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Conserved domains on  [gi|568930469|ref|XP_006538555|]
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agrin isoform X3 [Mus musculus]

Protein Classification

calcium-binding EGF-like domain-containing protein( domain architecture ID 11140811)

calcium-binding epidermal growth factor (EGF)-like domain-containing protein may play a crucial role in numerous protein-protein interactions

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Laminin_G_1 pfam00054
Laminin G domain;
1389-1520 3.19e-51

Laminin G domain;


:

Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 177.12  E-value: 3.19e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930469  1389 FRALETEGLLLYNGNARGKDFLALALLDGHVQFRFDTGSGPAVLTSLVPVEPGRWHRLELSRHWRQGTLSVDGEAPVVGE 1468
Cdd:pfam00054    1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGE 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 568930469  1469 SPSGTDG-LNLDTKLYVGGLPEEqvATVLDRTSVGIGLKGCIRMLDINNQQLE 1520
Cdd:pfam00054   81 SPLGATTdLDVDGPLYVGGLPSL--GVKKRRLAISPSFDGCIRDVIVNGKPLD 131
NtA pfam03146
Agrin NtA domain; Agrin is a multidomain heparan sulphate proteoglycan, that is a key ...
 33-148 7.34e-48

Agrin NtA domain; Agrin is a multidomain heparan sulphate proteoglycan, that is a key organizer for the induction of postsynaptic specializations at the neuromuscular junction. Binding of agrin to basement membranes requires the amino terminal (NtA) domain. This region mediates high affinity interaction with the coiled-coil domain of laminins. The binding of agrin to laminins via the NtA domain is subject to tissue-specific regulation. The NtA domain-containing form of agrin is expressed in non-neuronal cells or in neurons that project to non-neuronal cell such as motor neurons. The structure of this domain is an OB-fold.


:

Pssm-ID: 460825  Cd Length: 109  Bit Score: 166.42  E-value: 7.34e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930469    33 CPERALERREEEANVVLTGTVEEILNVDPVQHTYSCKVRVWRYLKGKDVVAQESLLDGGNKVVIGGFGDPLICDNQVSTG 112
Cdd:pfam03146    1 CPDRTLEEREEEANVVLTGTVEEVMNVDPDGKTYSASVRVKRVMKGKSLLTQLILLDGGNKVTVDGLGDPLICDSQVRRG 80

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 568930469   113 DTRIFFVNPAPPylwpahkNELMLNSSLMRITLRNL 148
Cdd:pfam03146   81 DTRIFFLNPAPD-------GELRLNSSLVRITLRNL 109
Laminin_G_1 pfam00054
Laminin G domain;
1657-1792 5.89e-46

Laminin G domain;


:

Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 162.10  E-value: 5.89e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930469  1657 FLARGPSGLLLYNGQKTDGkgDFVSLALHNRHLEFRYDLGKGAAIIRSKEPIALGTWVRVFLERNGRKGALQVGDGPRVL 1736
Cdd:pfam00054    1 FRTTEPSGLLLYNGTQTER--DFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPT 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 568930469  1737 GESPKSRKvphTMLNLKEPLYVGGAPDFSKLARGAAVASGFDGAIQLVSLRGHQLL 1792
Cdd:pfam00054   79 GESPLGAT---TDLDVDGPLYVGGLPSLGVKKRRLAISPSFDGCIRDVIVNGKPLD 131
Laminin_G_1 pfam00054
Laminin G domain;
1902-2032 1.96e-45

Laminin G domain;


:

Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 160.56  E-value: 1.96e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930469  1902 RTEATQGLVLWIGKVGERaDYMALAIVDGHLQLSYDLGSQPVVLRSTVKVNTNRWLRVRAHREHREGSLQVGNEAPVTGS 1981
Cdd:pfam00054    2 RTTEPSGLLLYNGTQTER-DFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGE 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568930469  1982 SPLGATQ-LDTDGALWLGGLQKLPVgQALPKAYGTGFVGCLRDVVVGHRQLH 2032
Cdd:pfam00054   81 SPLGATTdLDVDGPLYVGGLPSLGV-KKRRLAISPSFDGCIRDVIVNGKPLD 131
SEA smart00200
Domain found in sea urchin sperm protein, enterokinase, agrin; Proposed function of regulating ...
 1121-1245 4.48e-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: 4.48e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930469   1121 ATKAFQGVLELEGVEGQELFYTPEMADPKSELFGETARSIESTLDDLFRNSDVKKDFWSIRLRELGPGKLVRAIVDVHFD 1200
Cdd:smart00200    1 PTQSFGVSLSVLSVEGENLQYSPSLEDPSSEEYQELVRDVEKLLEQIYGKTDLKPDFVGTEVIEFRNGSVVVDLGLLFNE 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*
gi 568930469   1201 PTTAfqAPDVGQALLQQIQVSRpWALAVRRPlrEHVRFLDFDWFP 1245
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.
 795-837 3.52e-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: 71.23  E-value: 3.52e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 568930469   795 CHCNPHGSYSGTCDPVTGQCSCRPGVGGLRCDRCEPGFWNFRG 837
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPS 43
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 491-536 6.89e-13

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


:

Pssm-ID: 197624  Cd Length: 46  Bit Score: 64.62  E-value: 6.89e-13
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 568930469    491 ECQRVCSGGYDPVCGSDGVTYGSVCELESMACTLGREIRVARRGPC 536
Cdd:smart00280    1 DCPEACPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 556-601 1.17e-12

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


:

Pssm-ID: 197624  Cd Length: 46  Bit Score: 63.85  E-value: 1.17e-12
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 568930469    556 VCPSECVESAQPVCGSDGHTYASECELHVHACTHQISLYVASAGHC 601
Cdd:smart00280    1 DCPEACPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 198-244 1.29e-11

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


:

Pssm-ID: 197624  Cd Length: 46  Bit Score: 61.16  E-value: 1.29e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 568930469    198 VCKKNvCPAMVAPVCGSDASTYSNECELQRAQCNQQRRIRLLRQGPC 244
Cdd:smart00280    1 DCPEA-CPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 706-752 1.78e-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: 1.78e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 568930469    706 VCDFSCQSVLKsPVCGSDGVTYSTECHLKKARCEARQELYVAAQGAC 752
Cdd:smart00280    1 DCPEACPREYD-PVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 274-319 1.83e-10

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


:

Pssm-ID: 197624  Cd Length: 46  Bit Score: 57.69  E-value: 1.83e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 568930469    274 CPTTCFGAPDgTVCGSDGVDYPSECQLLRHACANQEHIFKKFDGPC 319
Cdd:smart00280    2 CPEACPREYD-PVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 621-666 6.58e-10

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


:

Pssm-ID: 197624  Cd Length: 46  Bit Score: 56.15  E-value: 6.58e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 568930469    621 VCPRCEHPPPGPVCGSDGVTYLSACELREAACQQQVQIEEARAGPC 666
Cdd:smart00280    1 DCPEACPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 924-971 8.16e-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: 8.16e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 568930469    924 VCPTlTCPEaNSTKVCGSDGVTYGNECQLKTIACRQRLDISIQSLGPC 971
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.
 849-885 1.83e-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: 55.05  E-value: 1.83e-09
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 568930469   849 CSCDPRGAVRDDCEQMTGLCSCRPGVAGPKCGQCPDG 885
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPG 37
Kazal_1 pfam00050
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 351-391 3.28e-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: 54.21  E-value: 3.28e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 568930469   351 CPAQHTPICGDDGVTYENDCVMSRIGAARGLLLQKVRSGQC 391
Cdd:pfam00050    9 CPRIYDPVCGTDGKTYSNECLFCAENGKRGTNLHKVHDGEC 49
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
 423-463 5.54e-09

