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Conserved domains on  [gi|568930475|ref|XP_006538558|]
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agrin isoform X7 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Laminin_G_1 pfam00054
Laminin G domain;
1282-1413 3.00e-51

Laminin G domain;


:

Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 177.12  E-value: 3.00e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930475  1282 FRALETEGLLLYNGNARGKDFLALALLDGHVQFRFDTGSGPAVLTSLVPVEPGRWHRLELSRHWRQGTLSVDGEAPVVGE 1361
Cdd:pfam00054    1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGE 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 568930475  1362 SPSGTDG-LNLDTKLYVGGLPEEqvATVLDRTSVGIGLKGCIRMLDINNQQLE 1413
Cdd:pfam00054   81 SPLGATTdLDVDGPLYVGGLPSL--GVKKRRLAISPSFDGCIRDVIVNGKPLD 131
Laminin_G_1 pfam00054
Laminin G domain;
1550-1685 5.54e-46

Laminin G domain;


:

Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 162.10  E-value: 5.54e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930475  1550 FLARGPSGLLLYNGQKTDGkgDFVSLALHNRHLEFRYDLGKGAAIIRSKEPIALGTWVRVFLERNGRKGALQVGDGPRVL 1629
Cdd:pfam00054    1 FRTTEPSGLLLYNGTQTER--DFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPT 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 568930475  1630 GESPKSRKvphTMLNLKEPLYVGGAPDFSKLARGAAVASGFDGAIQLVSLRGHQLL 1685
Cdd:pfam00054   79 GESPLGAT---TDLDVDGPLYVGGLPSLGVKKRRLAISPSFDGCIRDVIVNGKPLD 131
Laminin_G_1 pfam00054
Laminin G domain;
1784-1914 1.84e-45

Laminin G domain;


:

Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 160.56  E-value: 1.84e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930475  1784 RTEATQGLVLWIGKVGERaDYMALAIVDGHLQLSYDLGSQPVVLRSTVKVNTNRWLRVRAHREHREGSLQVGNEAPVTGS 1863
Cdd:pfam00054    2 RTTEPSGLLLYNGTQTER-DFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGE 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568930475  1864 SPLGATQ-LDTDGALWLGGLQKLPVgQALPKAYGTGFVGCLRDVVVGHRQLH 1914
Cdd:pfam00054   81 SPLGATTdLDVDGPLYVGGLPSLGV-KKRRLAISPSFDGCIRDVIVNGKPLD 131
SEA smart00200
Domain found in sea urchin sperm protein, enterokinase, agrin; Proposed function of regulating ...
 1014-1138 4.22e-31

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


:

Pssm-ID: 214554  Cd Length: 121  Bit Score: 119.05  E-value: 4.22e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930475   1014 ATKAFQGVLELEGVEGQELFYTPEMADPKSELFGETARSIESTLDDLFRNSDVKKDFWSIRLRELGPGKLVRAIVDVHFD 1093
Cdd:smart00200    1 PTQSFGVSLSVLSVEGENLQYSPSLEDPSSEEYQELVRDVEKLLEQIYGKTDLKPDFVGTEVIEFRNGSVVVDLGLLFNE 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*
gi 568930475   1094 PTTAfqAPDVGQALLQQIQVSRpWALAVRRPlrEHVRFLDFDWFP 1138
Cdd:smart00200   81 GVTN--GQDVEEDLLQVIKQAA-YSLKITNV--NVVDVLDPDSAD 120
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 688-730 5.14e-15

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


:

Pssm-ID: 395007  Cd Length: 49  Bit Score: 70.85  E-value: 5.14e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 568930475   688 CHCNPHGSYSGTCDPVTGQCSCRPGVGGLRCDRCEPGFWNFRG 730
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPS 43
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 384-429 8.97e-13

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


:

Pssm-ID: 197624  Cd Length: 46  Bit Score: 64.24  E-value: 8.97e-13
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 568930475    384 ECQRVCSGGYDPVCGSDGVTYGSVCELESMACTLGREIRVARRGPC 429
Cdd:smart00280    1 DCPEACPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 449-494 1.46e-12

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


:

Pssm-ID: 197624  Cd Length: 46  Bit Score: 63.47  E-value: 1.46e-12
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 568930475    449 VCPSECVESAQPVCGSDGHTYASECELHVHACTHQISLYVASAGHC 494
Cdd:smart00280    1 DCPEACPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 91-137 1.62e-11

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


:

Pssm-ID: 197624  Cd Length: 46  Bit Score: 60.77  E-value: 1.62e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 568930475     91 VCKKNvCPAMVAPVCGSDASTYSNECELQRAQCNQQRRIRLLRQGPC 137
Cdd:smart00280    1 DCPEA-CPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 599-645 2.15e-11

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


:

Pssm-ID: 197624  Cd Length: 46  Bit Score: 60.39  E-value: 2.15e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 568930475    599 VCDFSCQSVLKsPVCGSDGVTYSTECHLKKARCEARQELYVAAQGAC 645
Cdd:smart00280    1 DCPEACPREYD-PVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 167-212 2.29e-10

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


:

Pssm-ID: 197624  Cd Length: 46  Bit Score: 57.30  E-value: 2.29e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 568930475    167 CPTTCFGAPDgTVCGSDGVDYPSECQLLRHACANQEHIFKKFDGPC 212
Cdd:smart00280    2 CPEACPREYD-PVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 514-559 8.07e-10

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


:

Pssm-ID: 197624  Cd Length: 46  Bit Score: 55.76  E-value: 8.07e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 568930475    514 VCPRCEHPPPGPVCGSDGVTYLSACELREAACQQQVQIEEARAGPC 559
Cdd:smart00280    1 DCPEACPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 817-864 1.07e-09

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


:

Pssm-ID: 197624  Cd Length: 46  Bit Score: 55.38  E-value: 1.07e-09
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 568930475    817 VCPTlTCPEaNSTKVCGSDGVTYGNECQLKTIACRQRLDISIQSLGPC 864
Cdd:smart00280    1 DCPE-ACPR-EYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 742-778 2.33e-09

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


:

Pssm-ID: 395007  Cd Length: 49  Bit Score: 54.67  E-value: 2.33e-09
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 568930475   742 CSCDPRGAVRDDCEQMTGLCSCRPGVAGPKCGQCPDG 778
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPG 37
Kazal_1 pfam00050
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 244-284 3.87e-09

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: 53.83  E-value: 3.87e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 568930475   244 CPAQHTPICGDDGVTYENDCVMSRIGAARGLLLQKVRSGQC 284
Cdd:pfam00050    9 CPRIYDPVCGTDGKTYSNECLFCAENGKRGTNLHKVHDGEC 49
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
 316-356 6.74e-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: 53.04  E-value: 6.74e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 568930475  316 CDGAYRPVCAQDGHTYDNDCWRQQAECRQQQTIPPKHQGPC 356
Cdd:cd00104     1 CPKEYDPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 1707-1739 5.20e-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: 44.94  E-value: 5.20e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 568930475 1707 AVDNPCLNGGSCIPREATYECLCPGGFSGLHCE 1739
Cdd:cd00054     6 ASGNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
 
Name Accession Description Interval E-value
Laminin_G_1 pfam00054
Laminin G domain;
1282-1413 3.00e-51

Laminin G domain;


Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 177.12  E-value: 3.00e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930475  1282 FRALETEGLLLYNGNARGKDFLALALLDGHVQFRFDTGSGPAVLTSLVPVEPGRWHRLELSRHWRQGTLSVDGEAPVVGE 1361
Cdd:pfam00054    1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGE 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 568930475  1362 SPSGTDG-LNLDTKLYVGGLPEEqvATVLDRTSVGIGLKGCIRMLDINNQQLE 1413
Cdd:pfam00054   81 SPLGATTdLDVDGPLYVGGLPSL--GVKKRRLAISPSFDGCIRDVIVNGKPLD 131
Laminin_G_1 pfam00054
Laminin G domain;
1550-1685 5.54e-46

Laminin G domain;


Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 162.10  E-value: 5.54e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930475  1550 FLARGPSGLLLYNGQKTDGkgDFVSLALHNRHLEFRYDLGKGAAIIRSKEPIALGTWVRVFLERNGRKGALQVGDGPRVL 1629
Cdd:pfam00054    1 FRTTEPSGLLLYNGTQTER--DFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPT 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 568930475  1630 GESPKSRKvphTMLNLKEPLYVGGAPDFSKLARGAAVASGFDGAIQLVSLRGHQLL 1685
Cdd:pfam00054   79 GESPLGAT---TDLDVDGPLYVGGLPSLGVKKRRLAISPSFDGCIRDVIVNGKPLD 131
Laminin_G_1 pfam00054
Laminin G domain;
1784-1914 1.84e-45

Laminin G domain;


Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 160.56  E-value: 1.84e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930475  1784 RTEATQGLVLWIGKVGERaDYMALAIVDGHLQLSYDLGSQPVVLRSTVKVNTNRWLRVRAHREHREGSLQVGNEAPVTGS 1863
Cdd:pfam00054    2 RTTEPSGLLLYNGTQTER-DFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGE 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568930475  1864 SPLGATQ-LDTDGALWLGGLQKLPVgQALPKAYGTGFVGCLRDVVVGHRQLH 1914
Cdd:pfam00054   81 SPLGATTdLDVDGPLYVGGLPSLGV-KKRRLAISPSFDGCIRDVIVNGKPLD 131
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
 1259-1408 2.07e-45

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


Pssm-ID: 238058 [Multi-domain]  Cd Length: 151  Bit Score: 161.05  E-value: 2.07e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930475 1259 FKGHSFLAFPTLRA-YHTLRLALEFRALETEGLLLYNGNARGKDFLALALLDGHVQFRFDTGSGPAVLTSLVPVEPGRWH 1337
Cdd:cd00110     4 FSGSSYVRLPTLPApRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDGQWH 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568930475 1338 RLELSRHWRQGTLSVDGEAPVVGESPSGTDGLNLDTKLYVGGLPEEQVATvldRTSVGIGLKGCIRMLDIN 1408
Cdd:cd00110    84 SVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSP---GLPVSPGFVGCIRDLKVN 151
LamG smart00282
Laminin G domain;
1277-1410 1.33e-42

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 152.49  E-value: 1.33e-42
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930475   1277 RLALEFRALETEGLLLYNGNARGKDFLALALLDGHVQFRFDTGSGPAVLTS-LVPVEPGRWHRLELSRHWRQGTLSVDGE 1355
Cdd:smart00282    1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSdPTPLNDGQWHRVAVERNGRSVTLSVDGG 80

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 568930475   1356 APVVGESPSGTDGLNLDTKLYVGGLPEEQVATvldRTSVGIGLKGCIRMLDINNQ 1410
Cdd:smart00282   81 NRVSGESPGGLTILNLDGPLYLGGLPEDLKLP---PLPVTPGFRGCIRNLKVNGK 132
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
 1522-1679 8.02e-35

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


Pssm-ID: 238058 [Multi-domain]  Cd Length: 151  Bit Score: 131.00  E-value: 8.02e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930475 1522 FNGFSYLELKGLHTFERDlgekMALEMVFLARGPSGLLLYNGQKTdgKGDFVSLALHNRHLEFRYDLGKGAAIIRSKEPI 1601
Cdd:cd00110     4 FSGSSYVRLPTLPAPRTR----LSISFSFRTTSPNGLLLYAGSQN--GGDFLALELEDGRLVLRYDLGSGSLVLSSKTPL 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568930475 1602 ALGTWVRVFLERNGRKGALQVgDGPRVLgESPKSRKvpHTMLNLKEPLYVGGAPDFSKLaRGAAVASGFDGAIQLVSL 1679
Cdd:cd00110    78 NDGQWHSVSVERNGRSVTLSV-DGERVV-ESGSPGG--SALLNLDGPLYLGGLPEDLKS-PGLPVSPGFVGCIRDLKV 150
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
 1752-1908 1.58e-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: 130.23  E-value: 1.58e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930475 1752 TLAFDGRTYIEYLNavteSEKALQSNHFELSLRTEATQGLVLWIGkVGERADYMALAIVDGHLQLSYDLGSQPVVLRSTV 1831
Cdd:cd00110     1 GVSFSGSSYVRLPT----LPAPRTRLSISFSFRTTSPNGLLLYAG-SQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKT 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568930475 1832 KVNTNRWLRVRAHREHREGSLQVGNEAPVTGSSPLGATQLDTDGALWLGGLQklPVGQALPKAYGTGFVGCLRDVVV 1908
Cdd:cd00110    76 PLNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLP--EDLKSPGLPVSPGFVGCIRDLKV 150
LamG smart00282
Laminin G domain;
1778-1911 4.36e-32

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 122.45  E-value: 4.36e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930475   1778 HFELSLRTEATQGLVLWIGkVGERADYMALAIVDGHLQLSYDLGSQPVVLRST-VKVNTNRWLRVRAHREHREGSLQVGN 1856
Cdd:smart00282    1 SISFSFRTTSPNGLLLYAG-SKGGGDYLALELRDGRLVLRYDLGSGPARLTSDpTPLNDGQWHRVAVERNGRSVTLSVDG 79

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 568930475   1857 EAPVTGSSPLGATQLDTDGALWLGGlqkLPVGQALPK-AYGTGFVGCLRDVVVGHR 1911
Cdd:smart00282   80 GNRVSGESPGGLTILNLDGPLYLGG---LPEDLKLPPlPVTPGFRGCIRNLKVNGK 132
LamG smart00282
Laminin G domain;
1546-1682 1.13e-31

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 121.29  E-value: 1.13e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930475   1546 LEMVFLARGPSGLLLYNGQKtdGKGDFVSLALHNRHLEFRYDLGKGAAIIRSK-EPIALGTWVRVFLERNGRKGALQVGD 1624
Cdd:smart00282    2 ISFSFRTTSPNGLLLYAGSK--GGGDYLALELRDGRLVLRYDLGSGPARLTSDpTPLNDGQWHRVAVERNGRSVTLSVDG 79

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 568930475   1625 GPRVLGESPKSrkvpHTMLNLKEPLYVGGAPDFSKLARGaAVASGFDGAIQLVSLRGH 1682
Cdd:smart00282   80 GNRVSGESPGG----LTILNLDGPLYLGGLPEDLKLPPL-PVTPGFRGCIRNLKVNGK 132
SEA smart00200
Domain found in sea urchin sperm protein, enterokinase, agrin; Proposed function of regulating ...
 1014-1138 4.22e-31

