|
Name |
Accession |
Description |
Interval |
E-value |
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
49-302 |
1.08e-99 |
|
Laminin N-terminal (Domain VI);
:
Pssm-ID: 459653 Cd Length: 230 Bit Score: 320.68 E-value: 1.08e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 49 LHPPYFNLAEGARITASATCGEEAPTRsasrptedlYCKLVGGPvaggdpnqtiQGQYCDICIAANSNKAHPVSNAIDGT 128
Cdd:pfam00055 1 CYPAFGNLAFGREVSATSTCGLNGPER---------YCILSGLE----------GGKKCFICDSRDPHNSHPPSNLTDSN 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 129 ER----WWQSPPLSRgpEYNEVNVTLDLGQVFHVAYVLIKFAnSPRPDLWVLERSTDFGHTYQPWQFFASskrDCLERFG 204
Cdd:pfam00055 62 NGtnetWWQSETGVI--QYENVNLTLDLGKEFHFTYLILKFK-SPRPAAMVLERSTDFGKTWQPYQYFAS---DCRRTFG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 205 -PRTLERITQDDDVICTTEYSRIVPLENGEIVVSLVNGRPGARNFSYSPVLRDFTKATNIRLRFLRTNTLLGHLmgkaLR 283
Cdd:pfam00055 136 rPSGPSRGIKDDEVICTSEYSDISPLTGGEVIFSTLEGRPSANIFDYSPELQDWLTATNIRIRLLRLHTLGDEL----LD 211
|
250
....*....|....*....
gi 300798041 284 DPTVTRRYYYSIKDISIGG 302
Cdd:pfam00055 212 DPSVLRKYYYAISDISVGG 230
|
|
| Laminin_I super family |
cl26988 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
2193-2448 |
8.65e-65 |
|
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: 221.90 E-value: 8.65e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2193 LRGINASSTAWARLHRLNASIADLQSKLRSPLGPHNQTAEQLQTLEQQSISLQQDTERLGSQATGVQDQAGRLLDNTEST 2272
Cdd:pfam06008 1 LLSLNSLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2273 LVRAQKLLEIVQAVSRALNELASQ--GFPGNATTPSGEQLRWALAEVERLLWDMRTRDLGAPQAVAEAELAEAQRLMARV 2350
Cdd:pfam06008 81 LGHAKELAEAIKNLIDNIKEINEKvaTLGENDFALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQDLLSRI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2351 QEQLTSFWEENQALATHIRDQLAQYESGLMDLREALNHAVNTTREADELNSRNEERLREALQWKQELSQDNATLKATLQA 2430
Cdd:pfam06008 161 QTWFQSPQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEETLKT 240
|
250
....*....|....*...
gi 300798041 2431 ASLTLAHVSELLQGIDKA 2448
Cdd:pfam06008 241 ARDSLDAANLLLQEIDDA 258
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
1693-1829 |
3.13e-49 |
|
Laminin B (Domain IV);
:
Pssm-ID: 459652 Cd Length: 136 Bit Score: 172.45 E-value: 3.13e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 1693 YWQAPPSYLGDRVSSYGGTLHYELHSETRRGDVfiPYESRPDVVLQGNQMSIAFL--ELAYPSPGQVHRGQLQLVEGNFR 1770
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGGG--SLNSEPDVILEGNGLRLSYSspDQPPPDPGQEQTYSVRLHEENWR 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 300798041 1771 HlETHNPVSREELMMVLAGLEQLQIRALFSQTSSTVSLRRVVLEVASEAGGGPPASNVE 1829
Cdd:pfam00052 79 D-SDGAPVSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSAVPGGSGPPASWVE 136
|
|
| Laminin_II super family |
cl05515 |
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 ... |
2639-2760 |
7.26e-45 |
|
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: 159.96 E-value: 7.26e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2639 DTAAHVQSQLQGMQKNVERWQSQLGGLRGQ---------DLSQAERDASSSVSTLEKTLPQLLAKLSHLENRGVHNASLa 2709
Cdd:pfam06009 10 ETAKEVLEQLAPLSQNLENTSEKLSGINRSleetnelvnDANKALDDAGRSVKKLEELAPDLLDKLKPLKQLEVNSSSL- 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 300798041 2710 lSANIGRVRKLIAQARSAANKVKVSMKFNGRSGVRLRTPRDLADLAAYTAL 2760
Cdd:pfam06009 89 -SDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTSL 138
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
3514-3663 |
1.48e-27 |
|
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: 110.97 E-value: 1.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 3514 GLFFPGSeGAVTLELPKAKMPHVSLELEVRPLAAAGLIFHLGQAHATPYVQLQLLTEQVLLRANDGAGefSTWVTYP-KL 3592
Cdd:cd00110 1 GVSFSGS-SYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSG--SLVLSSKtPL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300798041 3593 CDGQWHQVTVIKGRNTLRLEVD-THSNHTTGRLPETLADSPALLHLGSPPKSEAAWPEP--PAYRGCLRKLLFN 3663
Cdd:cd00110 78 NDGQWHSVSVERNGRSVTLSVDgERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPvsPGFVGCIRDLKVN 151
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
3338-3490 |
1.11e-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: 108.27 E-value: 1.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 3338 PGPSYLQFVGvSPSHRNRLHLSMLVRPHgASQGLLLYVAPlSSHSPSLVLFLNHGRFVAQTEGPGPQLQAQSRQHSRAGQ 3417
Cdd:cd00110 5 SGSSYVRLPT-LPAPRTRLSISFSFRTT-SPNGLLLYAGS-QNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDGQ 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300798041 3418 WHRVSVRWGMQQVQLVVDGSQTWSQKAPHRRVHRaegPQHYTLFVGGLPAGSYSSKLPVSVGFSGCMKKLQLD 3490
Cdd:cd00110 82 WHSVSVERNGRSVTLSVDGERVVESGSPGGSALL---NLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
3151-3269 |
6.94e-17 |
|
Laminin G domain;
:
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 79.69 E-value: 6.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 3151 FGFRGTQDDNLLYYRTSPDGP--YQVSLRGGHVTLQFMN-----REVETQRVFADGAPHYVAFYSNVTRVWLYVDDQLQP 3223
Cdd:smart00282 4 FSFRTTSPNGLLLYAGSKGGGdyLALELRDGRLVLRYDLgsgpaRLTSDPTPLNDGQWHRVAVERNGRSVTLSVDGGNRV 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 300798041 3224 VKSREGTTPMLQLqpeePPRLLLGGLPMSG------TFHNFSGCISNVFVQR 3269
Cdd:smart00282 84 SGESPGGLTILNL----DGPLYLGGLPEDLklpplpVTPGFRGCIRNLKVNG 131
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1442-1490 |
1.15e-13 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
:
Pssm-ID: 395007 Cd Length: 49 Bit Score: 67.76 E-value: 1.15e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 300798041 1442 CGCHEVGAVGPTCEPFGGQCPCRGHVIGRDCSRCATGYWGFPNCRPCDC 1490
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2943-3095 |
1.83e-13 |
|
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: 70.52 E-value: 1.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2943 GSYLDGSGFARITFEKQFSNTKRFEQELRLVSYNGIIFFLKQENQ--FLCLAVQDGTLVLLYDFGSGLKRadpLQPPQAL 3020
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGgdFLALELEDGRLVLRYDLGSGSLV---LSSKTPL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300798041 3021 tAASKAIQVFLLAGARKRVLV--RVERATVFSVDQDNELEMADAYYLGGVPPEELPPSLrrlfPSGGSVRGCIKGIK 3095
Cdd:cd00110 78 -NDGQWHSVSVERNGRSVTLSvdGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGL----PVSPGFVGCIRDLK 149
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1581-1629 |
2.65e-13 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
:
Pssm-ID: 395007 Cd Length: 49 Bit Score: 66.61 E-value: 2.65e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 300798041 1581 CDCHEAGTMASVCDPFTGQCHCKENVQGSRCDQCRVGTFSLDAANPKGC 1629
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| LamG |
smart00282 |
Laminin G domain; |
2781-2908 |
2.67e-13 |
|
Laminin G domain;
:
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 69.29 E-value: 2.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2781 FVLYMGSRQaTGDYMGVSLRNQKVHWVYRLGeAGPTTLSIDE---NIGeQFAAVSIDRTLQFGHMSVTVEKHMVheikgd 2857
Cdd:smart00282 14 LLLYAGSKG-GGDYLALELRDGRLVLRYDLG-SGPARLTSDPtplNDG-QWHRVAVERNGRSVTLSVDGGNRVS------ 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 300798041 2858 TVAPGREGLLNLnpdDFVFYVGGYPSNFTPPEPLRFPGYLGCIEMDTLNEE 2908
Cdd:smart00282 85 GESPGGLTILNL---DGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
592-639 |
7.54e-13 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
:
Pssm-ID: 395007 Cd Length: 49 Bit Score: 65.45 E-value: 7.54e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 300798041 592 CGCSPAGTLPQGCD-ESGHCQCRPGFDGPHCDRCLPGYHGYPDCHACAC 639
Cdd:pfam00053 1 CDCNPHGSLSDTCDpETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
681-723 |
2.33e-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: 63.91 E-value: 2.33e-12
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 300798041 681 PCHCSADGSMHTTCDPTTGQCRCRPRVTGLRCDMCVPGAYNFP 723
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
2070-2116 |
4.57e-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: 63.14 E-value: 4.57e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 300798041 2070 PCAC-GPAAEGSECNPQTGQCHCRPGTTGPQCLECAPGYWGLPEK--GCR 2116
Cdd:cd00055 1 PCDCnGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQggGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
637-684 |
1.21e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
:
Pssm-ID: 395007 Cd Length: 49 Bit Score: 61.99 E-value: 1.21e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 300798041 637 CACDPRGSLDQQC-GAGGLCHCRPGYTGATCQECSPGFYGFPSCIPCHC 684
Cdd:pfam00053 1 CDCNPHGSLSDTCdPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1532-1583 |
1.86e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
:
Pssm-ID: 395007 Cd Length: 49 Bit Score: 61.22 E-value: 1.86e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 300798041 1532 CNCSGPGVqelTDPTCDMDSGQCRCRPNVAGRRCDTCAPGFYSYPSCRPCDC 1583
Cdd:pfam00053 1 CDCNPHGS---LSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1969-2022 |
2.60e-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: 60.83 E-value: 2.60e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 300798041 1969 PCDCSGNGDPNmifSDCDPLTGACRgCLRHTTGPRCESCAPGFYGNALLPGNCT 2022
Cdd:cd00055 1 PCDCNGHGSLS---GQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
499-546 |
3.49e-11 |
|
Laminin-type epidermal growth factor-like domai;
:
Pssm-ID: 214543 Cd Length: 46 Bit Score: 60.40 E-value: 3.49e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 300798041 499 CDCNAAGTQGNACrkDPRLGRCVCKPNFQGNHCELCAPGFYGPSCHPC 546
Cdd:smart00180 1 CDCDPGGSASGTC--DPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
2024-2068 |
3.77e-11 |
|
Laminin-type epidermal growth factor-like domai;
:
Pssm-ID: 214543 Cd Length: 46 Bit Score: 60.40 E-value: 3.77e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 300798041 2024 CDCSPCGT--ETCDPQTGRCLCKAGVTGQRCDHCLEGHFGfEQCQGC 2068
Cdd:smart00180 1 CDCDPGGSasGTCDPDTGQCECKPNVTGRRCDRCAPGYYG-DGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
545-588 |
7.41e-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: 59.68 E-value: 7.41e-11
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 300798041 545 PCQCSSPGVANGLCDPESGQCTCRTGFEGDKCDHCALGYFHFPL 588
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1914-1967 |
2.56e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
:
Pssm-ID: 395007 Cd Length: 49 Bit Score: 52.36 E-value: 2.56e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 300798041 1914 CPCPLAVPSNnfaDGCILRNGrtQCLCRPGYAGASCERCAPGFFGNPLVLGSSC 1967
Cdd:pfam00053 1 CDCNPHGSLS---DTCDPETG--QCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Smc super family |
cl34174 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2309-2616 |
3.87e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
The actual alignment was detected with superfamily member COG1196:
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.57 E-value: 3.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2309 QLRWALAEVERLLWDMRTRDLGAPQAVAEAELAEAQRLMARVQEQLtsfwEENQALATHIRDQLAQYESGLMDLREALNH 2388
Cdd:COG1196 217 ELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAEL----AELEAELEELRLELEELELELEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2389 AVNTTREADELNSRNEERLREALQWKQELSQDNATLKATLQAASLTLAhvsELLQGIDKAKEDLEHLAASLDGAWTPLLK 2468
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELE---ELEEELEEAEEELEEAEAELAEAEEALLE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2469 RMQAFSPASS-----KVDLVEAAEAHAQKLNQLAiNLSGIIQGINQDRfiQRAVEASNAYSSILQAVQAAEDAAGHALRQ 2543
Cdd:COG1196 370 AEAELAEAEEeleelAEELLEALRAAAELAAQLE-ELEEAEEALLERL--ERLEEELEELEEALAELEEEEEEEEEALEE 446
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300798041 2544 ASRTwemvvQRGLAAGARQLLANSSALVETILGHQERLGLAHGRLQAAGTQLRDVRAKKNQLAAQIQEAQAML 2616
Cdd:COG1196 447 AAEE-----EAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAAL 514
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1863-1899 |
4.72e-08 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
:
Pssm-ID: 238012 Cd Length: 50 Bit Score: 51.97 E-value: 4.72e-08
10 20 30 40
....*....|....*....|....*....|....*....|
gi 300798041 1863 PCQCHGH---SDRCLPGSGTCVgCQHNTEGDQCERCRPGF 1899
Cdd:cd00055 1 PCDCNGHgslSGQCDPGTGQCE-CKPNTTGRRCDRCAPGY 39
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
432-473 |
1.96e-07 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
:
Pssm-ID: 238012 Cd Length: 50 Bit Score: 50.05 E-value: 1.96e-07
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 300798041 432 PCDCESDFT-DGTCEDLTGRCYCRPNFTGERCSACAEGYVDFP 473
Cdd:cd00055 1 PCDCNGHGSlSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
303-351 |
4.87e-07 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
:
Pssm-ID: 238012 Cd Length: 50 Bit Score: 48.89 E-value: 4.87e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 300798041 303 RCVCHGHADVCDAKDPSDpfrLQCACQHNTCGGSCDRCCPGFNQQPWKP 351
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGT---GQCECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
832-871 |
1.22e-06 |
|
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: 47.73 E-value: 1.22e-06
10 20 30 40
....*....|....*....|....*....|....*....|
gi 300798041 832 SCRCDVGGALGQGCEPKTGACRCRPNTQGPSCSEPAKDHY 871
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYY 40
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
780-831 |
1.35e-06 |
|
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: 47.73 E-value: 1.35e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 300798041 780 RCSCDPRGTLGGvtEC-QGNGQCFCKAHVCGKTCAACKDGFFGLDhADYYGCR 831
Cdd:cd00055 1 PCDCNGHGSLSG--QCdPGTGQCECKPNTTGRRCDRCAPGYYGLP-SQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
362-425 |
5.68e-05 |
|
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: 43.11 E-value: 5.68e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300798041 362 SCNCHGHA---YDCYydpevdrrnasqnldnvyQGGGVCLdCQHHTTGINCERCVPGFYRAPDQPLD 425
Cdd:cd00055 1 PCDCNGHGslsGQCD------------------PGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
2118-2168 |
1.37e-04 |
|
Laminin-type epidermal growth factor-like domai;
:
Pssm-ID: 214543 Cd Length: 46 Bit Score: 41.91 E-value: 1.37e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 300798041 2118 CQC-PRGH----CDPHTGRCTCPPGLSGERCDTCsqqhqvpvpgRPGSHGIHCEVC 2168
Cdd:smart00180 1 CDCdPGGSasgtCDPDTGQCECKPNVTGRRCDRC----------APGYYGDGPPGC 46
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
49-302 |
1.08e-99 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 320.68 E-value: 1.08e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 49 LHPPYFNLAEGARITASATCGEEAPTRsasrptedlYCKLVGGPvaggdpnqtiQGQYCDICIAANSNKAHPVSNAIDGT 128
Cdd:pfam00055 1 CYPAFGNLAFGREVSATSTCGLNGPER---------YCILSGLE----------GGKKCFICDSRDPHNSHPPSNLTDSN 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 129 ER----WWQSPPLSRgpEYNEVNVTLDLGQVFHVAYVLIKFAnSPRPDLWVLERSTDFGHTYQPWQFFASskrDCLERFG 204
Cdd:pfam00055 62 NGtnetWWQSETGVI--QYENVNLTLDLGKEFHFTYLILKFK-SPRPAAMVLERSTDFGKTWQPYQYFAS---DCRRTFG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 205 -PRTLERITQDDDVICTTEYSRIVPLENGEIVVSLVNGRPGARNFSYSPVLRDFTKATNIRLRFLRTNTLLGHLmgkaLR 283
Cdd:pfam00055 136 rPSGPSRGIKDDEVICTSEYSDISPLTGGEVIFSTLEGRPSANIFDYSPELQDWLTATNIRIRLLRLHTLGDEL----LD 211
|
250
....*....|....*....