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


:

Pssm-ID: 238052 [Multi-domain]  Cd Length: 41  Bit Score: 53.43  E-value: 5.54e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 568930469  423 CDGAYRPVCAQDGHTYDNDCWRQQAECRQQQTIPPKHQGPC 463
Cdd:cd00104     1 CPKEYDPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 1814-1846 4.54e-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: 4.54e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 568930469 1814 AVDNPCLNGGSCIPREATYECLCPGGFSGLHCE 1846
Cdd:cd00054     6 ASGNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 1322-1352 9.31e-03

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


:

Pssm-ID: 394967  Cd Length: 31  Bit Score: 35.44  E-value: 9.31e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 568930469  1322 CDSQPCLHGGTCqdLDSGKGFSCSCTAGRAG 1352
Cdd:pfam00008    1 CAPNPCSNGGTC--VDTPGGYTCICPEGYTG 29
 
Name Accession Description Interval E-value
Laminin_G_1 pfam00054
Laminin G domain;
1389-1520 3.19e-51

Laminin G domain;


Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 177.12  E-value: 3.19e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930469  1389 FRALETEGLLLYNGNARGKDFLALALLDGHVQFRFDTGSGPAVLTSLVPVEPGRWHRLELSRHWRQGTLSVDGEAPVVGE 1468
Cdd:pfam00054    1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGE 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 568930469  1469 SPSGTDG-LNLDTKLYVGGLPEEqvATVLDRTSVGIGLKGCIRMLDINNQQLE 1520
Cdd:pfam00054   81 SPLGATTdLDVDGPLYVGGLPSL--GVKKRRLAISPSFDGCIRDVIVNGKPLD 131
NtA pfam03146
Agrin NtA domain; Agrin is a multidomain heparan sulphate proteoglycan, that is a key ...
 33-148 7.34e-48

Agrin NtA domain; Agrin is a multidomain heparan sulphate proteoglycan, that is a key organizer for the induction of postsynaptic specializations at the neuromuscular junction. Binding of agrin to basement membranes requires the amino terminal (NtA) domain. This region mediates high affinity interaction with the coiled-coil domain of laminins. The binding of agrin to laminins via the NtA domain is subject to tissue-specific regulation. The NtA domain-containing form of agrin is expressed in non-neuronal cells or in neurons that project to non-neuronal cell such as motor neurons. The structure of this domain is an OB-fold.


Pssm-ID: 460825  Cd Length: 109  Bit Score: 166.42  E-value: 7.34e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930469    33 CPERALERREEEANVVLTGTVEEILNVDPVQHTYSCKVRVWRYLKGKDVVAQESLLDGGNKVVIGGFGDPLICDNQVSTG 112
Cdd:pfam03146    1 CPDRTLEEREEEANVVLTGTVEEVMNVDPDGKTYSASVRVKRVMKGKSLLTQLILLDGGNKVTVDGLGDPLICDSQVRRG 80

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 568930469   113 DTRIFFVNPAPPylwpahkNELMLNSSLMRITLRNL 148
Cdd:pfam03146   81 DTRIFFLNPAPD-------GELRLNSSLVRITLRNL 109
Laminin_G_1 pfam00054
Laminin G domain;
1657-1792 5.89e-46

Laminin G domain;


Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 162.10  E-value: 5.89e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930469  1657 FLARGPSGLLLYNGQKTDGkgDFVSLALHNRHLEFRYDLGKGAAIIRSKEPIALGTWVRVFLERNGRKGALQVGDGPRVL 1736
Cdd:pfam00054    1 FRTTEPSGLLLYNGTQTER--DFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPT 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 568930469  1737 GESPKSRKvphTMLNLKEPLYVGGAPDFSKLARGAAVASGFDGAIQLVSLRGHQLL 1792
Cdd:pfam00054   79 GESPLGAT---TDLDVDGPLYVGGLPSLGVKKRRLAISPSFDGCIRDVIVNGKPLD 131
Laminin_G_1 pfam00054
Laminin G domain;
1902-2032 1.96e-45

Laminin G domain;


Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 160.56  E-value: 1.96e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930469  1902 RTEATQGLVLWIGKVGERaDYMALAIVDGHLQLSYDLGSQPVVLRSTVKVNTNRWLRVRAHREHREGSLQVGNEAPVTGS 1981
Cdd:pfam00054    2 RTTEPSGLLLYNGTQTER-DFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGE 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568930469  1982 SPLGATQ-LDTDGALWLGGLQKLPVgQALPKAYGTGFVGCLRDVVVGHRQLH 2032
Cdd:pfam00054   81 SPLGATTdLDVDGPLYVGGLPSLGV-KKRRLAISPSFDGCIRDVIVNGKPLD 131
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
 1366-1515 2.21e-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: 2.21e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930469 1366 FKGHSFLAFPTLRA-YHTLRLALEFRALETEGLLLYNGNARGKDFLALALLDGHVQFRFDTGSGPAVLTSLVPVEPGRWH 1444
Cdd:cd00110     4 FSGSSYVRLPTLPApRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDGQWH 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568930469 1445 RLELSRHWRQGTLSVDGEAPVVGESPSGTDGLNLDTKLYVGGLPEEQVATvldRTSVGIGLKGCIRMLDIN 1515
Cdd:cd00110    84 SVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSP---GLPVSPGFVGCIRDLKVN 151
LamG smart00282
Laminin G domain;
1384-1517 1.41e-42

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 152.49  E-value: 1.41e-42
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930469   1384 RLALEFRALETEGLLLYNGNARGKDFLALALLDGHVQFRFDTGSGPAVLTS-LVPVEPGRWHRLELSRHWRQGTLSVDGE 1462
Cdd:smart00282    1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSdPTPLNDGQWHRVAVERNGRSVTLSVDGG 80

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 568930469   1463 APVVGESPSGTDGLNLDTKLYVGGLPEEQVATvldRTSVGIGLKGCIRMLDINNQ 1517
Cdd:smart00282   81 NRVSGESPGGLTILNLDGPLYLGGLPEDLKLP---PLPVTPGFRGCIRNLKVNGK 132
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
 1629-1786 8.53e-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: 8.53e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930469 1629 FNGFSYLELKGLHTFERDlgekMALEMVFLARGPSGLLLYNGQKTdgKGDFVSLALHNRHLEFRYDLGKGAAIIRSKEPI 1708
Cdd:cd00110     4 FSGSSYVRLPTLPAPRTR----LSISFSFRTTSPNGLLLYAGSQN--GGDFLALELEDGRLVLRYDLGSGSLVLSSKTPL 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568930469 1709 ALGTWVRVFLERNGRKGALQVgDGPRVLgESPKSRKvpHTMLNLKEPLYVGGAPDFSKLaRGAAVASGFDGAIQLVSL 1786
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 ...
 1859-2026 3.22e-33