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


Pssm-ID: 214554  Cd Length: 121  Bit Score: 119.05  E-value: 4.22e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930475   1014 ATKAFQGVLELEGVEGQELFYTPEMADPKSELFGETARSIESTLDDLFRNSDVKKDFWSIRLRELGPGKLVRAIVDVHFD 1093
Cdd:smart00200    1 PTQSFGVSLSVLSVEGENLQYSPSLEDPSSEEYQELVRDVEKLLEQIYGKTDLKPDFVGTEVIEFRNGSVVVDLGLLFNE 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*
gi 568930475   1094 PTTAfqAPDVGQALLQQIQVSRpWALAVRRPlrEHVRFLDFDWFP 1138
Cdd:smart00200   81 GVTN--GQDVEEDLLQVIKQAA-YSLKITNV--NVVDVLDPDSAD 120
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 688-730 5.14e-15

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 70.85  E-value: 5.14e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 568930475   688 CHCNPHGSYSGTCDPVTGQCSCRPGVGGLRCDRCEPGFWNFRG 730
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPS 43
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 688-728 8.25e-15

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


Pssm-ID: 238012  Cd Length: 50  Bit Score: 70.08  E-value: 8.25e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 568930475  688 CHCNPHGSYSGTCDPVTGQCSCRPGVGGLRCDRCEPGFWNF 728
Cdd:cd00055     2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGL 42
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
688-730 1.19e-13

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 66.57  E-value: 1.19e-13
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 568930475    688 CHCNPHGSYSGTCDPVTGQCSCRPGVGGLRCDRCEPGFWNFRG 730
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 384-429 8.97e-13

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


Pssm-ID: 197624  Cd Length: 46  Bit Score: 64.24  E-value: 8.97e-13
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 568930475    384 ECQRVCSGGYDPVCGSDGVTYGSVCELESMACTLGREIRVARRGPC 429
Cdd:smart00280    1 DCPEACPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 449-494 1.46e-12

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


Pssm-ID: 197624  Cd Length: 46  Bit Score: 63.47  E-value: 1.46e-12
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 568930475    449 VCPSECVESAQPVCGSDGHTYASECELHVHACTHQISLYVASAGHC 494
Cdd:smart00280    1 DCPEACPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 91-137 1.62e-11

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


Pssm-ID: 197624  Cd Length: 46  Bit Score: 60.77  E-value: 1.62e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 568930475     91 VCKKNvCPAMVAPVCGSDASTYSNECELQRAQCNQQRRIRLLRQGPC 137
Cdd:smart00280    1 DCPEA-CPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 599-645 2.15e-11

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


Pssm-ID: 197624  Cd Length: 46  Bit Score: 60.39  E-value: 2.15e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 568930475    599 VCDFSCQSVLKsPVCGSDGVTYSTECHLKKARCEARQELYVAAQGAC 645
Cdd:smart00280    1 DCPEACPREYD-PVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
SEA pfam01390
SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed ...
 1032-1110 2.16e-11

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


Pssm-ID: 460188  Cd Length: 100  Bit Score: 62.26  E-value: 2.16e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930475  1032 LFYTPEMADPKSELFGETARSIESTLDDLFRNSDVKKDFWS---IRLRELGPGklVRAIVDVHFDPTTAFQAPDVGQ--- 1105
Cdd:pfam01390   12 LQYTPDLGNPSSQEFKSLSRRIESLLNELFRNSSLRKQYIKshvLRLRPDGGS--VVVDVVLVFRFPSTEPALDREKlie 89


                   ....*
gi 568930475  1106 ALLQQ 1110
Cdd:pfam01390   90 EILRQ 94
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
 389-429 1.16e-10

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


Pssm-ID: 238052 [Multi-domain]  Cd Length: 41  Bit Score: 58.05  E-value: 1.16e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 568930475  389 CSGGYDPVCGSDGVTYGSVCELESMACTLGREIRVARRGPC 429
Cdd:cd00104     1 CPKEYDPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
 97-137 1.54e-10

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


Pssm-ID: 238052 [Multi-domain]  Cd Length: 41  Bit Score: 57.66  E-value: 1.54e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 568930475   97 CPAMVAPVCGSDASTYSNECELQRAQCNQQRRIRLLRQGPC 137
Cdd:cd00104     1 CPKEYDPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 167-212 2.29e-10

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


Pssm-ID: 197624  Cd Length: 46  Bit Score: 57.30  E-value: 2.29e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 568930475    167 CPTTCFGAPDgTVCGSDGVDYPSECQLLRHACANQEHIFKKFDGPC 212
Cdd:smart00280    2 CPEACPREYD-PVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 514-559 8.07e-10

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


Pssm-ID: 197624  Cd Length: 46  Bit Score: 55.76  E-value: 8.07e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 568930475    514 VCPRCEHPPPGPVCGSDGVTYLSACELREAACQQQVQIEEARAGPC 559
Cdd:smart00280    1 DCPEACPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 817-864 1.07e-09

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


Pssm-ID: 197624  Cd Length: 46  Bit Score: 55.38  E-value: 1.07e-09
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 568930475    817 VCPTlTCPEaNSTKVCGSDGVTYGNECQLKTIACRQRLDISIQSLGPC 864
Cdd:smart00280    1 DCPE-ACPR-EYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
 454-494 1.24e-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: 55.35  E-value: 1.24e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 568930475  454 CVESAQPVCGSDGHTYASECELHVHACTHQISLYVASAGHC 494
Cdd:cd00104     1 CPKEYDPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 742-778 2.33e-09

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 54.67  E-value: 2.33e-09
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 568930475   742 CSCDPRGAVRDDCEQMTGLCSCRPGVAGPKCGQCPDG 778
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPG 37
Kazal_1 pfam00050
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 244-284 3.87e-09

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: 53.83  E-value: 3.87e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 568930475   244 CPAQHTPICGDDGVTYENDCVMSRIGAARGLLLQKVRSGQC 284
Cdd:pfam00050    9 CPRIYDPVCGTDGKTYSNECLFCAENGKRGTNLHKVHDGEC 49
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
 515-559 4.09e-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: 53.81  E-value: 4.09e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 568930475  515 CPRCEHPppgpVCGSDGVTYLSACELREAACQQQVQIEEARAGPC 559
Cdd:cd00104     1 CPKEYDP----VCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
 316-356 6.74e-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: 53.04  E-value: 6.74e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 568930475  316 CDGAYRPVCAQDGHTYDNDCWRQQAECRQQQTIPPKHQGPC 356
Cdd:cd00104     1 CPKEYDPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
 823-864 2.81e-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: 51.50  E-value: 2.81e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 568930475  823 CPEaNSTKVCGSDGVTYGNECQLKTIACRQRLDISIQSLGPC 864
Cdd:cd00104     1 CPK-EYDPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
 610-645 3.67e-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: 51.12  E-value: 3.67e-08
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 568930475  610 SPVCGSDGVTYSTECHLKKARCEARQELYVAAQGAC 645
Cdd:cd00104     6 DPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 741-778 4.64e-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: 50.82  E-value: 4.64e-08
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 568930475  741 PCSCDPRGAVRDDCEQMTGLCSCRPGVAGPKCGQCPDG 778
Cdd:cd00055     1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPG 38
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 311-356 6.48e-08

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


Pssm-ID: 197624  Cd Length: 46  Bit Score: 50.37  E-value: 6.48e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 568930475    311 CDRVtCDGAYRPVCAQDGHTYDNDCWRQQAECRQQQTIPPKHQGPC 356
Cdd:smart00280    2 CPEA-CPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
 179-212 1.58e-07

