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Conserved domains on  [gi|84794568|ref|NP_001034154|]
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laminin subunit alpha-4 precursor [Danio rerio]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
1535-1672 4.41e-36

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


:

Pssm-ID: 238058 [Multi-domain]  Cd Length: 151  Bit Score: 134.47  E-value: 4.41e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568 1535 SAIKHESHFSLSLKTRSAFGLIFYLADASGENSMALFLTHARLVFTFSSGQSQVRIRSKEKYNDGQWHDIIFIRAGNMGR 1614
Cdd:cd00110   16 PAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDGQWHSVSVERNGRSVT 95
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 84794568 1615 MLIDGLTVLEDRAPGRNTSLLVQDPLYVGGVPPHQamKNIQRTSVSSFTGCVRSLQLN 1672
Cdd:cd00110   96 LSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDL--KSPGLPVSPGFVGCIRDLKVN 151
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
1696-1847 1.23e-26

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: 107.50  E-value: 1.23e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568 1696 GTYFaEEGGYVLLDDSFHFGSSFKMAMEVRPRVASGVLLHV-FMEQKEYLTVYIYQSQVVVVVNNGiaEFSTHVSPTQEI 1774
Cdd:cd00110    1 GVSF-SGSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAgSQNGGDFLALELEDGRLVLRYDLG--SGSLVLSSKTPL 77
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 84794568 1775 CDGNWHKITVIRDGSVLQLDVDSE-VNHVVGSVSDAAQSSSSPVFIGGAPDSMLSHSLLSRRGFTGCMRSVSVN 1847
Cdd:cd00110   78 NDGQWHSVSVERNGRSVTLSVDGErVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
Laminin_I super family cl26988
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ...
356-611 7.47e-26

Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.


The actual alignment was detected with superfamily member pfam06008:

Pssm-ID: 310534 [Multi-domain]  Cd Length: 258  Bit Score: 108.65  E-value: 7.47e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568    356 VLNISTGAAANDRLKYYNYTAHRLQAQFRGWRKNYAMMSGDTDVLEEETQNLLTDMDQFAEEENEVQNLGKQVDQETLNS 435
Cdd:pfam06008    1 LLSLNSLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568    436 STRAKTLTANLSSLNVLIEDMIRDWELYGVYQELDPQVKLQ-KLAEAERILGWMRKLNLSPKEPLATDESSEAHELLRRV 514
Cdd:pfam06008   81 LGHAKELAEAIKNLIDNIKEINEKVATLGENDFALPSSDLSrMLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQDLLSRI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568    515 RS-FDRNLMTTQGRLPPMQEVLGRFTSKLLQAQDLLSKAEDALKQAINKYKSNQLKLQRREAQQQRLKDIQDGVDQTIVN 593
Cdd:pfam06008  161 QTwFQSPQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEETLKT 240
                          250
                   ....*....|....*...
gi 84794568    594 AAAVLSEANHTVLEVEDV 611
Cdd:pfam06008  241 ARDSLDAANLLLQEIDDA 258
Laminin_II super family cl05515
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 ...
790-919 2.06e-24

Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.


The actual alignment was detected with superfamily member pfam06009:

Pssm-ID: 368703 [Multi-domain]  Cd Length: 138  Bit Score: 100.64  E-value: 2.06e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568    790 TQEVAEGTLNRSAEVLEKVTPILKRVEQWDGNMKSEAYSAA-------AFDRTVLSAGEAVKDLSAIVPELLSKLRVVEE 862
Cdd:pfam06009    1 SKELAREANETAKEVLEQLAPLSQNLENTSEKLSGINRSLEetnelvnDANKALDDAGRSVKKLEELAPDLLDKLKPLKQ 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 84794568    863 KKP-VNNVTTSIMKIRGLIAQARSVAKKVQVSMKFDGQSAVEVHPHTNLDELKTVTSI 919
Cdd:pfam06009   81 LEVnSSSLSDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTSL 138
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
1104-1259 2.18e-20

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: 89.40  E-value: 2.18e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568 1104 SYLFDGTGYALVNNIERRGKIgvvTRFDIEVRTVANNGILFLMVNE--TNFFVLELKNGFLRLMYDFGfaNGPVIIETnl 1181
Cdd:cd00110    1 GVSFSGSSYVRLPTLPAPRTR---LSISFSFRTTSPNGLLLYAGSQngGDFLALELEDGRLVLRYDLG--SGSLVLSS-- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568 1182 aKLQINDARYHEVSVIyHHSKKIILLVDR-SHVKSFESEKKPL--PFSDIYIGGAPSRILQSRpeLTSLIGLKGCVKGFQ 1258
Cdd:cd00110   74 -KTPLNDGQWHSVSVE-RNGRSVTLSVDGeRVVESGSPGGSALlnLDGPLYLGGLPEDLKSPG--LPVSPGFVGCIRDLK 149

                 .
gi 84794568 1259 F 1259
Cdd:cd00110  150 V 150
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
893-1067 2.97e-16

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: 77.84  E-value: 2.97e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568  893 SMKFDGQSAVEVhphTNLDELKTVTSISFYIRvdPDKdpiEDRFLLYLGDKQGKrDYMGLAIKNDNLVYVYKLGEEEVEI 972
Cdd:cd00110    1 GVSFSGSSYVRL---PTLPAPRTRLSISFSFR--TTS---PNGLLLYAGSQNGG-DFLALELEDGRLVLRYDLGSGSLVL 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568  973 plsSKPVSSWPPVFNFVKVERLGRHgkVFLTVpsqDttaEQKFIQKGEPvgtDTLFDLDPKDMVFiVGGVPPGVTVPPIL 1052
Cdd:cd00110   72 ---SSKTPLNDGQWHSVSVERNGRS--VTLSV---D---GERVVESGSP---GGSALLNLDGPLY-LGGLPEDLKSPGLP 136
                        170
                 ....*....|....*
gi 84794568 1053 SLAPFVGCIELETLN 1067
Cdd:cd00110  137 VSPGFVGCIRDLKVN 151
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
1289-1422 6.31e-16

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: 76.69  E-value: 6.31e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568 1289 AYFTGNGYLSSSDKISPFQSFEGGLSFKTLQPSGLLFYH--RDGSDEFSLSLENGAVVLQ----AKGTRVKSqKKHYSDG 1362
Cdd:cd00110    2 VSFSGSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAgsQNGGDFLALELEDGRLVLRydlgSGSLVLSS-KTPLNDG 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 84794568 1363 RSHFLVASVTNQKYEIVIdDKDKQDKKKPSSTSQSDNTPKAFYYGGSTSSSIL-------NLTGCIS 1422
Cdd:cd00110   81 QWHSVSVERNGRSVTLSV-DGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSpglpvspGFVGCIR 146
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
209-247 3.94e-12

Laminin-type epidermal growth factor-like domai;


:

Pssm-ID: 214543  Cd Length: 46  Bit Score: 62.33  E-value: 3.94e-12
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 84794568     209 CQCNKCGTAS--CDDRSGVCHCKPGVTGQLCDRCEDGHSGF 247
Cdd:smart00180    1 CDCDPGGSASgtCDPDTGQCECKPNVTGRRCDRCAPGYYGD 41
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
155-207 7.43e-12

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: 61.60  E-value: 7.43e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 84794568  155 CDCNGNSDPNlifNECHNVTGKCLnCWGDTAGDNCERCAPGFYGDAISAKDCQ 207
Cdd:cd00055    2 CDCNGHGSLS---GQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
256-300 4.58e-11

Laminin-type epidermal growth factor-like domai;


:

Pssm-ID: 214543  Cd Length: 46  Bit Score: 59.25  E-value: 4.58e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 84794568     256 CEC-ASAALRATCHPLTHSCQCRPGAGGRYCERCLPGFWDYSPSGC 300
Cdd:smart00180    1 CDCdPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
99-152 2.95e-10

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


:

Pssm-ID: 395007  Cd Length: 49  Bit Score: 56.98  E-value: 2.95e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 84794568     99 CACPLSLESNnfaAHCDRRGefLRCVCQDGYAGHYCERCAPGYYGNPMELGNSC 152
Cdd:pfam00053    1 CDCNPHGSLS---DTCDPET--GQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
Cast super family cl37807
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
490-817 4.33e-05

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


The actual alignment was detected with superfamily member pfam10174:

Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 48.66  E-value: 4.33e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568    490 KLNLSPKEPLATDESSEAHELLRRVRSFDRNLMTTQGRLPPMQEVLGRFTSKLLQAQDLLskaeDALKQAIN----KYKS 565
Cdd:pfam10174  330 KESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDML----DVKERKINvlqkKIEN 405
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568    566 NQLKLQRREAQQQRLKDIQDGVDQTIVN---AAAVLSEAnhtVLEVEDVITNVREQHA--------EIDGARVLLERRTE 634
Cdd:pfam10174  406 LQEQLRDKDKQLAGLKERVKSLQTDSSNtdtALTTLEEA---LSEKERIIERLKEQREredrerleELESLKKENKDLKE 482
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568    635 KISQSDREL------VLRAEDHADQLQRHAEEPQHNLKGSDANghVQKALNAFNVYDNIVKSVDDANITSLTALNISSRt 708
Cdd:pfam10174  483 KVSALQPELtekessLIDLKEHASSLASSGLKKDSKLKSLEIA--VEQKKEECSKLENQLKKAHNAEEAVRTNPEINDR- 559
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568    709 hgaVDKLSSQLNLMRSQSAKVLNEASSLHFQQQDSESIVLDNKKYIEETNEMMDGSSKKIAKIITEINAIHTDRTPKRLQ 788
Cdd:pfam10174  560 ---IRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQ 636
                          330       340       350
                   ....*....|....*....|....*....|...
gi 84794568    789 FTQEVAEGTLNRSAEV----LEKVTPILKRVEQ 817
Cdd:pfam10174  637 LLEEARRREDNLADNSqqlqLEELMGALEKTRQ 669
 
Name Accession Description Interval E-value
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
1535-1672 4.41e-36