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


Pssm-ID: 238058 [Multi-domain]  Cd Length: 151  Bit Score: 126.38  E-value: 3.22e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930469 1859 TLAFDGRTYIEYLNAVTESPETldsralfsekalqsnHFELSLRTEATQGLVLWIGkVGERADYMALAIVDGHLQLSYDL 1938
Cdd:cd00110     1 GVSFSGSSYVRLPTLPAPRTRL---------------SISFSFRTTSPNGLLLYAG-SQNGGDFLALELEDGRLVLRYDL 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930469 1939 GSQPVVLRSTVKVNTNRWLRVRAHREHREGSLQVGNEAPVTGSSPLGATQLDTDGALWLGGLQklPVGQALPKAYGTGFV 2018
Cdd:cd00110    65 GSGSLVLSSKTPLNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLP--EDLKSPGLPVSPGFV 142


                  ....*...
gi 568930469 2019 GCLRDVVV 2026
Cdd:cd00110   143 GCIRDLKV 150
LamG smart00282
Laminin G domain;
1896-2029 4.64e-32

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 122.45  E-value: 4.64e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930469   1896 HFELSLRTEATQGLVLWIGkVGERADYMALAIVDGHLQLSYDLGSQPVVLRST-VKVNTNRWLRVRAHREHREGSLQVGN 1974
Cdd:smart00282    1 SISFSFRTTSPNGLLLYAG-SKGGGDYLALELRDGRLVLRYDLGSGPARLTSDpTPLNDGQWHRVAVERNGRSVTLSVDG 79

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 568930469   1975 EAPVTGSSPLGATQLDTDGALWLGGlqkLPVGQALPK-AYGTGFVGCLRDVVVGHR 2029
Cdd:smart00282   80 GNRVSGESPGGLTILNLDGPLYLGG---LPEDLKLPPlPVTPGFRGCIRNLKVNGK 132
LamG smart00282
Laminin G domain;
1653-1789 1.20e-31

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 121.29  E-value: 1.20e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930469   1653 LEMVFLARGPSGLLLYNGQKtdGKGDFVSLALHNRHLEFRYDLGKGAAIIRSK-EPIALGTWVRVFLERNGRKGALQVGD 1731
Cdd:smart00282    2 ISFSFRTTSPNGLLLYAGSK--GGGDYLALELRDGRLVLRYDLGSGPARLTSDpTPLNDGQWHRVAVERNGRSVTLSVDG 79

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 568930469   1732 GPRVLGESPKSrkvpHTMLNLKEPLYVGGAPDFSKLARGaAVASGFDGAIQLVSLRGH 1789
Cdd:smart00282   80 GNRVSGESPGG----LTILNLDGPLYLGGLPEDLKLPPL-PVTPGFRGCIRNLKVNGK 132
SEA smart00200
Domain found in sea urchin sperm protein, enterokinase, agrin; Proposed function of regulating ...
 1121-1245 4.48e-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: 4.48e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930469   1121 ATKAFQGVLELEGVEGQELFYTPEMADPKSELFGETARSIESTLDDLFRNSDVKKDFWSIRLRELGPGKLVRAIVDVHFD 1200
Cdd:smart00200    1 PTQSFGVSLSVLSVEGENLQYSPSLEDPSSEEYQELVRDVEKLLEQIYGKTDLKPDFVGTEVIEFRNGSVVVDLGLLFNE 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*
gi 568930469   1201 PTTAfqAPDVGQALLQQIQVSRpWALAVRRPlrEHVRFLDFDWFP 1245
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.
 795-837 3.52e-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: 71.23  E-value: 3.52e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 568930469   795 CHCNPHGSYSGTCDPVTGQCSCRPGVGGLRCDRCEPGFWNFRG 837
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPS 43
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 795-835 5.53e-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: 70.85  E-value: 5.53e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 568930469  795 CHCNPHGSYSGTCDPVTGQCSCRPGVGGLRCDRCEPGFWNF 835
Cdd:cd00055     2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGL 42
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
795-837 7.95e-14

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 67.34  E-value: 7.95e-14
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 568930469    795 CHCNPHGSYSGTCDPVTGQCSCRPGVGGLRCDRCEPGFWNFRG 837
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 491-536 6.89e-13

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


Pssm-ID: 197624  Cd Length: 46  Bit Score: 64.62  E-value: 6.89e-13
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 568930469    491 ECQRVCSGGYDPVCGSDGVTYGSVCELESMACTLGREIRVARRGPC 536
Cdd:smart00280    1 DCPEACPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 556-601 1.17e-12

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


Pssm-ID: 197624  Cd Length: 46  Bit Score: 63.85  E-value: 1.17e-12
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 568930469    556 VCPSECVESAQPVCGSDGHTYASECELHVHACTHQISLYVASAGHC 601
Cdd:smart00280    1 DCPEACPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 198-244 1.29e-11

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


Pssm-ID: 197624  Cd Length: 46  Bit Score: 61.16  E-value: 1.29e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 568930469    198 VCKKNvCPAMVAPVCGSDASTYSNECELQRAQCNQQRRIRLLRQGPC 244
Cdd:smart00280    1 DCPEA-CPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 706-752 1.78e-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: 1.78e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 568930469    706 VCDFSCQSVLKsPVCGSDGVTYSTECHLKKARCEARQELYVAAQGAC 752
Cdd:smart00280    1 DCPEACPREYD-PVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
SEA pfam01390
SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed ...
 1139-1217 2.29e-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: 2.29e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930469  1139 LFYTPEMADPKSELFGETARSIESTLDDLFRNSDVKKDFWS---IRLRELGPGklVRAIVDVHFDPTTAFQAPDVGQ--- 1212
Cdd:pfam01390   12 LQYTPDLGNPSSQEFKSLSRRIESLLNELFRNSSLRKQYIKshvLRLRPDGGS--VVVDVVLVFRFPSTEPALDREKlie 89


                   ....*
gi 568930469  1213 ALLQQ 1217
Cdd:pfam01390   90 EILRQ 94
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
 496-536 9.38e-11

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


Pssm-ID: 238052 [Multi-domain]  Cd Length: 41  Bit Score: 58.44  E-value: 9.38e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 568930469  496 CSGGYDPVCGSDGVTYGSVCELESMACTLGREIRVARRGPC 536
Cdd:cd00104     1 CPKEYDPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
 204-244 1.25e-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: 1.25e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 568930469  204 CPAMVAPVCGSDASTYSNECELQRAQCNQQRRIRLLRQGPC 244
Cdd:cd00104     1 CPKEYDPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 274-319 1.83e-10

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


Pssm-ID: 197624  Cd Length: 46  Bit Score: 57.69  E-value: 1.83e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 568930469    274 CPTTCFGAPDgTVCGSDGVDYPSECQLLRHACANQEHIFKKFDGPC 319
Cdd:smart00280    2 CPEACPREYD-PVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 621-666 6.58e-10

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


Pssm-ID: 197624  Cd Length: 46  Bit Score: 56.15  E-value: 6.58e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 568930469    621 VCPRCEHPPPGPVCGSDGVTYLSACELREAACQQQVQIEEARAGPC 666
Cdd:smart00280    1 DCPEACPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 924-971 8.16e-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: 8.16e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 568930469    924 VCPTlTCPEaNSTKVCGSDGVTYGNECQLKTIACRQRLDISIQSLGPC 971
Cdd:smart00280    1 DCPE-ACPR-EYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
 561-601 1.00e-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: 1.00e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 568930469  561 CVESAQPVCGSDGHTYASECELHVHACTHQISLYVASAGHC 601
Cdd:cd00104     1 CPKEYDPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 849-885 1.83e-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: 55.05  E-value: 1.83e-09
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 568930469   849 CSCDPRGAVRDDCEQMTGLCSCRPGVAGPKCGQCPDG 885
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPG 37
Kazal_1 pfam00050
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 351-391 3.28e-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: 54.21  E-value: 3.28e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 568930469   351 CPAQHTPICGDDGVTYENDCVMSRIGAARGLLLQKVRSGQC 391
Cdd:pfam00050    9 CPRIYDPVCGTDGKTYSNECLFCAENGKRGTNLHKVHDGEC 49
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
 622-666 3.33e-09

