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Conserved domains on  [gi|1487346303|ref|XP_026537342|]
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agrin [Notechis scutatus]

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;
987-1118 4.73e-47

Laminin G domain;


:

Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 164.80  E-value: 4.73e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487346303  987 FRASELSGLLLYNGQNRGKDFVSLALVNGFVELRFNTGSGTGVITSKVPIEPGQWHALVVNRNRRNGVLSVDGEPHMHGE 1066
Cdd:pfam00054    1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGE 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1487346303 1067 SPSGTDG-LNLDTDLFVGGAPEDQidVVAERTSVTAGLKGCIRLLDVNNQMYD 1118
Cdd:pfam00054   81 SPLGATTdLDVDGPLYVGGLPSLG--VKKRRLAISPSFDGCIRDVIVNGKPLD 131
Laminin_G_1 pfam00054
Laminin G domain;
1502-1633 4.98e-42

Laminin G domain;


:

Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 150.55  E-value: 4.98e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487346303 1502 IKTEATQGLILWSGKGLDRsDYIALAIVDGRVQMTYDLGSKPVILRSTVPINTNQWIQIKASRVHRDGSLQVGNESPIMG 1581
Cdd:pfam00054    1 FRTTEPSGLLLYNGTQTER-DFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTG 79
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1487346303 1582 SSPLGATQ-LDTDGALWLGGLEKLSLaHKLPKSFLTGFVGCIRDVVVDRQELH 1633
Cdd:pfam00054   80 ESPLGATTdLDVDGPLYVGGLPSLGV-KKRRLAISPSFDGCIRDVIVNGKPLD 131
Laminin_G_1 pfam00054
Laminin G domain;
1255-1386 7.73e-39

Laminin G domain;


:

Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 141.30  E-value: 7.73e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487346303 1255 FLSRNPNGLIFYNGQKTDGkgDFISLALHNGYLEYRYDLGKGAAVIKSRDPVPLNTWVSVSLERNARKGIMRINNGERTL 1334
Cdd:pfam00054    1 FRTTEPSGLLLYNGTQTER--DFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPT 78
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1487346303 1335 GESPL-PHTSLNLKEPLYVGGAPDFSQLARAAAASASFDGAIQKISIKGTPIL 1386
Cdd:pfam00054   79 GESPLgATTDLDVDGPLYVGGLPSLGVKKRRLAISPSFDGCIRDVIVNGKPLD 131
SEA smart00200
Domain found in sea urchin sperm protein, enterokinase, agrin; Proposed function of regulating ...
719-844 4.56e-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: 4.56e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487346303   719 ATKVFQGVLILEEVEGQELFYTPEMADPKSELFGETARSIESVLDELFRNSEVKRDFRSVQVRHLGQSSAVRVIVETHFD 798
Cdd:smart00200    1 PTQSFGVSLSVLSVEGENLQYSPSLEDPSSEEYQELVRDVEKLLEQIYGKTDLKPDFVGTEVIEFRNGSVVVDLGLLFNE 80
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*.
gi 1487346303   799 PATsyTAADIQRALLKQIKASKKKTilvKRPQQENIKFMDFDWIPQ 844
Cdd:smart00200   81 GVT--NGQDVEEDLLQVIKQAAYSL---KITNVNVVDVLDPDSADS 121
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
330-375 1.21e-13

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


:

Pssm-ID: 197624  Cd Length: 46  Bit Score: 66.55  E-value: 1.21e-13
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 1487346303   330 ECQQVCQSVYDPVCGSDNLTYSNPCELDAMACALRKEIRMKHKGPC 375
Cdd:smart00280    1 DCPEACPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
36-82 3.80e-12

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


:

Pssm-ID: 197624  Cd Length: 46  Bit Score: 62.31  E-value: 3.80e-12
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 1487346303    36 VCKKAtCPSVVAPVCGSDYSTYSNECELEKAQCNQQRRIKVMSKGAC 82
Cdd:smart00280    1 DCPEA-CPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
501-548 1.46e-10

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


:

Pssm-ID: 197624  Cd Length: 46  Bit Score: 57.69  E-value: 1.46e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1487346303   501 ECPSLlCTEaDASKVCGSDGVTYGDQCQLRTIACRQGKAIEVKHLGQC 548
Cdd:smart00280    1 DCPEA-CPR-EYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
124-157 1.47e-10

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


:

Pssm-ID: 197624  Cd Length: 46  Bit Score: 57.69  E-value: 1.47e-10
                            10        20        30
                    ....*....|....*....|....*....|....
gi 1487346303   124 VCGSDGKDYRSECHLNRHACDKQENIFKKFDGPC 157
Cdd:smart00280   13 VCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
426-462 9.84e-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: 55.44  E-value: 9.84e-10
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1487346303  426 CHCDPVGSVRDDCEQMTGLCSCKPGITGTKCKQCPSG 462
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPG 37
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
186-229 7.97e-09

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


:

Pssm-ID: 197624  Cd Length: 46  Bit Score: 52.68  E-value: 7.97e-09
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 1487346303   186 PESCPLKKEPVCGDDGVTYENECVLHRTGAIRGIEIQKLRSGQC 229
Cdd:smart00280    3 PEACPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
260-301 1.74e-08

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


:

Pssm-ID: 197624  Cd Length: 46  Bit Score: 51.91  E-value: 1.74e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|..
gi 1487346303   260 ICDGAYQPLCGRDSRTYFNDCERQKAECQQKAAIPVKHHGPC 301
Cdd:smart00280    5 ACPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
1409-1439 1.36e-06

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: 46.48  E-value: 1.36e-06
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1487346303 1409 PSPCQNSGTCQPRLESYECTCPRGFFGTHCE 1439
Cdd:cd00054      8 GNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
922-950 3.55e-05

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: 41.98  E-value: 3.55e-05
                           10        20
                   ....*....|....*....|....*....
gi 1487346303  922 CDSHPCLHGGTCEDDGRDFTCSCPAGKGG 950
Cdd:pfam00008    1 CAPNPCSNGGTCVDTPGGYTCICPEGYTG 29
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
1140-1171 6.91e-05

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: 41.21  E-value: 6.91e-05
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1487346303 1140 CQPNPCHHGGLCHTMEaEMFHCECLNGYTGPT 1171
Cdd:pfam00008    1 CAPNPCSNGGTCVDTP-GGYTCICPEGYTGKR 31
 
Name Accession Description Interval E-value
Laminin_G_1 pfam00054
Laminin G domain;
987-1118 4.73e-47

Laminin G domain;


Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 164.80  E-value: 4.73e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487346303  987 FRASELSGLLLYNGQNRGKDFVSLALVNGFVELRFNTGSGTGVITSKVPIEPGQWHALVVNRNRRNGVLSVDGEPHMHGE 1066
Cdd:pfam00054    1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGE 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1487346303 1067 SPSGTDG-LNLDTDLFVGGAPEDQidVVAERTSVTAGLKGCIRLLDVNNQMYD 1118
Cdd:pfam00054   81 SPLGATTdLDVDGPLYVGGLPSLG--VKKRRLAISPSFDGCIRDVIVNGKPLD 131
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
963-1113 6.16e-47

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: 165.28  E-value: 6.16e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487346303  963 SFGGKSYLAFKMMKA-YHTVRIAMEFRASELSGLLLYNGQNRGKDFVSLALVNGFVELRFNTGSGTGVITSKVPIEPGQW 1041
Cdd:cd00110      3 SFSGSSYVRLPTLPApRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDGQW 82
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1487346303 1042 HALVVNRNRRNGVLSVDGEPHMHGESPSGTDGLNLDTDLFVGGAPEDQidvVAERTSVTAGLKGCIRLLDVN 1113
Cdd:cd00110     83 HSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDL---KSPGLPVSPGFVGCIRDLKVN 151
LamG smart00282
Laminin G domain;
982-1115 1.63e-42

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 152.11  E-value: 1.63e-42
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487346303   982 RIAMEFRASELSGLLLYNGQNRGKDFVSLALVNGFVELRFNTGSGTGVITSK-VPIEPGQWHALVVNRNRRNGVLSVDGE 1060
Cdd:smart00282    1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDpTPLNDGQWHRVAVERNGRSVTLSVDGG 80
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 1487346303  1061 PHMHGESPSGTDGLNLDTDLFVGGAPEDQidvVAERTSVTAGLKGCIRLLDVNNQ 1115
Cdd:smart00282   81 NRVSGESPGGLTILNLDGPLYLGGLPEDL---KLPPLPVTPGFRGCIRNLKVNGK 132
Laminin_G_1 pfam00054
Laminin G domain;
1502-1633 4.98e-42

Laminin G domain;


Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 150.55  E-value: 4.98e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487346303 1502 IKTEATQGLILWSGKGLDRsDYIALAIVDGRVQMTYDLGSKPVILRSTVPINTNQWIQIKASRVHRDGSLQVGNESPIMG 1581
Cdd:pfam00054    1 FRTTEPSGLLLYNGTQTER-DFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTG 79
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1487346303 1582 SSPLGATQ-LDTDGALWLGGLEKLSLaHKLPKSFLTGFVGCIRDVVVDRQELH 1633
Cdd:pfam00054   80 ESPLGATTdLDVDGPLYVGGLPSLGV-KKRRLAISPSFDGCIRDVIVNGKPLD 131
Laminin_G_1 pfam00054
Laminin G domain;
1255-1386 7.73e-39

Laminin G domain;


Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 141.30  E-value: 7.73e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487346303 1255 FLSRNPNGLIFYNGQKTDGkgDFISLALHNGYLEYRYDLGKGAAVIKSRDPVPLNTWVSVSLERNARKGIMRINNGERTL 1334
Cdd:pfam00054    1 FRTTEPSGLLLYNGTQTER--DFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPT 78
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1487346303 1335 GESPL-PHTSLNLKEPLYVGGAPDFSQLARAAAASASFDGAIQKISIKGTPIL 1386
Cdd:pfam00054   79 GESPLgATTDLDVDGPLYVGGLPSLGVKKRRLAISPSFDGCIRDVIVNGKPLD 131
LamG smart00282
Laminin G domain;
1497-1630 3.93e-34

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 127.84  E-value: 3.93e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487346303  1497 YFELSIKTEATQGLILWSGkGLDRSDYIALAIVDGRVQMTYDLGSKPVILRST-VPINTNQWIQIKASRVHRDGSLQVGN 1575
Cdd:smart00282    1 SISFSFRTTSPNGLLLYAG-SKGGGDYLALELRDGRLVLRYDLGSGPARLTSDpTPLNDGQWHRVAVERNGRSVTLSVDG 79
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 1487346303  1576 ESPIMGSSPLGATQLDTDGALWLGGLEKLSLAHKLPKSflTGFVGCIRDVVVDRQ 1630
Cdd:smart00282   80 GNRVSGESPGGLTILNLDGPLYLGGLPEDLKLPPLPVT--PGFRGCIRNLKVNGK 132
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
1484-1628 4.07e-34

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: 128.69  E-value: 4.07e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487346303 1484 YHLDLSEKALQSNYFELSIKTEATQGLILWSGkGLDRSDYIALAIVDGRVQMTYDLGSKPVILRSTVPINTNQWIQIKAS 1563
Cdd:cd00110     10 VRLPTLPAPRTRLSISFSFRTTSPNGLLLYAG-SQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDGQWHSVSVE 88
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1487346303 1564 RVHRDGSLQVGNESPIMGSSPLGATQLDTDGALWLGGLEKLSLAHKLPKSflTGFVGCIRDVVVD 1628
Cdd:cd00110     89 RNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVS--PGFVGCIRDLKVN 151
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
1227-1380 2.76e-31

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: 120.60  E-value: 2.76e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487346303 1227 FNGFSYLELNGLQTFVPElqdkMTMEVAFLSRNPNGLIFYNGQKTdgKGDFISLALHNGYLEYRYDLGKGAAVIKSRDPV 1306
Cdd:cd00110      4 FSGSSYVRLPTLPAPRTR----LSISFSFRTTSPNGLLLYAGSQN--GGDFLALELEDGRLVLRYDLGSGSLVLSSKTPL 77
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1487346303 1307 PLNTWVSVSLERNARKGIMRINNGERTLGESPLPHTSLNLKEPLYVGGAPDfSQLARAAAASASFDGAIQKISI 1380
Cdd:cd00110     78 NDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPE-DLKSPGLPVSPGFVGCIRDLKV 150
LamG smart00282
Laminin G domain;
1250-1382 1.07e-30