gi 300798041 284 DPTVTRRYYYSIKDISIGG 302
Cdd:pfam00055 212 DPSVLRKYYYAISDISVGG 230
|
|
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
48-302 |
4.35e-98 |
|
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related protein such as Unc-6/ netrins.
Pssm-ID: 214532 Cd Length: 238 Bit Score: 316.61 E-value: 4.35e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 48 SLHPPYFNLAEGARITASATCGEEAPTRsasrptedlYCKLVGGpvaggdpnqTIQGQYCDICIAANSNKAHPVSNAIDG 127
Cdd:smart00136 6 SCYPPFVNLAFGREVTATSTCGEPGPER---------YCKLVGH---------TEQGKKCDYCDARNPRRSHPAENLTDG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 128 TE----RWWQSPPLSRGPEYneVNVTLDLGQVFHVAYVLIKFAnSPRPDLWVLERStDFGHTYQPWQFFASskrDCLERF 203
Cdd:smart00136 68 NNpnnpTWWQSEPLSNGPQN--VNLTLDLGKEFHVTYVILKFC-SPRPSLWILERS-DFGKTWQPWQYFSS---DCRRTF 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 204 G--PRTLERITQDDDVICTTEYSRIVPLENGEIVVSLVNGRPGARNFSYSPVLRDFTKATNIRLRFLRTNTLLGHLMGKA 281
Cdd:smart00136 141 GrpPRGPITKGNEDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDFDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDR 220
|
250 260
....*....|....*....|.
gi 300798041 282 lrdPTVTRRYYYSIKDISIGG 302
Cdd:smart00136 221 ---PEVTRRYYYAISDIAVGG 238
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
2193-2448 |
8.65e-65 |
|
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: 221.90 E-value: 8.65e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2193 LRGINASSTAWARLHRLNASIADLQSKLRSPLGPHNQTAEQLQTLEQQSISLQQDTERLGSQATGVQDQAGRLLDNTEST 2272
Cdd:pfam06008 1 LLSLNSLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2273 LVRAQKLLEIVQAVSRALNELASQ--GFPGNATTPSGEQLRWALAEVERLLWDMRTRDLGAPQAVAEAELAEAQRLMARV 2350
Cdd:pfam06008 81 LGHAKELAEAIKNLIDNIKEINEKvaTLGENDFALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQDLLSRI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2351 QEQLTSFWEENQALATHIRDQLAQYESGLMDLREALNHAVNTTREADELNSRNEERLREALQWKQELSQDNATLKATLQA 2430
Cdd:pfam06008 161 QTWFQSPQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEETLKT 240
|
250
....*....|....*...
gi 300798041 2431 ASLTLAHVSELLQGIDKA 2448
Cdd:pfam06008 241 ARDSLDAANLLLQEIDDA 258
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
1693-1829 |
3.13e-49 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 172.45 E-value: 3.13e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 1693 YWQAPPSYLGDRVSSYGGTLHYELHSETRRGDVfiPYESRPDVVLQGNQMSIAFL--ELAYPSPGQVHRGQLQLVEGNFR 1770
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGGG--SLNSEPDVILEGNGLRLSYSspDQPPPDPGQEQTYSVRLHEENWR 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 300798041 1771 HlETHNPVSREELMMVLAGLEQLQIRALFSQTSSTVSLRRVVLEVASEAGGGPPASNVE 1829
Cdd:pfam00052 79 D-SDGAPVSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSAVPGGSGPPASWVE 136
|
|
| LamB |
smart00281 |
Laminin B domain; |
1689-1818 |
3.27e-48 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 168.98 E-value: 3.27e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 1689 FPELYWQAPPSYLGDRVSSYGGTLHYELHSETRRGDvfiPYESRPDVVLQGNQMSIAFLELAYPSPGQVHRGQLQLVEGN 1768
Cdd:smart00281 2 NEPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRRGG---THVSAPDVILEGNGLRISHPAEGPPLPDELTTVEVRFREEN 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 300798041 1769 FRHLEtHNPVSREELMMVLAGLEQLQIRALFSQTSSTVSLRRVVLEVASE 1818
Cdd:smart00281 79 WQYYG-GRPVTREDLMMVLANLTAILIRATYSQQMAGSRLSDVSLEVAVP 127
|
|
| Laminin_II |
pfam06009 |
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 ... |
2639-2760 |
7.26e-45 |
|
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: 159.96 E-value: 7.26e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2639 DTAAHVQSQLQGMQKNVERWQSQLGGLRGQ---------DLSQAERDASSSVSTLEKTLPQLLAKLSHLENRGVHNASLa 2709
Cdd:pfam06009 10 ETAKEVLEQLAPLSQNLENTSEKLSGINRSleetnelvnDANKALDDAGRSVKKLEELAPDLLDKLKPLKQLEVNSSSL- 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 300798041 2710 lSANIGRVRKLIAQARSAANKVKVSMKFNGRSGVRLRTPRDLADLAAYTAL 2760
Cdd:pfam06009 89 -SDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTSL 138
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
3514-3663 |
1.48e-27 |
|
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: 110.97 E-value: 1.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 3514 GLFFPGSeGAVTLELPKAKMPHVSLELEVRPLAAAGLIFHLGQAHATPYVQLQLLTEQVLLRANDGAGefSTWVTYP-KL 3592
Cdd:cd00110 1 GVSFSGS-SYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSG--SLVLSSKtPL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300798041 3593 CDGQWHQVTVIKGRNTLRLEVD-THSNHTTGRLPETLADSPALLHLGSPPKSEAAWPEP--PAYRGCLRKLLFN 3663
Cdd:cd00110 78 NDGQWHSVSVERNGRSVTLSVDgERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPvsPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
3537-3664 |
9.56e-27 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 107.81 E-value: 9.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 3537 SLELEVRPLAAAGLIFHLGQAHATPYVQLQLLTEQVLLRANDGAGEFSTWVTYPKLCDGQWHQVTVIKGRNTLRLEVDtH 3616
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLNDGQWHRVAVERNGRSVTLSVD-G 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 300798041 3617 SNHTTGRLPE--TLADSPALLHLGSPPKSEAAWPEP--PAYRGCLRKLLFNG 3664
Cdd:smart00282 80 GNRVSGESPGglTILNLDGPLYLGGLPEDLKLPPLPvtPGFRGCIRNLKVNG 131
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
3338-3490 |
1.11e-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: 108.27 E-value: 1.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 3338 PGPSYLQFVGvSPSHRNRLHLSMLVRPHgASQGLLLYVAPlSSHSPSLVLFLNHGRFVAQTEGPGPQLQAQSRQHSRAGQ 3417
Cdd:cd00110 5 SGSSYVRLPT-LPAPRTRLSISFSFRTT-SPNGLLLYAGS-QNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDGQ 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300798041 3418 WHRVSVRWGMQQVQLVVDGSQTWSQKAPHRRVHRaegPQHYTLFVGGLPAGSYSSKLPVSVGFSGCMKKLQLD 3490
Cdd:cd00110 82 WHSVSVERNGRSVTLSVDGERVVESGSPGGSALL---NLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
3542-3664 |
1.67e-23 |
|
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: 98.26 E-value: 1.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 3542 VRPLAAAGLIFHLGQaHATPYVQLQLLTEQVLLRANDGAGEFSTWVTYPKLCDGQWHQVTVIKGRNTLRLEVDTHSNHTT 3621
Cdd:pfam02210 1 FRTRQPNGLLLYAGG-GGSDFLALELVNGRLVLRYDLGSGPESLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSS 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 300798041 3622 GRLPETLA-DSPALLHLGSPPKSEAAWPEP--PAYRGCLRKLLFNG 3664
Cdd:pfam02210 80 LPPGESLLlNLNGPLYLGGLPPLLLLPALPvrAGFVGCIRDVRVNG 125
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
3367-3492 |
1.90e-22 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 95.56 E-value: 1.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 3367 ASQGLLLYVAPLSSHSpsLVLFLNHGRFVAQTE-GPGPQLQAQSRQHSRAGQWHRVSVRWGMQQVQLVVDGSQTWSQKAP 3445
Cdd:pfam02210 5 QPNGLLLYAGGGGSDF--LALELVNGRLVLRYDlGSGPESLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSLPP 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 300798041 3446 HRRVHRaegPQHYTLFVGGLPAGSYSSKLPVSVGFSGCMKKLQLDKR 3492
Cdd:pfam02210 83 GESLLL---NLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| LamG |
smart00282 |
Laminin G domain; |
3357-3492 |
2.38e-20 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 89.71 E-value: 2.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 3357 HLSMLVRPHgASQGLLLYVAPlSSHSPSLVLFLNHGRFVAQTEGPGPQLQAQS-RQHSRAGQWHRVSVRWGMQQVQLVVD 3435
Cdd:smart00282 1 SISFSFRTT-SPNGLLLYAGS-KGGGDYLALELRDGRLVLRYDLGSGPARLTSdPTPLNDGQWHRVAVERNGRSVTLSVD 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 300798041 3436 GSQTWSQKAP-HRRVHRAEGPqhytLFVGGLPAGSYSSKLPVSVGFSGCMKKLQLDKR 3492
Cdd:smart00282 79 GGNRVSGESPgGLTILNLDGP----LYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| LamG |
smart00282 |
Laminin G domain; |
3151-3269 |
6.94e-17 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 79.69 E-value: 6.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 3151 FGFRGTQDDNLLYYRTSPDGP--YQVSLRGGHVTLQFMN-----REVETQRVFADGAPHYVAFYSNVTRVWLYVDDQLQP 3223
Cdd:smart00282 4 FSFRTTSPNGLLLYAGSKGGGdyLALELRDGRLVLRYDLgsgpaRLTSDPTPLNDGQWHRVAVERNGRSVTLSVDGGNRV 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 300798041 3224 VKSREGTTPMLQLqpeePPRLLLGGLPMSG------TFHNFSGCISNVFVQR 3269
Cdd:smart00282 84 SGESPGGLTILNL----DGPLYLGGLPEDLklpplpVTPGFRGCIRNLKVNG 131
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
3124-3267 |
4.64e-15 |
|
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: 75.15 E-value: 4.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 3124 TMTFHGHGFLplALPDVAPITGEVYSGFGFRGTQDDN-LLYYRTSPDGPY-QVSLRGGHVTLQFMNRE----VETQRVFA 3197
Cdd:cd00110 1 GVSFSGSSYV--RLPTLPAPRTRLSISFSFRTTSPNGlLLYAGSQNGGDFlALELEDGRLVLRYDLGSgslvLSSKTPLN 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 300798041 3198 DGAPHYVAFYSNVTRVWLYVDDqLQPVKSREGTTpmlQLQPEEPPRLLLGGLPMSGTF------HNFSGCISNVFV 3267
Cdd:cd00110 79 DGQWHSVSVERNGRSVTLSVDG-ERVVESGSPGG---SALLNLDGPLYLGGLPEDLKSpglpvsPGFVGCIRDLKV 150
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1442-1490 |
1.15e-13 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 67.76 E-value: 1.15e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 300798041 1442 CGCHEVGAVGPTCEPFGGQCPCRGHVIGRDCSRCATGYWGFPNCRPCDC 1490
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2943-3095 |
1.83e-13 |
|
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: 70.52 E-value: 1.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2943 GSYLDGSGFARITFEKQFSNTKRFEQELRLVSYNGIIFFLKQENQ--FLCLAVQDGTLVLLYDFGSGLKRadpLQPPQAL 3020
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGgdFLALELEDGRLVLRYDLGSGSLV---LSSKTPL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300798041 3021 tAASKAIQVFLLAGARKRVLV--RVERATVFSVDQDNELEMADAYYLGGVPPEELPPSLrrlfPSGGSVRGCIKGIK 3095
Cdd:cd00110 78 -NDGQWHSVSVERNGRSVTLSvdGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGL----PVSPGFVGCIRDLK 149
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1581-1629 |
2.65e-13 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 66.61 E-value: 2.65e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 300798041 1581 CDCHEAGTMASVCDPFTGQCHCKENVQGSRCDQCRVGTFSLDAANPKGC 1629
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| LamG |
smart00282 |
Laminin G domain; |
2781-2908 |
2.67e-13 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 69.29 E-value: 2.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2781 FVLYMGSRQaTGDYMGVSLRNQKVHWVYRLGeAGPTTLSIDE---NIGeQFAAVSIDRTLQFGHMSVTVEKHMVheikgd 2857
Cdd:smart00282 14 LLLYAGSKG-GGDYLALELRDGRLVLRYDLG-SGPARLTSDPtplNDG-QWHRVAVERNGRSVTLSVDGGNRVS------ 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 300798041 2858 TVAPGREGLLNLnpdDFVFYVGGYPSNFTPPEPLRFPGYLGCIEMDTLNEE 2908
Cdd:smart00282 85 GESPGGLTILNL---DGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
592-639 |
7.54e-13 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 65.45 E-value: 7.54e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 300798041 592 CGCSPAGTLPQGCD-ESGHCQCRPGFDGPHCDRCLPGYHGYPDCHACAC 639
Cdd:pfam00053 1 CDCNPHGSLSDTCDpETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
681-723 |
2.33e-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: 63.91 E-value: 2.33e-12
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 300798041 681 PCHCSADGSMHTTCDPTTGQCRCRPRVTGLRCDMCVPGAYNFP 723
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
2070-2116 |
4.57e-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: 63.14 E-value: 4.57e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 300798041 2070 PCAC-GPAAEGSECNPQTGQCHCRPGTTGPQCLECAPGYWGLPEK--GCR 2116
Cdd:cd00055 1 PCDCnGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQggGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1441-1483 |
7.52e-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: 62.37 E-value: 7.52e-12
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 300798041 1441 PCGCHEVGAVGPTCEPFGGQCPCRGHVIGRDCSRCATGYWGFP 1483
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1580-1630 |
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: 61.99 E-value: 1.02e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 300798041 1580 PCDCHEAGTMASVCDPFTGQCHCKENVQGSRCDQCRVGTFSlDAANPKGCT 1630
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYG-LPSQGGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
637-684 |
1.21e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 61.99 E-value: 1.21e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 300798041 637 CACDPRGSLDQQC-GAGGLCHCRPGYTGATCQECSPGFYGFPSCIPCHC 684
Cdd:pfam00053 1 CDCNPHGSLSDTCdPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