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


Pssm-ID: 238052 [Multi-domain]  Cd Length: 41  Bit Score: 54.20  E-value: 3.33e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 568930469  622 CPRCEHPppgpVCGSDGVTYLSACELREAACQQQVQIEEARAGPC 666
Cdd:cd00104     1 CPKEYDP----VCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
 423-463 5.54e-09

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


Pssm-ID: 238052 [Multi-domain]  Cd Length: 41  Bit Score: 53.43  E-value: 5.54e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 568930469  423 CDGAYRPVCAQDGHTYDNDCWRQQAECRQQQTIPPKHQGPC 463
Cdd:cd00104     1 CPKEYDPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
 930-971 2.29e-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: 2.29e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 568930469  930 CPEaNSTKVCGSDGVTYGNECQLKTIACRQRLDISIQSLGPC 971
Cdd:cd00104     1 CPK-EYDPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
 717-752 3.07e-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: 3.07e-08
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 568930469  717 SPVCGSDGVTYSTECHLKKARCEARQELYVAAQGAC 752
Cdd:cd00104     6 DPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 848-885 3.56e-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: 51.59  E-value: 3.56e-08
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 568930469  848 PCSCDPRGAVRDDCEQMTGLCSCRPGVAGPKCGQCPDG 885
Cdd:cd00055     1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPG 38
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 418-463 5.66e-08

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


Pssm-ID: 197624  Cd Length: 46  Bit Score: 50.76  E-value: 5.66e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 568930469    418 CDRVtCDGAYRPVCAQDGHTYDNDCWRQQAECRQQQTIPPKHQGPC 463
Cdd:smart00280    2 CPEA-CPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
 286-319 1.31e-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: 49.58  E-value: 1.31e-07
                          10        20        30
                  ....*....|....*....|....*....|....
gi 568930469  286 VCGSDGVDYPSECQLLRHACANQEHIFKKFDGPC 319
Cdd:cd00104     8 VCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 707-744 1.52e-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: 49.80  E-value: 1.52e-07
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 568930469   707 CDFSCQSVLKSPVCGSDGVTYSTECHLKKARCEARQEL 744
Cdd:pfam07648    2 CNCQCPKTEYEPVCGSDGVTYPSPCALCAAGCKLGKEV 39
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
849-885 1.74e-07

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 49.23  E-value: 1.74e-07
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 568930469    849 CSCDPRGAVRDDCEQMTGLCSCRPGVAGPKCGQCPDG 885
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPG 37
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 620-666 3.99e-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: 45.56  E-value: 3.99e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 568930469   620 CVCPRCEHPPPGPVCGSDGVTYLSACELREAACQQQVQIEEARA---GPC 666
Cdd:pfam07648    1 NCNCQCPKTEYEPVCGSDGVTYPSPCALCAAGCKLGKEVKEEKVkydGSC 50
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 1814-1846 4.54e-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: 4.54e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 568930469 1814 AVDNPCLNGGSCIPREATYECLCPGGFSGLHCE 1846
Cdd:cd00054     6 ASGNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
Kazal_1 pfam00050
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 200-244 6.27e-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: 6.27e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 568930469   200 KKNVCPAMVAPVCGSDASTYSNECELQRAQCNQQRRIRLLRQGPC 244
Cdd:pfam00050    5 PSGACPRIYDPVCGTDGKTYSNECLFCAENGKRGTNLHKVHDGEC 49
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 348-391 3.70e-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: 3.70e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 568930469    348 PENCPAQHTPICGDDGVTYENDCVMSRIGAARGLLLQKVRSGQC 391
Cdd:smart00280    3 PEACPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
Kazal_1 pfam00050
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 496-536 4.34e-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: 4.34e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 568930469   496 CSGGYDPVCGSDGVTYGSVCELESMACTLGREIRVARRGPC 536
Cdd:pfam00050    9 CPRIYDPVCGTDGKTYSNECLFCAENGKRGTNLHKVHDGEC 49
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
 351-391 9.20e-05

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: 41.49  E-value: 9.20e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 568930469  351 CPAQHTPICGDDGVTYENDCVMSRIGAARGLLLQKVRSGQC 391
Cdd:cd00104     1 CPKEYDPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 554-593 1.44e-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: 41.32  E-value: 1.44e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 568930469   554 RCVCPsecVESAQPVCGSDGHTYASECELHVHACTHQISL 593
Cdd:pfam07648    3 NCQCP---KTEYEPVCGSDGVTYPSPCALCAAGCKLGKEV 39
EGF_CA smart00179
Calcium-binding EGF-like domain;
1814-1846 1.76e-04

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 40.69  E-value: 1.76e-04
                            10        20        30
                    ....*....|....*....|....*....|....
gi 568930469   1814 AVDNPCLNGGSCIPREATYECLCPGGFS-GLHCE 1846
Cdd:smart00179    6 ASGNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 274-319 2.15e-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: 2.15e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 568930469   274 CPTTCFGAPDGTVCGSDGVDYPSECQLLRHACANQEHIFK---KFDGPC 319
Cdd:pfam07648    2 CNCQCPKTEYEPVCGSDGVTYPSPCALCAAGCKLGKEVKEekvKYDGSC 50
Kazal_1 pfam00050
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 926-971 2.18e-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: 40.73  E-value: 2.18e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 568930469   926 PTLTCPeANSTKVCGSDGVTYGNECQLKTIACRQRLDISIQSLGPC 971
Cdd:pfam00050    5 PSGACP-RIYDPVCGTDGKTYSNECLFCAENGKRGTNLHKVHDGEC 49
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 416-463 3.56e-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: 3.56e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 568930469   416 CSCDRVTcdgaYRPVCAQDGHTYDNDCWRQQAECRQQQTI---PPKHQGPC 463
Cdd:pfam07648    4 CQCPKTE----YEPVCGSDGVTYPSPCALCAAGCKLGKEVkeeKVKYDGSC 50
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 1816-1844 2.13e-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: 37.36  E-value: 2.13e-03
                           10        20
                   ....*....|....*....|....*....
gi 568930469  1816 DNPCLNGGSCIPREATYECLCPGGFSGLH 1844
Cdd:pfam00008    3 PNPCSNGGTCVDTPGGYTCICPEGYTGKR 31
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 1322-1352 9.31e-03

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


Pssm-ID: 394967  Cd Length: 31  Bit Score: 35.44  E-value: 9.31e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 568930469  1322 CDSQPCLHGGTCqdLDSGKGFSCSCTAGRAG 1352
Cdd:pfam00008    1 CAPNPCSNGGTC--VDTPGGYTCICPEGYTG 29
 
Name Accession Description Interval E-value
Laminin_G_1 pfam00054
Laminin G domain;
1389-1520 3.19e-51

Laminin G domain;


Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 177.12  E-value: 3.19e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930469  1389 FRALETEGLLLYNGNARGKDFLALALLDGHVQFRFDTGSGPAVLTSLVPVEPGRWHRLELSRHWRQGTLSVDGEAPVVGE 1468
Cdd:pfam00054    1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGE 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 568930469  1469 SPSGTDG-LNLDTKLYVGGLPEEqvATVLDRTSVGIGLKGCIRMLDINNQQLE 1520
Cdd:pfam00054   81 SPLGATTdLDVDGPLYVGGLPSL--GVKKRRLAISPSFDGCIRDVIVNGKPLD 131
NtA pfam03146
Agrin NtA domain; Agrin is a multidomain heparan sulphate proteoglycan, that is a key ...
 33-148 7.34e-48

Agrin NtA domain; Agrin is a multidomain heparan sulphate proteoglycan, that is a key organizer for the induction of postsynaptic specializations at the neuromuscular junction. Binding of agrin to basement membranes requires the amino terminal (NtA) domain. This region mediates high affinity interaction with the coiled-coil domain of laminins. The binding of agrin to laminins via the NtA domain is subject to tissue-specific regulation. The NtA domain-containing form of agrin is expressed in non-neuronal cells or in neurons that project to non-neuronal cell such as motor neurons. The structure of this domain is an OB-fold.