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 118.21  E-value: 1.07e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487346303  1250 TMEVAFLSRNPNGLIFYNGQKtdGKGDFISLALHNGYLEYRYDLGKGAAVIKSrDPVPLN--TWVSVSLERNARKGIMRI 1327
Cdd:smart00282    1 SISFSFRTTSPNGLLLYAGSK--GGGDYLALELRDGRLVLRYDLGSGPARLTS-DPTPLNdgQWHRVAVERNGRSVTLSV 77
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 1487346303  1328 NNGERTLGESPLPHTSLNLKEPLYVGGAPDfSQLARAAAASASFDGAIQKISIKG 1382
Cdd:smart00282   78 DGGNRVSGESPGGLTILNLDGPLYLGGLPE-DLKLPPLPVTPGFRGCIRNLKVNG 131
SEA smart00200
Domain found in sea urchin sperm protein, enterokinase, agrin; Proposed function of regulating ...
719-844 4.56e-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: 4.56e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487346303   719 ATKVFQGVLILEEVEGQELFYTPEMADPKSELFGETARSIESVLDELFRNSEVKRDFRSVQVRHLGQSSAVRVIVETHFD 798
Cdd:smart00200    1 PTQSFGVSLSVLSVEGENLQYSPSLEDPSSEEYQELVRDVEKLLEQIYGKTDLKPDFVGTEVIEFRNGSVVVDLGLLFNE 80
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*.
gi 1487346303   799 PATsyTAADIQRALLKQIKASKKKTilvKRPQQENIKFMDFDWIPQ 844
Cdd:smart00200   81 GVT--NGQDVEEDLLQVIKQAAYSL---KITNVNVVDVLDPDSADS 121
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
330-375 1.21e-13

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


Pssm-ID: 197624  Cd Length: 46  Bit Score: 66.55  E-value: 1.21e-13
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 1487346303   330 ECQQVCQSVYDPVCGSDNLTYSNPCELDAMACALRKEIRMKHKGPC 375
Cdd:smart00280    1 DCPEACPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
SEA pfam01390
SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed ...
737-821 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 1487346303  737 LFYTPEMADPKSELFGETARSIESVLDELFRNSEVKRDFRSVQVRHLGQSS-AVRVIVETHFDPATSYTAADIQR---AL 812
Cdd:pfam01390   12 LQYTPDLGNPSSQEFKSLSRRIESLLNELFRNSSLRKQYIKSHVLRLRPDGgSVVVDVVLVFRFPSTEPALDREKlieEI 91

                   ....*....
gi 1487346303  813 LKQIKASKK 821
Cdd:pfam01390   92 LRQTLNNTT 100
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
36-82 3.80e-12

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


Pssm-ID: 197624  Cd Length: 46  Bit Score: 62.31  E-value: 3.80e-12
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 1487346303    36 VCKKAtCPSVVAPVCGSDYSTYSNECELEKAQCNQQRRIKVMSKGAC 82
Cdd:smart00280    1 DCPEA-CPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
335-375 4.27e-12

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: 61.90  E-value: 4.27e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1487346303  335 CQSVYDPVCGSDNLTYSNPCELDAMACALRKEIRMKHKGPC 375
Cdd:cd00104      1 CPKEYDPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
42-82 3.53e-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: 59.21  E-value: 3.53e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1487346303   42 CPSVVAPVCGSDYSTYSNECELEKAQCNQQRRIKVMSKGAC 82
Cdd:cd00104      1 CPKEYDPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
501-548 1.46e-10

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


Pssm-ID: 197624  Cd Length: 46  Bit Score: 57.69  E-value: 1.46e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1487346303   501 ECPSLlCTEaDASKVCGSDGVTYGDQCQLRTIACRQGKAIEVKHLGQC 548
Cdd:smart00280    1 DCPEA-CPR-EYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
124-157 1.47e-10

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


Pssm-ID: 197624  Cd Length: 46  Bit Score: 57.69  E-value: 1.47e-10
                            10        20        30
                    ....*....|....*....|....*....|....
gi 1487346303   124 VCGSDGKDYRSECHLNRHACDKQENIFKKFDGPC 157
Cdd:smart00280   13 VCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
426-462 9.84e-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: 55.44  E-value: 9.84e-10
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1487346303  426 CHCDPVGSVRDDCEQMTGLCSCKPGITGTKCKQCPSG 462
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPG 37
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
124-157 4.92e-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: 53.43  E-value: 4.92e-09
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1487346303  124 VCGSDGKDYRSECHLNRHACDKQENIFKKFDGPC 157
Cdd:cd00104      8 VCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
186-229 7.97e-09

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


Pssm-ID: 197624  Cd Length: 46  Bit Score: 52.68  E-value: 7.97e-09
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 1487346303   186 PESCPLKKEPVCGDDGVTYENECVLHRTGAIRGIEIQKLRSGQC 229
Cdd:smart00280    3 PEACPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
260-301 1.74e-08

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


Pssm-ID: 197624  Cd Length: 46  Bit Score: 51.91  E-value: 1.74e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|..
gi 1487346303   260 ICDGAYQPLCGRDSRTYFNDCERQKAECQQKAAIPVKHHGPC 301
Cdd:smart00280    5 ACPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
507-548 4.73e-08

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: 50.35  E-value: 4.73e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1487346303  507 CTEaDASKVCGSDGVTYGDQCQLRTIACRQGKAIEVKHLGQC 548
Cdd:cd00104      1 CPK-EYDPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
261-301 5.37e-08

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: 50.35  E-value: 5.37e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1487346303  261 CDGAYQPLCGRDSRTYFNDCERQKAECQQKAAIPVKHHGPC 301
Cdd:cd00104      1 CPKEYDPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
425-462 6.86e-08

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: 50.43  E-value: 6.86e-08
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1487346303  425 SCHCDPVGSVRDDCEQMTGLCSCKPGITGTKCKQCPSG 462
Cdd:cd00055      1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPG 38
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
189-229 9.02e-08

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: 49.58  E-value: 9.02e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1487346303  189 CPLKKEPVCGDDGVTYENECVLHRTGAIRGIEIQKLRSGQC 229
Cdd:cd00104      1 CPKEYDPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
426-462 1.14e-07

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 49.62  E-value: 1.14e-07
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 1487346303   426 CHCDPVGSVRDDCEQMTGLCSCKPGITGTKCKQCPSG 462
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPG 37
Kazal_1 pfam00050
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
189-229 2.88e-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. Alignment also includes a single domain from transporters in the OATP/PGT family.