2071-2115 |
1.46e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 61.56 E-value: 1.46e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 300798041 2071 CACGPA-AEGSECNPQTGQCHCRPGTTGPQCLECAPGYWGLPEKGC 2115
Cdd:smart00180 1 CDCDPGgSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1581-1629 |
1.48e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 61.56 E-value: 1.48e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 300798041 1581 CDCHEAGTMASVCDPFTGQCHCKENVQGSRCDQCRVGTFsldAANPKGC 1629
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYY---GDGPPGC 46
|
|
| LamG |
smart00282 |
Laminin G domain; |
2965-3099 |
1.50e-11 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 64.28 E-value: 1.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2965 RFEQELRLVSYNGIIFFL--KQENQFLCLAVQDGTLVLLYDFGSGLKRadpLQPPQALTAASKAIQVFLLAGARKRVLV- 3041
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAgsKGGGDYLALELRDGRLVLRYDLGSGPAR---LTSDPTPLNDGQWHRVAVERNGRSVTLSv 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 300798041 3042 -RVERATVFSVDQDNELEMADAYYLGGVPPEELPPSLrrlfPSGGSVRGCIKGIKALGK 3099
Cdd:smart00282 78 dGGNRVSGESPGGLTILNLDGPLYLGGLPEDLKLPPL----PVTPGFRGCIRNLKVNGK 132
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1532-1583 |
1.86e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 61.22 E-value: 1.86e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 300798041 1532 CNCSGPGVqelTDPTCDMDSGQCRCRPNVAGRRCDTCAPGFYSYPSCRPCDC 1583
Cdd:pfam00053 1 CDCNPHGS---LSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1969-2022 |
2.60e-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: 60.83 E-value: 2.60e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 300798041 1969 PCDCSGNGDPNmifSDCDPLTGACRgCLRHTTGPRCESCAPGFYGNALLPGNCT 2022
Cdd:cd00055 1 PCDCNGHGSLS---GQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
499-546 |
3.49e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 60.40 E-value: 3.49e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 300798041 499 CDCNAAGTQGNACrkDPRLGRCVCKPNFQGNHCELCAPGFYGPSCHPC 546
Cdd:smart00180 1 CDCDPGGSASGTC--DPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1442-1485 |
3.73e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 60.40 E-value: 3.73e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 300798041 1442 CGCHEVGAVGPTCEPFGGQCPCRGHVIGRDCSRCATGYWG--FPNC 1485
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
2024-2068 |
3.77e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 60.40 E-value: 3.77e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 300798041 2024 CDCSPCGT--ETCDPQTGRCLCKAGVTGQRCDHCLEGHFGfEQCQGC 2068
Cdd:smart00180 1 CDCDPGGSasGTCDPDTGQCECKPNVTGRRCDRCAPGYYG-DGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
2071-2118 |
4.89e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 60.06 E-value: 4.89e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 300798041 2071 CACGP-AAEGSECNPQTGQCHCRPGTTGPQCLECAPGYWGLPEKGCRRC 2118
Cdd:pfam00053 1 CDCNPhGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2970-3095 |
5.13e-11 |
|
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: 62.82 E-value: 5.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2970 LRLVSYNGIIFFLKQE-NQFLCLAVQDGTLVLLYDFGSGlkradplqpPQALTAASKAiqvfLLAGARKRVLVRVERATV 3048
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGgSDFLALELVNGRLVLRYDLGSG---------PESLLSSGKN----LNDGQWHSVRVERNGNTL 67
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 300798041 3049 -FSVDQDNELEMA-----------DAYYLGGVPPEELPPSLrrlfPSGGSVRGCIKGIK 3095
Cdd:pfam02210 68 tLSVDGQTVVSSLppgeslllnlnGPLYLGGLPPLLLLPAL----PVRAGFVGCIRDVR 122
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
682-724 |
5.91e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 60.02 E-value: 5.91e-11
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 300798041 682 CHCSADGSMHTTCDPTTGQCRCRPRVTGLRCDMCVPGAYNFPY 724
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
2023-2069 |
7.33e-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: 59.68 E-value: 7.33e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 300798041 2023 RCDCSPCGT--ETCDPQTGRCLCKAGVTGQRCDHCLEGHFGF-EQCQGCH 2069
Cdd:cd00055 1 PCDCNGHGSlsGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLpSQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
592-633 |
7.41e-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: 59.68 E-value: 7.41e-11
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 300798041 592 CGCSPAGTLPQGCD-ESGHCQCRPGFDGPHCDRCLPGYHGYPD 633
Cdd:cd00055 2 CDCNGHGSLSGQCDpGTGQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
545-588 |
7.41e-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: 59.68 E-value: 7.41e-11
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 300798041 545 PCQCSSPGVANGLCDPESGQCTCRTGFEGDKCDHCALGYFHFPL 588
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
682-730 |
8.96e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 59.29 E-value: 8.96e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 300798041 682 CHCSADGSMHTTCDPTTGQCRCRPRVTGLRCDMCVPGAYNFPYCEAGSC 730
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1532-1578 |
9.64e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 59.25 E-value: 9.64e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 300798041 1532 CNCSGPGVQeltDPTCDMDSGQCRCRPNVAGRRCDTCAPGFY--SYPSC 1578
Cdd:smart00180 1 CDCDPGGSA---SGTCDPDTGQCECKPNVTGRRCDRCAPGYYgdGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1532-1577 |
1.08e-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: 59.29 E-value: 1.08e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 300798041 1532 CNCSGPGVQeltDPTCDMDSGQCRCRPNVAGRRCDTCAPGFYSYPS 1577
Cdd:cd00055 2 CDCNGHGSL---SGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
2024-2068 |
1.24e-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: 58.90 E-value: 1.24e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 300798041 2024 CDCSPCGT--ETCDPQTGRCLCKAGVTGQRCDHCLEGHFGFEQCQGC 2068
Cdd:pfam00053 1 CDCNPHGSlsDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQ 47
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
499-548 |
1.97e-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: 58.52 E-value: 1.97e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 300798041 499 CDCNAAGTQGNACrkDPRLGRCVCKPNFQGNHCELCAPGFYGPSCHPCQC 548
Cdd:cd00055 2 CDCNGHGSLSGQC--DPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
499-548 |
2.02e-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: 58.52 E-value: 2.02e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 300798041 499 CDCNAAGTQGNACrkDPRLGRCVCKPNFQGNHCELCAPGFYG-PSCHPCQC 548
Cdd:pfam00053 1 CDCNPHGSLSDTC--DPETGQCLCKPGVTGRHCDRCKPGYYGlPSDPPQGC 49
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2204-2732 |
2.59e-10 |
|
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: 67.00 E-value: 2.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2204 ARLHRLNASIADLQSKLRSPLGPHNQTAEQLQTLEQQSISLQQDTERLGSQATGVQ----------DQAGRLLDNTESTL 2273
Cdd:TIGR02168 295 NEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKeelesleaelEELEAELEELESRL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2274 VRAQKLLEivqAVSRALNELASQGFPGNAttpsgeQLRWALAEVERL-----LWDMRTRDLG-APQAVAEAELAEAQRLM 2347
Cdd:TIGR02168 375 EELEEQLE---TLRSKVAQLELQIASLNN------EIERLEARLERLedrreRLQQEIEELLkKLEEAELKELQAELEEL 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2348 ARVQEQLTSFWEENQALATHIRDQLAQYESGLMDLREALNHA---VNTTREADELNSRNEERLREALQWKQELSQDNATL 2424
Cdd:TIGR02168 446 EEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLqarLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVL 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2425 KATL-------QAASLTLAhvsELLQGI-----DKAKEDLEHLAASLDGAWTPL-LKRMQAFSPASSK------------ 2479
Cdd:TIGR02168 526 SELIsvdegyeAAIEAALG---GRLQAVvvenlNAAKKAIAFLKQNELGRVTFLpLDSIKGTEIQGNDreilkniegflg 602
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2480 --VDLVEAAEAhAQK-----LNQL--------AINL--------------------SGIIQG---------INQDRFIQR 2515
Cdd:TIGR02168 603 vaKDLVKFDPK-LRKalsylLGGVlvvddldnALELakklrpgyrivtldgdlvrpGGVITGgsaktnssiLERRREIEE 681
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2516 AV----EASNAYSSILQAVQAAE-------------DAAGHALRQASRTWEMVVQRgLAAGARQLLANSSALVETILGHQ 2578
Cdd:TIGR02168 682 LEekieELEEKIAELEKALAELRkeleeleeeleqlRKELEELSRQISALRKDLAR-LEAEVEQLEERIAQLSKELTELE 760
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2579 ERLGLAHGRLQAAGTQLRDVRAKKNQLAAQIQEAQAMLAMDTSETSEKiahaKAVAAEARDTAAHVQSQLQGMQKNVERW 2658
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL----RAELTLLNEEAANLRERLESLERRIAAT 836
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300798041 2659 QSQLGGLRGQ--DLSQAERDASSSVSTLEKTLPQLLAKLSHLEN-RGVHNASLALSANigRVRKLIAQARSAANKVK 2732
Cdd:TIGR02168 837 ERRLEDLEEQieELSEDIESLAAEIEELEELIEELESELEALLNeRASLEEALALLRS--ELEELSEELRELESKRS 911
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
3153-3267 |
2.59e-10 |
|
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: 60.90 E-value: 2.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 3153 FRGTQDDNLLYYRTSPDGPY-QVSLRGGHVTLQFM-----NREVETQRVFADGAPHYVAFYSNVTRVWLYVDDQlqPVKS 3226
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDFlALELVNGRLVLRYDlgsgpESLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQ--TVVS 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 300798041 3227 REGTTPMLQLQPEEPprLLLGGLP------MSGTFHNFSGCISNVFV 3267
Cdd:pfam02210 79 SLPPGESLLLNLNGP--LYLGGLPpllllpALPVRAGFVGCIRDVRV 123
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
592-632 |
3.44e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 57.71 E-value: 3.44e-10
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 300798041 592 CGCSPAGTLPQGCD-ESGHCQCRPGFDGPHCDRCLPGYHGYP 632
Cdd:smart00180 1 CDCDPGGSASGTCDpDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2174-2698 |
4.66e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 65.56 E-value: 4.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2174 LLLDDLERAGALLPSIREQLRGINAsstawARLHRLNASIADLQSKLRSplgpHNQTAEQLQTLEQQSISLQQDTERLgs 2253
Cdd:COG4717 46 MLLERLEKEADELFKPQGRKPELNL-----KELKELEEELKEAEEKEEE----YAELQEELEELEEELEELEAELEEL-- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2254 qatgvqdqagrllDNTESTLVRAQKLLEIVQAVSRALNELASqgFPGNAttpsgEQLRWALAEVERLLWDMRTRDLGApQ 2333
Cdd:COG4717 115 -------------REELEKLEKLLQLLPLYQELEALEAELAE--LPERL-----EELEERLEELRELEEELEELEAEL-A 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2334 AVAEAELAEAQRLMARVQEQLTSFWEENQALathiRDQLAQYESGLMDLREALNHAvntTREADEL-NSRNEERLREALQ 2412
Cdd:COG4717 174 ELQEELEELLEQLSLATEEELQDLAEELEEL----QQRLAELEEELEEAQEELEEL---EEELEQLeNELEAAALEERLK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2413 WKQELSQDNATLkATLQAASLTLAHVSELLQGI---------------DKAKEDLEHLAASLDGA----------WTPLL 2467
Cdd:COG4717 247 EARLLLLIAAAL-LALLGLGGSLLSLILTIAGVlflvlgllallflllAREKASLGKEAEELQALpaleeleeeeLEELL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2468 KRMQAfsPASSKVDLVEAAEAHAQKLNQLAINLSGIIQGINQDRFIQRAveasnaySSILQAVQAAEDAAghaLRQASRT 2547
Cdd:COG4717 326 AALGL--PPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEI-------AALLAEAGVEDEEE---LRAALEQ 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2548 WEMVVQ-RGLAAGARQLLANSSALVETILGHQERLGLAHgRLQAAGTQLRDVRAKKNQLAAQIQEAQAmlAMDTSETSEK 2626
Cdd:COG4717 394 AEEYQElKEELEELEEQLEELLGELEELLEALDEEELEE-ELEELEEELEELEEELEELREELAELEA--ELEQLEEDGE 470
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300798041 2627 IahakavaaeaRDTAAHVQSQLQGMQKNVERWQS-QLGglrGQDLSQAERDASssvstlEKTLPQLLAKLSHL 2698
Cdd:COG4717 471 L----------AELLQELEELKAELRELAEEWAAlKLA---LELLEEAREEYR------EERLPPVLERASEY 524
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
546-587 |
1.26e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.17 E-value: 1.26e-09
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 300798041 546 CQCSSPGVANGLCDPESGQCTCRTGFEGDKCDHCALGYFHFP 587
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2734-2901 |
1.31e-09 |
|
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: 59.35 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2734 SMKFNGRSGVRLRTPRDLADlaaYTALKFYIQSPVPapepgenTGdrFVLYMGSrQATGDYMGVSLRNQKVHWVYRLGEa 2813
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRT---RLSISFSFRTTSP-------NG--LLLYAGS-QNGGDFLALELEDGRLVLRYDLGS- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2814 GPTTLSIDENIGE-QFAAVSIDRTLQFGHMSVTVEKHMvheikgDTVAPGREGLLNLNPDdfvFYVGGYPSNFTPPEPLR 2892
Cdd:cd00110 67 GSLVLSSKTPLNDgQWHSVSVERNGRSVTLSVDGERVV------ESGSPGGSALLNLDGP---LYLGGLPEDLKSPGLPV 137
|
....*....