Pssm-ID: 460825  Cd Length: 109  Bit Score: 166.42  E-value: 7.34e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930469    33 CPERALERREEEANVVLTGTVEEILNVDPVQHTYSCKVRVWRYLKGKDVVAQESLLDGGNKVVIGGFGDPLICDNQVSTG 112
Cdd:pfam03146    1 CPDRTLEEREEEANVVLTGTVEEVMNVDPDGKTYSASVRVKRVMKGKSLLTQLILLDGGNKVTVDGLGDPLICDSQVRRG 80

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 568930469   113 DTRIFFVNPAPPylwpahkNELMLNSSLMRITLRNL 148
Cdd:pfam03146   81 DTRIFFLNPAPD-------GELRLNSSLVRITLRNL 109
Laminin_G_1 pfam00054
Laminin G domain;
1657-1792 5.89e-46

Laminin G domain;


Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 162.10  E-value: 5.89e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930469  1657 FLARGPSGLLLYNGQKTDGkgDFVSLALHNRHLEFRYDLGKGAAIIRSKEPIALGTWVRVFLERNGRKGALQVGDGPRVL 1736
Cdd:pfam00054    1 FRTTEPSGLLLYNGTQTER--DFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPT 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 568930469  1737 GESPKSRKvphTMLNLKEPLYVGGAPDFSKLARGAAVASGFDGAIQLVSLRGHQLL 1792
Cdd:pfam00054   79 GESPLGAT---TDLDVDGPLYVGGLPSLGVKKRRLAISPSFDGCIRDVIVNGKPLD 131
Laminin_G_1 pfam00054
Laminin G domain;
1902-2032 1.96e-45

Laminin G domain;


Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 160.56  E-value: 1.96e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930469  1902 RTEATQGLVLWIGKVGERaDYMALAIVDGHLQLSYDLGSQPVVLRSTVKVNTNRWLRVRAHREHREGSLQVGNEAPVTGS 1981
Cdd:pfam00054    2 RTTEPSGLLLYNGTQTER-DFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGE 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568930469  1982 SPLGATQ-LDTDGALWLGGLQKLPVgQALPKAYGTGFVGCLRDVVVGHRQLH 2032
Cdd:pfam00054   81 SPLGATTdLDVDGPLYVGGLPSLGV-KKRRLAISPSFDGCIRDVIVNGKPLD 131
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
 1366-1515 2.21e-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: 2.21e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930469 1366 FKGHSFLAFPTLRA-YHTLRLALEFRALETEGLLLYNGNARGKDFLALALLDGHVQFRFDTGSGPAVLTSLVPVEPGRWH 1444
Cdd:cd00110     4 FSGSSYVRLPTLPApRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDGQWH 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568930469 1445 RLELSRHWRQGTLSVDGEAPVVGESPSGTDGLNLDTKLYVGGLPEEQVATvldRTSVGIGLKGCIRMLDIN 1515
Cdd:cd00110    84 SVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSP---GLPVSPGFVGCIRDLKVN 151
LamG smart00282
Laminin G domain;
1384-1517 1.41e-42

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 152.49  E-value: 1.41e-42
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930469   1384 RLALEFRALETEGLLLYNGNARGKDFLALALLDGHVQFRFDTGSGPAVLTS-LVPVEPGRWHRLELSRHWRQGTLSVDGE 1462
Cdd:smart00282    1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSdPTPLNDGQWHRVAVERNGRSVTLSVDGG 80

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 568930469   1463 APVVGESPSGTDGLNLDTKLYVGGLPEEQVATvldRTSVGIGLKGCIRMLDINNQ 1517
Cdd:smart00282   81 NRVSGESPGGLTILNLDGPLYLGGLPEDLKLP---PLPVTPGFRGCIRNLKVNGK 132
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
 1629-1786 8.53e-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: 8.53e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930469 1629 FNGFSYLELKGLHTFERDlgekMALEMVFLARGPSGLLLYNGQKTdgKGDFVSLALHNRHLEFRYDLGKGAAIIRSKEPI 1708
Cdd:cd00110     4 FSGSSYVRLPTLPAPRTR----LSISFSFRTTSPNGLLLYAGSQN--GGDFLALELEDGRLVLRYDLGSGSLVLSSKTPL 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568930469 1709 ALGTWVRVFLERNGRKGALQVgDGPRVLgESPKSRKvpHTMLNLKEPLYVGGAPDFSKLaRGAAVASGFDGAIQLVSL 1786
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 ...
 1859-2026 3.22e-33

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


Pssm-ID: 238058 [Multi-domain]  Cd Length: 151  Bit Score: 126.38  E-value: 3.22e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930469 1859 TLAFDGRTYIEYLNAVTESPETldsralfsekalqsnHFELSLRTEATQGLVLWIGkVGERADYMALAIVDGHLQLSYDL 1938
Cdd:cd00110     1 GVSFSGSSYVRLPTLPAPRTRL---------------SISFSFRTTSPNGLLLYAG-SQNGGDFLALELEDGRLVLRYDL 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930469 1939 GSQPVVLRSTVKVNTNRWLRVRAHREHREGSLQVGNEAPVTGSSPLGATQLDTDGALWLGGLQklPVGQALPKAYGTGFV 2018
Cdd:cd00110    65 GSGSLVLSSKTPLNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLP--EDLKSPGLPVSPGFV 142


                  ....*...
gi 568930469 2019 GCLRDVVV 2026
Cdd:cd00110   143 GCIRDLKV 150
LamG smart00282
Laminin G domain;
1896-2029 4.64e-32

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 122.45  E-value: 4.64e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930469   1896 HFELSLRTEATQGLVLWIGkVGERADYMALAIVDGHLQLSYDLGSQPVVLRST-VKVNTNRWLRVRAHREHREGSLQVGN 1974
Cdd:smart00282    1 SISFSFRTTSPNGLLLYAG-SKGGGDYLALELRDGRLVLRYDLGSGPARLTSDpTPLNDGQWHRVAVERNGRSVTLSVDG 79

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 568930469   1975 EAPVTGSSPLGATQLDTDGALWLGGlqkLPVGQALPK-AYGTGFVGCLRDVVVGHR 2029
Cdd:smart00282   80 GNRVSGESPGGLTILNLDGPLYLGG---LPEDLKLPPlPVTPGFRGCIRNLKVNGK 132
LamG smart00282
Laminin G domain;
1653-1789 1.20e-31