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


Pssm-ID: 238058 [Multi-domain]  Cd Length: 151  Bit Score: 134.47  E-value: 4.41e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568 1535 SAIKHESHFSLSLKTRSAFGLIFYLADASGENSMALFLTHARLVFTFSSGQSQVRIRSKEKYNDGQWHDIIFIRAGNMGR 1614
Cdd:cd00110   16 PAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDGQWHSVSVERNGRSVT 95
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 84794568 1615 MLIDGLTVLEDRAPGRNTSLLVQDPLYVGGVPPHQamKNIQRTSVSSFTGCVRSLQLN 1672
Cdd:cd00110   96 LSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDL--KSPGLPVSPGFVGCIRDLKVN 151
LamG smart00282
Laminin G domain;
1542-1674 5.28e-32

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 122.06  E-value: 5.28e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568    1542 HFSLSLKTRSAFGLIFYLADASGENSMALFLTHARLVFTFSSGQSQVRIRSK-EKYNDGQWHDIIFIRAGNMGRMLIDGL 1620
Cdd:smart00282    1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDpTPLNDGQWHRVAVERNGRSVTLSVDGG 80
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....
gi 84794568    1621 TVLEDRAPGRNTSLLVQDPLYVGGVPPHQAMKNIQRTsvSSFTGCVRSLQLNGR 1674
Cdd:smart00282   81 NRVSGESPGGLTILNLDGPLYLGGLPEDLKLPPLPVT--PGFRGCIRNLKVNGK 132
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
1547-1674 6.44e-28

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: 110.20  E-value: 6.44e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568   1547 LKTRSAFGLIFYLADASGEnSMALFLTHARLVFTFSSGQSQVRIRS-KEKYNDGQWHDIIFIRAGNMGRMLIDGLTVLED 1625
Cdd:pfam02210    1 FRTRQPNGLLLYAGGGGSD-FLALELVNGRLVLRYDLGSGPESLLSsGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSS 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 84794568   1626 RAPGRNTSLLVQDPLYVGGVPPHQAMKNIQRTsvSSFTGCVRSLQLNGR 1674
Cdd:pfam02210   80 LPPGESLLLNLNGPLYLGGLPPLLLLPALPVR--AGFVGCIRDVRVNGE 126
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
1696-1847 1.23e-26

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: 107.50  E-value: 1.23e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568 1696 GTYFaEEGGYVLLDDSFHFGSSFKMAMEVRPRVASGVLLHV-FMEQKEYLTVYIYQSQVVVVVNNGiaEFSTHVSPTQEI 1774
Cdd:cd00110    1 GVSF-SGSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAgSQNGGDFLALELEDGRLVLRYDLG--SGSLVLSSKTPL 77
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 84794568 1775 CDGNWHKITVIRDGSVLQLDVDSE-VNHVVGSVSDAAQSSSSPVFIGGAPDSMLSHSLLSRRGFTGCMRSVSVN 1847
Cdd:cd00110   78 NDGQWHSVSVERNGRSVTLSVDGErVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
Laminin_I pfam06008
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ...
356-611 7.47e-26

Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.


Pssm-ID: 310534 [Multi-domain]  Cd Length: 258  Bit Score: 108.65  E-value: 7.47e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568    356 VLNISTGAAANDRLKYYNYTAHRLQAQFRGWRKNYAMMSGDTDVLEEETQNLLTDMDQFAEEENEVQNLGKQVDQETLNS 435
Cdd:pfam06008    1 LLSLNSLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568    436 STRAKTLTANLSSLNVLIEDMIRDWELYGVYQELDPQVKLQ-KLAEAERILGWMRKLNLSPKEPLATDESSEAHELLRRV 514
Cdd:pfam06008   81 LGHAKELAEAIKNLIDNIKEINEKVATLGENDFALPSSDLSrMLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQDLLSRI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568    515 RS-FDRNLMTTQGRLPPMQEVLGRFTSKLLQAQDLLSKAEDALKQAINKYKSNQLKLQRREAQQQRLKDIQDGVDQTIVN 593
Cdd:pfam06008  161 QTwFQSPQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEETLKT 240
                          250
                   ....*....|....*...
gi 84794568    594 AAAVLSEANHTVLEVEDV 611
Cdd:pfam06008  241 ARDSLDAANLLLQEIDDA 258
Laminin_II pfam06009
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 ...
790-919 2.06e-24

Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.


Pssm-ID: 368703 [Multi-domain]  Cd Length: 138  Bit Score: 100.64  E-value: 2.06e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568    790 TQEVAEGTLNRSAEVLEKVTPILKRVEQWDGNMKSEAYSAA-------AFDRTVLSAGEAVKDLSAIVPELLSKLRVVEE 862
Cdd:pfam06009    1 SKELAREANETAKEVLEQLAPLSQNLENTSEKLSGINRSLEetnelvnDANKALDDAGRSVKKLEELAPDLLDKLKPLKQ 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 84794568    863 KKP-VNNVTTSIMKIRGLIAQARSVAKKVQVSMKFDGQSAVEVHPHTNLDELKTVTSI 919
Cdd:pfam06009   81 LEVnSSSLSDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTSL 138
LamG smart00282
Laminin G domain;
1719-1848 1.10e-22

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 95.48  E-value: 1.10e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568    1719 KMAMEVRPRVASGVLLHV-FMEQKEYLTVYIYQSQVVVVVNNGIAEFSTHVSPTQeICDGNWHKITVIRDGSVLQLDVDS 1797
Cdd:smart00282    1 SISFSFRTTSPNGLLLYAgSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTP-LNDGQWHRVAVERNGRSVTLSVDG 79
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|...
gi 84794568    1798 EvNHVVGSVSDAAQSSS--SPVFIGGAPDSMLSHSLLSRRGFTGCMRSVSVNE 1848
Cdd:smart00282   80 G-NRVSGESPGGLTILNldGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNG 131
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
1724-1849 9.36e-21

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: 89.79  E-value: 9.36e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568   1724 VRPRVASGVLLHVFMEQKEYLTVYIYQSQVVVVVNNGIAEFSTHVSPTQeICDGNWHKITVIRDGSVLQLDVDSEVNHVV 1803
Cdd:pfam02210    1 FRTRQPNGLLLYAGGGGSDFLALELVNGRLVLRYDLGSGPESLLSSGKN-LNDGQWHSVRVERNGNTLTLSVDGQTVVSS 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 84794568   1804 GSVSDAAQ-SSSSPVFIGGAPDSMLSHSLLSRRGFTGCMRSVSVNET 1849
Cdd:pfam02210   80 LPPGESLLlNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVNGE 126
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
1104-1259 2.18e-20

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: 89.40  E-value: 2.18e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568 1104 SYLFDGTGYALVNNIERRGKIgvvTRFDIEVRTVANNGILFLMVNE--TNFFVLELKNGFLRLMYDFGfaNGPVIIETnl 1181
Cdd:cd00110    1 GVSFSGSSYVRLPTLPAPRTR---LSISFSFRTTSPNGLLLYAGSQngGDFLALELEDGRLVLRYDLG--SGSLVLSS-- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568 1182 aKLQINDARYHEVSVIyHHSKKIILLVDR-SHVKSFESEKKPL--PFSDIYIGGAPSRILQSRpeLTSLIGLKGCVKGFQ 1258
Cdd:cd00110   74 -KTPLNDGQWHSVSVE-RNGRSVTLSVDGeRVVESGSPGGSALlnLDGPLYLGGLPEDLKSPG--LPVSPGFVGCIRDLK 149

                 .
gi 84794568 1259 F 1259
Cdd:cd00110  150 V 150
LamG smart00282
Laminin G domain;
1129-1262 4.56e-18

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 82.39  E-value: 4.56e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568    1129 RFDIEVRTVANNGILFLM--VNETNFFVLELKNGFLRLMYDFGfaNGPVIIETNlaKLQINDARYHEVSVIYHHsKKIIL 1206
Cdd:smart00282    1 SISFSFRTTSPNGLLLYAgsKGGGDYLALELRDGRLVLRYDLG--SGPARLTSD--PTPLNDGQWHRVAVERNG-RSVTL 75
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 84794568    1207 LVD---RSHVKSFESEKKPLPFSDIYIGGAPSriLQSRPELTSLIGLKGCVKGFQFQKE 1262
Cdd:smart00282   76 SVDggnRVSGESPGGLTILNLDGPLYLGGLPE--DLKLPPLPVTPGFRGCIRNLKVNGK 132
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
1134-1259 5.73e-17

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: 79.00  E-value: 5.73e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568   1134 VRTVANNGILFLMVNETN-FFVLELKNGFLRLMYDFGfaNGPVIIETNLAKLqiNDARYHEVSVIYhHSKKIILLVDRSH 1212
Cdd:pfam02210    1 FRTRQPNGLLLYAGGGGSdFLALELVNGRLVLRYDLG--SGPESLLSSGKNL--NDGQWHSVRVER-NGNTLTLSVDGQT 75
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 84794568   1213 VKSFESEKKPLPF---SDIYIGGAPSRILQSRPELTSliGLKGCVKGFQF 1259
Cdd:pfam02210   76 VVSSLPPGESLLLnlnGPLYLGGLPPLLLLPALPVRA--GFVGCIRDVRV 123
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
893-1067 2.97e-16

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: 77.84  E-value: 2.97e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568  893 SMKFDGQSAVEVhphTNLDELKTVTSISFYIRvdPDKdpiEDRFLLYLGDKQGKrDYMGLAIKNDNLVYVYKLGEEEVEI 972
Cdd:cd00110    1 GVSFSGSSYVRL---PTLPAPRTRLSISFSFR--TTS---PNGLLLYAGSQNGG-DFLALELEDGRLVLRYDLGSGSLVL 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568  973 plsSKPVSSWPPVFNFVKVERLGRHgkVFLTVpsqDttaEQKFIQKGEPvgtDTLFDLDPKDMVFiVGGVPPGVTVPPIL 1052
Cdd:cd00110   72 ---SSKTPLNDGQWHSVSVERNGRS--VTLSV---D---GERVVESGSP---GGSALLNLDGPLY-LGGLPEDLKSPGLP 136
                        170
                 ....*....|....*
gi 84794568 1053 SLAPFVGCIELETLN 1067
Cdd:cd00110  137 VSPGFVGCIRDLKVN 151
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
1289-1422 6.31e-16