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


Pssm-ID: 238052 [Multi-domain]  Cd Length: 41  Bit Score: 49.19  E-value: 1.58e-07
                          10        20        30
                  ....*....|....*....|....*....|....
gi 568930475  179 VCGSDGVDYPSECQLLRHACANQEHIFKKFDGPC 212
Cdd:cd00104     8 VCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 600-637 1.94e-07

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


Pssm-ID: 400135  Cd Length: 50  Bit Score: 49.41  E-value: 1.94e-07
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 568930475   600 CDFSCQSVLKSPVCGSDGVTYSTECHLKKARCEARQEL 637
Cdd:pfam07648    2 CNCQCPKTEYEPVCGSDGVTYPSPCALCAAGCKLGKEV 39
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
742-778 2.22e-07

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 48.85  E-value: 2.22e-07
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 568930475    742 CSCDPRGAVRDDCEQMTGLCSCRPGVAGPKCGQCPDG 778
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPG 37
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 513-559 4.95e-06

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


Pssm-ID: 400135  Cd Length: 50  Bit Score: 45.18  E-value: 4.95e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 568930475   513 CVCPRCEHPPPGPVCGSDGVTYLSACELREAACQQQVQIEEARA---GPC 559
Cdd:pfam07648    1 NCNCQCPKTEYEPVCGSDGVTYPSPCALCAAGCKLGKEVKEEKVkydGSC 50
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 1707-1739 5.20e-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: 44.94  E-value: 5.20e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 568930475 1707 AVDNPCLNGGSCIPREATYECLCPGGFSGLHCE 1739
Cdd:cd00054     6 ASGNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
Kazal_1 pfam00050
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 93-137 6.98e-06

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


Pssm-ID: 395004  Cd Length: 49  Bit Score: 44.97  E-value: 6.98e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 568930475    93 KKNVCPAMVAPVCGSDASTYSNECELQRAQCNQQRRIRLLRQGPC 137
Cdd:pfam00050    5 PSGACPRIYDPVCGTDGKTYSNECLFCAENGKRGTNLHKVHDGEC 49
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 241-284 4.29e-05

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


Pssm-ID: 197624  Cd Length: 46  Bit Score: 42.67  E-value: 4.29e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 568930475    241 PENCPAQHTPICGDDGVTYENDCVMSRIGAARGLLLQKVRSGQC 284
Cdd:smart00280    3 PEACPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
Kazal_1 pfam00050
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 389-429 4.70e-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: 4.70e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 568930475   389 CSGGYDPVCGSDGVTYGSVCELESMACTLGREIRVARRGPC 429
Cdd:pfam00050    9 CPRIYDPVCGTDGKTYSNECLFCAENGKRGTNLHKVHDGEC 49
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
 244-284 1.03e-04

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: 41.10  E-value: 1.03e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 568930475  244 CPAQHTPICGDDGVTYENDCVMSRIGAARGLLLQKVRSGQC 284
Cdd:cd00104     1 CPKEYDPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 447-486 1.79e-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: 1.79e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 568930475   447 RCVCPsecVESAQPVCGSDGHTYASECELHVHACTHQISL 486
Cdd:pfam07648    3 NCQCP---KTEYEPVCGSDGVTYPSPCALCAAGCKLGKEV 39
EGF_CA smart00179
Calcium-binding EGF-like domain;
1707-1739 1.92e-04

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 40.31  E-value: 1.92e-04
                            10        20        30
                    ....*....|....*....|....*....|....
gi 568930475   1707 AVDNPCLNGGSCIPREATYECLCPGGFS-GLHCE 1739
Cdd:smart00179    6 ASGNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
Kazal_1 pfam00050
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 819-864 2.47e-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: 40.35  E-value: 2.47e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 568930475   819 PTLTCPeANSTKVCGSDGVTYGNECQLKTIACRQRLDISIQSLGPC 864
Cdd:pfam00050    5 PSGACP-RIYDPVCGTDGKTYSNECLFCAENGKRGTNLHKVHDGEC 49
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 167-212 2.60e-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: 40.55  E-value: 2.60e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 568930475   167 CPTTCFGAPDGTVCGSDGVDYPSECQLLRHACANQEHIFK---KFDGPC 212
Cdd:pfam07648    2 CNCQCPKTEYEPVCGSDGVTYPSPCALCAAGCKLGKEVKEekvKYDGSC 50
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 309-356 4.24e-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: 39.78  E-value: 4.24e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 568930475   309 CSCDRVTcdgaYRPVCAQDGHTYDNDCWRQQAECRQQQTI---PPKHQGPC 356
Cdd:pfam07648    4 CQCPKTE----YEPVCGSDGVTYPSPCALCAAGCKLGKEVkeeKVKYDGSC 50
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 1709-1737 2.62e-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: 36.98  E-value: 2.62e-03
                           10        20
                   ....*....|....*....|....*....
gi 568930475  1709 DNPCLNGGSCIPREATYECLCPGGFSGLH 1737
Cdd:pfam00008    3 PNPCSNGGTCVDTPGGYTCICPEGYTGKR 31
 
Name Accession Description Interval E-value
Laminin_G_1 pfam00054
Laminin G domain;
1282-1413 3.00e-51

Laminin G domain;


Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 177.12  E-value: 3.00e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930475  1282 FRALETEGLLLYNGNARGKDFLALALLDGHVQFRFDTGSGPAVLTSLVPVEPGRWHRLELSRHWRQGTLSVDGEAPVVGE 1361
Cdd:pfam00054    1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGE 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 568930475  1362 SPSGTDG-LNLDTKLYVGGLPEEqvATVLDRTSVGIGLKGCIRMLDINNQQLE 1413
Cdd:pfam00054   81 SPLGATTdLDVDGPLYVGGLPSL--GVKKRRLAISPSFDGCIRDVIVNGKPLD 131
Laminin_G_1 pfam00054
Laminin G domain;
1550-1685 5.54e-46

Laminin G domain;


Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 162.10  E-value: 5.54e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930475  1550 FLARGPSGLLLYNGQKTDGkgDFVSLALHNRHLEFRYDLGKGAAIIRSKEPIALGTWVRVFLERNGRKGALQVGDGPRVL 1629
Cdd:pfam00054    1 FRTTEPSGLLLYNGTQTER--DFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPT 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 568930475  1630 GESPKSRKvphTMLNLKEPLYVGGAPDFSKLARGAAVASGFDGAIQLVSLRGHQLL 1685
Cdd:pfam00054   79 GESPLGAT---TDLDVDGPLYVGGLPSLGVKKRRLAISPSFDGCIRDVIVNGKPLD 131
Laminin_G_1 pfam00054
Laminin G domain;
1784-1914 1.84e-45

Laminin G domain;


Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 160.56  E-value: 1.84e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930475  1784 RTEATQGLVLWIGKVGERaDYMALAIVDGHLQLSYDLGSQPVVLRSTVKVNTNRWLRVRAHREHREGSLQVGNEAPVTGS 1863
Cdd:pfam00054    2 RTTEPSGLLLYNGTQTER-DFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGE 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568930475  1864 SPLGATQ-LDTDGALWLGGLQKLPVgQALPKAYGTGFVGCLRDVVVGHRQLH 1914
Cdd:pfam00054   81 SPLGATTdLDVDGPLYVGGLPSLGV-KKRRLAISPSFDGCIRDVIVNGKPLD 131
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
 1259-1408 2.07e-45