Pssm-ID: 395004  Cd Length: 49  Bit Score: 48.44  E-value: 2.88e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1487346303  189 CPLKKEPVCGDDGVTYENECVLHRTGAIRGIEIQKLRSGQC 229
Cdd:pfam00050    9 CPRIYDPVCGTDGKTYSNECLFCAENGKRGTNLHKVHDGEC 49
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
330-375 4.93e-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: 4.93e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1487346303  330 ECQQVCQ-SVYDPVCGSDNLTYSNPCELDAMACALRKEIRM---KHKGPC 375
Cdd:pfam07648    1 NCNCQCPkTEYEPVCGSDGVTYPSPCALCAAGCKLGKEVKEekvKYDGSC 50
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
1409-1439 1.36e-06

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: 46.48  E-value: 1.36e-06
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1487346303 1409 PSPCQNSGTCQPRLESYECTCPRGFFGTHCE 1439
Cdd:cd00054      8 GNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
41-82 2.63e-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.


Pssm-ID: 400135  Cd Length: 50  Bit Score: 42.87  E-value: 2.63e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1487346303   41 TCPSVV-APVCGSDYSTYSNECELEKAQCNQQRRIK---VMSKGAC 82
Cdd:pfam07648    5 QCPKTEyEPVCGSDGVTYPSPCALCAAGCKLGKEVKeekVKYDGSC 50
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
922-950 3.55e-05

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: 41.98  E-value: 3.55e-05
                           10        20
                   ....*....|....*....|....*....
gi 1487346303  922 CDSHPCLHGGTCEDDGRDFTCSCPAGKGG 950
Cdd:pfam00008    1 CAPNPCSNGGTCVDTPGGYTCICPEGYTG 29
EGF_CA smart00179
Calcium-binding EGF-like domain;
1409-1439 4.32e-05

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 42.23  E-value: 4.32e-05
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1487346303  1409 PSPCQNSGTCQPRLESYECTCPRGF-FGTHCE 1439
Cdd:smart00179    8 GNPCQNGGTCVNTVGSYRCECPPGYtDGRNCE 39
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
499-548 5.88e-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.


Pssm-ID: 400135  Cd Length: 50  Bit Score: 42.09  E-value: 5.88e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1487346303  499 QCECpslLCTEADASKVCGSDGVTYGDQCQLRTIACRQG---KAIEVKHLGQC 548
Cdd:pfam07648    1 NCNC---QCPKTEYEPVCGSDGVTYPSPCALCAAGCKLGkevKEEKVKYDGSC 50
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
1140-1171 6.91e-05

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: 41.21  E-value: 6.91e-05
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1487346303 1140 CQPNPCHHGGLCHTMEaEMFHCECLNGYTGPT 1171
Cdd:pfam00008    1 CAPNPCSNGGTCVDTP-GGYTCICPEGYTGKR 31
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
112-157 1.72e-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: 40.94  E-value: 1.72e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1487346303  112 CMSFCGGLPENTVCGSDGKDYRSECHLNRHACDKQENIFK---KFDGPC 157
Cdd:pfam07648    2 CNCQCPKTEYEPVCGSDGVTYPSPCALCAAGCKLGKEVKEekvKYDGSC 50
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
922-954 6.79e-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: 38.77  E-value: 6.79e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1487346303  922 CDS-HPCLHGGTCEDDGRDFTCSCPAGKGGAVCE 954
Cdd:cd00054      5 CASgNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
1138-1172 2.28e-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: 37.23  E-value: 2.28e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1487346303 1138 NPCQ-PNPCHHGGLCHtMEAEMFHCECLNGYTGPTC 1172
Cdd:cd00054      3 DECAsGNPCQNGGTCV-NTVGSYRCSCPPGYTGRNC 37
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
258-301 5.66e-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.


Pssm-ID: 400135  Cd Length: 50  Bit Score: 36.32  E-value: 5.66e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1487346303  258 RIICDGA-YQPLCGRDSRTYFNDCERQKAEC---QQKAAIPVKHHGPC 301
Cdd:pfam07648    3 NCQCPKTeYEPVCGSDGVTYPSPCALCAAGCklgKEVKEEKVKYDGSC 50
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
1408-1435 6.29e-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: 6.29e-03
                           10        20
                   ....*....|....*....|....*...
gi 1487346303 1408 KPSPCQNSGTCQPRLESYECTCPRGFFG 1435
Cdd:pfam00008    2 APNPCSNGGTCVDTPGGYTCICPEGYTG 29
EGF_CA smart00179
Calcium-binding EGF-like domain;
922-954 7.78e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 35.69  E-value: 7.78e-03
                            10        20        30
                    ....*....|....*....|....*....|....*
gi 1487346303   922 CDS-HPCLHGGTCEDDGRDFTCSCPAG-KGGAVCE 954
Cdd:smart00179    5 CASgNPCQNGGTCVNTVGSYRCECPPGyTDGRNCE 39
 
Name Accession Description Interval E-value
Laminin_G_1 pfam00054
Laminin G domain;
987-1118 4.73e-47

Laminin G domain;


Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 164.80  E-value: 4.73e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487346303  987 FRASELSGLLLYNGQNRGKDFVSLALVNGFVELRFNTGSGTGVITSKVPIEPGQWHALVVNRNRRNGVLSVDGEPHMHGE 1066
Cdd:pfam00054    1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGE 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1487346303 1067 SPSGTDG-LNLDTDLFVGGAPEDQidVVAERTSVTAGLKGCIRLLDVNNQMYD 1118
Cdd:pfam00054   81 SPLGATTdLDVDGPLYVGGLPSLG--VKKRRLAISPSFDGCIRDVIVNGKPLD 131
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
963-1113 6.16e-47

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: 165.28  E-value: 6.16e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487346303  963 SFGGKSYLAFKMMKA-YHTVRIAMEFRASELSGLLLYNGQNRGKDFVSLALVNGFVELRFNTGSGTGVITSKVPIEPGQW 1041
Cdd:cd00110      3 SFSGSSYVRLPTLPApRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDGQW 82
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1487346303 1042 HALVVNRNRRNGVLSVDGEPHMHGESPSGTDGLNLDTDLFVGGAPEDQidvVAERTSVTAGLKGCIRLLDVN 1113
Cdd:cd00110     83 HSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDL---KSPGLPVSPGFVGCIRDLKVN 151
LamG smart00282
Laminin G domain;
982-1115 1.63e-42

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 152.11  E-value: 1.63e-42
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487346303   982 RIAMEFRASELSGLLLYNGQNRGKDFVSLALVNGFVELRFNTGSGTGVITSK-VPIEPGQWHALVVNRNRRNGVLSVDGE 1060
Cdd:smart00282    1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDpTPLNDGQWHRVAVERNGRSVTLSVDGG 80
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 1487346303  1061 PHMHGESPSGTDGLNLDTDLFVGGAPEDQidvVAERTSVTAGLKGCIRLLDVNNQ 1115
Cdd:smart00282   81 NRVSGESPGGLTILNLDGPLYLGGLPEDL---KLPPLPVTPGFRGCIRNLKVNGK 132
Laminin_G_1 pfam00054
Laminin G domain;
1502-1633 4.98e-42