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: 76.69  E-value: 6.31e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568 1289 AYFTGNGYLSSSDKISPFQSFEGGLSFKTLQPSGLLFYH--RDGSDEFSLSLENGAVVLQ----AKGTRVKSqKKHYSDG 1362
Cdd:cd00110    2 VSFSGSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAgsQNGGDFLALELEDGRLVLRydlgSGSLVLSS-KTPLNDG 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 84794568 1363 RSHFLVASVTNQKYEIVIdDKDKQDKKKPSSTSQSDNTPKAFYYGGSTSSSIL-------NLTGCIS 1422
Cdd:cd00110   81 QWHSVSVERNGRSVTLSV-DGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSpglpvspGFVGCIR 146
LamG smart00282
Laminin G domain;
918-1068 9.54e-15

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 72.76  E-value: 9.54e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568     918 SISFYIRvdpdkdPIEDR-FLLYLGDKQGKrDYMGLAIKNDNLVYVYKLGEEEVEIPLSSKPVS--SWppvfNFVKVERL 994
Cdd:smart00282    1 SISFSFR------TTSPNgLLLYAGSKGGG-DYLALELRDGRLVLRYDLGSGPARLTSDPTPLNdgQW----HRVAVERN 69
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 84794568     995 GRHgkVFLTVPSQDTTAEQKFIQKgepvgtdtlFDLDPKDMVFiVGGVPPGVTVPPILSLAPFVGCIELETLNN 1068
Cdd:smart00282   70 GRS--VTLSVDGGNRVSGESPGGL---------TILNLDGPLY-LGGLPEDLKLPPLPVTPGFRGCIRNLKVNG 131
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
1315-1429 1.43e-12

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: 66.29  E-value: 1.43e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568   1315 FKTLQPSGLLFYHRDGSDEF-SLSLENGAVVLQ----AKGTRVKSQKKHYSDGRSHFLVASVTNQKYEIVIDDKDKQDKK 1389
Cdd:pfam02210    1 FRTRQPNGLLLYAGGGGSDFlALELVNGRLVLRydlgSGPESLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSL 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 84794568   1390 KPSSTSQsDNTPKAFYYGG-------STSSSILNLTGCISYAYISRQ 1429
Cdd:pfam02210   81 PPGESLL-LNLNGPLYLGGlppllllPALPVRAGFVGCIRDVRVNGE 126
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
209-247 3.94e-12

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 62.33  E-value: 3.94e-12
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 84794568     209 CQCNKCGTAS--CDDRSGVCHCKPGVTGQLCDRCEDGHSGF 247
Cdd:smart00180    1 CDCDPGGSASgtCDPDTGQCECKPNVTGRRCDRCAPGYYGD 41
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
155-207 7.43e-12

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: 61.60  E-value: 7.43e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 84794568  155 CDCNGNSDPNlifNECHNVTGKCLnCWGDTAGDNCERCAPGFYGDAISAKDCQ 207
Cdd:cd00055    2 CDCNGHGSLS---GQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
209-253 8.16e-12

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 61.60  E-value: 8.16e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 84794568    209 CQCNKCGTAS--CDDRSGVCHCKPGVTGQLCDRCEDGHSGFCTCMGC 253
Cdd:pfam00053    1 CDCNPHGSLSdtCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQ 47
LamG smart00282
Laminin G domain;
1313-1429 9.60e-12

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 64.28  E-value: 9.60e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568    1313 LSFKTLQPSGLLFYH--RDGSDEFSLSLENGAVVLQ----AKGTRVKSQKKHYSDGRSHFLVASVTNQKYEIVIDDKDKQ 1386
Cdd:smart00282    4 FSFRTTSPNGLLLYAgsKGGGDYLALELRDGRLVLRydlgSGPARLTSDPTPLNDGQWHRVAVERNGRSVTLSVDGGNRV 83
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|
gi 84794568    1387 DKKKPSSTSQSdNTPKAFYYGGSTSSSIL-------NLTGCISYAYISRQ 1429
Cdd:smart00282   84 SGESPGGLTIL-NLDGPLYLGGLPEDLKLpplpvtpGFRGCIRNLKVNGK 132
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
209-247 1.02e-11

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: 61.22  E-value: 1.02e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 84794568  209 CQCNKCGTAS--CDDRSGVCHCKPGVTGQLCDRCEDGHSGF 247
Cdd:cd00055    2 CDCNGHGSLSgqCDPGTGQCECKPNTTGRRCDRCAPGYYGL 42
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
256-300 4.58e-11

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 59.25  E-value: 4.58e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 84794568     256 CEC-ASAALRATCHPLTHSCQCRPGAGGRYCERCLPGFWDYSPSGC 300
Cdd:smart00180    1 CDCdPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
256-303 1.17e-10

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 58.13  E-value: 1.17e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 84794568    256 CEC-ASAALRATCHPLTHSCQCRPGAGGRYCERCLPGFWDYSPSGCRKC 303
Cdd:pfam00053    1 CDCnPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
255-301 2.37e-10

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: 57.36  E-value: 2.37e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 84794568  255 RCEC-ASAALRATCHPLTHSCQCRPGAGGRYCERCLPGFWDYS--PSGCR 301
Cdd:cd00055    1 PCDCnGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPsqGGGCQ 50
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
99-152 2.95e-10

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 56.98  E-value: 2.95e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 84794568     99 CACPLSLESNnfaAHCDRRGefLRCVCQDGYAGHYCERCAPGYYGNPMELGNSC 152
Cdd:pfam00053    1 CDCNPHGSLS---DTCDPET--GQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
936-1068 1.21e-09

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: 57.81  E-value: 1.21e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568    936 FLLYLGDKQGkrDYMGLAIKNDNLVYVYKLGEEEVEIPLSSKPVS--SWppvfNFVKVERLGRHgkVFLTVPSQDTTAEQ 1013
Cdd:pfam02210    9 LLLYAGGGGS--DFLALELVNGRLVLRYDLGSGPESLLSSGKNLNdgQW----HSVRVERNGNT--LTLSVDGQTVVSSL 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 84794568   1014 KfiqKGEPVGTDTLFDLdpkdmvfIVGGVPPGVTVPPILSLAPFVGCIELETLNN 1068
Cdd:pfam02210   81 P---PGESLLLNLNGPL-------YLGGLPPLLLLPALPVRAGFVGCIRDVRVNG 125
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
155-206 1.44e-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: 1.44e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 84794568    155 CDCNGNSDPNlifNECHNVTGKCLnCWGDTAGDNCERCAPGFYGDAI-SAKDC 206
Cdd:pfam00053    1 CDCNPHGSLS---DTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSdPPQGC 49
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
98-153 1.00e-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: 52.74  E-value: 1.00e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 84794568   98 PCACPLSLESNNfaaHCDRRGefLRCVCQDGYAGHYCERCAPGYYGNPmELGNSCK 153
Cdd:cd00055    1 PCDCNGHGSLSG---QCDPGT--GQCECKPNTTGRRCDRCAPGYYGLP-SQGGGCQ 50
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
99-152 6.78e-08

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 50.39  E-value: 6.78e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 84794568      99 CACPLSlesNNFAAHCDRRGefLRCVCQDGYAGHYCERCAPGYYGNPmelGNSC 152
Cdd:smart00180    1 CDCDPG---GSASGTCDPDT--GQCECKPNVTGRRCDRCAPGYYGDG---PPGC 46
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
155-206 9.37e-08

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 50.00  E-value: 9.37e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 84794568     155 CDCN--GNSDpnlifNECHNVTGKCLnCWGDTAGDNCERCAPGFYGDaiSAKDC 206
Cdd:smart00180    1 CDCDpgGSAS-----GTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD--GPPGC 46
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
402-658 1.51e-06

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.52  E-value: 1.51e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568    402 EETQNLLTDM-DQFAEEENEVQNLGKQVDQ---ETLNSSTRAKTLTANLSSLNVLIEDMIRDWElygVYQELDPQVKLQK 477
Cdd:TIGR02168  242 EELQEELKEAeEELEELTAELQELEEKLEElrlEVSELEEEIEELQKELYALANEISRLEQQKQ---ILRERLANLERQL 318
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568    478 LAEAERILGWMRKLNLSPKEplATDESSEAHELLRRVRSFdrnlmttQGRLPPMQEVLGRFTSKLLQAQDLLSKAEDALK 557
Cdd:TIGR02168  319 EELEAQLEELESKLDELAEE--LAELEEKLEELKEELESL-------EAELEELEAELEELESRLEELEEQLETLRSKVA 389
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568    558 QAINKYKSNQLKLQRREAQQQRLKDIQDGVDQTIVNAAAVLSEANhtVLEVEDVITNVREQHAEIDGARVLLERRTEKIS 637
Cdd:TIGR02168  390 QLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE--LKELQAELEELEEELEELQEELERLEEALEELR 467
                          250       260
                   ....*....|....*....|.
gi 84794568    638 QSDRELVLRAEDHADQLQRHA 658
Cdd:TIGR02168  468 EELEEAEQALDAAERELAQLQ 488
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
488-863 6.03e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 50.67  E-value: 6.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568  488 MRKLNLSPKEPLATDESSE-AHELLRRVRSFDRNLMTTQGRLPPMQEVLGRFTSKLLQAQDLLSKAEDALKQAINKYKSN 566
Cdd:COG4372   13 LSLFGLRPKTGILIAALSEqLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAA 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568  567 QLKLQRREAQ----QQRLKDIQDGVDQTIVNAAAVLSEANHTVLEVEDVITNVREQHAEIDGARVLLERRTEKISQSDRE 642
Cdd:COG4372   93 QAELAQAQEEleslQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQE 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568  643 LVLRAEDHADQ-LQRHAEEpqhnlkgsdANGHVQKALNAFNVYDNIVKSVDDANITSLTALNISSRTHGAVDKLSSQlnl 721
Cdd:COG4372  173 LQALSEAEAEQaLDELLKE---------ANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLD--- 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568  722 mrsqsAKVLNEASSLHFQQQDSESIVLDNKKYIEETNEMMDGSSKKIAKIITEINAIhtDRTPKRLQFTQEVAEGTLNRS 801
Cdd:COG4372  241 -----ALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAA--LELKLLALLLNLAALSLIGAL 313
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 84794568  802 AEVLEKVTPILKRVEQwdgnmksEAYSAAAFDRTVLSAGEAVKDLSAIVPELLSKLRVVEEK 863
Cdd:COG4372  314 EDALLAALLELAKKLE-------LALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVA 368
PRK10246 PRK10246
exonuclease subunit SbcC; Provisional
442-584 9.06e-06

exonuclease subunit SbcC; Provisional


Pssm-ID: 182330 [Multi-domain]  Cd Length: 1047  Bit Score: 50.95  E-value: 9.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568   442 LTANLSSLNV-LIE-DMIRDW--ELYGVYQELDPQV--KLQKLAEAERILGWMRKLNLSPKEPLA--TDESSEAHELLRR 513
Cdd:PRK10246  341 LQAQQQSLNTwLAEhDRFRQWnnELAGWRAQFSQQTsdREQLRQWQQQLTHAEQKLNALPAITLTltADEVAAALAQHAE 420
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 84794568   514 VRSFDRNLMTTQGRLPPMQEVLGRFTSKLLQAQDLLSKAEDALKQAINKYKSNQLKLQRREA---QQQRLKDIQ 584
Cdd:PRK10246  421 QRPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLADVKTiceQEARIKDLE 494
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
378-803 2.38e-05