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


Pssm-ID: 238058 [Multi-domain]  Cd Length: 151  Bit Score: 161.05  E-value: 2.07e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930475 1259 FKGHSFLAFPTLRA-YHTLRLALEFRALETEGLLLYNGNARGKDFLALALLDGHVQFRFDTGSGPAVLTSLVPVEPGRWH 1337
Cdd:cd00110     4 FSGSSYVRLPTLPApRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDGQWH 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568930475 1338 RLELSRHWRQGTLSVDGEAPVVGESPSGTDGLNLDTKLYVGGLPEEQVATvldRTSVGIGLKGCIRMLDIN 1408
Cdd:cd00110    84 SVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSP---GLPVSPGFVGCIRDLKVN 151
LamG smart00282
Laminin G domain;
1277-1410 1.33e-42

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 152.49  E-value: 1.33e-42
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930475   1277 RLALEFRALETEGLLLYNGNARGKDFLALALLDGHVQFRFDTGSGPAVLTS-LVPVEPGRWHRLELSRHWRQGTLSVDGE 1355
Cdd:smart00282    1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSdPTPLNDGQWHRVAVERNGRSVTLSVDGG 80

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 568930475   1356 APVVGESPSGTDGLNLDTKLYVGGLPEEQVATvldRTSVGIGLKGCIRMLDINNQ 1410
Cdd:smart00282   81 NRVSGESPGGLTILNLDGPLYLGGLPEDLKLP---PLPVTPGFRGCIRNLKVNGK 132
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
 1522-1679 8.02e-35

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


Pssm-ID: 238058 [Multi-domain]  Cd Length: 151  Bit Score: 131.00  E-value: 8.02e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930475 1522 FNGFSYLELKGLHTFERDlgekMALEMVFLARGPSGLLLYNGQKTdgKGDFVSLALHNRHLEFRYDLGKGAAIIRSKEPI 1601
Cdd:cd00110     4 FSGSSYVRLPTLPAPRTR----LSISFSFRTTSPNGLLLYAGSQN--GGDFLALELEDGRLVLRYDLGSGSLVLSSKTPL 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568930475 1602 ALGTWVRVFLERNGRKGALQVgDGPRVLgESPKSRKvpHTMLNLKEPLYVGGAPDFSKLaRGAAVASGFDGAIQLVSL 1679
Cdd:cd00110    78 NDGQWHSVSVERNGRSVTLSV-DGERVV-ESGSPGG--SALLNLDGPLYLGGLPEDLKS-PGLPVSPGFVGCIRDLKV 150
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
 1752-1908 1.58e-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: 130.23  E-value: 1.58e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930475 1752 TLAFDGRTYIEYLNavteSEKALQSNHFELSLRTEATQGLVLWIGkVGERADYMALAIVDGHLQLSYDLGSQPVVLRSTV 1831
Cdd:cd00110     1 GVSFSGSSYVRLPT----LPAPRTRLSISFSFRTTSPNGLLLYAG-SQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKT 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568930475 1832 KVNTNRWLRVRAHREHREGSLQVGNEAPVTGSSPLGATQLDTDGALWLGGLQklPVGQALPKAYGTGFVGCLRDVVV 1908
Cdd:cd00110    76 PLNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLP--EDLKSPGLPVSPGFVGCIRDLKV 150
LamG smart00282
Laminin G domain;
1778-1911 4.36e-32

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 122.45  E-value: 4.36e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930475   1778 HFELSLRTEATQGLVLWIGkVGERADYMALAIVDGHLQLSYDLGSQPVVLRST-VKVNTNRWLRVRAHREHREGSLQVGN 1856
Cdd:smart00282    1 SISFSFRTTSPNGLLLYAG-SKGGGDYLALELRDGRLVLRYDLGSGPARLTSDpTPLNDGQWHRVAVERNGRSVTLSVDG 79

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 568930475   1857 EAPVTGSSPLGATQLDTDGALWLGGlqkLPVGQALPK-AYGTGFVGCLRDVVVGHR 1911
Cdd:smart00282   80 GNRVSGESPGGLTILNLDGPLYLGG---LPEDLKLPPlPVTPGFRGCIRNLKVNGK 132
LamG smart00282
Laminin G domain;
1546-1682 1.13e-31

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 121.29  E-value: 1.13e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930475   1546 LEMVFLARGPSGLLLYNGQKtdGKGDFVSLALHNRHLEFRYDLGKGAAIIRSK-EPIALGTWVRVFLERNGRKGALQVGD 1624
Cdd:smart00282    2 ISFSFRTTSPNGLLLYAGSK--GGGDYLALELRDGRLVLRYDLGSGPARLTSDpTPLNDGQWHRVAVERNGRSVTLSVDG 79

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 568930475   1625 GPRVLGESPKSrkvpHTMLNLKEPLYVGGAPDFSKLARGaAVASGFDGAIQLVSLRGH 1682
Cdd:smart00282   80 GNRVSGESPGG----LTILNLDGPLYLGGLPEDLKLPPL-PVTPGFRGCIRNLKVNGK 132
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
 1282-1410 3.13e-31

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


Pssm-ID: 460494 [Multi-domain]  Cd Length: 126  Bit Score: 119.83  E-value: 3.13e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930475  1282 FRALETEGLLLYNGNARGkDFLALALLDGHVQFRFDTGSGPAVLTSL-VPVEPGRWHRLELSRHWRQGTLSVDGEAPVVG 1360
Cdd:pfam02210    1 FRTRQPNGLLLYAGGGGS-DFLALELVNGRLVLRYDLGSGPESLLSSgKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSS 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 568930475  1361 ESPSGTDGLNLDTKLYVGGLPEEqvaTVLDRTSVGIGLKGCIRMLDINNQ 1410
Cdd:pfam02210   80 LPPGESLLLNLNGPLYLGGLPPL---LLLPALPVRAGFVGCIRDVRVNGE 126
SEA smart00200
Domain found in sea urchin sperm protein, enterokinase, agrin; Proposed function of regulating ...
 1014-1138 4.22e-31

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


Pssm-ID: 214554  Cd Length: 121  Bit Score: 119.05  E-value: 4.22e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930475   1014 ATKAFQGVLELEGVEGQELFYTPEMADPKSELFGETARSIESTLDDLFRNSDVKKDFWSIRLRELGPGKLVRAIVDVHFD 1093
Cdd:smart00200    1 PTQSFGVSLSVLSVEGENLQYSPSLEDPSSEEYQELVRDVEKLLEQIYGKTDLKPDFVGTEVIEFRNGSVVVDLGLLFNE 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*
gi 568930475   1094 PTTAfqAPDVGQALLQQIQVSRpWALAVRRPlrEHVRFLDFDWFP 1138
Cdd:smart00200   81 GVTN--GQDVEEDLLQVIKQAA-YSLKITNV--NVVDVLDPDSAD 120
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
 1783-1911 3.17e-27

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


Pssm-ID: 460494 [Multi-domain]  Cd Length: 126  Bit Score: 108.28  E-value: 3.17e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930475  1783 LRTEATQGLVLWIGkvGERADYMALAIVDGHLQLSYDLGSQPVVLRST-VKVNTNRWLRVRAHREHREGSLQVGNEAPVT 1861
Cdd:pfam02210    1 FRTRQPNGLLLYAG--GGGSDFLALELVNGRLVLRYDLGSGPESLLSSgKNLNDGQWHSVRVERNGNTLTLSVDGQTVVS 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 568930475  1862 GSSPLGATQLDTDGALWLGGLQKLPVGQALPkaYGTGFVGCLRDVVVGHR 1911
Cdd:pfam02210   79 SLPPGESLLLNLNGPLYLGGLPPLLLLPALP--VRAGFVGCIRDVRVNGE 126
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
 1550-1682 1.48e-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: 1.48e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930475  1550 FLARGPSGLLLYNGqktDGKGDFVSLALHNRHLEFRYDLGKGAAIIRS-KEPIALGTWVRVFLERNGRKGALQVGDGPRV 1628
Cdd:pfam02210    1 FRTRQPNGLLLYAG---GGGSDFLALELVNGRLVLRYDLGSGPESLLSsGKNLNDGQWHSVRVERNGNTLTLSVDGQTVV 77