Laminin G domain;


Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 150.55  E-value: 4.98e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487346303 1502 IKTEATQGLILWSGKGLDRsDYIALAIVDGRVQMTYDLGSKPVILRSTVPINTNQWIQIKASRVHRDGSLQVGNESPIMG 1581
Cdd:pfam00054    1 FRTTEPSGLLLYNGTQTER-DFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTG 79
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1487346303 1582 SSPLGATQ-LDTDGALWLGGLEKLSLaHKLPKSFLTGFVGCIRDVVVDRQELH 1633
Cdd:pfam00054   80 ESPLGATTdLDVDGPLYVGGLPSLGV-KKRRLAISPSFDGCIRDVIVNGKPLD 131
Laminin_G_1 pfam00054
Laminin G domain;
1255-1386 7.73e-39

Laminin G domain;


Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 141.30  E-value: 7.73e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487346303 1255 FLSRNPNGLIFYNGQKTDGkgDFISLALHNGYLEYRYDLGKGAAVIKSRDPVPLNTWVSVSLERNARKGIMRINNGERTL 1334
Cdd:pfam00054    1 FRTTEPSGLLLYNGTQTER--DFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPT 78
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1487346303 1335 GESPL-PHTSLNLKEPLYVGGAPDFSQLARAAAASASFDGAIQKISIKGTPIL 1386
Cdd:pfam00054   79 GESPLgATTDLDVDGPLYVGGLPSLGVKKRRLAISPSFDGCIRDVIVNGKPLD 131
LamG smart00282
Laminin G domain;
1497-1630 3.93e-34

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 127.84  E-value: 3.93e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487346303  1497 YFELSIKTEATQGLILWSGkGLDRSDYIALAIVDGRVQMTYDLGSKPVILRST-VPINTNQWIQIKASRVHRDGSLQVGN 1575
Cdd:smart00282    1 SISFSFRTTSPNGLLLYAG-SKGGGDYLALELRDGRLVLRYDLGSGPARLTSDpTPLNDGQWHRVAVERNGRSVTLSVDG 79
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 1487346303  1576 ESPIMGSSPLGATQLDTDGALWLGGLEKLSLAHKLPKSflTGFVGCIRDVVVDRQ 1630
Cdd:smart00282   80 GNRVSGESPGGLTILNLDGPLYLGGLPEDLKLPPLPVT--PGFRGCIRNLKVNGK 132
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
1484-1628 4.07e-34

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: 128.69  E-value: 4.07e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487346303 1484 YHLDLSEKALQSNYFELSIKTEATQGLILWSGkGLDRSDYIALAIVDGRVQMTYDLGSKPVILRSTVPINTNQWIQIKAS 1563
Cdd:cd00110     10 VRLPTLPAPRTRLSISFSFRTTSPNGLLLYAG-SQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDGQWHSVSVE 88
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1487346303 1564 RVHRDGSLQVGNESPIMGSSPLGATQLDTDGALWLGGLEKLSLAHKLPKSflTGFVGCIRDVVVD 1628
Cdd:cd00110     89 RNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVS--PGFVGCIRDLKVN 151
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
1227-1380 2.76e-31

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: 120.60  E-value: 2.76e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487346303 1227 FNGFSYLELNGLQTFVPElqdkMTMEVAFLSRNPNGLIFYNGQKTdgKGDFISLALHNGYLEYRYDLGKGAAVIKSRDPV 1306
Cdd:cd00110      4 FSGSSYVRLPTLPAPRTR----LSISFSFRTTSPNGLLLYAGSQN--GGDFLALELEDGRLVLRYDLGSGSLVLSSKTPL 77
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1487346303 1307 PLNTWVSVSLERNARKGIMRINNGERTLGESPLPHTSLNLKEPLYVGGAPDfSQLARAAAASASFDGAIQKISI 1380
Cdd:cd00110     78 NDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPE-DLKSPGLPVSPGFVGCIRDLKV 150
LamG smart00282
Laminin G domain;
1250-1382 1.07e-30

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 118.21  E-value: 1.07e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487346303  1250 TMEVAFLSRNPNGLIFYNGQKtdGKGDFISLALHNGYLEYRYDLGKGAAVIKSrDPVPLN--TWVSVSLERNARKGIMRI 1327
Cdd:smart00282    1 SISFSFRTTSPNGLLLYAGSK--GGGDYLALELRDGRLVLRYDLGSGPARLTS-DPTPLNdgQWHRVAVERNGRSVTLSV 77
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 1487346303  1328 NNGERTLGESPLPHTSLNLKEPLYVGGAPDfSQLARAAAASASFDGAIQKISIKG 1382
Cdd:smart00282   78 DGGNRVSGESPGGLTILNLDGPLYLGGLPE-DLKLPPLPVTPGFRGCIRNLKVNG 131
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
987-1115 2.38e-30

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: 117.14  E-value: 2.38e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487346303  987 FRASELSGLLLYNGqNRGKDFVSLALVNGFVELRFNTGSGTGVITS-KVPIEPGQWHALVVNRNRRNGVLSVDGEPHMHG 1065
Cdd:pfam02210    1 FRTRQPNGLLLYAG-GGGSDFLALELVNGRLVLRYDLGSGPESLLSsGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSS 79
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1487346303 1066 ESPSGTDGLNLDTDLFVGGAPEDQIDVVaerTSVTAGLKGCIRLLDVNNQ 1115
Cdd:pfam02210   80 LPPGESLLLNLNGPLYLGGLPPLLLLPA---LPVRAGFVGCIRDVRVNGE 126
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
1502-1630 5.35e-26