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.38  E-value: 2.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568  378 RLQAQFRGWRKNYAMMSGDTDVLEEETQNLLTDMDQFAEEENEVQNLGKQVDQetlnSSTRAKTLTANLSSLnvliEDMI 457
Cdd:COG4717   54 EADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEE----LEAELEELREELEKL----EKLL 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568  458 RDWELYGVYQEL-----DPQVKLQKL-AEAERILGWMRKLnlspkePLATDESSEAHELLRRVRsfDRNLMTTQGRLPPM 531
Cdd:COG4717  126 QLLPLYQELEALeaelaELPERLEELeERLEELRELEEEL------EELEAELAELQEELEELL--EQLSLATEEELQDL 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568  532 QEVLGRFTSKLLQAQDLLSKAEDALKQAINKYKSNQLKLQrREAQQQRLKdiQDGVDQTIVNAAAVLSEANHTVLEVEDV 611
Cdd:COG4717  198 AEELEELQQRLAELEEELEEAQEELEELEEELEQLENELE-AAALEERLK--EARLLLLIAAALLALLGLGGSLLSLILT 274
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568  612 ITNVREQHAEIDGARVLLERRTEKISQSDRELV--------LRAEDHADQLQRH----AEEPQHNLKGSDANGHVQKALN 679
Cdd:COG4717  275 IAGVLFLVLGLLALLFLLLAREKASLGKEAEELqalpaleeLEEEELEELLAALglppDLSPEELLELLDRIEELQELLR 354
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568  680 AFN----------VYDNIVKSVDDANITSLTALNISSRTHGAVDKLSSQLNLMRSQSAKVLNEASSLHfQQQDSESI--- 746
Cdd:COG4717  355 EAEeleeelqleeLEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELL-EALDEEELeee 433
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 84794568  747 VLDNKKYIEETNEMMDGSSKKIAKIITEINAIHTDRTPKRLQFTQEVAEGTLNRSAE 803
Cdd:COG4717  434 LEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAE 490
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
474-665 3.97e-05

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 46.67  E-value: 3.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568  474 KLQKLA-EAERILGWMRKlnlspKEPLATDES-----SEAHELLRRVRSFDRNLMTTQGRLPPMQEV------LGRFTSK 541
Cdd:cd00176    1 KLQQFLrDADELEAWLSE-----KEELLSSTDygddlESVEALLKKHEALEAELAAHEERVEALNELgeqlieEGHPDAE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568  542 LLQA-QDLLSKAEDALKQAINKYKSnqlKLQRREAQQQRLKDIQDgVDQTIVNAAAVLS--EANHTVLEVEDVITNVREQ 618
Cdd:cd00176   76 EIQErLEELNQRWEELRELAEERRQ---RLEEALDLQQFFRDADD-LEQWLEEKEAALAseDLGKDLESVEELLKKHKEL 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 84794568  619 HAEIDG-----------ARVLLERRTEKISQSDRELVLRAEDHADQLQRHAEEPQHNL 665
Cdd:cd00176  152 EEELEAheprlkslnelAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKL 209
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
490-817 4.33e-05

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 48.66  E-value: 4.33e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568    490 KLNLSPKEPLATDESSEAHELLRRVRSFDRNLMTTQGRLPPMQEVLGRFTSKLLQAQDLLskaeDALKQAIN----KYKS 565
Cdd:pfam10174  330 KESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDML----DVKERKINvlqkKIEN 405
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568    566 NQLKLQRREAQQQRLKDIQDGVDQTIVN---AAAVLSEAnhtVLEVEDVITNVREQHA--------EIDGARVLLERRTE 634
Cdd:pfam10174  406 LQEQLRDKDKQLAGLKERVKSLQTDSSNtdtALTTLEEA---LSEKERIIERLKEQREredrerleELESLKKENKDLKE 482
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568    635 KISQSDREL------VLRAEDHADQLQRHAEEPQHNLKGSDANghVQKALNAFNVYDNIVKSVDDANITSLTALNISSRt 708
Cdd:pfam10174  483 KVSALQPELtekessLIDLKEHASSLASSGLKKDSKLKSLEIA--VEQKKEECSKLENQLKKAHNAEEAVRTNPEINDR- 559
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568    709 hgaVDKLSSQLNLMRSQSAKVLNEASSLHFQQQDSESIVLDNKKYIEETNEMMDGSSKKIAKIITEINAIHTDRTPKRLQ 788
Cdd:pfam10174  560 ---IRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQ 636
                          330       340       350
                   ....*....|....*....|....*....|...
gi 84794568    789 FTQEVAEGTLNRSAEV----LEKVTPILKRVEQ 817
Cdd:pfam10174  637 LLEEARRREDNLADNSqqlqLEELMGALEKTRQ 669
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
508-862 3.03e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.74  E-value: 3.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568    508 HELLRRVRSFDRNLMttqgRLppmQEVLGRFTSKL--LQAQdlLSKAE------DALKQA-----INKYKSNQLKLQRRE 574
Cdd:TIGR02168  175 KETERKLERTRENLD----RL---EDILNELERQLksLERQ--AEKAErykelkAELRELelallVLRLEELREELEELQ 245
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568    575 AQQQRLKDIQDGVDQTIVNAAAVLSEANHTVLEVEDVI----TNVREQHAEIDGarvlLERRTEKISQSDRELV---LRA 647
Cdd:TIGR02168  246 EELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIeelqKELYALANEISR----LEQQKQILRERLANLErqlEEL 321
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568    648 EDHADQLQRHAEEPQHNLKGSDANGHVQKalnafNVYDNIVKSVDDANITSLTALNISSRTHGAVDKLSSQLNLMRSQSA 727
Cdd:TIGR02168  322 EAQLEELESKLDELAEELAELEEKLEELK-----EELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568    728 KVLNEASSLHFQQQDSESIVLDNKKYIEETNEMMDgsSKKIAKIITEINAihTDRTPKRLQFTQEVAEGTLNRSAEVLEK 807
Cdd:TIGR02168  397 SLNNEIERLEARLERLEDRRERLQQEIEELLKKLE--EAELKELQAELEE--LEEELEELQEELERLEEALEELREELEE 472
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 84794568    808 VTPILKRVEQWDGNMKSEAYSAAAFDRTVLSAGEAVK-------DLSAIVPELLSKLRVVEE 862
Cdd:TIGR02168  473 AEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKallknqsGLSGILGVLSELISVDEG 534
CHAD smart00880
The CHAD domain is an alpha-helical domain functionally associated with some members of the ...
396-580 5.19e-03

The CHAD domain is an alpha-helical domain functionally associated with some members of the adenylate cyclase family; It has conserved histidines that may chelate metals.


Pssm-ID: 214880 [Multi-domain]  Cd Length: 262  Bit Score: 40.84  E-value: 5.19e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568     396 DTDVLEEETQNLLtdmDQFAEEENEVQNLGKQVDQETlnSSTRAKTLTAnLSSLNVLieDMIRDWEL------YGVYQEL 469
Cdd:smart00880   70 DLDVLLERLLELL---AALLPELPALDALVAALEARR--AAARRALLAA-LDSARYT--ALLLDLSRwlatppWQPAADD 141
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568     470 DPQVKLQKLAeAERILGWMRKLNLSPKEPLATDESSEAHEL---LRRVR----SF-----DRNLMTTQGRLPPMQEVLGR 537
Cdd:smart00880  142 KAARPLADFA-AKALRRLLRKLRRAFPAARALLDDEALHRLrkrLKRLRyaaeFFaplydAKARKRFLKRLKDLQDALGD 220
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|...
gi 84794568     538 FTSkLLQAQDLLSKAEDALKQAINKYKSNQLKLQRREAQQQRL 580
Cdd:smart00880  221 LND-LAVARALLEDLADEAEAAQLERGLLAAERSRLEARRQAR 262
 
Name Accession Description Interval E-value
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
1535-1672 4.41e-36

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


Pssm-ID: 238058 [Multi-domain]  Cd Length: 151  Bit Score: 134.47  E-value: 4.41e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568 1535 SAIKHESHFSLSLKTRSAFGLIFYLADASGENSMALFLTHARLVFTFSSGQSQVRIRSKEKYNDGQWHDIIFIRAGNMGR 1614
Cdd:cd00110   16 PAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDGQWHSVSVERNGRSVT 95
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 84794568 1615 MLIDGLTVLEDRAPGRNTSLLVQDPLYVGGVPPHQamKNIQRTSVSSFTGCVRSLQLN 1672
Cdd:cd00110   96 LSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDL--KSPGLPVSPGFVGCIRDLKVN 151
LamG smart00282
Laminin G domain;
1542-1674 5.28e-32

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 122.06  E-value: 5.28e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568    1542 HFSLSLKTRSAFGLIFYLADASGENSMALFLTHARLVFTFSSGQSQVRIRSK-EKYNDGQWHDIIFIRAGNMGRMLIDGL 1620
Cdd:smart00282    1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDpTPLNDGQWHRVAVERNGRSVTLSVDGG 80
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....
gi 84794568    1621 TVLEDRAPGRNTSLLVQDPLYVGGVPPHQAMKNIQRTsvSSFTGCVRSLQLNGR 1674
Cdd:smart00282   81 NRVSGESPGGLTILNLDGPLYLGGLPEDLKLPPLPVT--PGFRGCIRNLKVNGK 132
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
1547-1674 6.44e-28

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: 110.20  E-value: 6.44e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568   1547 LKTRSAFGLIFYLADASGEnSMALFLTHARLVFTFSSGQSQVRIRS-KEKYNDGQWHDIIFIRAGNMGRMLIDGLTVLED 1625
Cdd:pfam02210    1 FRTRQPNGLLLYAGGGGSD-FLALELVNGRLVLRYDLGSGPESLLSsGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSS 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 84794568   1626 RAPGRNTSLLVQDPLYVGGVPPHQAMKNIQRTsvSSFTGCVRSLQLNGR 1674
Cdd:pfam02210   80 LPPGESLLLNLNGPLYLGGLPPLLLLPALPVR--AGFVGCIRDVRVNGE 126
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
1696-1847 1.23e-26

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: 107.50  E-value: 1.23e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568 1696 GTYFaEEGGYVLLDDSFHFGSSFKMAMEVRPRVASGVLLHV-FMEQKEYLTVYIYQSQVVVVVNNGiaEFSTHVSPTQEI 1774
Cdd:cd00110    1 GVSF-SGSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAgSQNGGDFLALELEDGRLVLRYDLG--SGSLVLSSKTPL 77
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 84794568 1775 CDGNWHKITVIRDGSVLQLDVDSE-VNHVVGSVSDAAQSSSSPVFIGGAPDSMLSHSLLSRRGFTGCMRSVSVN 1847
Cdd:cd00110   78 NDGQWHSVSVERNGRSVTLSVDGErVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
Laminin_I pfam06008
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ...
356-611 7.47e-26

Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.