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 568930475  1629 LGESPKsrkvPHTMLNLKEPLYVGGAPDFSKLaRGAAVASGFDGAIQLVSLRGH 1682
Cdd:pfam02210   78 SSLPPG----ESLLLNLNGPLYLGGLPPLLLL-PALPVRAGFVGCIRDVRVNGE 126
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 688-730 5.14e-15

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 70.85  E-value: 5.14e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 568930475   688 CHCNPHGSYSGTCDPVTGQCSCRPGVGGLRCDRCEPGFWNFRG 730
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPS 43
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 688-728 8.25e-15

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


Pssm-ID: 238012  Cd Length: 50  Bit Score: 70.08  E-value: 8.25e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 568930475  688 CHCNPHGSYSGTCDPVTGQCSCRPGVGGLRCDRCEPGFWNF 728
Cdd:cd00055     2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGL 42
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
688-730 1.19e-13

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 66.57  E-value: 1.19e-13
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 568930475    688 CHCNPHGSYSGTCDPVTGQCSCRPGVGGLRCDRCEPGFWNFRG 730
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 384-429 8.97e-13

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


Pssm-ID: 197624  Cd Length: 46  Bit Score: 64.24  E-value: 8.97e-13
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 568930475    384 ECQRVCSGGYDPVCGSDGVTYGSVCELESMACTLGREIRVARRGPC 429
Cdd:smart00280    1 DCPEACPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 449-494 1.46e-12

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


Pssm-ID: 197624  Cd Length: 46  Bit Score: 63.47  E-value: 1.46e-12
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 568930475    449 VCPSECVESAQPVCGSDGHTYASECELHVHACTHQISLYVASAGHC 494
Cdd:smart00280    1 DCPEACPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 91-137 1.62e-11

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


Pssm-ID: 197624  Cd Length: 46  Bit Score: 60.77  E-value: 1.62e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 568930475     91 VCKKNvCPAMVAPVCGSDASTYSNECELQRAQCNQQRRIRLLRQGPC 137
Cdd:smart00280    1 DCPEA-CPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 599-645 2.15e-11

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


Pssm-ID: 197624  Cd Length: 46  Bit Score: 60.39  E-value: 2.15e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 568930475    599 VCDFSCQSVLKsPVCGSDGVTYSTECHLKKARCEARQELYVAAQGAC 645
Cdd:smart00280    1 DCPEACPREYD-PVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
SEA pfam01390
SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed ...
 1032-1110 2.16e-11

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


Pssm-ID: 460188  Cd Length: 100  Bit Score: 62.26  E-value: 2.16e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930475  1032 LFYTPEMADPKSELFGETARSIESTLDDLFRNSDVKKDFWS---IRLRELGPGklVRAIVDVHFDPTTAFQAPDVGQ--- 1105
Cdd:pfam01390   12 LQYTPDLGNPSSQEFKSLSRRIESLLNELFRNSSLRKQYIKshvLRLRPDGGS--VVVDVVLVFRFPSTEPALDREKlie 89


                   ....*
gi 568930475  1106 ALLQQ 1110
Cdd:pfam01390   90 EILRQ 94
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
 389-429 1.16e-10

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


Pssm-ID: 238052 [Multi-domain]  Cd Length: 41  Bit Score: 58.05  E-value: 1.16e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 568930475  389 CSGGYDPVCGSDGVTYGSVCELESMACTLGREIRVARRGPC 429
Cdd:cd00104     1 CPKEYDPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
 97-137 1.54e-10

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


Pssm-ID: 238052 [Multi-domain]  Cd Length: 41  Bit Score: 57.66  E-value: 1.54e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 568930475   97 CPAMVAPVCGSDASTYSNECELQRAQCNQQRRIRLLRQGPC 137
Cdd:cd00104     1 CPKEYDPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 167-212 2.29e-10

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


Pssm-ID: 197624  Cd Length: 46  Bit Score: 57.30  E-value: 2.29e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 568930475    167 CPTTCFGAPDgTVCGSDGVDYPSECQLLRHACANQEHIFKKFDGPC 212
Cdd:smart00280    2 CPEACPREYD-PVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 514-559 8.07e-10

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


Pssm-ID: 197624  Cd Length: 46  Bit Score: 55.76  E-value: 8.07e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 568930475    514 VCPRCEHPPPGPVCGSDGVTYLSACELREAACQQQVQIEEARAGPC 559
Cdd:smart00280    1 DCPEACPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 817-864 1.07e-09

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


Pssm-ID: 197624  Cd Length: 46  Bit Score: 55.38  E-value: 1.07e-09
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 568930475    817 VCPTlTCPEaNSTKVCGSDGVTYGNECQLKTIACRQRLDISIQSLGPC 864
Cdd:smart00280    1 DCPE-ACPR-EYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
 454-494 1.24e-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: 55.35  E-value: 1.24e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 568930475  454 CVESAQPVCGSDGHTYASECELHVHACTHQISLYVASAGHC 494
Cdd:cd00104     1 CPKEYDPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 742-778 2.33e-09

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 54.67  E-value: 2.33e-09
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 568930475   742 CSCDPRGAVRDDCEQMTGLCSCRPGVAGPKCGQCPDG 778
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPG 37
Kazal_1 pfam00050
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 244-284 3.87e-09

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: 53.83  E-value: 3.87e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 568930475   244 CPAQHTPICGDDGVTYENDCVMSRIGAARGLLLQKVRSGQC 284
Cdd:pfam00050    9 CPRIYDPVCGTDGKTYSNECLFCAENGKRGTNLHKVHDGEC 49
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
 515-559 4.09e-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: 53.81  E-value: 4.09e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 568930475  515 CPRCEHPppgpVCGSDGVTYLSACELREAACQQQVQIEEARAGPC 559
Cdd:cd00104     1 CPKEYDP----VCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
 316-356 6.74e-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: 53.04  E-value: 6.74e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 568930475  316 CDGAYRPVCAQDGHTYDNDCWRQQAECRQQQTIPPKHQGPC 356
Cdd:cd00104     1 CPKEYDPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
 823-864 2.81e-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: 51.50  E-value: 2.81e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 568930475  823 CPEaNSTKVCGSDGVTYGNECQLKTIACRQRLDISIQSLGPC 864
Cdd:cd00104     1 CPK-EYDPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
 610-645 3.67e-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: 51.12  E-value: 3.67e-08
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 568930475  610 SPVCGSDGVTYSTECHLKKARCEARQELYVAAQGAC 645
Cdd:cd00104     6 DPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 741-778 4.64e-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: 50.82  E-value: 4.64e-08
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 568930475  741 PCSCDPRGAVRDDCEQMTGLCSCRPGVAGPKCGQCPDG 778
Cdd:cd00055     1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPG 38
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 311-356 6.48e-08

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


Pssm-ID: 197624  Cd Length: 46  Bit Score: 50.37  E-value: 6.48e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 568930475    311 CDRVtCDGAYRPVCAQDGHTYDNDCWRQQAECRQQQTIPPKHQGPC 356
Cdd:smart00280    2 CPEA-CPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
 179-212 1.58e-07