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: 104.42  E-value: 5.35e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487346303 1502 IKTEATQGLILWSGKGldRSDYIALAIVDGRVQMTYDLGSKPVILRST-VPINTNQWIQIKASRVHRDGSLQVGNESPIM 1580
Cdd:pfam02210    1 FRTRQPNGLLLYAGGG--GSDFLALELVNGRLVLRYDLGSGPESLLSSgKNLNDGQWHSVRVERNGNTLTLSVDGQTVVS 78
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1487346303 1581 GSSPLGATQLDTDGALWLGGLEKLSLAHKLPKSflTGFVGCIRDVVVDRQ 1630
Cdd:pfam02210   79 SLPPGESLLLNLNGPLYLGGLPPLLLLPALPVR--AGFVGCIRDVRVNGE 126
SEA smart00200
Domain found in sea urchin sperm protein, enterokinase, agrin; Proposed function of regulating ...
719-844 4.56e-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: 4.56e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487346303   719 ATKVFQGVLILEEVEGQELFYTPEMADPKSELFGETARSIESVLDELFRNSEVKRDFRSVQVRHLGQSSAVRVIVETHFD 798
Cdd:smart00200    1 PTQSFGVSLSVLSVEGENLQYSPSLEDPSSEEYQELVRDVEKLLEQIYGKTDLKPDFVGTEVIEFRNGSVVVDLGLLFNE 80
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*.
gi 1487346303   799 PATsyTAADIQRALLKQIKASKKKTilvKRPQQENIKFMDFDWIPQ 844
Cdd:smart00200   81 GVT--NGQDVEEDLLQVIKQAAYSL---KITNVNVVDVLDPDSADS 121
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
1255-1383 1.46e-20

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


Pssm-ID: 460494 [Multi-domain]  Cd Length: 126  Bit Score: 89.02  E-value: 1.46e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487346303 1255 FLSRNPNGLIFYNGqktDGKGDFISLALHNGYLEYRYDLGKGAAVIKSRdPVPLN--TWVSVSLERNARKGIMRINNGER 1332
Cdd:pfam02210    1 FRTRQPNGLLLYAG---GGGSDFLALELVNGRLVLRYDLGSGPESLLSS-GKNLNdgQWHSVRVERNGNTLTLSVDGQTV 76
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1487346303 1333 TLGESPLPHTSLNLKEPLYVGGAPDFSqLARAAAASASFDGAIQKISIKGT 1383
Cdd:pfam02210   77 VSSLPPGESLLLNLNGPLYLGGLPPLL-LLPALPVRAGFVGCIRDVRVNGE 126
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
330-375 1.21e-13

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


Pssm-ID: 197624  Cd Length: 46  Bit Score: 66.55  E-value: 1.21e-13
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 1487346303   330 ECQQVCQSVYDPVCGSDNLTYSNPCELDAMACALRKEIRMKHKGPC 375
Cdd:smart00280    1 DCPEACPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
SEA pfam01390
SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed ...
737-821 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 1487346303  737 LFYTPEMADPKSELFGETARSIESVLDELFRNSEVKRDFRSVQVRHLGQSS-AVRVIVETHFDPATSYTAADIQR---AL 812
Cdd:pfam01390   12 LQYTPDLGNPSSQEFKSLSRRIESLLNELFRNSSLRKQYIKSHVLRLRPDGgSVVVDVVLVFRFPSTEPALDREKlieEI 91

                   ....*....
gi 1487346303  813 LKQIKASKK 821
Cdd:pfam01390   92 LRQTLNNTT 100
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
36-82 3.80e-12

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


Pssm-ID: 197624  Cd Length: 46  Bit Score: 62.31  E-value: 3.80e-12
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 1487346303    36 VCKKAtCPSVVAPVCGSDYSTYSNECELEKAQCNQQRRIKVMSKGAC 82
Cdd:smart00280    1 DCPEA-CPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
335-375 4.27e-12

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: 61.90  E-value: 4.27e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1487346303  335 CQSVYDPVCGSDNLTYSNPCELDAMACALRKEIRMKHKGPC 375
Cdd:cd00104      1 CPKEYDPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
42-82 3.53e-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: 59.21  E-value: 3.53e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1487346303   42 CPSVVAPVCGSDYSTYSNECELEKAQCNQQRRIKVMSKGAC 82
Cdd:cd00104      1 CPKEYDPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
501-548 1.46e-10

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


Pssm-ID: 197624  Cd Length: 46  Bit Score: 57.69  E-value: 1.46e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1487346303   501 ECPSLlCTEaDASKVCGSDGVTYGDQCQLRTIACRQGKAIEVKHLGQC 548
Cdd:smart00280    1 DCPEA-CPR-EYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
124-157 1.47e-10

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


Pssm-ID: 197624  Cd Length: 46  Bit Score: 57.69  E-value: 1.47e-10
                            10        20        30
                    ....*....|....*....|....*....|....
gi 1487346303   124 VCGSDGKDYRSECHLNRHACDKQENIFKKFDGPC 157
Cdd:smart00280   13 VCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
426-462 9.84e-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: 55.44  E-value: 9.84e-10
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1487346303  426 CHCDPVGSVRDDCEQMTGLCSCKPGITGTKCKQCPSG 462
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPG 37
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
124-157 4.92e-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: 53.43  E-value: 4.92e-09
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1487346303  124 VCGSDGKDYRSECHLNRHACDKQENIFKKFDGPC 157
Cdd:cd00104      8 VCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
186-229 7.97e-09

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


Pssm-ID: 197624  Cd Length: 46  Bit Score: 52.68  E-value: 7.97e-09
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 1487346303   186 PESCPLKKEPVCGDDGVTYENECVLHRTGAIRGIEIQKLRSGQC 229
Cdd:smart00280    3 PEACPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
260-301 1.74e-08

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


Pssm-ID: 197624  Cd Length: 46  Bit Score: 51.91  E-value: 1.74e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|..
gi 1487346303   260 ICDGAYQPLCGRDSRTYFNDCERQKAECQQKAAIPVKHHGPC 301
Cdd:smart00280    5 ACPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
507-548 4.73e-08

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: 50.35  E-value: 4.73e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1487346303  507 CTEaDASKVCGSDGVTYGDQCQLRTIACRQGKAIEVKHLGQC 548
Cdd:cd00104      1 CPK-EYDPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
261-301 5.37e-08

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: 50.35  E-value: 5.37e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1487346303  261 CDGAYQPLCGRDSRTYFNDCERQKAECQQKAAIPVKHHGPC 301
Cdd:cd00104      1 CPKEYDPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
425-462 6.86e-08

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: 50.43  E-value: 6.86e-08
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1487346303  425 SCHCDPVGSVRDDCEQMTGLCSCKPGITGTKCKQCPSG 462
Cdd:cd00055      1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPG 38
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
189-229 9.02e-08

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: 49.58  E-value: 9.02e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1487346303  189 CPLKKEPVCGDDGVTYENECVLHRTGAIRGIEIQKLRSGQC 229
Cdd:cd00104      1 CPKEYDPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
426-462 1.14e-07

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 49.62  E-value: 1.14e-07
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 1487346303   426 CHCDPVGSVRDDCEQMTGLCSCKPGITGTKCKQCPSG 462
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPG 37
KAZAL_PSTI cd01327
Kazal-type pancreatic secretory trypsin inhibitors (PSTI) and related proteins, including the ...
189-229 1.82e-07

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: 48.82  E-value: 1.82e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1487346303  189 CPLKKEPVCGDDGVTYENECVLHRTGAIRGIEIQKLRSGQC 229
Cdd:cd01327      5 CPKDYDPVCGTDGVTYSNECLLCAENLKRQTNIRIKHDGEC 45
Kazal_1 pfam00050
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
189-229 2.88e-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. Alignment also includes a single domain from transporters in the OATP/PGT family.