gi 300798041 2893 FPGYLGCIE 2901
Cdd:cd00110 138 SPGFVGCIR 146
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
546-594 |
1.97e-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: 55.82 E-value: 1.97e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 300798041 546 CQCSSPGVANGLCDPESGQCTCRTGFEGDKCDHCALGYFHFPLCQLCGC 594
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
636-678 |
3.14e-09 |
|
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: 55.05 E-value: 3.14e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 300798041 636 ACACDPRGSLDQQCGAG-GLCHCRPGYTGATCQECSPGFYGFPS 678
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGtGQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1970-2020 |
6.63e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 54.28 E-value: 6.63e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 300798041 1970 CDCSGNGDPNmifSDCDPLTGACRgCLRHTTGPRCESCAPGFYGNALLPGN 2020
Cdd:pfam00053 1 CDCNPHGSLS---DTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQ 47
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2783-2901 |
7.31e-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: 56.66 E-value: 7.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2783 LYMGSRQatGDYMGVSLRNQKVHWVYRLGEAGPTTLSIDENI--GeQFAAVSIDRTLQfgHMSVTVEKHMVHEikgdTVA 2860
Cdd:pfam02210 11 LYAGGGG--SDFLALELVNGRLVLRYDLGSGPESLLSSGKNLndG-QWHSVRVERNGN--TLTLSVDGQTVVS----SLP 81
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 300798041 2861 PGREGLLNLNPDdfvFYVGGYPSNFTPPEPLRFPGYLGCIE 2901
Cdd:pfam02210 82 PGESLLLNLNGP---LYLGGLPPLLLLPALPVRAGFVGCIR 119
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
637-679 |
1.03e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 53.47 E-value: 1.03e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 300798041 637 CACDPRGSLDQQC-GAGGLCHCRPGYTGATCQECSPGFYG--FPSC 679
Cdd:smart00180 1 CDCDPGGSASGTCdPDTGQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1914-1967 |
2.56e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 52.36 E-value: 2.56e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 300798041 1914 CPCPLAVPSNnfaDGCILRNGrtQCLCRPGYAGASCERCAPGFFGNPLVLGSSC 1967
Cdd:pfam00053 1 CDCNPHGSLS---DTCDPETG--QCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2309-2616 |
3.87e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.57 E-value: 3.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2309 QLRWALAEVERLLWDMRTRDLGAPQAVAEAELAEAQRLMARVQEQLtsfwEENQALATHIRDQLAQYESGLMDLREALNH 2388
Cdd:COG1196 217 ELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAEL----AELEAELEELRLELEELELELEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2389 AVNTTREADELNSRNEERLREALQWKQELSQDNATLKATLQAASLTLAhvsELLQGIDKAKEDLEHLAASLDGAWTPLLK 2468
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELE---ELEEELEEAEEELEEAEAELAEAEEALLE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2469 RMQAFSPASS-----KVDLVEAAEAHAQKLNQLAiNLSGIIQGINQDRfiQRAVEASNAYSSILQAVQAAEDAAGHALRQ 2543
Cdd:COG1196 370 AEAELAEAEEeleelAEELLEALRAAAELAAQLE-ELEEAEEALLERL--ERLEEELEELEEALAELEEEEEEEEEALEE 446
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300798041 2544 ASRTwemvvQRGLAAGARQLLANSSALVETILGHQERLGLAHGRLQAAGTQLRDVRAKKNQLAAQIQEAQAML 2616
Cdd:COG1196 447 AAEE-----EAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAAL 514
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2175-2718 |
4.54e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 59.28 E-value: 4.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2175 LLDDL----------ERAG-------ALLPSIREQLRGINA------SSTAWARLHRLNASIADLQSKLR---------- 2221
Cdd:PRK02224 154 MIDDLlqlgkleeyrERASdarlgveRVLSDQRGSLDQLKAqieekeEKDLHERLNGLESELAELDEEIEryeeqreqar 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2222 -------SPLGPHNQTAEQLQTLEQQSISLQQD---TER----LGSQATGVQDQAGRLLDNTESTLVRAQKLLEIVQAVS 2287
Cdd:PRK02224 234 etrdeadEVLEEHEERREELETLEAEIEDLRETiaeTERereeLAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2288 RALNELASQgfpgnattpsgeqlrwaLAEVERLLWDMRTrDLGAPQAVAEAELAEAQRLMARVQE------QLTSFWEEN 2361
Cdd:PRK02224 314 ARREELEDR-----------------DEELRDRLEECRV-AAQAHNEEAESLREDADDLEERAEElreeaaELESELEEA 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2362 QALATHIRDQLAQYESGLMDLREALNhavNTTREADELNSRNEERLREalqwKQELSQDNATLKATLQAASLTLAHVSEL 2441
Cdd:PRK02224 376 REAVEDRREEIEELEEEIEELRERFG---DAPVDLGNAEDFLEELREE----RDELREREAELEATLRTARERVEEAEAL 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2442 LQ------------------GIDKAKEDLEHLAASLDGAWTPLLKRMQAFSPASskvDLVEaAEAHAQKLNQLAINLSGI 2503
Cdd:PRK02224 449 LEagkcpecgqpvegsphveTIEEDRERVEELEAELEDLEEEVEEVEERLERAE---DLVE-AEDRIERLEERREDLEEL 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2504 I----QGINQDRfiqRAVEASNAYSSILQA-VQAAEDAAGHALRQASRTWEMVV----QRGLAAGARQLLANSSALVETI 2574
Cdd:PRK02224 525 IaerrETIEEKR---ERAEELRERAAELEAeAEEKREAAAEAEEEAEEAREEVAelnsKLAELKERIESLERIRTLLAAI 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2575 LGHQERLGLAHGRLQAAGT-------QLRDVRAKKNQLAAQIQEAQAMLAMDTSETSEKIAhakavaaeardtaAHVQSQ 2647
Cdd:PRK02224 602 ADAEDEIERLREKREALAElnderreRLAEKRERKRELEAEFDEARIEEAREDKERAEEYL-------------EQVEEK 668
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 300798041 2648 LQGMQKNVERWQSQLGGLRGQdLSQAErdasssvsTLEKTLPQLLAKLSHLENrgVHNASLALSANIGRVR 2718
Cdd:PRK02224 669 LDELREERDDLQAEIGAVENE-LEELE--------ELRERREALENRVEALEA--LYDEAEELESMYGDLR 728
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
2172-2662 |
4.64e-08 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 59.15 E-value: 4.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2172 VVLLLDDLERAgallpsIREQ---LRG--INASSTAWARLHRLNASIADLQSKLRSPLGPHNQTAEQLQTLE-------- 2238
Cdd:COG5278 48 VLRALEELLSA------LLDAetgQRGylLTGDESFLEPYEEARAEIDELLAELRSLTADNPEQQARLDELEalidqwla 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2239 --QQSISLQQDTERLGSQATGVQDQAGRLLDNTESTLVRAQKLLEIVQAVSRALNELASQgfpgnattpSGEQLRWALAE 2316
Cdd:COG5278 122 elEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLA---------LAALLALAELL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2317 VERLLwdMRTRDLGAPQAVAEAELAEAQRLMARVQEQLTSFWEENQALATHIRDQLAQYESGLMDLREALNHAVNTTREA 2396
Cdd:COG5278 193 LLALA--RALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLAAALLAL 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2397 DELNSRNEERLREALQWKQELSQDNATLKATLQAASLTLAHVSELLQGIDKAKEDLEHLAASLDGAwtpLLKRMQAFSPA 2476
Cdd:COG5278 271 AALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATA---LAAAAAALALL 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2477 SSKVDLVEAAEAHAQKLNQLAINLSGIIQGINQDRFIQRAVEASNAyssILQAVQAAEDAAGHALRQASRTWEMVVQRGL 2556
Cdd:COG5278 348 AALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVL---AIAAAAAAAAAEAAAAAAAAAAASAAEALEL 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2557 AAGARQLLANSSALVETILGHQERLGLAHGRLQAAGTQLRDVRAKKNQLAAQIQEAQAMLAMDTSETSEKIAHAKAVAAE 2636
Cdd:COG5278 425 AEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLALA 504
|
490 500
....*....|....*....|....*.
gi 300798041 2637 ARDTAAHVQSQLQGMQKNVERWQSQL 2662
Cdd:COG5278 505 LAALLLAAAEAALAAALAAALASAEL 530
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1863-1899 |
4.72e-08 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 51.97 E-value: 4.72e-08
10 20 30 40
....*....|....*....|....*....|....*....|
gi 300798041 1863 PCQCHGH---SDRCLPGSGTCVgCQHNTEGDQCERCRPGF 1899
Cdd:cd00055 1 PCDCNGHgslSGQCDPGTGQCE-CKPNTTGRRCDRCAPGY 39
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1864-1911 |
7.67e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 51.20 E-value: 7.67e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 300798041 1864 CQCHGH---SDRCLPGSGTCVgCQHNTEGDQCERCRPGFVsSDPSDPASPC 1911
Cdd:pfam00053 1 CDCNPHgslSDTCDPETGQCL-CKPGVTGRHCDRCKPGYY-GLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1914-1960 |
1.79e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 50.00 E-value: 1.79e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 300798041 1914 CPCPlavPSNNFADGCILRNGrtQCLCRPGYAGASCERCAPGFFGNP 1960
Cdd:smart00180 1 CDCD---PGGSASGTCDPDTG--QCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
432-473 |
1.96e-07 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 50.05 E-value: 1.96e-07
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 300798041 432 PCDCESDFT-DGTCEDLTGRCYCRPNFTGERCSACAEGYVDFP 473
Cdd:cd00055 1 PCDCNGHGSlSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
303-351 |
4.87e-07 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 48.89 E-value: 4.87e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 300798041 303 RCVCHGHADVCDAKDPSDpfrLQCACQHNTCGGSCDRCCPGFNQQPWKP 351
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGT---GQCECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
433-475 |
8.42e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 48.08 E-value: 8.42e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 300798041 433 CDCESDFT-DGTCEDLTGRCYCRPNFTGERCSACAEGY--VDFPHC 475
Cdd:smart00180 1 CDCDPGGSaSGTCDPDTGQCECKPNVTGRRCDRCAPGYygDGPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1970-2014 |
1.05e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 47.69 E-value: 1.05e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 300798041 1970 CDCSGNGdpnMIFSDCDPLTGACRgCLRHTTGPRCESCAPGFYGN 2014
Cdd:smart00180 1 CDCDPGG---SASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD 41
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1913-1968 |
1.12e-06 |
|
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: 47.73 E-value: 1.12e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 300798041 1913 SCPCPLAVPSNNfadGCILRNGrtQCLCRPGYAGASCERCAPGFFGNPLVlGSSCQ 1968
Cdd:cd00055 1 PCDCNGHGSLSG---QCDPGTG--QCECKPNTTGRRCDRCAPGYYGLPSQ-GGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
832-871 |
1.22e-06 |
|
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: 47.73 E-value: 1.22e-06
10 20 30 40
....*....|....*....|....*....|....*....|
gi 300798041 832 SCRCDVGGALGQGCEPKTGACRCRPNTQGPSCSEPAKDHY 871
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYY 40
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
780-831 |
1.35e-06 |
|
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: 47.73 E-value: 1.35e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 300798041 780 RCSCDPRGTLGGvtEC-QGNGQCFCKAHVCGKTCAACKDGFFGLDhADYYGCR 831
Cdd:cd00055 1 PCDCNGHGSLSG--QCdPGTGQCECKPNTTGRRCDRCAPGYYGLP-SQGGGCQ 50
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2172-2459 |
2.39e-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: 53.91 E-value: 2.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2172 VVLLLDDLERAGALLPSIREQLRGINASSTAWA-RLHRLNASIADLQSKLRSPLGPHNQTAEQLQTLEQQSISLQQDTER 2250
Cdd:TIGR02168 714 LEQLRKELEELSRQISALRKDLARLEAEVEQLEeRIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ 793
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2251 -------LGSQATGVQDQAGRLLDNTESTLVRAQKLLEIVQAVSRALNELASQGfpgnattpsgEQLRWALAEVERLLWD 2323
Cdd:TIGR02168 794 lkeelkaLREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQI----------EELSEDIESLAAEIEE 863
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2324 MRTrdlgapqavaeaelaeaqrLMARVQEQLTSFWEENQALATHIRDQLAQYESGLMDLREALNHAVNTTREADELNSRN 2403
Cdd:TIGR02168 864 LEE-------------------LIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL 924
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 300798041 2404 EE-RLRealqwKQELSQDNATLKATLQA-ASLTLAHVSELLQGIDKAKEDLEHLAASL 2459
Cdd:TIGR02168 925 AQlELR-----LEGLEVRIDNLQERLSEeYSLTLEEAEALENKIEDDEEEARRRLKRL 977
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
781-830 |
3.31e-06 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 46.58 E-value: 3.31e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 300798041 781 CSCDPRGTLGGvtEC-QGNGQCFCKAHVCGKTCAACKDGFFGLDHADYYGC 830
Cdd:pfam00053 1 CDCNPHGSLSD--TCdPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2367-2698 |
3.35e-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: 3.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2367 HIRDQLAQYESGLMDLREALNhavnttrEADELNSRNEERLREALQWKQELSQDNATLKATLQAASLTLAHVSELLQGID 2446
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALA-------ELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2447 KAKEDLEHLAASLDgawtplLKRMQAFspasskvDLVEAAEAHAQKLNQLainlsgiiqginqdrfIQRAVEASNAYSSI 2526
Cdd:TIGR02168 754 KELTELEAEIEELE------ERLEEAE-------EELAEAEAEIEELEAQ----------------IEQLKEELKALREA 804
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2527 LQAVQAAEDAAGHALRQASRTWEMVVQRglAAGARQLLANSSALVETILGHQERLGLAHGRLQAAGTQLRD-------VR 2599
Cdd:TIGR02168 805 LDELRAELTLLNEEAANLRERLESLERR--IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESeleallnER 882
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2600 AKKNQLAAQIQEAQAMLAMDTSETSEKIAHAKAVAAEARDTAAHVQSQLQGMQKNVERWQSQL---GGLRGQDLSQAERD 2676
Cdd:TIGR02168 883 ASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLseeYSLTLEEAEALENK 962
|
330 340
....*....|....*....|..
gi 300798041 2677 ASSSVSTLEKTLPQLLAKLSHL 2698
Cdd:TIGR02168 963 IEDDEEEARRRLKRLENKIKEL 984
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
433-477 |
3.48e-06 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 46.58 E-value: 3.48e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 300798041 433 CDC-ESDFTDGTCEDLTGRCYCRPNFTGERCSACAEGYVDFPHCYP 477
Cdd:pfam00053 1 CDCnPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPP 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
833-871 |
3.93e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 46.15 E-value: 3.93e-06
10 20 30
....*....|....*....|....*....|....*....
gi 300798041 833 CRCDVGGALGQGCEPKTGACRCRPNTQGPSCSEPAKDHY 871
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYY 39
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
781-821 |
7.00e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 45.38 E-value: 7.00e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 300798041 781 CSCDPRGTLGGvtEC-QGNGQCFCKAHVCGKTCAACKDGFFG 821
Cdd:smart00180 1 CDCDPGGSASG--TCdPDTGQCECKPNVTGRRCDRCAPGYYG 40
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1864-1899 |
1.16e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 44.99 E-value: 1.16e-05
10 20 30
....*....|....*....|....*....|....*....
