKP---GNWHHVVGNRNRRSGMLSVDGEPHLIGESPPGTDGLNLDTDLFLGGTPEDe 779
Cdd:pfam02210   26 VNGRLVLRYDLG--SGPESLLSSGKNlndGQWHSVRVERNGNTLTLSVDGQTVVSSLPPGESLLLNLNGPLYLGGLPPL- 102
                           90       100
                   ....*....|....*....|....*
gi 2494281     780 mtLVTERTTATKGLQGCIRLLDVNN 804
Cdd:pfam02210  103 --LLLPALPVRAGFVGCIRDVRVNG 125
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
79-119 5.90e-14

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: 67.38  E-value: 5.90e-14
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 2494281    79 CECNRYGSYSKTCSPSSGQCSCKPGVGGLKCDRCEPGFWNF 119
Cdd:cd00055    2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGL 42
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
79-130 8.19e-14

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 66.99  E-value: 8.19e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2494281      79 CECNRYGSYSKTCSPSSGQCSCKPGVGGLKCDRCEPGFWNFRGivtDEKSGC 130
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPS---DPPQGC 49
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
208-255 1.16e-13

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


Pssm-ID: 197624  Cd Length: 46  Bit Score: 66.16  E-value: 1.16e-13
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 2494281      208 ECPpSICPKNKQfKVCGSDGVTYANECQLKTIACRQGSVINILHQGPC 255
Cdd:smart00280    1 DCP-EACPREYD-PVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
79-121 1.65e-13

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 65.80  E-value: 1.65e-13
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 2494281       79 CECNRYGSYSKTCSPSSGQCSCKPGVGGLKCDRCEPGFWNFRG 121
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
SEA pfam01390
SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed ...
429-511 1.93e-13

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: 67.65  E-value: 1.93e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494281     429 LFYTPEMDDPKSELFGETARSIENALNELFGNSNVKKDFKSVRVHGLGPSDP-VRIIVEVHFDPRTSYNSHDVQR---AL 504
Cdd:pfam01390   12 LQYTPDLGNPSSQEFKSLSRRIESLLNELFRNSSLRKQYIKSHVLRLRPDGGsVVVDVVLVFRFPSTEPALDREKlieEI 91

                   ....*..
gi 2494281     505 LQQVKQS 511
Cdd:pfam01390   92 LRQTLNN 98
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
214-255 2.25e-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: 59.59  E-value: 2.25e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 2494281   214 CPKNkQFKVCGSDGVTYANECQLKTIACRQGSVINILHQGPC 255
Cdd:cd00104    1 CPKE-YDPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
133-180 6.00e-09

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 53.13  E-value: 6.00e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 2494281     133 CNCYPLGAVRDDCEQMSGLCSCKAGISGMKCNQCPNGSKLGPSGCDQD 180
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQG 48
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
3-39 1.69e-08

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


Pssm-ID: 197624  Cd Length: 46  Bit Score: 51.53  E-value: 1.69e-08
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 2494281        3 LSPVCGSDGVTYDSECALKLMRCMIQKDLHVVMLSPC 39
Cdd:smart00280   10 YDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
132-169 1.26e-07

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: 49.27  E-value: 1.26e-07
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 2494281   132 PCNCYPLGAVRDDCEQMSGLCSCKAGISGMKCNQCPNG 169
Cdd:cd00055    1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPG 38
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
209-255 1.59e-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: 49.03  E-value: 1.59e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2494281     209 CPPSICPKNKQFKVCGSDGVTYANECQLKTIACRQGSVIN---ILHQGPC 255
Cdd:pfam07648    1 NCNCQCPKTEYEPVCGSDGVTYPSPCALCAAGCKLGKEVKeekVKYDGSC 50
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
133-169 2.75e-07

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 48.08  E-value: 2.75e-07
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 2494281      133 CNCYPLGAVRDDCEQMSGLCSCKAGISGMKCNQCPNG 169
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPG 37
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
4-39 2.95e-07

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: 48.04  E-value: 2.95e-07
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 2494281     4 SPVCGSDGVTYDSECALKLMRCMIQKDLHVVMLSPC 39
Cdd:cd00104    6 DPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
Kazal_1 pfam00050
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
207-255 4.84e-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. Alignment also includes a single domain from transporters in the OATP/PGT family.


Pssm-ID: 395004  Cd Length: 49  Bit Score: 44.97  E-value: 4.84e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2494281     207 CECPPS-ICPKNKQfKVCGSDGVTYANECQLKTIACRQGSVINILHQGPC 255
Cdd:pfam00050    1 CSDYPSgACPRIYD-PVCGTDGKTYSNECLFCAENGKRGTNLHKVHDGEC 49
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
612-640 5.29e-06

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: 44.30  E-value: 5.29e-06
                           10        20
                   ....*....|....*....|....*....
gi 2494281     612 CDSQPCLHGGTCEDDGVSYTCSCPAGRGG 640
Cdd:pfam00008    1 CAPNPCSNGGTCVDTPGGYTCICPEGYTG 29
KAZAL_PSTI cd01327
Kazal-type pancreatic secretory trypsin inhibitors (PSTI) and related proteins, including the ...
213-255 1.64e-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: 43.04  E-value: 1.64e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 2494281   213 ICPKNKQfKVCGSDGVTYANECQLKTIACRQGSVINILHQGPC 255
Cdd:cd01327    4 GCPKDYD-PVCGTDGVTYSNECLLCAENLKRQTNIRIKHDGEC 45
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
612-644 8.28e-05

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: 41.08  E-value: 8.28e-05
                         10        20        30
                 ....*....|....*....|....*....|....
gi 2494281   612 CDSQ-PCLHGGTCEDDGVSYTCSCPAGRGGAVCE 644
Cdd:cd00054    5 CASGnPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
1104-1135 1.70e-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: 39.93  E-value: 1.70e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 2494281  1104 TRNPCQNGGVCSPRLREYDCMCQRGFSGPQCE 1135
Cdd:cd00054    7 SGNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
3-36 1.97e-04

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: 40.17  E-value: 1.97e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2494281       3 LSPVCGSDGVTYDSECALKLMRCMIQKDLHVVML 36
Cdd:pfam07648   11 YEPVCGSDGVTYPSPCALCAAGCKLGKEVKEEKV 44
Laminin_G_3 pfam13385
Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin ...
673-776 2.98e-04

Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin A-like lectin/glucanases superfamily.