Pssm-ID: 395004  Cd Length: 49  Bit Score: 48.44  E-value: 2.88e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1487346303  189 CPLKKEPVCGDDGVTYENECVLHRTGAIRGIEIQKLRSGQC 229
Cdd:pfam00050    9 CPRIYDPVCGTDGKTYSNECLFCAENGKRGTNLHKVHDGEC 49
KAZAL_PSTI cd01327
Kazal-type pancreatic secretory trypsin inhibitors (PSTI) and related proteins, including the ...
332-375 3.51e-07

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: 48.05  E-value: 3.51e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1487346303  332 QQVCQSVYDPVCGSDNLTYSNPCELdamaCALRKE----IRMKHKGPC 375
Cdd:cd01327      2 VFGCPKDYDPVCGTDGVTYSNECLL----CAENLKrqtnIRIKHDGEC 45
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
330-375 4.93e-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: 4.93e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1487346303  330 ECQQVCQ-SVYDPVCGSDNLTYSNPCELDAMACALRKEIRM---KHKGPC 375
Cdd:pfam07648    1 NCNCQCPkTEYEPVCGSDGVTYPSPCALCAAGCKLGKEVKEekvKYDGSC 50
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
1409-1439 1.36e-06

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: 46.48  E-value: 1.36e-06
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1487346303 1409 PSPCQNSGTCQPRLESYECTCPRGFFGTHCE 1439
Cdd:cd00054      8 GNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
KAZAL_PSTI cd01327
Kazal-type pancreatic secretory trypsin inhibitors (PSTI) and related proteins, including the ...
42-82 1.00e-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: 44.20  E-value: 1.00e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1487346303   42 CPSVVAPVCGSDYSTYSNECELEKAQCNQQRRIKVMSKGAC 82
Cdd:cd01327      5 CPKDYDPVCGTDGVTYSNECLLCAENLKRQTNIRIKHDGEC 45
FSL_SPARC cd01328
Follistatin-like SPARC (secreted protein, acidic, and rich in cysteines) domain; SPARC/BM-40 ...
308-363 1.57e-05

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: 44.78  E-value: 1.57e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487346303  308 PCLSVECQFGATCVV-KNQEAICECQQVCQSVYDP---VCGSDNLTYSNPCELDAMACAL 363
Cdd:cd01328      1 PCENHHCGAGKVCEVdDENTPKCVCIDPCPEEVDDrrkVCTNDNETFDSDCELYRTRCLC 60
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
41-82 2.63e-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.


Pssm-ID: 400135  Cd Length: 50  Bit Score: 42.87  E-value: 2.63e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1487346303   41 TCPSVV-APVCGSDYSTYSNECELEKAQCNQQRRIK---VMSKGAC 82
Cdd:pfam07648    5 QCPKTEyEPVCGSDGVTYPSPCALCAAGCKLGKEVKeekVKYDGSC 50
Kazal_1 pfam00050
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
334-375 3.26e-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: 42.66  E-value: 3.26e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1487346303  334 VCQSVYDPVCGSDNLTYSNPCELdamaCALRKE----IRMKHKGPC 375
Cdd:pfam00050    8 ACPRIYDPVCGTDGKTYSNECLF----CAENGKrgtnLHKVHDGEC 49
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
922-950 3.55e-05

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: 41.98  E-value: 3.55e-05
                           10        20
                   ....*....|....*....|....*....
gi 1487346303  922 CDSHPCLHGGTCEDDGRDFTCSCPAGKGG 950
Cdd:pfam00008    1 CAPNPCSNGGTCVDTPGGYTCICPEGYTG 29
EGF_CA smart00179
Calcium-binding EGF-like domain;
1409-1439 4.32e-05

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 42.23  E-value: 4.32e-05
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1487346303  1409 PSPCQNSGTCQPRLESYECTCPRGF-FGTHCE 1439
Cdd:smart00179    8 GNPCQNGGTCVNTVGSYRCECPPGYtDGRNCE 39
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
499-548 5.88e-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.


Pssm-ID: 400135  Cd Length: 50  Bit Score: 42.09  E-value: 5.88e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1487346303  499 QCECpslLCTEADASKVCGSDGVTYGDQCQLRTIACRQG---KAIEVKHLGQC 548
Cdd:pfam07648    1 NCNC---QCPKTEYEPVCGSDGVTYPSPCALCAAGCKLGkevKEEKVKYDGSC 50
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
1140-1171 6.91e-05

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: 41.21  E-value: 6.91e-05
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1487346303 1140 CQPNPCHHGGLCHTMEaEMFHCECLNGYTGPT 1171
Cdd:pfam00008    1 CAPNPCSNGGTCVDTP-GGYTCICPEGYTGKR 31
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
112-157 1.72e-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: 40.94  E-value: 1.72e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1487346303  112 CMSFCGGLPENTVCGSDGKDYRSECHLNRHACDKQENIFK---KFDGPC 157
Cdd:pfam07648    2 CNCQCPKTEYEPVCGSDGVTYPSPCALCAAGCKLGKEVKEekvKYDGSC 50
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
1407-1439 1.83e-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: 40.15  E-value: 1.83e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1487346303 1407 QKPSPCQNSGTCQPRLESYECTCPRGFFG-THCE 1439
Cdd:cd00053      3 AASNPCSNGGTCVNTPGSYRCVCPPGYTGdRSCE 36
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
186-225 5.32e-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: 39.40  E-value: 5.32e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1487346303  186 PESCP-LKKEPVCGDDGVTYENECVLHRTGAIRGIEIQKLR 225
Cdd:pfam07648    3 NCQCPkTEYEPVCGSDGVTYPSPCALCAAGCKLGKEVKEEK 43
KAZAL_PSTI cd01327
Kazal-type pancreatic secretory trypsin inhibitors (PSTI) and related proteins, including the ...
124-157 5.49e-04

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: 39.19  E-value: 5.49e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1487346303  124 VCGSDGKDYRSECHLNRHACDKQENIFKKFDGPC 157
Cdd:cd01327     12 VCGTDGVTYSNECLLCAENLKRQTNIRIKHDGEC 45
Kazal_1 pfam00050
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
38-82 6.05e-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. Alignment also includes a single domain from transporters in the OATP/PGT family.