Pssm-ID: 310534 [Multi-domain]  Cd Length: 258  Bit Score: 108.65  E-value: 7.47e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568    356 VLNISTGAAANDRLKYYNYTAHRLQAQFRGWRKNYAMMSGDTDVLEEETQNLLTDMDQFAEEENEVQNLGKQVDQETLNS 435
Cdd:pfam06008    1 LLSLNSLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568    436 STRAKTLTANLSSLNVLIEDMIRDWELYGVYQELDPQVKLQ-KLAEAERILGWMRKLNLSPKEPLATDESSEAHELLRRV 514
Cdd:pfam06008   81 LGHAKELAEAIKNLIDNIKEINEKVATLGENDFALPSSDLSrMLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQDLLSRI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568    515 RS-FDRNLMTTQGRLPPMQEVLGRFTSKLLQAQDLLSKAEDALKQAINKYKSNQLKLQRREAQQQRLKDIQDGVDQTIVN 593
Cdd:pfam06008  161 QTwFQSPQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEETLKT 240
                          250
                   ....*....|....*...
gi 84794568    594 AAAVLSEANHTVLEVEDV 611
Cdd:pfam06008  241 ARDSLDAANLLLQEIDDA 258
Laminin_II pfam06009
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 ...
790-919 2.06e-24

Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.


Pssm-ID: 368703 [Multi-domain]  Cd Length: 138  Bit Score: 100.64  E-value: 2.06e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568    790 TQEVAEGTLNRSAEVLEKVTPILKRVEQWDGNMKSEAYSAA-------AFDRTVLSAGEAVKDLSAIVPELLSKLRVVEE 862
Cdd:pfam06009    1 SKELAREANETAKEVLEQLAPLSQNLENTSEKLSGINRSLEetnelvnDANKALDDAGRSVKKLEELAPDLLDKLKPLKQ 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 84794568    863 KKP-VNNVTTSIMKIRGLIAQARSVAKKVQVSMKFDGQSAVEVHPHTNLDELKTVTSI 919
Cdd:pfam06009   81 LEVnSSSLSDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTSL 138
LamG smart00282
Laminin G domain;
1719-1848 1.10e-22

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 95.48  E-value: 1.10e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568    1719 KMAMEVRPRVASGVLLHV-FMEQKEYLTVYIYQSQVVVVVNNGIAEFSTHVSPTQeICDGNWHKITVIRDGSVLQLDVDS 1797
Cdd:smart00282    1 SISFSFRTTSPNGLLLYAgSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTP-LNDGQWHRVAVERNGRSVTLSVDG 79
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|...
gi 84794568    1798 EvNHVVGSVSDAAQSSS--SPVFIGGAPDSMLSHSLLSRRGFTGCMRSVSVNE 1848
Cdd:smart00282   80 G-NRVSGESPGGLTILNldGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNG 131
Laminin_G_1 pfam00054
Laminin G domain;
1548-1676 3.29e-21

Laminin G domain;


Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 91.22  E-value: 3.29e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568   1548 KTRSAFGLIFYLADASGENSMALFLTHARLVFTFSSGQSQVRIRSKEKYNDGQWHDIIFIRAGNMGRMLIDGLTVLEDRA 1627
Cdd:pfam00054    2 RTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGES 81
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 84794568   1628 P-GRNTSLLVQDPLYVGGVPPhQAMKNIQRTSVSSFTGCVRSLQLNGRSL 1676
Cdd:pfam00054   82 PlGATTDLDVDGPLYVGGLPS-LGVKKRRLAISPSFDGCIRDVIVNGKPL 130
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
1724-1849 9.36e-21

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: 89.79  E-value: 9.36e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568   1724 VRPRVASGVLLHVFMEQKEYLTVYIYQSQVVVVVNNGIAEFSTHVSPTQeICDGNWHKITVIRDGSVLQLDVDSEVNHVV 1803
Cdd:pfam02210    1 FRTRQPNGLLLYAGGGGSDFLALELVNGRLVLRYDLGSGPESLLSSGKN-LNDGQWHSVRVERNGNTLTLSVDGQTVVSS 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 84794568   1804 GSVSDAAQ-SSSSPVFIGGAPDSMLSHSLLSRRGFTGCMRSVSVNET 1849
Cdd:pfam02210   80 LPPGESLLlNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVNGE 126
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
1104-1259 2.18e-20

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: 89.40  E-value: 2.18e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568 1104 SYLFDGTGYALVNNIERRGKIgvvTRFDIEVRTVANNGILFLMVNE--TNFFVLELKNGFLRLMYDFGfaNGPVIIETnl 1181
Cdd:cd00110    1 GVSFSGSSYVRLPTLPAPRTR---LSISFSFRTTSPNGLLLYAGSQngGDFLALELEDGRLVLRYDLG--SGSLVLSS-- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568 1182 aKLQINDARYHEVSVIyHHSKKIILLVDR-SHVKSFESEKKPL--PFSDIYIGGAPSRILQSRpeLTSLIGLKGCVKGFQ 1258
Cdd:cd00110   74 -KTPLNDGQWHSVSVE-RNGRSVTLSVDGeRVVESGSPGGSALlnLDGPLYLGGLPEDLKSPG--LPVSPGFVGCIRDLK 149

                 .
gi 84794568 1259 F 1259
Cdd:cd00110  150 V 150
LamG smart00282
Laminin G domain;
1129-1262 4.56e-18

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 82.39  E-value: 4.56e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568    1129 RFDIEVRTVANNGILFLM--VNETNFFVLELKNGFLRLMYDFGfaNGPVIIETNlaKLQINDARYHEVSVIYHHsKKIIL 1206
Cdd:smart00282    1 SISFSFRTTSPNGLLLYAgsKGGGDYLALELRDGRLVLRYDLG--SGPARLTSD--PTPLNDGQWHRVAVERNG-RSVTL 75
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 84794568    1207 LVD---RSHVKSFESEKKPLPFSDIYIGGAPSriLQSRPELTSLIGLKGCVKGFQFQKE 1262
Cdd:smart00282   76 SVDggnRVSGESPGGLTILNLDGPLYLGGLPE--DLKLPPLPVTPGFRGCIRNLKVNGK 132
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
1134-1259 5.73e-17

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: 79.00  E-value: 5.73e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568   1134 VRTVANNGILFLMVNETN-FFVLELKNGFLRLMYDFGfaNGPVIIETNLAKLqiNDARYHEVSVIYhHSKKIILLVDRSH 1212
Cdd:pfam02210    1 FRTRQPNGLLLYAGGGGSdFLALELVNGRLVLRYDLG--SGPESLLSSGKNL--NDGQWHSVRVER-NGNTLTLSVDGQT 75
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 84794568   1213 VKSFESEKKPLPF---SDIYIGGAPSRILQSRPELTSliGLKGCVKGFQF 1259
Cdd:pfam02210   76 VVSSLPPGESLLLnlnGPLYLGGLPPLLLLPALPVRA--GFVGCIRDVRV 123
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
893-1067 2.97e-16

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: 77.84  E-value: 2.97e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568  893 SMKFDGQSAVEVhphTNLDELKTVTSISFYIRvdPDKdpiEDRFLLYLGDKQGKrDYMGLAIKNDNLVYVYKLGEEEVEI 972
Cdd:cd00110    1 GVSFSGSSYVRL---PTLPAPRTRLSISFSFR--TTS---PNGLLLYAGSQNGG-DFLALELEDGRLVLRYDLGSGSLVL 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568  973 plsSKPVSSWPPVFNFVKVERLGRHgkVFLTVpsqDttaEQKFIQKGEPvgtDTLFDLDPKDMVFiVGGVPPGVTVPPIL 1052
Cdd:cd00110   72 ---SSKTPLNDGQWHSVSVERNGRS--VTLSV---D---GERVVESGSP---GGSALLNLDGPLY-LGGLPEDLKSPGLP 136
                        170
                 ....*....|....*
gi 84794568 1053 SLAPFVGCIELETLN 1067
Cdd:cd00110  137 VSPGFVGCIRDLKVN 151
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
1289-1422 6.31e-16

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: 76.69  E-value: 6.31e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568 1289 AYFTGNGYLSSSDKISPFQSFEGGLSFKTLQPSGLLFYH--RDGSDEFSLSLENGAVVLQ----AKGTRVKSqKKHYSDG 1362
Cdd:cd00110    2 VSFSGSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAgsQNGGDFLALELEDGRLVLRydlgSGSLVLSS-KTPLNDG 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 84794568 1363 RSHFLVASVTNQKYEIVIdDKDKQDKKKPSSTSQSDNTPKAFYYGGSTSSSIL-------NLTGCIS 1422
Cdd:cd00110   81 QWHSVSVERNGRSVTLSV-DGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSpglpvspGFVGCIR 146
LamG smart00282
Laminin G domain;
918-1068 9.54e-15