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


Pssm-ID: 238052 [Multi-domain]  Cd Length: 41  Bit Score: 49.19  E-value: 1.58e-07
                          10        20        30
                  ....*....|....*....|....*....|....
gi 568930475  179 VCGSDGVDYPSECQLLRHACANQEHIFKKFDGPC 212
Cdd:cd00104     8 VCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 600-637 1.94e-07

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


Pssm-ID: 400135  Cd Length: 50  Bit Score: 49.41  E-value: 1.94e-07
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 568930475   600 CDFSCQSVLKSPVCGSDGVTYSTECHLKKARCEARQEL 637
Cdd:pfam07648    2 CNCQCPKTEYEPVCGSDGVTYPSPCALCAAGCKLGKEV 39
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
742-778 2.22e-07

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 48.85  E-value: 2.22e-07
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 568930475    742 CSCDPRGAVRDDCEQMTGLCSCRPGVAGPKCGQCPDG 778
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPG 37
KAZAL_PSTI cd01327
Kazal-type pancreatic secretory trypsin inhibitors (PSTI) and related proteins, including the ...
 94-137 4.58e-06

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: 45.35  E-value: 4.58e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 568930475   94 KNVCPAMVAPVCGSDASTYSNECELQRAQCNQQRRIRLLRQGPC 137
Cdd:cd01327     2 VFGCPKDYDPVCGTDGVTYSNECLLCAENLKRQTNIRIKHDGEC 45
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 513-559 4.95e-06

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


Pssm-ID: 400135  Cd Length: 50  Bit Score: 45.18  E-value: 4.95e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 568930475   513 CVCPRCEHPPPGPVCGSDGVTYLSACELREAACQQQVQIEEARA---GPC 559
Cdd:pfam07648    1 NCNCQCPKTEYEPVCGSDGVTYPSPCALCAAGCKLGKEVKEEKVkydGSC 50
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 1707-1739 5.20e-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: 44.94  E-value: 5.20e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 568930475 1707 AVDNPCLNGGSCIPREATYECLCPGGFSGLHCE 1739
Cdd:cd00054     6 ASGNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
Kazal_1 pfam00050
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 93-137 6.98e-06

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


Pssm-ID: 395004  Cd Length: 49  Bit Score: 44.97  E-value: 6.98e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 568930475    93 KKNVCPAMVAPVCGSDASTYSNECELQRAQCNQQRRIRLLRQGPC 137
Cdd:pfam00050    5 PSGACPRIYDPVCGTDGKTYSNECLFCAENGKRGTNLHKVHDGEC 49
FSL_SPARC cd01328
Follistatin-like SPARC (secreted protein, acidic, and rich in cysteines) domain; SPARC/BM-40 ...
 362-417 3.94e-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: 44.01  E-value: 3.94e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930475  362 PCRGAQCAFGATCTV-KNGKAVCECQRVCSGGYDP---VCGSDGVTYGSVCELESMACTL 417
Cdd:cd01328     1 PCENHHCGAGKVCEVdDENTPKCVCIDPCPEEVDDrrkVCTNDNETFDSDCELYRTRCLC 60
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 241-284 4.29e-05

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


Pssm-ID: 197624  Cd Length: 46  Bit Score: 42.67  E-value: 4.29e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 568930475    241 PENCPAQHTPICGDDGVTYENDCVMSRIGAARGLLLQKVRSGQC 284
Cdd:smart00280    3 PEACPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
Kazal_1 pfam00050
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 389-429 4.70e-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: 4.70e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 568930475   389 CSGGYDPVCGSDGVTYGSVCELESMACTLGREIRVARRGPC 429
Cdd:pfam00050    9 CPRIYDPVCGTDGKTYSNECLFCAENGKRGTNLHKVHDGEC 49
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 102-137 5.49e-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: 42.48  E-value: 5.49e-05
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 568930475   102 APVCGSDASTYSNECELQRAQCNQQRRIR---LLRQGPC 137
Cdd:pfam07648   12 EPVCGSDGVTYPSPCALCAAGCKLGKEVKeekVKYDGSC 50
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 384-429 6.68e-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: 6.68e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 568930475   384 ECQRVCSG-GYDPVCGSDGVTYGSVCELESMACTLGREIR---VARRGPC 429
Cdd:pfam07648    1 NCNCQCPKtEYEPVCGSDGVTYPSPCALCAAGCKLGKEVKeekVKYDGSC 50
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
 244-284 1.03e-04

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: 41.10  E-value: 1.03e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 568930475  244 CPAQHTPICGDDGVTYENDCVMSRIGAARGLLLQKVRSGQC 284
Cdd:cd00104     1 CPKEYDPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
KAZAL_PSTI cd01327
Kazal-type pancreatic secretory trypsin inhibitors (PSTI) and related proteins, including the ...
 389-429 1.07e-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: 41.50  E-value: 1.07e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 568930475  389 CSGGYDPVCGSDGVTYGSVCELESMACTLGREIRVARRGPC 429
Cdd:cd01327     5 CPKDYDPVCGTDGVTYSNECLLCAENLKRQTNIRIKHDGEC 45
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 447-486 1.79e-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: 1.79e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 568930475   447 RCVCPsecVESAQPVCGSDGHTYASECELHVHACTHQISL 486
Cdd:pfam07648    3 NCQCP---KTEYEPVCGSDGVTYPSPCALCAAGCKLGKEV 39
EGF_CA smart00179
Calcium-binding EGF-like domain;
1707-1739 1.92e-04

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 40.31  E-value: 1.92e-04
                            10        20        30
                    ....*....|....*....|....*....|....
gi 568930475   1707 AVDNPCLNGGSCIPREATYECLCPGGFS-GLHCE 1739
Cdd:smart00179    6 ASGNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
FSL_SPARC cd01328
Follistatin-like SPARC (secreted protein, acidic, and rich in cysteines) domain; SPARC/BM-40 ...
 67-123 2.41e-04

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


Pssm-ID: 238649 [Multi-domain]  Cd Length: 86  Bit Score: 41.70  E-value: 2.41e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930475   67 CRGMLCGFGAVCEpsVEDPGRASCVCKKNvCPAMVAP---VCGSDASTYSNECELQRAQC 123
Cdd:cd01328     2 CENHHCGAGKVCE--VDDENTPKCVCIDP-CPEEVDDrrkVCTNDNETFDSDCELYRTRC 58
Kazal_1 pfam00050
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 819-864 2.47e-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: 40.35  E-value: 2.47e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 568930475   819 PTLTCPeANSTKVCGSDGVTYGNECQLKTIACRQRLDISIQSLGPC 864
Cdd:pfam00050    5 PSGACP-RIYDPVCGTDGKTYSNECLFCAENGKRGTNLHKVHDGEC 49
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 167-212 2.60e-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: 40.55  E-value: 2.60e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 568930475   167 CPTTCFGAPDGTVCGSDGVDYPSECQLLRHACANQEHIFK---KFDGPC 212
Cdd:pfam07648    2 CNCQCPKTEYEPVCGSDGVTYPSPCALCAAGCKLGKEVKEekvKYDGSC 50
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 822-864 3.13e-04