gi 300798041 1864 CQCHG---HSDRCLPGSGTCVgCQHNTEGDQCERCRPGF 1899
Cdd:smart00180 1 CDCDPggsASGTCDPDTGQCE-CKPNVTGRRCDRCAPGY 38
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
2397-2617 |
3.53e-05 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 48.07 E-value: 3.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2397 DELNSRNE---------ERLREALQW---KQELSQDNATLKATLQAASltlahvsellQGIDKAKEDLEHLAASLDGAWT 2464
Cdd:pfam12795 3 DELEKAKLdeaakkkllQDLQQALSLldkIDASKQRAAAYQKALDDAP----------AELRELRQELAALQAKAEAAPK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2465 PLLKRM------QAFSPASSkvDLVEAAEAhAQKLNQLAINLSGIIQGINQDrfIQRAVEASNAYSSILQAVQAAEDAAG 2538
Cdd:pfam12795 73 EILASLsleeleQRLLQTSA--QLQELQNQ-LAQLNSQLIELQTRPERAQQQ--LSEARQRLQQIRNRLNGPAPPGEPLS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2539 HALRQASRTwEMVVQRGLAAGARQLLANSSALVETILGHQERLGLAHGRLQAAGTQLRD-VRAKKNQLAAQIQEAQAMLA 2617
Cdd:pfam12795 148 EAQRWALQA-ELAALKAQIDMLEQELLSNNNRQDLLKARRDLLTLRIQRLEQQLQALQElLNEKRLQEAEQAVAQTEQLA 226
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
362-425 |
5.68e-05 |
|
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: 43.11 E-value: 5.68e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300798041 362 SCNCHGHA---YDCYydpevdrrnasqnldnvyQGGGVCLdCQHHTTGINCERCVPGFYRAPDQPLD 425
Cdd:cd00055 1 PCDCNGHGslsGQCD------------------PGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
833-871 |
9.33e-05 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 42.34 E-value: 9.33e-05
10 20 30
....*....|....*....|....*....|....*....
gi 300798041 833 CRCDVGGALGQGCEPKTGACRCRPNTQGPSCSEPAKDHY 871
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYY 39
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
2118-2168 |
1.37e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 41.91 E-value: 1.37e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 300798041 2118 CQC-PRGH----CDPHTGRCTCPPGLSGERCDTCsqqhqvpvpgRPGSHGIHCEVC 2168
Cdd:smart00180 1 CDCdPGGSasgtCDPDTGQCECKPNVTGRRCDRC----------APGYYGDGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
2118-2146 |
3.59e-04 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 40.80 E-value: 3.59e-04
10 20 30
....*....|....*....|....*....|....
gi 300798041 2118 CQCP-----RGHCDPHTGRCTCPPGLSGERCDTC 2146
Cdd:pfam00053 1 CDCNphgslSDTCDPETGQCLCKPGVTGRHCDRC 34
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
2117-2146 |
6.01e-04 |
|
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: 40.03 E-value: 6.01e-04
10 20 30
....*....|....*....|....*....|....*
gi 300798041 2117 RCQCP-----RGHCDPHTGRCTCPPGLSGERCDTC 2146
Cdd:cd00055 1 PCDCNghgslSGQCDPGTGQCECKPNTTGRRCDRC 35
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
304-349 |
9.82e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 39.60 E-value: 9.82e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 300798041 304 CVCH--GHAD-VCDakdpsdPFRLQCACQHNTCGGSCDRCCPGFNQQPW 349
Cdd:smart00180 1 CDCDpgGSASgTCD------PDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
391-420 |
1.50e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 38.83 E-value: 1.50e-03
10 20 30
....*....|....*....|....*....|
gi 300798041 391 YQGGGVCLdCQHHTTGINCERCVPGFYRAP 420
Cdd:smart00180 14 DPDTGQCE-CKPNVTGRRCDRCAPGYYGDG 42
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
304-360 |
2.35e-03 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 38.49 E-value: 2.35e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 300798041 304 CVCHGHADVcdaKDPSDPFRLQCACQHNTCGGSCDRCCPGFNQQPwkpatTDSANEC 360
Cdd:pfam00053 1 CDCNPHGSL---SDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLP-----SDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
363-430 |
3.62e-03 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 38.10 E-value: 3.62e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 300798041 363 CNCHGHAydcyydpevdrrnasQNLDNVYQGGGVCLdCQHHTTGINCERCVPGFYRapdQPLDSPHVC 430
Cdd:pfam00053 1 CDCNPHG---------------SLSDTCDPETGQCL-CKPGVTGRHCDRCKPGYYG---LPSDPPQGC 49
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
2596-2750 |
4.45e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 42.34 E-value: 4.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2596 RDVRAKKNQLAAQIQEAQAMLAMDTSETSEKiahakAVAAEARDTAAHVQSQLQGMQKNVERWQSqlggLRGQDL-SQAE 2674
Cdd:COG1566 79 TDLQAALAQAEAQLAAAEAQLARLEAELGAE-----AEIAAAEAQLAAAQAQLDLAQRELERYQA----LYKKGAvSQQE 149
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300798041 2675 RD-ASSSVSTLEKTLPQLLAKLSHLEnrgvhnASLALSANIGRVRKLIAQARSAANKVKVSMKFngrsgVRLRTPRD 2750
Cdd:COG1566 150 LDeARAALDAAQAQLEAAQAQLAQAQ------AGLREEEELAAAQAQVAQAEAALAQAELNLAR-----TTIRAPVD 215
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
49-302 |
1.08e-99 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 320.68 E-value: 1.08e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 49 LHPPYFNLAEGARITASATCGEEAPTRsasrptedlYCKLVGGPvaggdpnqtiQGQYCDICIAANSNKAHPVSNAIDGT 128
Cdd:pfam00055 1 CYPAFGNLAFGREVSATSTCGLNGPER---------YCILSGLE----------GGKKCFICDSRDPHNSHPPSNLTDSN 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 129 ER----WWQSPPLSRgpEYNEVNVTLDLGQVFHVAYVLIKFAnSPRPDLWVLERSTDFGHTYQPWQFFASskrDCLERFG 204
Cdd:pfam00055 62 NGtnetWWQSETGVI--QYENVNLTLDLGKEFHFTYLILKFK-SPRPAAMVLERSTDFGKTWQPYQYFAS---DCRRTFG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 205 -PRTLERITQDDDVICTTEYSRIVPLENGEIVVSLVNGRPGARNFSYSPVLRDFTKATNIRLRFLRTNTLLGHLmgkaLR 283
Cdd:pfam00055 136 rPSGPSRGIKDDEVICTSEYSDISPLTGGEVIFSTLEGRPSANIFDYSPELQDWLTATNIRIRLLRLHTLGDEL----LD 211
|
250
....*....|....*....
gi 300798041 284 DPTVTRRYYYSIKDISIGG 302
Cdd:pfam00055 212 DPSVLRKYYYAISDISVGG 230
|
|
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
48-302 |
4.35e-98 |
|
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related protein such as Unc-6/ netrins.
Pssm-ID: 214532 Cd Length: 238 Bit Score: 316.61 E-value: 4.35e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 48 SLHPPYFNLAEGARITASATCGEEAPTRsasrptedlYCKLVGGpvaggdpnqTIQGQYCDICIAANSNKAHPVSNAIDG 127
Cdd:smart00136 6 SCYPPFVNLAFGREVTATSTCGEPGPER---------YCKLVGH---------TEQGKKCDYCDARNPRRSHPAENLTDG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 128 TE----RWWQSPPLSRGPEYneVNVTLDLGQVFHVAYVLIKFAnSPRPDLWVLERStDFGHTYQPWQFFASskrDCLERF 203
Cdd:smart00136 68 NNpnnpTWWQSEPLSNGPQN--VNLTLDLGKEFHVTYVILKFC-SPRPSLWILERS-DFGKTWQPWQYFSS---DCRRTF 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 204 G--PRTLERITQDDDVICTTEYSRIVPLENGEIVVSLVNGRPGARNFSYSPVLRDFTKATNIRLRFLRTNTLLGHLMGKA 281
Cdd:smart00136 141 GrpPRGPITKGNEDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDFDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDR 220
|
250 260
....*....|....*....|.
gi 300798041 282 lrdPTVTRRYYYSIKDISIGG 302
Cdd:smart00136 221 ---PEVTRRYYYAISDIAVGG 238
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
2193-2448 |
8.65e-65 |
|
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: 221.90 E-value: 8.65e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2193 LRGINASSTAWARLHRLNASIADLQSKLRSPLGPHNQTAEQLQTLEQQSISLQQDTERLGSQATGVQDQAGRLLDNTEST 2272
Cdd:pfam06008 1 LLSLNSLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2273 LVRAQKLLEIVQAVSRALNELASQ--GFPGNATTPSGEQLRWALAEVERLLWDMRTRDLGAPQAVAEAELAEAQRLMARV 2350
Cdd:pfam06008 81 LGHAKELAEAIKNLIDNIKEINEKvaTLGENDFALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQDLLSRI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2351 QEQLTSFWEENQALATHIRDQLAQYESGLMDLREALNHAVNTTREADELNSRNEERLREALQWKQELSQDNATLKATLQA 2430
Cdd:pfam06008 161 QTWFQSPQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEETLKT 240
|
250
....*....|....*...
gi 300798041 2431 ASLTLAHVSELLQGIDKA 2448
Cdd:pfam06008 241 ARDSLDAANLLLQEIDDA 258
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
1693-1829 |
3.13e-49 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 172.45 E-value: 3.13e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 1693 YWQAPPSYLGDRVSSYGGTLHYELHSETRRGDVfiPYESRPDVVLQGNQMSIAFL--ELAYPSPGQVHRGQLQLVEGNFR 1770
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGGG--SLNSEPDVILEGNGLRLSYSspDQPPPDPGQEQTYSVRLHEENWR 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 300798041 1771 HlETHNPVSREELMMVLAGLEQLQIRALFSQTSSTVSLRRVVLEVASEAGGGPPASNVE 1829
Cdd:pfam00052 79 D-SDGAPVSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSAVPGGSGPPASWVE 136
|
|
| LamB |
smart00281 |
Laminin B domain; |
1689-1818 |
3.27e-48 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 168.98 E-value: 3.27e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 1689 FPELYWQAPPSYLGDRVSSYGGTLHYELHSETRRGDvfiPYESRPDVVLQGNQMSIAFLELAYPSPGQVHRGQLQLVEGN 1768
Cdd:smart00281 2 NEPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRRGG---THVSAPDVILEGNGLRISHPAEGPPLPDELTTVEVRFREEN 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 300798041 1769 FRHLEtHNPVSREELMMVLAGLEQLQIRALFSQTSSTVSLRRVVLEVASE 1818
Cdd:smart00281 79 WQYYG-GRPVTREDLMMVLANLTAILIRATYSQQMAGSRLSDVSLEVAVP 127
|
|
| Laminin_II |
pfam06009 |
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 ... |
2639-2760 |
7.26e-45 |
|
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: 159.96 E-value: 7.26e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2639 DTAAHVQSQLQGMQKNVERWQSQLGGLRGQ---------DLSQAERDASSSVSTLEKTLPQLLAKLSHLENRGVHNASLa 2709
Cdd:pfam06009 10 ETAKEVLEQLAPLSQNLENTSEKLSGINRSleetnelvnDANKALDDAGRSVKKLEELAPDLLDKLKPLKQLEVNSSSL- 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 300798041 2710 lSANIGRVRKLIAQARSAANKVKVSMKFNGRSGVRLRTPRDLADLAAYTAL 2760
Cdd:pfam06009 89 -SDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTSL 138
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
3514-3663 |
1.48e-27 |
|
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: 110.97 E-value: 1.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 3514 GLFFPGSeGAVTLELPKAKMPHVSLELEVRPLAAAGLIFHLGQAHATPYVQLQLLTEQVLLRANDGAGefSTWVTYP-KL 3592
Cdd:cd00110 1 GVSFSGS-SYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSG--SLVLSSKtPL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300798041 3593 CDGQWHQVTVIKGRNTLRLEVD-THSNHTTGRLPETLADSPALLHLGSPPKSEAAWPEP--PAYRGCLRKLLFN 3663
Cdd:cd00110 78 NDGQWHSVSVERNGRSVTLSVDgERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPvsPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
3537-3664 |
9.56e-27 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 107.81 E-value: 9.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 3537 SLELEVRPLAAAGLIFHLGQAHATPYVQLQLLTEQVLLRANDGAGEFSTWVTYPKLCDGQWHQVTVIKGRNTLRLEVDtH 3616
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLNDGQWHRVAVERNGRSVTLSVD-G 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 300798041 3617 SNHTTGRLPE--TLADSPALLHLGSPPKSEAAWPEP--PAYRGCLRKLLFNG 3664
Cdd:smart00282 80 GNRVSGESPGglTILNLDGPLYLGGLPEDLKLPPLPvtPGFRGCIRNLKVNG 131
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
3338-3490 |
1.11e-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: 108.27 E-value: 1.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 3338 PGPSYLQFVGvSPSHRNRLHLSMLVRPHgASQGLLLYVAPlSSHSPSLVLFLNHGRFVAQTEGPGPQLQAQSRQHSRAGQ 3417
Cdd:cd00110 5 SGSSYVRLPT-LPAPRTRLSISFSFRTT-SPNGLLLYAGS-QNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDGQ 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300798041 3418 WHRVSVRWGMQQVQLVVDGSQTWSQKAPHRRVHRaegPQHYTLFVGGLPAGSYSSKLPVSVGFSGCMKKLQLD 3490
Cdd:cd00110 82 WHSVSVERNGRSVTLSVDGERVVESGSPGGSALL---NLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
3542-3664 |
1.67e-23 |
|
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: 98.26 E-value: 1.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 3542 VRPLAAAGLIFHLGQaHATPYVQLQLLTEQVLLRANDGAGEFSTWVTYPKLCDGQWHQVTVIKGRNTLRLEVDTHSNHTT 3621
Cdd:pfam02210 1 FRTRQPNGLLLYAGG-GGSDFLALELVNGRLVLRYDLGSGPESLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSS 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 300798041 3622 GRLPETLA-DSPALLHLGSPPKSEAAWPEP--PAYRGCLRKLLFNG 3664
Cdd:pfam02210 80 LPPGESLLlNLNGPLYLGGLPPLLLLPALPvrAGFVGCIRDVRVNG 125
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
3367-3492 |
1.90e-22 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 95.56 E-value: 1.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 3367 ASQGLLLYVAPLSSHSpsLVLFLNHGRFVAQTE-GPGPQLQAQSRQHSRAGQWHRVSVRWGMQQVQLVVDGSQTWSQKAP 3445
Cdd:pfam02210 5 QPNGLLLYAGGGGSDF--LALELVNGRLVLRYDlGSGPESLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSLPP 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 300798041 3446 HRRVHRaegPQHYTLFVGGLPAGSYSSKLPVSVGFSGCMKKLQLDKR 3492
Cdd:pfam02210 83 GESLLL---NLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| LamG |
smart00282 |
Laminin G domain; |
3357-3492 |
2.38e-20 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 89.71 E-value: 2.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 3357 HLSMLVRPHgASQGLLLYVAPlSSHSPSLVLFLNHGRFVAQTEGPGPQLQAQS-RQHSRAGQWHRVSVRWGMQQVQLVVD 3435
Cdd:smart00282 1 SISFSFRTT-SPNGLLLYAGS-KGGGDYLALELRDGRLVLRYDLGSGPARLTSdPTPLNDGQWHRVAVERNGRSVTLSVD 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 300798041 3436 GSQTWSQKAP-HRRVHRAEGPqhytLFVGGLPAGSYSSKLPVSVGFSGCMKKLQLDKR 3492
Cdd:smart00282 79 GGNRVSGESPgGLTILNLDGP----LYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| LamG |
smart00282 |
Laminin G domain; |
3151-3269 |