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 72.76  E-value: 9.54e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568     918 SISFYIRvdpdkdPIEDR-FLLYLGDKQGKrDYMGLAIKNDNLVYVYKLGEEEVEIPLSSKPVS--SWppvfNFVKVERL 994
Cdd:smart00282    1 SISFSFR------TTSPNgLLLYAGSKGGG-DYLALELRDGRLVLRYDLGSGPARLTSDPTPLNdgQW----HRVAVERN 69
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 84794568     995 GRHgkVFLTVPSQDTTAEQKFIQKgepvgtdtlFDLDPKDMVFiVGGVPPGVTVPPILSLAPFVGCIELETLNN 1068
Cdd:smart00282   70 GRS--VTLSVDGGNRVSGESPGGL---------TILNLDGPLY-LGGLPEDLKLPPLPVTPGFRGCIRNLKVNG 131
Laminin_G_1 pfam00054
Laminin G domain;
1134-1255 1.95e-14

Laminin G domain;


Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 71.96  E-value: 1.95e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568   1134 VRTVANNGILFLM--VNETNFFVLELKNGFLRLMYDFGfaNGPVIIEtnlAKLQINDARYHEVSVIYHHsKKIILLVDRS 1211
Cdd:pfam00054    1 FRTTEPSGLLLYNgtQTERDFLALELRDGRLEVSYDLG--SGAAVVR---SGDKLNDGKWHSVELERNG-RSGTLSVDGE 74
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 84794568   1212 HVKSFESEKKPLPFSD----IYIGGAPSRILQSRPeLTSLIGLKGCVK 1255
Cdd:pfam00054   75 ARPTGESPLGATTDLDvdgpLYVGGLPSLGVKKRR-LAISPSFDGCIR 121
Laminin_G_1 pfam00054
Laminin G domain;
1766-1851 1.30e-13

Laminin G domain;


Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 69.27  E-value: 1.30e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568   1766 THVSPTQEICDGNWHKITVIRDGSVLQLDVDSEVNHVVGSVSDAAQ--SSSSPVFIGGAPDSMLSHSLL-SRRGFTGCMR 1842
Cdd:pfam00054   42 AVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGESPLGATTdlDVDGPLYVGGLPSLGVKKRRLaISPSFDGCIR 121

                   ....*....
gi 84794568   1843 SVSVNETPV 1851
Cdd:pfam00054  122 DVIVNGKPL 130
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
1315-1429 1.43e-12

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: 66.29  E-value: 1.43e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568   1315 FKTLQPSGLLFYHRDGSDEF-SLSLENGAVVLQ----AKGTRVKSQKKHYSDGRSHFLVASVTNQKYEIVIDDKDKQDKK 1389
Cdd:pfam02210    1 FRTRQPNGLLLYAGGGGSDFlALELVNGRLVLRydlgSGPESLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSL 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 84794568   1390 KPSSTSQsDNTPKAFYYGG-------STSSSILNLTGCISYAYISRQ 1429
Cdd:pfam02210   81 PPGESLL-LNLNGPLYLGGlppllllPALPVRAGFVGCIRDVRVNGE 126
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
209-247 3.94e-12

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 62.33  E-value: 3.94e-12
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 84794568     209 CQCNKCGTAS--CDDRSGVCHCKPGVTGQLCDRCEDGHSGF 247
Cdd:smart00180    1 CDCDPGGSASgtCDPDTGQCECKPNVTGRRCDRCAPGYYGD 41
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
155-207 7.43e-12

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: 61.60  E-value: 7.43e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 84794568  155 CDCNGNSDPNlifNECHNVTGKCLnCWGDTAGDNCERCAPGFYGDAISAKDCQ 207
Cdd:cd00055    2 CDCNGHGSLS---GQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
209-253 8.16e-12

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 61.60  E-value: 8.16e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 84794568    209 CQCNKCGTAS--CDDRSGVCHCKPGVTGQLCDRCEDGHSGFCTCMGC 253
Cdd:pfam00053    1 CDCNPHGSLSdtCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQ 47
LamG smart00282
Laminin G domain;
1313-1429 9.60e-12

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 64.28  E-value: 9.60e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568    1313 LSFKTLQPSGLLFYH--RDGSDEFSLSLENGAVVLQ----AKGTRVKSQKKHYSDGRSHFLVASVTNQKYEIVIDDKDKQ 1386
Cdd:smart00282    4 FSFRTTSPNGLLLYAgsKGGGDYLALELRDGRLVLRydlgSGPARLTSDPTPLNDGQWHRVAVERNGRSVTLSVDGGNRV 83
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|
gi 84794568    1387 DKKKPSSTSQSdNTPKAFYYGGSTSSSIL-------NLTGCISYAYISRQ 1429
Cdd:smart00282   84 SGESPGGLTIL-NLDGPLYLGGLPEDLKLpplpvtpGFRGCIRNLKVNGK 132
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
209-247 1.02e-11

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: 61.22  E-value: 1.02e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 84794568  209 CQCNKCGTAS--CDDRSGVCHCKPGVTGQLCDRCEDGHSGF 247
Cdd:cd00055    2 CDCNGHGSLSgqCDPGTGQCECKPNTTGRRCDRCAPGYYGL 42
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
256-300 4.58e-11

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 59.25  E-value: 4.58e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 84794568     256 CEC-ASAALRATCHPLTHSCQCRPGAGGRYCERCLPGFWDYSPSGC 300
Cdd:smart00180    1 CDCdPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
256-303 1.17e-10

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 58.13  E-value: 1.17e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 84794568    256 CEC-ASAALRATCHPLTHSCQCRPGAGGRYCERCLPGFWDYSPSGCRKC 303
Cdd:pfam00053    1 CDCnPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
255-301 2.37e-10

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: 57.36  E-value: 2.37e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 84794568  255 RCEC-ASAALRATCHPLTHSCQCRPGAGGRYCERCLPGFWDYS--PSGCR 301
Cdd:cd00055    1 PCDCnGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPsqGGGCQ 50
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
99-152 2.95e-10

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 56.98  E-value: 2.95e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 84794568     99 CACPLSLESNnfaAHCDRRGefLRCVCQDGYAGHYCERCAPGYYGNPMELGNSC 152
Cdd:pfam00053    1 CDCNPHGSLS---DTCDPET--GQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
936-1068 1.21e-09

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: 57.81  E-value: 1.21e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568    936 FLLYLGDKQGkrDYMGLAIKNDNLVYVYKLGEEEVEIPLSSKPVS--SWppvfNFVKVERLGRHgkVFLTVPSQDTTAEQ 1013
Cdd:pfam02210    9 LLLYAGGGGS--DFLALELVNGRLVLRYDLGSGPESLLSSGKNLNdgQW----HSVRVERNGNT--LTLSVDGQTVVSSL 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 84794568   1014 KfiqKGEPVGTDTLFDLdpkdmvfIVGGVPPGVTVPPILSLAPFVGCIELETLNN 1068
Cdd:pfam02210   81 P---PGESLLLNLNGPL-------YLGGLPPLLLLPALPVRAGFVGCIRDVRVNG 125
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
155-206 1.44e-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: 1.44e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 84794568    155 CDCNGNSDPNlifNECHNVTGKCLnCWGDTAGDNCERCAPGFYGDAI-SAKDC 206
Cdd:pfam00053    1 CDCNPHGSLS---DTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSdPPQGC 49
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
98-153 1.00e-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: 52.74  E-value: 1.00e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 84794568   98 PCACPLSLESNNfaaHCDRRGefLRCVCQDGYAGHYCERCAPGYYGNPmELGNSCK 153
Cdd:cd00055    1 PCDCNGHGSLSG---QCDPGT--GQCECKPNTTGRRCDRCAPGYYGLP-SQGGGCQ 50
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
99-152 6.78e-08

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 50.39  E-value: 6.78e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 84794568      99 CACPLSlesNNFAAHCDRRGefLRCVCQDGYAGHYCERCAPGYYGNPmelGNSC 152
Cdd:smart00180    1 CDCDPG---GSASGTCDPDT--GQCECKPNVTGRRCDRCAPGYYGDG---PPGC 46
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
155-206 9.37e-08

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 50.00  E-value: 9.37e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 84794568     155 CDCN--GNSDpnlifNECHNVTGKCLnCWGDTAGDNCERCAPGFYGDaiSAKDC 206
Cdd:smart00180    1 CDCDpgGSAS-----GTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD--GPPGC 46
Laminin_G_1 pfam00054
Laminin G domain;
1315-1429 1.64e-07

Laminin G domain;


Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 51.93  E-value: 1.64e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568   1315 FKTLQPSGLLFYH-------------RDGSDEFSLSLENGAVVLQAkGTRVksqkkhySDGRSHFLVASVTNQKYEIVID 1381
Cdd:pfam00054    1 FRTTEPSGLLLYNgtqterdflalelRDGRLEVSYDLGSGAAVVRS-GDKL-------NDGKWHSVELERNGRSGTLSVD 72
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 84794568   1382 DKDKQDKKKPSSTSQSDNTPKAFYYGGSTSSSILN--------LTGCISYAYISRQ 1429
Cdd:pfam00054   73 GEARPTGESPLGATTDLDVDGPLYVGGLPSLGVKKrrlaispsFDGCIRDVIVNGK 128
TNFRSF4 cd13406
Tumor necrosis factor receptor superfamily member 4 (TNFRSF4), also known as CD134 or OXO40; ...
121-274 1.96e-07

Tumor necrosis factor receptor superfamily member 4 (TNFRSF4), also known as CD134 or OXO40; TNFRSF4 (also known as OX40, ACT35, CD134, IMD16, TXGP1L) activates NF-kappaB through its interaction with adaptor proteins TRAF2 and TRAF5. It also promotes the expression of apoptosis inhibitors BCL2 and BCL2lL1/BCL2-XL, and thus suppresses apoptosis. It is primarily expressed on activated CD4+ and CD8+ T cells, where it is transiently expressed and upregulated on the most recently antigen-activated T cells within inflammatory lesions. This makes it an attractive target to modulate immune responses, i.e. TNFRSF4 (OX40) blocking agents to inhibit adverse inflammation or agonists to enhance immune responses. An artificially created biologic fusion protein, OX40-immunoglobulin (OX40-Ig), prevents OX40 from reaching the T-cell receptors, thus reducing the T-cell response. Some single nucleotide polymorphisms (SNPs) of its natural ligand OX40 ligand (OX40L, CD252), which is also found on activated T cells, have been associated with systemic lupus erythematosus.