Pssm-ID: 395004  Cd Length: 49  Bit Score: 39.19  E-value: 6.05e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1487346303   38 KKATCPSVVAPVCGSDYSTYSNECELEKAQCNQQRRIKVMSKGAC 82
Cdd:pfam00050    5 PSGACPRIYDPVCGTDGKTYSNECLFCAENGKRGTNLHKVHDGEC 49
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
922-954 6.79e-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: 38.77  E-value: 6.79e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1487346303  922 CDS-HPCLHGGTCEDDGRDFTCSCPAGKGGAVCE 954
Cdd:cd00054      5 CASgNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
Kazal_1 pfam00050
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
122-157 1.29e-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: 38.03  E-value: 1.29e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1487346303  122 NTVCGSDGKDYRSECHLNRHACDKQENIFKKFDGPC 157
Cdd:pfam00050   14 DPVCGTDGKTYSNECLFCAENGKRGTNLHKVHDGEC 49
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
1138-1172 2.28e-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: 37.23  E-value: 2.28e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1487346303 1138 NPCQ-PNPCHHGGLCHtMEAEMFHCECLNGYTGPTC 1172
Cdd:cd00054      3 DECAsGNPCQNGGTCV-NTVGSYRCSCPPGYTGRNC 37
MFS_SLCO_OATP cd17336
Solute carrier organic anion transporters of the Major Facilitator Superfamily of transporters; ...
329-354 3.18e-03

Solute carrier organic anion transporters of the Major Facilitator Superfamily of transporters; Solute carrier organic anion transporters (SLCOs) are also called organic anion transporting polypeptides (OATPs) or SLC21 (Solute carrier family 21) proteins. They are sodium-independent transporters that mediate the transport of a broad range of endo- as well as xenobiotics. Their substrates are mainly amphipathic organic anions with a molecular weight of more than 300Da, although there are a few known neutral or positively charged substrates. These include drugs including statins, angiotensin-converting enzyme inhibitors, angiotensin receptor blockers, antibiotics, antihistaminics, antihypertensives, and anticancer drugs. SLCOs/OATPs can be classified into 6 families (SLCO1-6 or OATP1-6) and each family may have subfamilies (e.g. OATP1A, OATP1B, OATP1C). Within the subfamilies, individual members are numbered according to the chronology of their identification and if there is already an ortholog known, they are given the same number. For example, the first SLCO identified, is rat OATP1A1 (encoded by the Slco1a1 gene). The second SLCO identified is the first human SLCO from the same subfamily and is called OATP1A2 (encoded by the SLCO1A2 gene). There are 11 human SLCOs/OATPs. SLCOs belong to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.


Pssm-ID: 340894 [Multi-domain]  Cd Length: 411  Bit Score: 41.84  E-value: 3.18e-03
                           10        20
                   ....*....|....*....|....*.
gi 1487346303  329 CECQQvcqSVYDPVCGSDNLTYSNPC 354
Cdd:cd17336    316 CNCSD---SSFSPVCGSDGITYFSPC 338
FSL_SPARC cd01328
Follistatin-like SPARC (secreted protein, acidic, and rich in cysteines) domain; SPARC/BM-40 ...
87-143 3.86e-03

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: 38.23  E-value: 3.86e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1487346303   87 PCAEVVCSFGSTCVRSTDGqSAKCICMSFCGGL--PENTVCGSDGKDYRSECHLNRHAC 143
Cdd:cd01328      1 PCENHHCGAGKVCEVDDEN-TPKCVCIDPCPEEvdDRRKVCTNDNETFDSDCELYRTRC 58
FSL_SPARC cd01328
Follistatin-like SPARC (secreted protein, acidic, and rich in cysteines) domain; SPARC/BM-40 ...
12-68 4.34e-03

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: 37.84  E-value: 4.34e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487346303   12 CRGMLCGFGAVCEKNpaDASQGVCVCKKaTCPSVVAP---VCGSDYSTYSNECELEKAQC 68
Cdd:cd01328      2 CENHHCGAGKVCEVD--DENTPKCVCID-PCPEEVDDrrkVCTNDNETFDSDCELYRTRC 58
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
923-954 5.30e-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: 36.30  E-value: 5.30e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1487346303  923 DSHPCLHGGTCEDDGRDFTCSCPAG-KGGAVCE 954
Cdd:cd00053      4 ASNPCSNGGTCVNTPGSYRCVCPPGyTGDRSCE 36
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
258-301 5.66e-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.


Pssm-ID: 400135  Cd Length: 50  Bit Score: 36.32  E-value: 5.66e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1487346303  258 RIICDGA-YQPLCGRDSRTYFNDCERQKAEC---QQKAAIPVKHHGPC 301
Cdd:pfam07648    3 NCQCPKTeYEPVCGSDGVTYPSPCALCAAGCklgKEVKEEKVKYDGSC 50
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
1408-1435 6.29e-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: 6.29e-03
                           10        20
                   ....*....|....*....|....*...
gi 1487346303 1408 KPSPCQNSGTCQPRLESYECTCPRGFFG 1435
Cdd:pfam00008    2 APNPCSNGGTCVDTPGGYTCICPEGYTG 29
Laminin_G_3 pfam13385
Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin ...
1019-1086 6.52e-03

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: 38.90  E-value: 6.52e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1487346303 1019 LRFNTGSGTG---VITSKVPIEPGQWHALVVNRNRRNGVLSVDGEPhMHGESPSGTDGLNLDTDLFVGGAP 1086
Cdd:pfam13385   56 LRFAVNGGNGgwdTVTSGASVPLGQWTHVAVTYDGGTLRLYVNGVL-VGSSTLTGGPPPGTGGPLYIGRSP 125
EGF_CA smart00179
Calcium-binding EGF-like domain;
922-954 7.78e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 35.69  E-value: 7.78e-03
                            10        20        30
                    ....*....|....*....|....*....|....*
gi 1487346303   922 CDS-HPCLHGGTCEDDGRDFTCSCPAG-KGGAVCE 954
Cdd:smart00179    5 CASgNPCQNGGTCVNTVGSYRCECPPGyTDGRNCE 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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