6.94e-17 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 79.69 E-value: 6.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 3151 FGFRGTQDDNLLYYRTSPDGP--YQVSLRGGHVTLQFMN-----REVETQRVFADGAPHYVAFYSNVTRVWLYVDDQLQP 3223
Cdd:smart00282 4 FSFRTTSPNGLLLYAGSKGGGdyLALELRDGRLVLRYDLgsgpaRLTSDPTPLNDGQWHRVAVERNGRSVTLSVDGGNRV 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 300798041 3224 VKSREGTTPMLQLqpeePPRLLLGGLPMSG------TFHNFSGCISNVFVQR 3269
Cdd:smart00282 84 SGESPGGLTILNL----DGPLYLGGLPEDLklpplpVTPGFRGCIRNLKVNG 131
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
3124-3267 |
4.64e-15 |
|
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: 75.15 E-value: 4.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 3124 TMTFHGHGFLplALPDVAPITGEVYSGFGFRGTQDDN-LLYYRTSPDGPY-QVSLRGGHVTLQFMNRE----VETQRVFA 3197
Cdd:cd00110 1 GVSFSGSSYV--RLPTLPAPRTRLSISFSFRTTSPNGlLLYAGSQNGGDFlALELEDGRLVLRYDLGSgslvLSSKTPLN 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 300798041 3198 DGAPHYVAFYSNVTRVWLYVDDqLQPVKSREGTTpmlQLQPEEPPRLLLGGLPMSGTF------HNFSGCISNVFV 3267
Cdd:cd00110 79 DGQWHSVSVERNGRSVTLSVDG-ERVVESGSPGG---SALLNLDGPLYLGGLPEDLKSpglpvsPGFVGCIRDLKV 150
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1442-1490 |
1.15e-13 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 67.76 E-value: 1.15e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 300798041 1442 CGCHEVGAVGPTCEPFGGQCPCRGHVIGRDCSRCATGYWGFPNCRPCDC 1490
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2943-3095 |
1.83e-13 |
|
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: 70.52 E-value: 1.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2943 GSYLDGSGFARITFEKQFSNTKRFEQELRLVSYNGIIFFLKQENQ--FLCLAVQDGTLVLLYDFGSGLKRadpLQPPQAL 3020
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGgdFLALELEDGRLVLRYDLGSGSLV---LSSKTPL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300798041 3021 tAASKAIQVFLLAGARKRVLV--RVERATVFSVDQDNELEMADAYYLGGVPPEELPPSLrrlfPSGGSVRGCIKGIK 3095
Cdd:cd00110 78 -NDGQWHSVSVERNGRSVTLSvdGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGL----PVSPGFVGCIRDLK 149
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1581-1629 |
2.65e-13 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 66.61 E-value: 2.65e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 300798041 1581 CDCHEAGTMASVCDPFTGQCHCKENVQGSRCDQCRVGTFSLDAANPKGC 1629
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| LamG |
smart00282 |
Laminin G domain; |
2781-2908 |
2.67e-13 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 69.29 E-value: 2.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2781 FVLYMGSRQaTGDYMGVSLRNQKVHWVYRLGeAGPTTLSIDE---NIGeQFAAVSIDRTLQFGHMSVTVEKHMVheikgd 2857
Cdd:smart00282 14 LLLYAGSKG-GGDYLALELRDGRLVLRYDLG-SGPARLTSDPtplNDG-QWHRVAVERNGRSVTLSVDGGNRVS------ 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 300798041 2858 TVAPGREGLLNLnpdDFVFYVGGYPSNFTPPEPLRFPGYLGCIEMDTLNEE 2908
Cdd:smart00282 85 GESPGGLTILNL---DGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
592-639 |
7.54e-13 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 65.45 E-value: 7.54e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 300798041 592 CGCSPAGTLPQGCD-ESGHCQCRPGFDGPHCDRCLPGYHGYPDCHACAC 639
Cdd:pfam00053 1 CDCNPHGSLSDTCDpETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
681-723 |
2.33e-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: 63.91 E-value: 2.33e-12
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 300798041 681 PCHCSADGSMHTTCDPTTGQCRCRPRVTGLRCDMCVPGAYNFP 723
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
2070-2116 |
4.57e-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: 63.14 E-value: 4.57e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 300798041 2070 PCAC-GPAAEGSECNPQTGQCHCRPGTTGPQCLECAPGYWGLPEK--GCR 2116
Cdd:cd00055 1 PCDCnGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQggGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1441-1483 |
7.52e-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: 62.37 E-value: 7.52e-12
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 300798041 1441 PCGCHEVGAVGPTCEPFGGQCPCRGHVIGRDCSRCATGYWGFP 1483
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1580-1630 |
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: 61.99 E-value: 1.02e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 300798041 1580 PCDCHEAGTMASVCDPFTGQCHCKENVQGSRCDQCRVGTFSlDAANPKGCT 1630
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYG-LPSQGGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
637-684 |
1.21e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 61.99 E-value: 1.21e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 300798041 637 CACDPRGSLDQQC-GAGGLCHCRPGYTGATCQECSPGFYGFPSCIPCHC 684
Cdd:pfam00053 1 CDCNPHGSLSDTCdPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
2071-2115 |
1.46e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 61.56 E-value: 1.46e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 300798041 2071 CACGPA-AEGSECNPQTGQCHCRPGTTGPQCLECAPGYWGLPEKGC 2115
Cdd:smart00180 1 CDCDPGgSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1581-1629 |
1.48e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 61.56 E-value: 1.48e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 300798041 1581 CDCHEAGTMASVCDPFTGQCHCKENVQGSRCDQCRVGTFsldAANPKGC 1629
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYY---GDGPPGC 46
|
|
| LamG |
smart00282 |
Laminin G domain; |
2965-3099 |
1.50e-11 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 64.28 E-value: 1.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2965 RFEQELRLVSYNGIIFFL--KQENQFLCLAVQDGTLVLLYDFGSGLKRadpLQPPQALTAASKAIQVFLLAGARKRVLV- 3041
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAgsKGGGDYLALELRDGRLVLRYDLGSGPAR---LTSDPTPLNDGQWHRVAVERNGRSVTLSv 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 300798041 3042 -RVERATVFSVDQDNELEMADAYYLGGVPPEELPPSLrrlfPSGGSVRGCIKGIKALGK 3099
Cdd:smart00282 78 dGGNRVSGESPGGLTILNLDGPLYLGGLPEDLKLPPL----PVTPGFRGCIRNLKVNGK 132
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1532-1583 |
1.86e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 61.22 E-value: 1.86e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 300798041 1532 CNCSGPGVqelTDPTCDMDSGQCRCRPNVAGRRCDTCAPGFYSYPSCRPCDC 1583
Cdd:pfam00053 1 CDCNPHGS---LSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1969-2022 |
2.60e-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: 60.83 E-value: 2.60e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 300798041 1969 PCDCSGNGDPNmifSDCDPLTGACRgCLRHTTGPRCESCAPGFYGNALLPGNCT 2022
Cdd:cd00055 1 PCDCNGHGSLS---GQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
499-546 |
3.49e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 60.40 E-value: 3.49e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 300798041 499 CDCNAAGTQGNACrkDPRLGRCVCKPNFQGNHCELCAPGFYGPSCHPC 546
Cdd:smart00180 1 CDCDPGGSASGTC--DPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1442-1485 |
3.73e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 60.40 E-value: 3.73e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 300798041 1442 CGCHEVGAVGPTCEPFGGQCPCRGHVIGRDCSRCATGYWG--FPNC 1485
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
2024-2068 |
3.77e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 60.40 E-value: 3.77e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 300798041 2024 CDCSPCGT--ETCDPQTGRCLCKAGVTGQRCDHCLEGHFGfEQCQGC 2068
Cdd:smart00180 1 CDCDPGGSasGTCDPDTGQCECKPNVTGRRCDRCAPGYYG-DGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
2071-2118 |
4.89e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 60.06 E-value: 4.89e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 300798041 2071 CACGP-AAEGSECNPQTGQCHCRPGTTGPQCLECAPGYWGLPEKGCRRC 2118
Cdd:pfam00053 1 CDCNPhGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2970-3095 |
5.13e-11 |
|
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: 62.82 E-value: 5.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2970 LRLVSYNGIIFFLKQE-NQFLCLAVQDGTLVLLYDFGSGlkradplqpPQALTAASKAiqvfLLAGARKRVLVRVERATV 3048
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGgSDFLALELVNGRLVLRYDLGSG---------PESLLSSGKN----LNDGQWHSVRVERNGNTL 67
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 300798041 3049 -FSVDQDNELEMA-----------DAYYLGGVPPEELPPSLrrlfPSGGSVRGCIKGIK 3095
Cdd:pfam02210 68 tLSVDGQTVVSSLppgeslllnlnGPLYLGGLPPLLLLPAL----PVRAGFVGCIRDVR 122
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
3542-3668 |
5.53e-11 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 62.72 E-value: 5.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 3542 VRPLAAAGLIFHLGQAHATPYVQLQLLTEQVLLRANDGAGEFSTwVTYPKLCDGQWHQVTVIKGRNTLRLEVDTHSNHTT 3621
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVV-RSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTG 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 300798041 3622 GRL--PETLADSPALLHLGS-PPKSEAAWPEP--PAYRGCLRKLLFNGAPVN 3668
Cdd:pfam00054 80 ESPlgATTDLDVDGPLYVGGlPSLGVKKRRLAisPSFDGCIRDVIVNGKPLD 131
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
682-724 |
5.91e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 60.02 E-value: 5.91e-11
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 300798041 682 CHCSADGSMHTTCDPTTGQCRCRPRVTGLRCDMCVPGAYNFPY 724
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
2023-2069 |
7.33e-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: 59.68 E-value: 7.33e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 300798041 2023 RCDCSPCGT--ETCDPQTGRCLCKAGVTGQRCDHCLEGHFGF-EQCQGCH 2069
Cdd:cd00055 1 PCDCNGHGSlsGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLpSQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
592-633 |
7.41e-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: 59.68 E-value: 7.41e-11
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 300798041 592 CGCSPAGTLPQGCD-ESGHCQCRPGFDGPHCDRCLPGYHGYPD 633
Cdd:cd00055 2 CDCNGHGSLSGQCDpGTGQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
545-588 |
7.41e-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: 59.68 E-value: 7.41e-11
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 300798041 545 PCQCSSPGVANGLCDPESGQCTCRTGFEGDKCDHCALGYFHFPL 588
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
682-730 |
8.96e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 59.29 E-value: 8.96e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 300798041 682 CHCSADGSMHTTCDPTTGQCRCRPRVTGLRCDMCVPGAYNFPYCEAGSC 730
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1532-1578 |
9.64e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 59.25 E-value: 9.64e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 300798041 1532 CNCSGPGVQeltDPTCDMDSGQCRCRPNVAGRRCDTCAPGFY--SYPSC 1578
Cdd:smart00180 1 CDCDPGGSA---SGTCDPDTGQCECKPNVTGRRCDRCAPGYYgdGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1532-1577 |
1.08e-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: 59.29 E-value: 1.08e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 300798041 1532 CNCSGPGVQeltDPTCDMDSGQCRCRPNVAGRRCDTCAPGFYSYPS 1577
Cdd:cd00055 2 CDCNGHGSL---SGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
2024-2068 |
1.24e-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: 58.90 E-value: 1.24e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 300798041 2024 CDCSPCGT--ETCDPQTGRCLCKAGVTGQRCDHCLEGHFGFEQCQGC 2068
Cdd:pfam00053 1 CDCNPHGSlsDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQ 47
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
499-548 |
1.97e-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: 58.52 E-value: 1.97e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 300798041 499 CDCNAAGTQGNACrkDPRLGRCVCKPNFQGNHCELCAPGFYGPSCHPCQC 548
Cdd:cd00055 2 CDCNGHGSLSGQC--DPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
499-548 |
2.02e-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: 58.52 E-value: 2.02e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 300798041 499 CDCNAAGTQGNACrkDPRLGRCVCKPNFQGNHCELCAPGFYG-PSCHPCQC 548
Cdd:pfam00053 1 CDCNPHGSLSDTC--DPETGQCLCKPGVTGRHCDRCKPGYYGlPSDPPQGC 49
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2204-2732 |
2.59e-10 |
|
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: 67.00 E-value: 2.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2204 ARLHRLNASIADLQSKLRSPLGPHNQTAEQLQTLEQQSISLQQDTERLGSQATGVQ----------DQAGRLLDNTESTL 2273
Cdd:TIGR02168 295 NEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKeelesleaelEELEAELEELESRL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2274 VRAQKLLEivqAVSRALNELASQGFPGNAttpsgeQLRWALAEVERL-----LWDMRTRDLG-APQAVAEAELAEAQRLM 2347
Cdd:TIGR02168 375 EELEEQLE---TLRSKVAQLELQIASLNN------EIERLEARLERLedrreRLQQEIEELLkKLEEAELKELQAELEEL 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2348 ARVQEQLTSFWEENQALATHIRDQLAQYESGLMDLREALNHA---VNTTREADELNSRNEERLREALQWKQELSQDNATL 2424
Cdd:TIGR02168 446 EEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLqarLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVL 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2425 KATL-------QAASLTLAhvsELLQGI-----DKAKEDLEHLAASLDGAWTPL-LKRMQAFSPASSK------------ 2479
Cdd:TIGR02168 526 SELIsvdegyeAAIEAALG---GRLQAVvvenlNAAKKAIAFLKQNELGRVTFLpLDSIKGTEIQGNDreilkniegflg 602