Pssm-ID: 276911 [Multi-domain]  Cd Length: 142  Bit Score: 52.02  E-value: 1.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568  121 LRCVcQDGYAGHY--CERCAPGYygnPMElgnsckkCDCNGNSDPNlifnechnvtgkclncwgdtagdnCERCAPGFYG 198
Cdd:cd13406    1 LHCV-GDTYPSGEkcCHECPPGE---GME-------SRCTGTQDTV------------------------CSPCEPGFYN 45
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568  199 DAISAKDCQEC-QCNK----CGTASCDDRSG-VCHCKPGVT-------GQLCDRCEDGHsgfCTCMGCRRCE----CASA 261
Cdd:cd13406   46 EAVNYEPCKPCtQCNQrsgsEEKQKCTKTSDtVCRCRPGTQpldsykpGVDCVPCPPGH---FSRGDNQACKpwtnCSLA 122
                        170
                 ....*....|...
gi 84794568  262 ALRaTCHPLTHSC 274
Cdd:cd13406  123 GKR-TLRPGSSTS 134
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
402-658 1.51e-06

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.52  E-value: 1.51e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568    402 EETQNLLTDM-DQFAEEENEVQNLGKQVDQ---ETLNSSTRAKTLTANLSSLNVLIEDMIRDWElygVYQELDPQVKLQK 477
Cdd:TIGR02168  242 EELQEELKEAeEELEELTAELQELEEKLEElrlEVSELEEEIEELQKELYALANEISRLEQQKQ---ILRERLANLERQL 318
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568    478 LAEAERILGWMRKLNLSPKEplATDESSEAHELLRRVRSFdrnlmttQGRLPPMQEVLGRFTSKLLQAQDLLSKAEDALK 557
Cdd:TIGR02168  319 EELEAQLEELESKLDELAEE--LAELEEKLEELKEELESL-------EAELEELEAELEELESRLEELEEQLETLRSKVA 389
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568    558 QAINKYKSNQLKLQRREAQQQRLKDIQDGVDQTIVNAAAVLSEANhtVLEVEDVITNVREQHAEIDGARVLLERRTEKIS 637
Cdd:TIGR02168  390 QLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE--LKELQAELEELEEELEELQEELERLEEALEELR 467
                          250       260
                   ....*....|....*....|.
gi 84794568    638 QSDRELVLRAEDHADQLQRHA 658
Cdd:TIGR02168  468 EELEEAEQALDAAERELAQLQ 488
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
488-863 6.03e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 50.67  E-value: 6.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568  488 MRKLNLSPKEPLATDESSE-AHELLRRVRSFDRNLMTTQGRLPPMQEVLGRFTSKLLQAQDLLSKAEDALKQAINKYKSN 566
Cdd:COG4372   13 LSLFGLRPKTGILIAALSEqLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAA 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568  567 QLKLQRREAQ----QQRLKDIQDGVDQTIVNAAAVLSEANHTVLEVEDVITNVREQHAEIDGARVLLERRTEKISQSDRE 642
Cdd:COG4372   93 QAELAQAQEEleslQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQE 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568  643 LVLRAEDHADQ-LQRHAEEpqhnlkgsdANGHVQKALNAFNVYDNIVKSVDDANITSLTALNISSRTHGAVDKLSSQlnl 721
Cdd:COG4372  173 LQALSEAEAEQaLDELLKE---------ANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLD--- 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568  722 mrsqsAKVLNEASSLHFQQQDSESIVLDNKKYIEETNEMMDGSSKKIAKIITEINAIhtDRTPKRLQFTQEVAEGTLNRS 801
Cdd:COG4372  241 -----ALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAA--LELKLLALLLNLAALSLIGAL 313
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 84794568  802 AEVLEKVTPILKRVEQwdgnmksEAYSAAAFDRTVLSAGEAVKDLSAIVPELLSKLRVVEEK 863
Cdd:COG4372  314 EDALLAALLELAKKLE-------LALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVA 368
PRK10246 PRK10246
exonuclease subunit SbcC; Provisional
442-584 9.06e-06

exonuclease subunit SbcC; Provisional


Pssm-ID: 182330 [Multi-domain]  Cd Length: 1047  Bit Score: 50.95  E-value: 9.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568   442 LTANLSSLNV-LIE-DMIRDW--ELYGVYQELDPQV--KLQKLAEAERILGWMRKLNLSPKEPLA--TDESSEAHELLRR 513
Cdd:PRK10246  341 LQAQQQSLNTwLAEhDRFRQWnnELAGWRAQFSQQTsdREQLRQWQQQLTHAEQKLNALPAITLTltADEVAAALAQHAE 420
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 84794568   514 VRSFDRNLMTTQGRLPPMQEVLGRFTSKLLQAQDLLSKAEDALKQAINKYKSNQLKLQRREA---QQQRLKDIQ 584
Cdd:PRK10246  421 QRPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLADVKTiceQEARIKDLE 494
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
378-803 2.38e-05

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.38  E-value: 2.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568  378 RLQAQFRGWRKNYAMMSGDTDVLEEETQNLLTDMDQFAEEENEVQNLGKQVDQetlnSSTRAKTLTANLSSLnvliEDMI 457
Cdd:COG4717   54 EADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEE----LEAELEELREELEKL----EKLL 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568  458 RDWELYGVYQEL-----DPQVKLQKL-AEAERILGWMRKLnlspkePLATDESSEAHELLRRVRsfDRNLMTTQGRLPPM 531
Cdd:COG4717  126 QLLPLYQELEALeaelaELPERLEELeERLEELRELEEEL------EELEAELAELQEELEELL--EQLSLATEEELQDL 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568  532 QEVLGRFTSKLLQAQDLLSKAEDALKQAINKYKSNQLKLQrREAQQQRLKdiQDGVDQTIVNAAAVLSEANHTVLEVEDV 611
Cdd:COG4717  198 AEELEELQQRLAELEEELEEAQEELEELEEELEQLENELE-AAALEERLK--EARLLLLIAAALLALLGLGGSLLSLILT 274
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568  612 ITNVREQHAEIDGARVLLERRTEKISQSDRELV--------LRAEDHADQLQRH----AEEPQHNLKGSDANGHVQKALN 679
Cdd:COG4717  275 IAGVLFLVLGLLALLFLLLAREKASLGKEAEELqalpaleeLEEEELEELLAALglppDLSPEELLELLDRIEELQELLR 354
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568  680 AFN----------VYDNIVKSVDDANITSLTALNISSRTHGAVDKLSSQLNLMRSQSAKVLNEASSLHfQQQDSESI--- 746
Cdd:COG4717  355 EAEeleeelqleeLEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELL-EALDEEELeee 433
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 84794568  747 VLDNKKYIEETNEMMDGSSKKIAKIITEINAIHTDRTPKRLQFTQEVAEGTLNRSAE 803
Cdd:COG4717  434 LEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAE 490
Laminin_G_1 pfam00054
Laminin G domain;
937-1068 3.00e-05

Laminin G domain;


Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 45.39  E-value: 3.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568    937 LLYLGDKQGKRDYMGLAIKNDNLVYVYKLGeeeveiplsSKPVSSWPPV------FNFVKVERLGRHGkvFLTVpsqDTT 1010
Cdd:pfam00054    9 LLLYNGTQTERDFLALELRDGRLEVSYDLG---------SGAAVVRSGDklndgkWHSVELERNGRSG--TLSV---DGE 74
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 84794568   1011 AEQKFIQkgePVGTDTlfDLDPKDMVFiVGGVPPGVTVPPILSLAP-FVGCIELETLNN 1068
Cdd:pfam00054   75 ARPTGES---PLGATT--DLDVDGPLY-VGGLPSLGVKKRRLAISPsFDGCIRDVIVNG 127
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
474-665 3.97e-05

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 46.67  E-value: 3.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568  474 KLQKLA-EAERILGWMRKlnlspKEPLATDES-----SEAHELLRRVRSFDRNLMTTQGRLPPMQEV------LGRFTSK 541
Cdd:cd00176    1 KLQQFLrDADELEAWLSE-----KEELLSSTDygddlESVEALLKKHEALEAELAAHEERVEALNELgeqlieEGHPDAE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568  542 LLQA-QDLLSKAEDALKQAINKYKSnqlKLQRREAQQQRLKDIQDgVDQTIVNAAAVLS--EANHTVLEVEDVITNVREQ 618
Cdd:cd00176   76 EIQErLEELNQRWEELRELAEERRQ---RLEEALDLQQFFRDADD-LEQWLEEKEAALAseDLGKDLESVEELLKKHKEL 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 84794568  619 HAEIDG-----------ARVLLERRTEKISQSDRELVLRAEDHADQLQRHAEEPQHNL 665
Cdd:cd00176  152 EEELEAheprlkslnelAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKL 209
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
490-817 4.33e-05

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 48.66  E-value: 4.33e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568    490 KLNLSPKEPLATDESSEAHELLRRVRSFDRNLMTTQGRLPPMQEVLGRFTSKLLQAQDLLskaeDALKQAIN----KYKS 565
Cdd:pfam10174  330 KESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDML----DVKERKINvlqkKIEN 405
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568    566 NQLKLQRREAQQQRLKDIQDGVDQTIVN---AAAVLSEAnhtVLEVEDVITNVREQHA--------EIDGARVLLERRTE 634
Cdd:pfam10174  406 LQEQLRDKDKQLAGLKERVKSLQTDSSNtdtALTTLEEA---LSEKERIIERLKEQREredrerleELESLKKENKDLKE 482
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568    635 KISQSDREL------VLRAEDHADQLQRHAEEPQHNLKGSDANghVQKALNAFNVYDNIVKSVDDANITSLTALNISSRt 708
Cdd:pfam10174  483 KVSALQPELtekessLIDLKEHASSLASSGLKKDSKLKSLEIA--VEQKKEECSKLENQLKKAHNAEEAVRTNPEINDR- 559
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568    709 hgaVDKLSSQLNLMRSQSAKVLNEASSLHFQQQDSESIVLDNKKYIEETNEMMDGSSKKIAKIITEINAIHTDRTPKRLQ 788
Cdd:pfam10174  560 ---IRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQ 636
                          330       340       350
                   ....*....|....*....|....*....|...
gi 84794568    789 FTQEVAEGTLNRSAEV----LEKVTPILKRVEQ 817
Cdd:pfam10174  637 LLEEARRREDNLADNSqqlqLEELMGALEKTRQ 669
Laminin_G_3 pfam13385
Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin ...
1543-1679 6.75e-05