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 121.29  E-value: 1.20e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930469   1653 LEMVFLARGPSGLLLYNGQKtdGKGDFVSLALHNRHLEFRYDLGKGAAIIRSK-EPIALGTWVRVFLERNGRKGALQVGD 1731
Cdd:smart00282    2 ISFSFRTTSPNGLLLYAGSK--GGGDYLALELRDGRLVLRYDLGSGPARLTSDpTPLNDGQWHRVAVERNGRSVTLSVDG 79

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 568930469   1732 GPRVLGESPKSrkvpHTMLNLKEPLYVGGAPDFSKLARGaAVASGFDGAIQLVSLRGH 1789
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 ...
 1389-1517 3.33e-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: 3.33e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930469  1389 FRALETEGLLLYNGNARGkDFLALALLDGHVQFRFDTGSGPAVLTSL-VPVEPGRWHRLELSRHWRQGTLSVDGEAPVVG 1467
Cdd:pfam02210    1 FRTRQPNGLLLYAGGGGS-DFLALELVNGRLVLRYDLGSGPESLLSSgKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSS 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 568930469  1468 ESPSGTDGLNLDTKLYVGGLPEEqvaTVLDRTSVGIGLKGCIRMLDINNQ 1517
Cdd:pfam02210   80 LPPGESLLLNLNGPLYLGGLPPL---LLLPALPVRAGFVGCIRDVRVNGE 126
SEA smart00200
Domain found in sea urchin sperm protein, enterokinase, agrin; Proposed function of regulating ...
 1121-1245 4.48e-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: 4.48e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930469   1121 ATKAFQGVLELEGVEGQELFYTPEMADPKSELFGETARSIESTLDDLFRNSDVKKDFWSIRLRELGPGKLVRAIVDVHFD 1200
Cdd:smart00200    1 PTQSFGVSLSVLSVEGENLQYSPSLEDPSSEEYQELVRDVEKLLEQIYGKTDLKPDFVGTEVIEFRNGSVVVDLGLLFNE 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*
gi 568930469   1201 PTTAfqAPDVGQALLQQIQVSRpWALAVRRPlrEHVRFLDFDWFP 1245
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 ...
 1901-2029 3.38e-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: 3.38e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930469  1901 LRTEATQGLVLWIGkvGERADYMALAIVDGHLQLSYDLGSQPVVLRST-VKVNTNRWLRVRAHREHREGSLQVGNEAPVT 1979
Cdd:pfam02210    1 FRTRQPNGLLLYAG--GGGSDFLALELVNGRLVLRYDLGSGPESLLSSgKNLNDGQWHSVRVERNGNTLTLSVDGQTVVS 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 568930469  1980 GSSPLGATQLDTDGALWLGGLQKLPVGQALPkaYGTGFVGCLRDVVVGHR 2029
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 ...
 1657-1789 1.58e-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: 1.58e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930469  1657 FLARGPSGLLLYNGqktDGKGDFVSLALHNRHLEFRYDLGKGAAIIRS-KEPIALGTWVRVFLERNGRKGALQVGDGPRV 1735
Cdd:pfam02210    1 FRTRQPNGLLLYAG---GGGSDFLALELVNGRLVLRYDLGSGPESLLSsGKNLNDGQWHSVRVERNGNTLTLSVDGQTVV 77

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 568930469  1736 LGESPKsrkvPHTMLNLKEPLYVGGAPDFSKLaRGAAVASGFDGAIQLVSLRGH 1789
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.
 795-837 3.52e-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: 71.23  E-value: 3.52e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 568930469   795 CHCNPHGSYSGTCDPVTGQCSCRPGVGGLRCDRCEPGFWNFRG 837
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPS 43
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 795-835 5.53e-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: 70.85  E-value: 5.53e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 568930469  795 CHCNPHGSYSGTCDPVTGQCSCRPGVGGLRCDRCEPGFWNF 835
Cdd:cd00055     2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGL 42
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
795-837 7.95e-14

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 67.34  E-value: 7.95e-14
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 568930469    795 CHCNPHGSYSGTCDPVTGQCSCRPGVGGLRCDRCEPGFWNFRG 837
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 491-536 6.89e-13

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


Pssm-ID: 197624  Cd Length: 46  Bit Score: 64.62  E-value: 6.89e-13
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 568930469    491 ECQRVCSGGYDPVCGSDGVTYGSVCELESMACTLGREIRVARRGPC 536
Cdd:smart00280    1 DCPEACPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 556-601 1.17e-12

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


Pssm-ID: 197624  Cd Length: 46  Bit Score: 63.85  E-value: 1.17e-12
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 568930469    556 VCPSECVESAQPVCGSDGHTYASECELHVHACTHQISLYVASAGHC 601
Cdd:smart00280    1 DCPEACPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 198-244 1.29e-11

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


Pssm-ID: 197624  Cd Length: 46  Bit Score: 61.16  E-value: 1.29e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 568930469    198 VCKKNvCPAMVAPVCGSDASTYSNECELQRAQCNQQRRIRLLRQGPC 244
Cdd:smart00280    1 DCPEA-CPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 706-752 1.78e-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: 1.78e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 568930469    706 VCDFSCQSVLKsPVCGSDGVTYSTECHLKKARCEARQELYVAAQGAC 752
Cdd:smart00280    1 DCPEACPREYD-PVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
SEA pfam01390
SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed ...
 1139-1217 2.29e-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: 2.29e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930469  1139 LFYTPEMADPKSELFGETARSIESTLDDLFRNSDVKKDFWS---IRLRELGPGklVRAIVDVHFDPTTAFQAPDVGQ--- 1212
Cdd:pfam01390   12 LQYTPDLGNPSSQEFKSLSRRIESLLNELFRNSSLRKQYIKshvLRLRPDGGS--VVVDVVLVFRFPSTEPALDREKlie 89


                   ....*
gi 568930469  1213 ALLQQ 1217
Cdd:pfam01390   90 EILRQ 94
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
 496-536 9.38e-11

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


Pssm-ID: 238052 [Multi-domain]  Cd Length: 41  Bit Score: 58.44  E-value: 9.38e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 568930469  496 CSGGYDPVCGSDGVTYGSVCELESMACTLGREIRVARRGPC 536
Cdd:cd00104     1 CPKEYDPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
 204-244 1.25e-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: 1.25e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 568930469  204 CPAMVAPVCGSDASTYSNECELQRAQCNQQRRIRLLRQGPC 244
Cdd:cd00104     1 CPKEYDPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 274-319 1.83e-10

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


Pssm-ID: 197624  Cd Length: 46  Bit Score: 57.69  E-value: 1.83e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 568930469    274 CPTTCFGAPDgTVCGSDGVDYPSECQLLRHACANQEHIFKKFDGPC 319
Cdd:smart00280    2 CPEACPREYD-PVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 621-666 6.58e-10

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


Pssm-ID: 197624  Cd Length: 46  Bit Score: 56.15  E-value: 6.58e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 568930469    621 VCPRCEHPPPGPVCGSDGVTYLSACELREAACQQQVQIEEARAGPC 666
Cdd:smart00280    1 DCPEACPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 924-971 8.16e-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: 8.16e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 568930469    924 VCPTlTCPEaNSTKVCGSDGVTYGNECQLKTIACRQRLDISIQSLGPC 971
Cdd:smart00280    1 DCPE-ACPR-EYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
 561-601 1.00e-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: 1.00e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 568930469  561 CVESAQPVCGSDGHTYASECELHVHACTHQISLYVASAGHC 601
Cdd:cd00104     1 CPKEYDPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 849-885 1.83e-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: 55.05  E-value: 1.83e-09
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 568930469   849 CSCDPRGAVRDDCEQMTGLCSCRPGVAGPKCGQCPDG 885
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPG 37
Kazal_1 pfam00050
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 351-391 3.28e-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: 54.21  E-value: 3.28e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 568930469   351 CPAQHTPICGDDGVTYENDCVMSRIGAARGLLLQKVRSGQC 391
Cdd:pfam00050    9 CPRIYDPVCGTDGKTYSNECLFCAENGKRGTNLHKVHDGEC 49
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
 622-666 3.33e-09