Pssm-ID: 463865 [Multi-domain]  Cd Length: 151  Bit Score: 42.76  E-value: 2.98e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2494281     673 ISMEFRASNLDGL-PLVQWTEKGKGLHFYRPSEGYVELRFNHGVWDG-VITSKTLIKPGNWHHVVGNRNRRSGMLSVDGE 750
Cdd:pfam13385   21 VSAWVKPDSLPGWaRAIISSSGGGGYSLGLDGDGRLRFAVNGGNGGWdTVTSGASVPLGQWTHVAVTYDGGTLRLYVNGV 100
                           90       100
                   ....*....|....*....|....*...
gi 2494281     751 phLIGESpPGTDGLNLDTD--LFLGGTP 776
Cdd:pfam13385  101 --LVGSS-TLTGGPPPGTGgpLYIGRSP 125
EGF_CA smart00179
Calcium-binding EGF-like domain;
612-644 6.13e-04

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 38.38  E-value: 6.13e-04
                            10        20        30
                    ....*....|....*....|....*....|....*
gi 2494281      612 CDS-QPCLHGGTCEDDGVSYTCSCPAG-RGGAVCE 644
Cdd:smart00179    5 CASgNPCQNGGTCVNTVGSYRCECPPGyTDGRNCE 39
KAZAL_PSTI cd01327
Kazal-type pancreatic secretory trypsin inhibitors (PSTI) and related proteins, including the ...
3-20 1.05e-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: 38.03  E-value: 1.05e-03
                         10
                 ....*....|....*...
gi 2494281     3 LSPVCGSDGVTYDSECAL 20
Cdd:cd01327    9 YDPVCGTDGVTYSNECLL 26
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
613-644 1.20e-03

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: 37.84  E-value: 1.20e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 2494281   613 DSQPCLHGGTCEDDGVSYTCSCPAG-RGGAVCE 644
Cdd:cd00053    4 ASNPCSNGGTCVNTPGSYRCVCPPGyTGDRSCE 36
Kazal_1 pfam00050
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
3-20 2.50e-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: 37.26  E-value: 2.50e-03
                           10
                   ....*....|....*...
gi 2494281       3 LSPVCGSDGVTYDSECAL 20
Cdd:pfam00050   13 YDPVCGTDGKTYSNECLF 30
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
1106-1133 5.53e-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: 35.82  E-value: 5.53e-03
                           10        20
                   ....*....|....*....|....*...
gi 2494281    1106 NPCQNGGVCSPRLREYDCMCQRGFSGPQ 1133
Cdd:pfam00008    4 NPCSNGGTCVDTPGGYTCICPEGYTGKR 31
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
1104-1135 7.19e-03

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: 35.53  E-value: 7.19e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 2494281  1104 TRNPCQNGGVCSPRLREYDCMCQRGFSGPQ-CE 1135
Cdd:cd00053    4 ASNPCSNGGTCVNTPGSYRCVCPPGYTGDRsCE 36
hEGF pfam12661
Human growth factor-like EGF; hEGF, or human growth factor-like EGF, domains have six ...
617-637 8.23e-03

Human growth factor-like EGF; hEGF, or human growth factor-like EGF, domains have six conserved residues disulfide-bonded into the characteriztic 'ababcc' pattern. They are involved in growth and proliferation of cells, in proteins of the Notch/Delta pathway, neurogulin and selectins. hEGFs are also found in mosaic proteins with four-disulfide laminin EGFs such as aggrecan and perlecan. The core fold of the EGF domain consists of two small beta-hairpins packed against each other. Two major structural variants have been identified based on the structural context of the C-terminal Cys residue of disulfide 'c' in the C-terminal hairpin: hEGFs and cEGFs. In hEGFs the C-terminal thiol resides in the beta-turn, resulting in shorter loop-lengths between the Cys residues of disulfide 'c', typically C[8-9]XC. These shorter loop-lengths are also typical of the four-disulfide EGF domains, laminin ad integrin. Tandem hEGF domains have six linking residues between terminal cysteines of adjacent domains. hEGF domains may or may not bind calcium in the linker region. hEGF domains with the consensus motif CXD4X[F,Y]XCXC are hydroxylated exclusively in the Asp residue.


Pssm-ID: 463660  Cd Length: 22  Bit Score: 35.00  E-value: 8.23e-03
                           10        20
                   ....*....|....*....|.
gi 2494281     617 CLHGGTCEDDGVSYTCSCPAG 637
Cdd:pfam12661    1 CQNGGTCVDGVNGYKCQCPPG 21
EGF_CA smart00179
Calcium-binding EGF-like domain;
1104-1135 8.93e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 35.30  E-value: 8.93e-03
                            10        20        30
                    ....*....|....*....|....*....|...
gi 2494281     1104 TRNPCQNGGVCSPRLREYDCMCQRGFS-GPQCE 1135
Cdd:smart00179    7 SGNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
 
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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