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


Pssm-ID: 463865 [Multi-domain]  Cd Length: 151  Bit Score: 45.07  E-value: 6.75e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568   1543 FSLSL--KTRSAFGLIFYLADASGENSMALFLTHA-RLVFTFSSGQSQVR-IRSKEKYNDGQWHDIIFIRAGNMGRMLID 1618
Cdd:pfam13385   19 FTVSAwvKPDSLPGWARAIISSSGGGGYSLGLDGDgRLRFAVNGGNGGWDtVTSGASVPLGQWTHVAVTYDGGTLRLYVN 98
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 84794568   1619 GltVLEDRAPGRNTSLLVQD-PLYVGGVPPHQamkniqrtsvSSFTGCVRSLQLNGRSLTSA 1679
Cdd:pfam13385   99 G--VLVGSSTLTGGPPPGTGgPLYIGRSPGGD----------DYFNGLIDEVRIYDRALSAA 148
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
466-666 1.60e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.85  E-value: 1.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568  466 YQELdpQVKLQKLaEAERILGWMRKLNLSpkeplATDESSEAHELLRRVRSFDRNLMTTQGRLPPMQEVLGRFTSKLLQA 545
Cdd:COG1196  215 YREL--KEELKEL-EAELLLLKLRELEAE-----LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEA 286
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568  546 QDLLSKAEDALKQAINKYKSNQLKLQRREAQQQRLKDIQDGVDQTIVNAAAVLSEANHTVLEVEDVITNVREQHAEIDGA 625
Cdd:COG1196  287 QAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 84794568  626 RVLLERRTEKISQSDRELVLRAEDHADQLQRHAEEPQHNLK 666
Cdd:COG1196  367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE 407
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
445-660 2.85e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.06  E-value: 2.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568  445 NLSSLNVLIEDMIRDwelygvyqelDPQVklqkLAEAERILGWMRKLNlspkeplatdessEAHELLRRVRsfdRNLMTt 524
Cdd:COG4913  205 PIGDLDDFVREYMLE----------EPDT----FEAADALVEHFDDLE-------------RAHEALEDAR---EQIEL- 253
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568  525 qgrLPPMQEVLGRFTSKLLQAQDLlskaeDALKQAINKYKsNQLKLQRREAQQQRLKDIQDGVDQTIVNAAAVLSEAnht 604
Cdd:COG4913  254 ---LEPIRELAERYAAARERLAEL-----EYLRAALRLWF-AQRRLELLEAELEELRAELARLEAELERLEARLDAL--- 321
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 84794568  605 vlevEDVITNVREQHAEIDGARvlLERRTEKISQSDRELVlRAEDHADQLQRHAEE 660
Cdd:COG4913  322 ----REELDELEAQIRGNGGDR--LEQLEREIERLERELE-ERERRRARLEALLAA 370
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
443-654 2.90e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.91  E-value: 2.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568  443 TANLSSLNVLIEDMIRDWELYGVYQELDPQVKLQKLAEAERILgwMRKLNLSPKEPLAT--DESSEAHELLRRVRSFDRN 520
Cdd:COG4717  333 DLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAL--LAEAGVEDEEELRAalEQAEEYQELKEELEELEEQ 410
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568  521 LmttQGRLPPMQEVLGRFTSKLLQAQdlLSKAEDALKQAINKYKSNQLKLQRREAQQQRLKDiqdgvDQTivnaaavLSE 600
Cdd:COG4717  411 L---EELLGELEELLEALDEEELEEE--LEELEEELEELEEELEELREELAELEAELEQLEE-----DGE-------LAE 473
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 84794568  601 ANHTVLEVEDVITNVREQHAEIDGARVLLERRTEKISQSDRELVL-RAEDHADQL 654
Cdd:COG4717  474 LLQELEELKAELRELAEEWAALKLALELLEEAREEYREERLPPVLeRASEYFSRL 528
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
401-756 5.43e-04

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 45.01  E-value: 5.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568    401 EEETQNLLTDMDQFAEE----ENEVQNLGKQV--DQETLNSS-TRAKTLTANLSSLN-----------VLIEDMIRdwel 462
Cdd:TIGR04523   32 DTEEKQLEKKLKTIKNElknkEKELKNLDKNLnkDEEKINNSnNKIKILEQQIKDLNdklkknkdkinKLNSDLSK---- 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568    463 ygvyqeLDPQVKLQK---------LAEAERILGWMRKL------NLSPKEPLATDESSEAHELLRRVRSFDRNLMTTQGR 527
Cdd:TIGR04523  108 ------INSEIKNDKeqknkleveLNKLEKQKKENKKNidkfltEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKE 181
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568    528 LPPMQEVLGRFTSKLLQAQDLLSKaedaLKQAINKYKSNQLKLQRREAQQQRLKDIQDGVDQTIVNAAAVLSEANHTVLE 607
Cdd:TIGR04523  182 KLNIQKNIDKIKNKLLKLELLLSN----LKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQ 257
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568    608 VEDVITNVREQhaeidgarvlLERRTEKISQSDRELvlraEDHADQLQrhaeepQHNLKGSDANGhvQKALNAFNVYDNI 687
Cdd:TIGR04523  258 LKDEQNKIKKQ----------LSEKQKELEQNNKKI----KELEKQLN------QLKSEISDLNN--QKEQDWNKELKSE 315
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 84794568    688 VKSVDDANITSLTALnisSRTHGAVDKLSSQLNLMRSQSAKVLNEASSLHFQ----QQDSESIVLDNKKYIEE 756
Cdd:TIGR04523  316 LKNQEKKLEEIQNQI---SQNNKIISQLNEQISQLKKELTNSESENSEKQREleekQNEIEKLKKENQSYKQE 385
VSP pfam03302
Giardia variant-specific surface protein;
134-334 8.89e-04

Giardia variant-specific surface protein;


Pssm-ID: 146106 [Multi-domain]  Cd Length: 397  Bit Score: 43.80  E-value: 8.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568    134 CERCAPGYYGNpmelGNSCKKCD-----CNGNSDPNLifNEChnVTGKCLNCWGDTAGDNC-ERCAPGfygdaISAKDCQ 207
Cdd:pfam03302   93 CQACNDGFYKS----GDACSPCHescktCSGGTASDC--TEC--LTGKALRYGNDGTKGTCgEGCTTG-----TGAGACK 159
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568    208 EC--------QCNKCGTASCDDRSGVCHCKPGVTGQLCDRC--EDGHSGFCTCM------GCR-------RCECASAALR 264
Cdd:pfam03302  160 TCgltidgtsYCSECATETEYPQNGVCTSTAARATATCKASsvANGMCSSCANGyfrmngGCYettkfpgKSVCEEANSG 239
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568    265 ATCHP------------LTHSCQCRPGAGGRYCERCLPGFWDYSpSGCRKCDCPEENCDLHTGECLPELSQISECNISCD 332
Cdd:pfam03302  240 GTCQKeapgyklnngdlVTCSPGCKTCTSNTVCTTCMDGYVKTS-DSCTKCDSSCETCTGATTTCKTCATGYYKSGTGCV 318

                   ..
gi 84794568    333 AC 334
Cdd:pfam03302  319 SC 320
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
508-862 3.03e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.74  E-value: 3.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568    508 HELLRRVRSFDRNLMttqgRLppmQEVLGRFTSKL--LQAQdlLSKAE------DALKQA-----INKYKSNQLKLQRRE 574
Cdd:TIGR02168  175 KETERKLERTRENLD----RL---EDILNELERQLksLERQ--AEKAErykelkAELRELelallVLRLEELREELEELQ 245
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568    575 AQQQRLKDIQDGVDQTIVNAAAVLSEANHTVLEVEDVI----TNVREQHAEIDGarvlLERRTEKISQSDRELV---LRA 647
Cdd:TIGR02168  246 EELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIeelqKELYALANEISR----LEQQKQILRERLANLErqlEEL 321
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568    648 EDHADQLQRHAEEPQHNLKGSDANGHVQKalnafNVYDNIVKSVDDANITSLTALNISSRTHGAVDKLSSQLNLMRSQSA 727
Cdd:TIGR02168  322 EAQLEELESKLDELAEELAELEEKLEELK-----EELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568    728 KVLNEASSLHFQQQDSESIVLDNKKYIEETNEMMDgsSKKIAKIITEINAihTDRTPKRLQFTQEVAEGTLNRSAEVLEK 807
Cdd:TIGR02168  397 SLNNEIERLEARLERLEDRRERLQQEIEELLKKLE--EAELKELQAELEE--LEEELEELQEELERLEEALEELREELEE 472
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 84794568    808 VTPILKRVEQWDGNMKSEAYSAAAFDRTVLSAGEAVK-------DLSAIVPELLSKLRVVEE 862
Cdd:TIGR02168  473 AEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKallknqsGLSGILGVLSELISVDEG 534
CHAD smart00880
The CHAD domain is an alpha-helical domain functionally associated with some members of the ...
396-580 5.19e-03

The CHAD domain is an alpha-helical domain functionally associated with some members of the adenylate cyclase family; It has conserved histidines that may chelate metals.


Pssm-ID: 214880 [Multi-domain]  Cd Length: 262  Bit Score: 40.84  E-value: 5.19e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568     396 DTDVLEEETQNLLtdmDQFAEEENEVQNLGKQVDQETlnSSTRAKTLTAnLSSLNVLieDMIRDWEL------YGVYQEL 469
Cdd:smart00880   70 DLDVLLERLLELL---AALLPELPALDALVAALEARR--AAARRALLAA-LDSARYT--ALLLDLSRwlatppWQPAADD 141
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84794568     470 DPQVKLQKLAeAERILGWMRKLNLSPKEPLATDESSEAHEL---LRRVR----SF-----DRNLMTTQGRLPPMQEVLGR 537
Cdd:smart00880  142 KAARPLADFA-AKALRRLLRKLRRAFPAARALLDDEALHRLrkrLKRLRyaaeFFaplydAKARKRFLKRLKDLQDALGD 220
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|...
gi 84794568     538 FTSkLLQAQDLLSKAEDALKQAINKYKSNQLKLQRREAQQQRL 580
Cdd:smart00880  221 LND-LAVARALLEDLADEAEAAQLERGLLAAERSRLEARRQAR 262
 
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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