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


Pssm-ID: 238052 [Multi-domain]  Cd Length: 41  Bit Score: 54.20  E-value: 3.33e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 568930469  622 CPRCEHPppgpVCGSDGVTYLSACELREAACQQQVQIEEARAGPC 666
Cdd:cd00104     1 CPKEYDP----VCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
 423-463 5.54e-09

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


Pssm-ID: 238052 [Multi-domain]  Cd Length: 41  Bit Score: 53.43  E-value: 5.54e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 568930469  423 CDGAYRPVCAQDGHTYDNDCWRQQAECRQQQTIPPKHQGPC 463
Cdd:cd00104     1 CPKEYDPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
 930-971 2.29e-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: 2.29e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 568930469  930 CPEaNSTKVCGSDGVTYGNECQLKTIACRQRLDISIQSLGPC 971
Cdd:cd00104     1 CPK-EYDPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
 717-752 3.07e-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: 3.07e-08
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 568930469  717 SPVCGSDGVTYSTECHLKKARCEARQELYVAAQGAC 752
Cdd:cd00104     6 DPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 848-885 3.56e-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: 51.59  E-value: 3.56e-08
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 568930469  848 PCSCDPRGAVRDDCEQMTGLCSCRPGVAGPKCGQCPDG 885
Cdd:cd00055     1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPG 38
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 418-463 5.66e-08

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


Pssm-ID: 197624  Cd Length: 46  Bit Score: 50.76  E-value: 5.66e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 568930469    418 CDRVtCDGAYRPVCAQDGHTYDNDCWRQQAECRQQQTIPPKHQGPC 463
Cdd:smart00280    2 CPEA-CPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
 286-319 1.31e-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: 49.58  E-value: 1.31e-07
                          10        20        30
                  ....*....|....*....|....*....|....
gi 568930469  286 VCGSDGVDYPSECQLLRHACANQEHIFKKFDGPC 319
Cdd:cd00104     8 VCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 707-744 1.52e-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: 49.80  E-value: 1.52e-07
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 568930469   707 CDFSCQSVLKSPVCGSDGVTYSTECHLKKARCEARQEL 744
Cdd:pfam07648    2 CNCQCPKTEYEPVCGSDGVTYPSPCALCAAGCKLGKEV 39
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
849-885 1.74e-07

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 49.23  E-value: 1.74e-07
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 568930469    849 CSCDPRGAVRDDCEQMTGLCSCRPGVAGPKCGQCPDG 885
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPG 37
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 620-666 3.99e-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: 45.56  E-value: 3.99e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 568930469   620 CVCPRCEHPPPGPVCGSDGVTYLSACELREAACQQQVQIEEARA---GPC 666
Cdd:pfam07648    1 NCNCQCPKTEYEPVCGSDGVTYPSPCALCAAGCKLGKEVKEEKVkydGSC 50
KAZAL_PSTI cd01327
Kazal-type pancreatic secretory trypsin inhibitors (PSTI) and related proteins, including the ...
 201-244 4.36e-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: 4.36e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 568930469  201 KNVCPAMVAPVCGSDASTYSNECELQRAQCNQQRRIRLLRQGPC 244
Cdd:cd01327     2 VFGCPKDYDPVCGTDGVTYSNECLLCAENLKRQTNIRIKHDGEC 45
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 1814-1846 4.54e-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: 4.54e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 568930469 1814 AVDNPCLNGGSCIPREATYECLCPGGFSGLHCE 1846
Cdd:cd00054     6 ASGNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
Kazal_1 pfam00050
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 200-244 6.27e-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: 6.27e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 568930469   200 KKNVCPAMVAPVCGSDASTYSNECELQRAQCNQQRRIRLLRQGPC 244
Cdd:pfam00050    5 PSGACPRIYDPVCGTDGKTYSNECLFCAENGKRGTNLHKVHDGEC 49
FSL_SPARC cd01328
Follistatin-like SPARC (secreted protein, acidic, and rich in cysteines) domain; SPARC/BM-40 ...
 469-524 3.55e-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: 3.55e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930469  469 PCRGAQCAFGATCTV-KNGKAVCECQRVCSGGYDP---VCGSDGVTYGSVCELESMACTL 524
Cdd:cd01328     1 PCENHHCGAGKVCEVdDENTPKCVCIDPCPEEVDDrrkVCTNDNETFDSDCELYRTRCLC 60
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 348-391 3.70e-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: 3.70e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 568930469    348 PENCPAQHTPICGDDGVTYENDCVMSRIGAARGLLLQKVRSGQC 391
Cdd:smart00280    3 PEACPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 209-244 4.30e-05

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


Pssm-ID: 400135  Cd Length: 50  Bit Score: 42.87  E-value: 4.30e-05
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 568930469   209 APVCGSDASTYSNECELQRAQCNQQRRIR---LLRQGPC 244
Cdd:pfam07648   12 EPVCGSDGVTYPSPCALCAAGCKLGKEVKeekVKYDGSC 50
Kazal_1 pfam00050
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 496-536 4.34e-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: 4.34e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 568930469   496 CSGGYDPVCGSDGVTYGSVCELESMACTLGREIRVARRGPC 536
Cdd:pfam00050    9 CPRIYDPVCGTDGKTYSNECLFCAENGKRGTNLHKVHDGEC 49
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 491-536 5.18e-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: 5.18e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 568930469   491 ECQRVCSG-GYDPVCGSDGVTYGSVCELESMACTLGREIR---VARRGPC 536
Cdd:pfam07648    1 NCNCQCPKtEYEPVCGSDGVTYPSPCALCAAGCKLGKEVKeekVKYDGSC 50
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
 351-391 9.20e-05

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: 41.49  E-value: 9.20e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 568930469  351 CPAQHTPICGDDGVTYENDCVMSRIGAARGLLLQKVRSGQC 391
Cdd:cd00104     1 CPKEYDPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
KAZAL_PSTI cd01327
Kazal-type pancreatic secretory trypsin inhibitors (PSTI) and related proteins, including the ...
 496-536 1.02e-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: 1.02e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 568930469  496 CSGGYDPVCGSDGVTYGSVCELESMACTLGREIRVARRGPC 536
Cdd:cd01327     5 CPKDYDPVCGTDGVTYSNECLLCAENLKRQTNIRIKHDGEC 45
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 554-593 1.44e-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: 41.32  E-value: 1.44e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 568930469   554 RCVCPsecVESAQPVCGSDGHTYASECELHVHACTHQISL 593
Cdd:pfam07648    3 NCQCP---KTEYEPVCGSDGVTYPSPCALCAAGCKLGKEV 39
EGF_CA smart00179
Calcium-binding EGF-like domain;
1814-1846 1.76e-04

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 40.69  E-value: 1.76e-04
                            10        20        30
                    ....*....|....*....|....*....|....
gi 568930469   1814 AVDNPCLNGGSCIPREATYECLCPGGFS-GLHCE 1846
Cdd:smart00179    6 ASGNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
FSL_SPARC cd01328
Follistatin-like SPARC (secreted protein, acidic, and rich in cysteines) domain; SPARC/BM-40 ...
 174-230 2.10e-04