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


Pssm-ID: 400135  Cd Length: 50  Bit Score: 40.17  E-value: 3.13e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 568930475   822 TCPEANSTKVCGSDGVTYGNECQLKTIACRQRLDIS---IQSLGPC 864
Cdd:pfam07648    5 QCPKTEYEPVCGSDGVTYPSPCALCAAGCKLGKEVKeekVKYDGSC 50
KAZAL_PSTI cd01327
Kazal-type pancreatic secretory trypsin inhibitors (PSTI) and related proteins, including the ...
 818-864 4.17e-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: 39.57  E-value: 4.17e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 568930475  818 CPTLTCPeanstkVCGSDGVTYGNECQLKTIACRQRLDISIQSLGPC 864
Cdd:cd01327     5 CPKDYDP------VCGTDGVTYSNECLLCAENLKRQTNIRIKHDGEC 45
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 309-356 4.24e-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: 39.78  E-value: 4.24e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 568930475   309 CSCDRVTcdgaYRPVCAQDGHTYDNDCWRQQAECRQQQTI---PPKHQGPC 356
Cdd:pfam07648    4 CQCPKTE----YEPVCGSDGVTYPSPCALCAAGCKLGKEVkeeKVKYDGSC 50
Kazal_1 pfam00050
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 611-645 5.60e-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: 39.58  E-value: 5.60e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 568930475   611 PVCGSDGVTYSTECHLKKARCEARQELYVAAQGAC 645
Cdd:pfam00050   15 PVCGTDGKTYSNECLFCAENGKRGTNLHKVHDGEC 49
KAZAL_PSTI cd01327
Kazal-type pancreatic secretory trypsin inhibitors (PSTI) and related proteins, including the ...
 244-284 6.49e-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: 6.49e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 568930475  244 CPAQHTPICGDDGVTYENDCVMSRIGAARGLLLQKVRSGQC 284
Cdd:cd01327     5 CPKDYDPVCGTDGVTYSNECLLCAENLKRQTNIRIKHDGEC 45
FSL_SPARC cd01328
Follistatin-like SPARC (secreted protein, acidic, and rich in cysteines) domain; SPARC/BM-40 ...
 428-481 7.42e-04

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


Pssm-ID: 238649 [Multi-domain]  Cd Length: 86  Bit Score: 40.15  E-value: 7.42e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930475  428 PCDRcGQCRFGSLCEV---ETGRCVCPSECVESAQP---VCGSDGHTYASECELHVHACT 481
Cdd:cd01328     1 PCEN-HHCGAGKVCEVddeNTPKCVCIDPCPEEVDDrrkVCTNDNETFDSDCELYRTRCL 59
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
 1707-1739 1.63e-03

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


Pssm-ID: 238010  Cd Length: 36  Bit Score: 37.84  E-value: 1.63e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 568930475 1707 AVDNPCLNGGSCIPREATYECLCPGGFSG-LHCE 1739
Cdd:cd00053     3 AASNPCSNGGTCVNTPGSYRCVCPPGYTGdRSCE 36
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 1709-1737 2.62e-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: 36.98  E-value: 2.62e-03
                           10        20
                   ....*....|....*....|....*....
gi 568930475  1709 DNPCLNGGSCIPREATYECLCPGGFSGLH 1737
Cdd:pfam00008    3 PNPCSNGGTCVDTPGGYTCICPEGYTGKR 31
KAZAL_PSTI cd01327
Kazal-type pancreatic secretory trypsin inhibitors (PSTI) and related proteins, including the ...
 601-626 2.79e-03

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


Pssm-ID: 238648  Cd Length: 45  Bit Score: 37.26  E-value: 2.79e-03
                          10        20
                  ....*....|....*....|....*.
gi 568930475  601 DFSCQSVLKsPVCGSDGVTYSTECHL 626
Cdd:cd01327     2 VFGCPKDYD-PVCGTDGVTYSNECLL 26
Kazal_1 pfam00050
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 314-356 3.93e-03

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


Pssm-ID: 395004  Cd Length: 49  Bit Score: 36.88  E-value: 3.93e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 568930475   314 VTCDGAYRPVCAQDGHTYDNDCWRQQAECRQQQTIPPKHQGPC 356
Cdd:pfam00050    7 GACPRIYDPVCGTDGKTYSNECLFCAENGKRGTNLHKVHDGEC 49
KAZAL_PSTI cd01327
Kazal-type pancreatic secretory trypsin inhibitors (PSTI) and related proteins, including the ...
 316-356 5.72e-03

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


Pssm-ID: 238648  Cd Length: 45  Bit Score: 36.49  E-value: 5.72e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 568930475  316 CDGAYRPVCAQDGHTYDNDCWRQQAECRQQQTIPPKHQGPC 356
Cdd:cd01327     5 CPKDYDPVCGTDGVTYSNECLLCAENLKRQTNIRIKHDGEC 45
MFS_SLCO_OATP cd17336
Solute carrier organic anion transporters of the Major Facilitator Superfamily of transporters; ...
 448-518 6.78e-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: 41.07  E-value: 6.78e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568930475  448 CVCPSEcveSAQPVCGSDGHTYASECelhvHA-CTHQISLYVASA-GHCqTCGETVCTFGAVCSAGQCVCPRC 518
Cdd:cd17336   316 CNCSDS---SFSPVCGSDGITYFSPC----HAgCTSSDAGNGTKTySNC-SCINSGTATSSGCPPDCSVAPNC 380
MFS_SLCO4A_OATP4A cd17462
Solute carrier organic anion transporter 4A subfamily of the Major Facilitator Superfamily of ...
 597-691 8.01e-03

Solute carrier organic anion transporter 4A subfamily of the Major Facilitator Superfamily of transporters; The Solute carrier organic anion transporter 4A (SLCO4A), also called Organic anion-transporting polypeptide 4A (OATP4A), subfamily has one mammalian member, OATP4A1 (encoded by SLCO4A1). It is ubiquitously expressed and it mediates the Na(+)-independent transport of the thyroid hormones T3 (triiodo-L-thyronine), T4 (thyroxine) and rT3, and other organic anions such as estrone sulfate and taurocholate. OATP4A1 is the most abundantly expressed transporter colorectal cancer (CRC) and its role in the transport of estrone sulfate, which is used in hormone replacement therapy (HRT), affects the outcome of the treatment. The SLCO4A/OATP4A subfamily belongs to the Solute carrier organic anion transporter [SLCO, also called organic anion transporting polypeptides (OATPs) or Solute carrier family 21] family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.


Pssm-ID: 341020 [Multi-domain]  Cd Length: 427  Bit Score: 40.97  E-value: 8.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930475  597 PCVCDFSCQSVLKSPVCGSDGVTYSTECHlkkARCEARQELYVAAQGACRGptlapllpmasphCAqtpygCCQDNVTAA 676
Cdd:cd17462   326 LCNADCRCLEEIYSPVCGADGLMYYSPCH---AGCSEAYSDIRNGQKVYQD-------------CS-----CVAGNLSVG 384

                          90
                  ....*....|....*
gi 568930475  677 QGvGLAGCPSTCHCN 691
Cdd:cd17462   385 FG-EASAGKCTSNCN 398
KAZAL_PSTI cd01327
Kazal-type pancreatic secretory trypsin inhibitors (PSTI) and related proteins, including the ...
 179-212 9.84e-03

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


Pssm-ID: 238648  Cd Length: 45  Bit Score: 35.72  E-value: 9.84e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 568930475  179 VCGSDGVDYPSECQLLRHACANQEHIFKKFDGPC 212
Cdd:cd01327    12 VCGTDGVTYSNECLLCAENLKRQTNIRIKHDGEC 45
 
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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