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2480 --VDLVEAAEAhAQK-----LNQL--------AINL--------------------SGIIQG---------INQDRFIQR 2515
Cdd:TIGR02168 603 vaKDLVKFDPK-LRKalsylLGGVlvvddldnALELakklrpgyrivtldgdlvrpGGVITGgsaktnssiLERRREIEE 681
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2516 AV----EASNAYSSILQAVQAAE-------------DAAGHALRQASRTWEMVVQRgLAAGARQLLANSSALVETILGHQ 2578
Cdd:TIGR02168 682 LEekieELEEKIAELEKALAELRkeleeleeeleqlRKELEELSRQISALRKDLAR-LEAEVEQLEERIAQLSKELTELE 760
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2579 ERLGLAHGRLQAAGTQLRDVRAKKNQLAAQIQEAQAMLAMDTSETSEKiahaKAVAAEARDTAAHVQSQLQGMQKNVERW 2658
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL----RAELTLLNEEAANLRERLESLERRIAAT 836
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300798041 2659 QSQLGGLRGQ--DLSQAERDASSSVSTLEKTLPQLLAKLSHLEN-RGVHNASLALSANigRVRKLIAQARSAANKVK 2732
Cdd:TIGR02168 837 ERRLEDLEEQieELSEDIESLAAEIEELEELIEELESELEALLNeRASLEEALALLRS--ELEELSEELRELESKRS 911
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
3153-3267 |
2.59e-10 |
|
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: 60.90 E-value: 2.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 3153 FRGTQDDNLLYYRTSPDGPY-QVSLRGGHVTLQFM-----NREVETQRVFADGAPHYVAFYSNVTRVWLYVDDQlqPVKS 3226
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDFlALELVNGRLVLRYDlgsgpESLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQ--TVVS 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 300798041 3227 REGTTPMLQLQPEEPprLLLGGLP------MSGTFHNFSGCISNVFV 3267
Cdd:pfam02210 79 SLPPGESLLLNLNGP--LYLGGLPpllllpALPVRAGFVGCIRDVRV 123
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
592-632 |
3.44e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 57.71 E-value: 3.44e-10
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 300798041 592 CGCSPAGTLPQGCD-ESGHCQCRPGFDGPHCDRCLPGYHGYP 632
Cdd:smart00180 1 CDCDPGGSASGTCDpDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2174-2698 |
4.66e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 65.56 E-value: 4.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2174 LLLDDLERAGALLPSIREQLRGINAsstawARLHRLNASIADLQSKLRSplgpHNQTAEQLQTLEQQSISLQQDTERLgs 2253
Cdd:COG4717 46 MLLERLEKEADELFKPQGRKPELNL-----KELKELEEELKEAEEKEEE----YAELQEELEELEEELEELEAELEEL-- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2254 qatgvqdqagrllDNTESTLVRAQKLLEIVQAVSRALNELASqgFPGNAttpsgEQLRWALAEVERLLWDMRTRDLGApQ 2333
Cdd:COG4717 115 -------------REELEKLEKLLQLLPLYQELEALEAELAE--LPERL-----EELEERLEELRELEEELEELEAEL-A 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2334 AVAEAELAEAQRLMARVQEQLTSFWEENQALathiRDQLAQYESGLMDLREALNHAvntTREADEL-NSRNEERLREALQ 2412
Cdd:COG4717 174 ELQEELEELLEQLSLATEEELQDLAEELEEL----QQRLAELEEELEEAQEELEEL---EEELEQLeNELEAAALEERLK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2413 WKQELSQDNATLkATLQAASLTLAHVSELLQGI---------------DKAKEDLEHLAASLDGA----------WTPLL 2467
Cdd:COG4717 247 EARLLLLIAAAL-LALLGLGGSLLSLILTIAGVlflvlgllallflllAREKASLGKEAEELQALpaleeleeeeLEELL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2468 KRMQAfsPASSKVDLVEAAEAHAQKLNQLAINLSGIIQGINQDRFIQRAveasnaySSILQAVQAAEDAAghaLRQASRT 2547
Cdd:COG4717 326 AALGL--PPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEI-------AALLAEAGVEDEEE---LRAALEQ 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2548 WEMVVQ-RGLAAGARQLLANSSALVETILGHQERLGLAHgRLQAAGTQLRDVRAKKNQLAAQIQEAQAmlAMDTSETSEK 2626
Cdd:COG4717 394 AEEYQElKEELEELEEQLEELLGELEELLEALDEEELEE-ELEELEEELEELEEELEELREELAELEA--ELEQLEEDGE 470
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300798041 2627 IahakavaaeaRDTAAHVQSQLQGMQKNVERWQS-QLGglrGQDLSQAERDASssvstlEKTLPQLLAKLSHL 2698
Cdd:COG4717 471 L----------AELLQELEELKAELRELAEEWAAlKLA---LELLEEAREEYR------EERLPPVLERASEY 524
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
546-587 |
1.26e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.17 E-value: 1.26e-09
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 300798041 546 CQCSSPGVANGLCDPESGQCTCRTGFEGDKCDHCALGYFHFP 587
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2734-2901 |
1.31e-09 |
|
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: 59.35 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2734 SMKFNGRSGVRLRTPRDLADlaaYTALKFYIQSPVPapepgenTGdrFVLYMGSrQATGDYMGVSLRNQKVHWVYRLGEa 2813
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRT---RLSISFSFRTTSP-------NG--LLLYAGS-QNGGDFLALELEDGRLVLRYDLGS- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2814 GPTTLSIDENIGE-QFAAVSIDRTLQFGHMSVTVEKHMvheikgDTVAPGREGLLNLNPDdfvFYVGGYPSNFTPPEPLR 2892
Cdd:cd00110 67 GSLVLSSKTPLNDgQWHSVSVERNGRSVTLSVDGERVV------ESGSPGGSALLNLDGP---LYLGGLPEDLKSPGLPV 137
|
....*....
gi 300798041 2893 FPGYLGCIE 2901
Cdd:cd00110 138 SPGFVGCIR 146
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
546-594 |
1.97e-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: 55.82 E-value: 1.97e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 300798041 546 CQCSSPGVANGLCDPESGQCTCRTGFEGDKCDHCALGYFHFPLCQLCGC 594
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
636-678 |
3.14e-09 |
|
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: 55.05 E-value: 3.14e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 300798041 636 ACACDPRGSLDQQCGAG-GLCHCRPGYTGATCQECSPGFYGFPS 678
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGtGQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1970-2020 |
6.63e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 54.28 E-value: 6.63e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 300798041 1970 CDCSGNGDPNmifSDCDPLTGACRgCLRHTTGPRCESCAPGFYGNALLPGN 2020
Cdd:pfam00053 1 CDCNPHGSLS---DTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQ 47
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2783-2901 |
7.31e-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: 56.66 E-value: 7.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2783 LYMGSRQatGDYMGVSLRNQKVHWVYRLGEAGPTTLSIDENI--GeQFAAVSIDRTLQfgHMSVTVEKHMVHEikgdTVA 2860
Cdd:pfam02210 11 LYAGGGG--SDFLALELVNGRLVLRYDLGSGPESLLSSGKNLndG-QWHSVRVERNGN--TLTLSVDGQTVVS----SLP 81
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 300798041 2861 PGREGLLNLNPDdfvFYVGGYPSNFTPPEPLRFPGYLGCIE 2901
Cdd:pfam02210 82 PGESLLLNLNGP---LYLGGLPPLLLLPALPVRAGFVGCIR 119
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
637-679 |
1.03e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 53.47 E-value: 1.03e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 300798041 637 CACDPRGSLDQQC-GAGGLCHCRPGYTGATCQECSPGFYG--FPSC 679
Cdd:smart00180 1 CDCDPGGSASGTCdPDTGQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1914-1967 |
2.56e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 52.36 E-value: 2.56e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 300798041 1914 CPCPLAVPSNnfaDGCILRNGrtQCLCRPGYAGASCERCAPGFFGNPLVLGSSC 1967
Cdd:pfam00053 1 CDCNPHGSLS---DTCDPETG--QCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2204-2731 |
2.72e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.34 E-value: 2.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2204 ARLHRLNASIADLQSKLRsplgphnQTAEQLQTLEQQSISLQQDTERLGSQATGVQDQAgRLLDNTESTLVRAQKLLEiv 2283
Cdd:COG1196 239 AELEELEAELEELEAELE-------ELEAELAELEAELEELRLELEELELELEEAQAEE-YELLAELARLEQDIARLE-- 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2284 QAVSRALNELasqgfpgnattpsgEQLRWALAEVERllwdmRTRDLGAPQAVAEAELAEAQRLMARVQEQLTSFWEENQA 2363
Cdd:COG1196 309 ERRRELEERL--------------EELEEELAELEE-----ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2364 LATHIRDQLAQYESGLMDLREALNHAVNTTREADELNSRNEERLREALQWKQELSQDNATLKATLQAASLTLAHVSELLQ 2443
Cdd:COG1196 370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2444 GIDKAKEDLEHLAASLdgawtpllkrmqafspasskVDLVEAAEAHAQKLNQLAINLSGIIQgiNQDRFIQRAVEASNAY 2523
Cdd:COG1196 450 EEAELEEEEEALLELL--------------------AELLEEAALLEAALAELLEELAEAAA--RLLLLLEAEADYEGFL 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2524 SSILQAVQAAEDAAGHALRQASRTWEMVVQRGL-----AAGARQLLANSSALVETILGHQERLGLAHGRLQAAGTQLRDV 2598
Cdd:COG1196 508 EGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALeaalaAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAA 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2599 RAKKNQLAAqIQEAQAMLAMDTSETSEKIAHAKAVAAEARDTAAHVQSQLQGMQKNVERWQSQL----GGLRGQDLSQAE 2674
Cdd:COG1196 588 LAAALARGA-IGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTlegeGGSAGGSLTGGS 666
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 300798041 2675 RDASSSVSTLEKTLPQLLAKLSHLENRGVHNASLALSANIGRVRKLIAQARSAANKV 2731
Cdd:COG1196 667 RRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEE 723
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2309-2616 |
3.87e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.57 E-value: 3.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2309 QLRWALAEVERLLWDMRTRDLGAPQAVAEAELAEAQRLMARVQEQLtsfwEENQALATHIRDQLAQYESGLMDLREALNH 2388
Cdd:COG1196 217 ELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAEL----AELEAELEELRLELEELELELEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2389 AVNTTREADELNSRNEERLREALQWKQELSQDNATLKATLQAASLTLAhvsELLQGIDKAKEDLEHLAASLDGAWTPLLK 2468
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELE---ELEEELEEAEEELEEAEAELAEAEEALLE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2469 RMQAFSPASS-----KVDLVEAAEAHAQKLNQLAiNLSGIIQGINQDRfiQRAVEASNAYSSILQAVQAAEDAAGHALRQ 2543
Cdd:COG1196 370 AEAELAEAEEeleelAEELLEALRAAAELAAQLE-ELEEAEEALLERL--ERLEEELEELEEALAELEEEEEEEEEALEE 446
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300798041 2544 ASRTwemvvQRGLAAGARQLLANSSALVETILGHQERLGLAHGRLQAAGTQLRDVRAKKNQLAAQIQEAQAML 2616
Cdd:COG1196 447 AAEE-----EAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAAL 514
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2175-2718 |
4.54e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 59.28 E-value: 4.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2175 LLDDL----------ERAG-------ALLPSIREQLRGINA------SSTAWARLHRLNASIADLQSKLR---------- 2221
Cdd:PRK02224 154 MIDDLlqlgkleeyrERASdarlgveRVLSDQRGSLDQLKAqieekeEKDLHERLNGLESELAELDEEIEryeeqreqar 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2222 -------SPLGPHNQTAEQLQTLEQQSISLQQD---TER----LGSQATGVQDQAGRLLDNTESTLVRAQKLLEIVQAVS 2287
Cdd:PRK02224 234 etrdeadEVLEEHEERREELETLEAEIEDLRETiaeTERereeLAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2288 RALNELASQgfpgnattpsgeqlrwaLAEVERLLWDMRTrDLGAPQAVAEAELAEAQRLMARVQE------QLTSFWEEN 2361
Cdd:PRK02224 314 ARREELEDR-----------------DEELRDRLEECRV-AAQAHNEEAESLREDADDLEERAEElreeaaELESELEEA 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2362 QALATHIRDQLAQYESGLMDLREALNhavNTTREADELNSRNEERLREalqwKQELSQDNATLKATLQAASLTLAHVSEL 2441
Cdd:PRK02224 376 REAVEDRREEIEELEEEIEELRERFG---DAPVDLGNAEDFLEELREE----RDELREREAELEATLRTARERVEEAEAL 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2442 LQ------------------GIDKAKEDLEHLAASLDGAWTPLLKRMQAFSPASskvDLVEaAEAHAQKLNQLAINLSGI 2503
Cdd:PRK02224 449 LEagkcpecgqpvegsphveTIEEDRERVEELEAELEDLEEEVEEVEERLERAE---DLVE-AEDRIERLEERREDLEEL 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2504 I----QGINQDRfiqRAVEASNAYSSILQA-VQAAEDAAGHALRQASRTWEMVV----QRGLAAGARQLLANSSALVETI 2574
Cdd:PRK02224 525 IaerrETIEEKR---ERAEELRERAAELEAeAEEKREAAAEAEEEAEEAREEVAelnsKLAELKERIESLERIRTLLAAI 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2575 LGHQERLGLAHGRLQAAGT-------QLRDVRAKKNQLAAQIQEAQAMLAMDTSETSEKIAhakavaaeardtaAHVQSQ 2647
Cdd:PRK02224 602 ADAEDEIERLREKREALAElnderreRLAEKRERKRELEAEFDEARIEEAREDKERAEEYL-------------EQVEEK 668
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 300798041 2648 LQGMQKNVERWQSQLGGLRGQdLSQAErdasssvsTLEKTLPQLLAKLSHLENrgVHNASLALSANIGRVR 2718
Cdd:PRK02224 669 LDELREERDDLQAEIGAVENE-LEELE--------ELRERREALENRVEALEA--LYDEAEELESMYGDLR 728
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
2172-2662 |
4.64e-08 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 59.15 E-value: 4.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2172 VVLLLDDLERAgallpsIREQ---LRG--INASSTAWARLHRLNASIADLQSKLRSPLGPHNQTAEQLQTLE-------- 2238
Cdd:COG5278 48 VLRALEELLSA------LLDAetgQRGylLTGDESFLEPYEEARAEIDELLAELRSLTADNPEQQARLDELEalidqwla 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2239 --QQSISLQQDTERLGSQATGVQDQAGRLLDNTESTLVRAQKLLEIVQAVSRALNELASQgfpgnattpSGEQLRWALAE 2316
Cdd:COG5278 122 elEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLA---------LAALLALAELL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2317 VERLLwdMRTRDLGAPQAVAEAELAEAQRLMARVQEQLTSFWEENQALATHIRDQLAQYESGLMDLREALNHAVNTTREA 2396
Cdd:COG5278 193 LLALA--RALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLAAALLAL 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2397 DELNSRNEERLREALQWKQELSQDNATLKATLQAASLTLAHVSELLQGIDKAKEDLEHLAASLDGAwtpLLKRMQAFSPA 2476
Cdd:COG5278 271 AALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATA---LAAAAAALALL 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2477 SSKVDLVEAAEAHAQKLNQLAINLSGIIQGINQDRFIQRAVEASNAyssILQAVQAAEDAAGHALRQASRTWEMVVQRGL 2556
Cdd:COG5278 348 AALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVL---AIAAAAAAAAAEAAAAAAAAAAASAAEALEL 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2557 AAGARQLLANSSALVETILGHQERLGLAHGRLQAAGTQLRDVRAKKNQLAAQIQEAQAMLAMDTSETSEKIAHAKAVAAE 2636
Cdd:COG5278 425 AEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLALA 504
|
490 500
....*....|....*....|....*.