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


Pssm-ID: 238649 [Multi-domain]  Cd Length: 86  Bit Score: 42.08  E-value: 2.10e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930469  174 CRGMLCGFGAVCEpsVEDPGRASCVCKKNvCPAMVAP---VCGSDASTYSNECELQRAQC 230
Cdd:cd01328     2 CENHHCGAGKVCE--VDDENTPKCVCIDP-CPEEVDDrrkVCTNDNETFDSDCELYRTRC 58
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 274-319 2.15e-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: 2.15e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 568930469   274 CPTTCFGAPDGTVCGSDGVDYPSECQLLRHACANQEHIFK---KFDGPC 319
Cdd:pfam07648    2 CNCQCPKTEYEPVCGSDGVTYPSPCALCAAGCKLGKEVKEekvKYDGSC 50
Kazal_1 pfam00050
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 926-971 2.18e-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: 40.73  E-value: 2.18e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 568930469   926 PTLTCPeANSTKVCGSDGVTYGNECQLKTIACRQRLDISIQSLGPC 971
Cdd:pfam00050    5 PSGACP-RIYDPVCGTDGKTYSNECLFCAENGKRGTNLHKVHDGEC 49
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 929-971 2.57e-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: 2.57e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 568930469   929 TCPEANSTKVCGSDGVTYGNECQLKTIACRQRLDIS---IQSLGPC 971
Cdd:pfam07648    5 QCPKTEYEPVCGSDGVTYPSPCALCAAGCKLGKEVKeekVKYDGSC 50
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 416-463 3.56e-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: 3.56e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 568930469   416 CSCDRVTcdgaYRPVCAQDGHTYDNDCWRQQAECRQQQTI---PPKHQGPC 463
Cdd:pfam07648    4 CQCPKTE----YEPVCGSDGVTYPSPCALCAAGCKLGKEVkeeKVKYDGSC 50
KAZAL_PSTI cd01327
Kazal-type pancreatic secretory trypsin inhibitors (PSTI) and related proteins, including the ...
 925-971 3.89e-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: 39.96  E-value: 3.89e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 568930469  925 CPTLTCPeanstkVCGSDGVTYGNECQLKTIACRQRLDISIQSLGPC 971
Cdd:cd01327     5 CPKDYDP------VCGTDGVTYSNECLLCAENLKRQTNIRIKHDGEC 45
Kazal_1 pfam00050
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 718-752 5.07e-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: 5.07e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 568930469   718 PVCGSDGVTYSTECHLKKARCEARQELYVAAQGAC 752
Cdd:pfam00050   15 PVCGTDGKTYSNECLFCAENGKRGTNLHKVHDGEC 49
KAZAL_PSTI cd01327
Kazal-type pancreatic secretory trypsin inhibitors (PSTI) and related proteins, including the ...
 351-391 6.30e-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: 6.30e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 568930469  351 CPAQHTPICGDDGVTYENDCVMSRIGAARGLLLQKVRSGQC 391
Cdd:cd01327     5 CPKDYDPVCGTDGVTYSNECLLCAENLKRQTNIRIKHDGEC 45
FSL_SPARC cd01328
Follistatin-like SPARC (secreted protein, acidic, and rich in cysteines) domain; SPARC/BM-40 ...
 535-588 6.48e-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: 40.54  E-value: 6.48e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930469  535 PCDRcGQCRFGSLCEV---ETGRCVCPSECVESAQP---VCGSDGHTYASECELHVHACT 588
Cdd:cd01328     1 PCEN-HHCGAGKVCEVddeNTPKCVCIDPCPEEVDDrrkVCTNDNETFDSDCELYRTRCL 59
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
 1814-1846 1.34e-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: 38.23  E-value: 1.34e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 568930469 1814 AVDNPCLNGGSCIPREATYECLCPGGFSG-LHCE 1846
Cdd:cd00053     3 AASNPCSNGGTCVNTPGSYRCVCPPGYTGdRSCE 36
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 1816-1844 2.13e-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: 37.36  E-value: 2.13e-03
                           10        20
                   ....*....|....*....|....*....
gi 568930469  1816 DNPCLNGGSCIPREATYECLCPGGFSGLH 1844
Cdd:pfam00008    3 PNPCSNGGTCVDTPGGYTCICPEGYTGKR 31
KAZAL_PSTI cd01327
Kazal-type pancreatic secretory trypsin inhibitors (PSTI) and related proteins, including the ...
 708-733 2.63e-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: 37.65  E-value: 2.63e-03
                          10        20
                  ....*....|....*....|....*.
gi 568930469  708 DFSCQSVLKsPVCGSDGVTYSTECHL 733
Cdd:cd01327     2 VFGCPKDYD-PVCGTDGVTYSNECLL 26
Kazal_1 pfam00050
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 421-463 3.53e-03

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


Pssm-ID: 395004  Cd Length: 49  Bit Score: 37.26  E-value: 3.53e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 568930469   421 VTCDGAYRPVCAQDGHTYDNDCWRQQAECRQQQTIPPKHQGPC 463
Cdd:pfam00050    7 GACPRIYDPVCGTDGKTYSNECLFCAENGKRGTNLHKVHDGEC 49
KAZAL_PSTI cd01327
Kazal-type pancreatic secretory trypsin inhibitors (PSTI) and related proteins, including the ...
 423-463 5.50e-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: 5.50e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 568930469  423 CDGAYRPVCAQDGHTYDNDCWRQQAECRQQQTIPPKHQGPC 463
Cdd:cd01327     5 CPKDYDPVCGTDGVTYSNECLLCAENLKRQTNIRIKHDGEC 45
MFS_SLCO_OATP cd17336
Solute carrier organic anion transporters of the Major Facilitator Superfamily of transporters; ...
 555-625 6.14e-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: 41.46  E-value: 6.14e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568930469  555 CVCPSEcveSAQPVCGSDGHTYASECelhvHA-CTHQISLYVASA-GHCqTCGETVCTFGAVCSAGQCVCPRC 625
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 ...
 704-798 6.66e-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: 41.36  E-value: 6.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930469  704 PCVCDFSCQSVLKSPVCGSDGVTYSTECHlkkARCEARQELYVAAQGACRGptlapllpmasphCAqtpygCCQDNVTAA 783
Cdd:cd17462   326 LCNADCRCLEEIYSPVCGADGLMYYSPCH---AGCSEAYSDIRNGQKVYQD-------------CS-----CVAGNLSVG 384

                          90
                  ....*....|....*
gi 568930469  784 QGvGLAGCPSTCHCN 798
Cdd:cd17462   385 FG-EASAGKCTSNCN 398
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 1322-1352 9.31e-03

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


Pssm-ID: 394967  Cd Length: 31  Bit Score: 35.44  E-value: 9.31e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 568930469  1322 CDSQPCLHGGTCqdLDSGKGFSCSCTAGRAG 1352
Cdd:pfam00008    1 CAPNPCSNGGTC--VDTPGGYTCICPEGYTG 29
KAZAL_PSTI cd01327
Kazal-type pancreatic secretory trypsin inhibitors (PSTI) and related proteins, including the ...
 286-319 9.55e-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: 36.11  E-value: 9.55e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 568930469  286 VCGSDGVDYPSECQLLRHACANQEHIFKKFDGPC 319
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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