gi 300798041 2637 ARDTAAHVQSQLQGMQKNVERWQSQL 2662
Cdd:COG5278 505 LAALLLAAAEAALAAALAAALASAEL 530
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1863-1899 |
4.72e-08 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 51.97 E-value: 4.72e-08
10 20 30 40
....*....|....*....|....*....|....*....|
gi 300798041 1863 PCQCHGH---SDRCLPGSGTCVgCQHNTEGDQCERCRPGF 1899
Cdd:cd00055 1 PCDCNGHgslSGQCDPGTGQCE-CKPNTTGRRCDRCAPGY 39
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1864-1911 |
7.67e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 51.20 E-value: 7.67e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 300798041 1864 CQCHGH---SDRCLPGSGTCVgCQHNTEGDQCERCRPGFVsSDPSDPASPC 1911
Cdd:pfam00053 1 CDCNPHgslSDTCDPETGQCL-CKPGVTGRHCDRCKPGYY-GLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1914-1960 |
1.79e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 50.00 E-value: 1.79e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 300798041 1914 CPCPlavPSNNFADGCILRNGrtQCLCRPGYAGASCERCAPGFFGNP 1960
Cdd:smart00180 1 CDCD---PGGSASGTCDPDTG--QCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
432-473 |
1.96e-07 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 50.05 E-value: 1.96e-07
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 300798041 432 PCDCESDFT-DGTCEDLTGRCYCRPNFTGERCSACAEGYVDFP 473
Cdd:cd00055 1 PCDCNGHGSlSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
3367-3494 |
2.35e-07 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 52.32 E-value: 2.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 3367 ASQGLLLYVAPlSSHSPSLVLFLNHGRfvaqtegpgpqLQAQSRQHSRA-----------GQWHRVSVRWGMQQVQLVVD 3435
Cdd:pfam00054 5 EPSGLLLYNGT-QTERDFLALELRDGR-----------LEVSYDLGSGAavvrsgdklndGKWHSVELERNGRSGTLSVD 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 3436 GSQTWSQKAPHRRVhrAEGPQHYTLFVGGLPAGSYS-SKLPVSVGFSGCMKKLQLDKRPL 3494
Cdd:pfam00054 73 GEARPTGESPLGAT--TDLDVDGPLYVGGLPSLGVKkRRLAISPSFDGCIRDVIVNGKPL 130
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
303-351 |
4.87e-07 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 48.89 E-value: 4.87e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 300798041 303 RCVCHGHADVCDAKDPSDpfrLQCACQHNTCGGSCDRCCPGFNQQPWKP 351
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGT---GQCECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
433-475 |
8.42e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 48.08 E-value: 8.42e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 300798041 433 CDCESDFT-DGTCEDLTGRCYCRPNFTGERCSACAEGY--VDFPHC 475
Cdd:smart00180 1 CDCDPGGSaSGTCDPDTGQCECKPNVTGRRCDRCAPGYygDGPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1970-2014 |
1.05e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 47.69 E-value: 1.05e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 300798041 1970 CDCSGNGdpnMIFSDCDPLTGACRgCLRHTTGPRCESCAPGFYGN 2014
Cdd:smart00180 1 CDCDPGG---SASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD 41
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1913-1968 |
1.12e-06 |
|
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: 47.73 E-value: 1.12e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 300798041 1913 SCPCPLAVPSNNfadGCILRNGrtQCLCRPGYAGASCERCAPGFFGNPLVlGSSCQ 1968
Cdd:cd00055 1 PCDCNGHGSLSG---QCDPGTG--QCECKPNTTGRRCDRCAPGYYGLPSQ-GGGCQ 50
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
2360-2619 |
1.15e-06 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 54.70 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2360 ENQAL---ATHIR--DQLAQYESGLMDLREALNHAVNTTREADELNSRNEERLREA--LQWK-QELsqDNATLKA----T 2427
Cdd:COG0497 133 EHQSLldpDAQREllDAFAGLEELLEEYREAYRAWRALKKELEELRADEAERARELdlLRFQlEEL--EAAALQPgeeeE 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2428 LQAASLTLAHVSELLQGIDKAkedLEHLAASLDGAwTPLLKR-MQAFSPASskvDLVEAAEAHAQKLNQLAINLSGIIQG 2506
Cdd:COG0497 211 LEEERRRLSNAEKLREALQEA---LEALSGGEGGA-LDLLGQaLRALERLA---EYDPSLAELAERLESALIELEEAASE 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2507 INQdrfIQRAVEASNAyssILQAVQA--AedaaghALRQASR----TWEMVVQrgLAAGARQLLANSSALVETILGHQER 2580
Cdd:COG0497 284 LRR---YLDSLEFDPE---RLEEVEErlA------LLRRLARkygvTVEELLA--YAEELRAELAELENSDERLEELEAE 349
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 300798041 2581 LGLAHGRLQAAGTQLRDVRAKK-NQLAAQIQEAQAMLAMD 2619
Cdd:COG0497 350 LAEAEAELLEAAEKLSAARKKAaKKLEKAVTAELADLGMP 389
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
832-871 |
1.22e-06 |
|
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: 47.73 E-value: 1.22e-06
10 20 30 40
....*....|....*....|....*....|....*....|
gi 300798041 832 SCRCDVGGALGQGCEPKTGACRCRPNTQGPSCSEPAKDHY 871
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYY 40
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
780-831 |
1.35e-06 |
|
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: 47.73 E-value: 1.35e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 300798041 780 RCSCDPRGTLGGvtEC-QGNGQCFCKAHVCGKTCAACKDGFFGLDhADYYGCR 831
Cdd:cd00055 1 PCDCNGHGSLSG--QCdPGTGQCECKPNTTGRRCDRCAPGYYGLP-SQGGGCQ 50
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2172-2459 |
2.39e-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: 53.91 E-value: 2.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2172 VVLLLDDLERAGALLPSIREQLRGINASSTAWA-RLHRLNASIADLQSKLRSPLGPHNQTAEQLQTLEQQSISLQQDTER 2250
Cdd:TIGR02168 714 LEQLRKELEELSRQISALRKDLARLEAEVEQLEeRIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ 793
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2251 -------LGSQATGVQDQAGRLLDNTESTLVRAQKLLEIVQAVSRALNELASQGfpgnattpsgEQLRWALAEVERLLWD 2323
Cdd:TIGR02168 794 lkeelkaLREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQI----------EELSEDIESLAAEIEE 863
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2324 MRTrdlgapqavaeaelaeaqrLMARVQEQLTSFWEENQALATHIRDQLAQYESGLMDLREALNHAVNTTREADELNSRN 2403
Cdd:TIGR02168 864 LEE-------------------LIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL 924
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 300798041 2404 EE-RLRealqwKQELSQDNATLKATLQA-ASLTLAHVSELLQGIDKAKEDLEHLAASL 2459
Cdd:TIGR02168 925 AQlELR-----LEGLEVRIDNLQERLSEeYSLTLEEAEALENKIEDDEEEARRRLKRL 977
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
781-830 |
3.31e-06 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 46.58 E-value: 3.31e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 300798041 781 CSCDPRGTLGGvtEC-QGNGQCFCKAHVCGKTCAACKDGFFGLDHADYYGC 830
Cdd:pfam00053 1 CDCNPHGSLSD--TCdPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2367-2698 |
3.35e-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: 3.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2367 HIRDQLAQYESGLMDLREALNhavnttrEADELNSRNEERLREALQWKQELSQDNATLKATLQAASLTLAHVSELLQGID 2446
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALA-------ELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2447 KAKEDLEHLAASLDgawtplLKRMQAFspasskvDLVEAAEAHAQKLNQLainlsgiiqginqdrfIQRAVEASNAYSSI 2526
Cdd:TIGR02168 754 KELTELEAEIEELE------ERLEEAE-------EELAEAEAEIEELEAQ----------------IEQLKEELKALREA 804
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2527 LQAVQAAEDAAGHALRQASRTWEMVVQRglAAGARQLLANSSALVETILGHQERLGLAHGRLQAAGTQLRD-------VR 2599
Cdd:TIGR02168 805 LDELRAELTLLNEEAANLRERLESLERR--IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESeleallnER 882
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2600 AKKNQLAAQIQEAQAMLAMDTSETSEKIAHAKAVAAEARDTAAHVQSQLQGMQKNVERWQSQL---GGLRGQDLSQAERD 2676
Cdd:TIGR02168 883 ASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLseeYSLTLEEAEALENK 962
|
330 340
....*....|....*....|..
gi 300798041 2677 ASSSVSTLEKTLPQLLAKLSHL 2698
Cdd:TIGR02168 963 IEDDEEEARRRLKRLENKIKEL 984
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
433-477 |
3.48e-06 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 46.58 E-value: 3.48e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 300798041 433 CDC-ESDFTDGTCEDLTGRCYCRPNFTGERCSACAEGYVDFPHCYP 477
Cdd:pfam00053 1 CDCnPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPP 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
833-871 |
3.93e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 46.15 E-value: 3.93e-06
10 20 30
....*....|....*....|....*....|....*....
gi 300798041 833 CRCDVGGALGQGCEPKTGACRCRPNTQGPSCSEPAKDHY 871
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYY 39
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2175-2521 |
5.17e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.83 E-value: 5.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2175 LLDDLERAGALLPSIREQLRGINAS-STAWARLHRLNASIADLQSKLRSPLGPHNQTAEQLQTLEQQSISLQQDTERLGS 2253
Cdd:COG4372 43 LQEELEQLREELEQAREELEQLEEElEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQK 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2254 QATGVQDQAGRLLDntestlvRAQKLLEIVQAVSRALNELAsqgfpgnattpsgEQLRWALAEVERLLWDMRTRDLgapq 2333
Cdd:COG4372 123 ERQDLEQQRKQLEA-------QIAELQSEIAEREEELKELE-------------EQLESLQEELAALEQELQALSE---- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2334 avaeaelaeaQRLMARVQEQLTSfWEENQALATHIRDQLAQYESGLMDLREALNHAVNTTREADELNSRNEERLREaLQW 2413
Cdd:COG4372 179 ----------AEAEQALDELLKE-ANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALE-LEE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2414 KQELSQDNATLKATLQAASLTLAHVSELLQGIDKAKEDLEHLAASLDGAWTPLLKRMQAFSPAS------SKVDLVEAAE 2487
Cdd:COG4372 247 DKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIgaledaLLAALLELAK 326
|
330 340 350
....*....|....*....|....*....|....
gi 300798041 2488 AHAQKLNQLAINLSGIIQGINQDRFIQRAVEASN 2521
Cdd:COG4372 327 KLELALAILLAELADLLQLLLVGLLDNDVLELLS 360
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
781-821 |
7.00e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 45.38 E-value: 7.00e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 300798041 781 CSCDPRGTLGGvtEC-QGNGQCFCKAHVCGKTCAACKDGFFG 821
Cdd:smart00180 1 CDCDPGGSASG--TCdPDTGQCECKPNVTGRRCDRCAPGYYG 40
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2347-2612 |
1.09e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.06 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2347 MARVQEQLTSfweenqalathIRDQLAQYESGLMDLREALNHAVNTTREA-DELNSRNEE--RLREALqwkQELSQDNAT 2423
Cdd:COG4372 61 LEQLEEELEQ-----------ARSELEQLEEELEELNEQLQAAQAELAQAqEELESLQEEaeELQEEL---EELQKERQD 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2424 LKATLQAASltlAHVSELLQGIDKAKEDLEHLAASLDGAWTPLLKRMQAFS-----PASSKVD-LVEAAEAHAQKLNQLA 2497
Cdd:COG4372 127 LEQQRKQLE---AQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQalseaEAEQALDeLLKEANRNAEKEEELA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2498 INLSGIIQG-INQDRFIQRAVEASNAYSSILQAVQAAEDAAGHALRQASRTWEMVVQRGLAAGARQLLANSSALVETILG 2576
Cdd:COG4372 204 EAEKLIESLpRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAAL 283
|
250 260 270
....*....|....*....|....*....|....*.
gi 300798041 2577 HQERLGLAHGRLQAAGTQLRDVRAKKNQLAAQIQEA 2612
Cdd:COG4372 284 ELEALEEAALELKLLALLLNLAALSLIGALEDALLA 319
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2177-2704 |
1.15e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.45 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2177 DDLERAGALLPSIREQ---LRGINASSTAWARLHRlnasIADLQSKLRSPLGP-HNQTA-----EQLQTLEQQSISLQQD 2247
Cdd:COG4913 235 DDLERAHEALEDAREQielLEPIRELAERYAAARE----RLAELEYLRAALRLwFAQRRlelleAELEELRAELARLEAE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2248 TERLGSQATGVQDQA-----------GRLLDNTESTLVRAQKLLEIVQAVSRALNELAsqgfpgnattpsgEQLRWALAE 2316
Cdd:COG4913 311 LERLEARLDALREELdeleaqirgngGDRLEQLEREIERLERELEERERRRARLEALL-------------AALGLPLPA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2317 VERLLWDMRTRdlgaPQAVAEAELAEAQRLMARVQEQLTSFWEENQALAThIRDQLAQYESG-------LMDLREALNHA 2389
Cdd:COG4913 378 SAEEFAALRAE----AAALLEALEEELEALEEALAEAEAALRDLRRELRE-LEAEIASLERRksniparLLALRDALAEA 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2390 VNTT-------------READE---------LNSR------NEERLREALQWkqelsqdnatLKATLQAASLTLAHVSEL 2441
Cdd:COG4913 453 LGLDeaelpfvgelievRPEEErwrgaiervLGGFaltllvPPEHYAAALRW----------VNRLHLRGRLVYERVRTG 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2442 LQGIDKAKEDLEHLAASLDGAWTP----LLKRMQAFSPASsKVDLVEAAEAHAQklnqlAINLSGIIQG----------- 2506
Cdd:COG4913 523 LPDPERPRLDPDSLAGKLDFKPHPfrawLEAELGRRFDYV-CVDSPEELRRHPR-----AITRAGQVKGngtrhekddrr 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2507 -INQDRFI-------------------QRAVEASNAYSSILQAVQAAEDAAGHALRQASRTWEMV----VQRGLAAGARQ 2562
Cdd:COG4913 597 rIRSRYVLgfdnraklaaleaelaeleEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvasAEREIAELEAE 676
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2563 L--LANSSALVETIlghQERLGLAHGRLQAAGTQLRDVRAKKNQLAAQIQEAQAML--AMDTSETSEKIAHAKAVAA--- 2635
Cdd:COG4913 677 LerLDASSDDLAAL---EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELdeLQDRLEAAEDLARLELRALlee 753
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 300798041 2636 --EARDTAAHVQSQLQGMQKNVERWQSQLGGLRgQDLSQAERD-------ASSSVSTLEKTLPQLLAKLSHLENRGVH 2704
Cdd:COG4913 754 rfAAALGDAVERELRENLEERIDALRARLNRAE-EELERAMRAfnrewpaETADLDADLESLPEYLALLDRLEEDGLP 830
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1864-1899 |
1.16e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 44.99 E-value: 1.16e-05
10 20 30
....*....|....*....|....*....|....*....
gi 300798041 1864 CQCHG---HSDRCLPGSGTCVgCQHNTEGDQCERCRPGF 1899
Cdd:smart00180 1 CDCDPggsASGTCDPDTGQCE-CKPNVTGRRCDRCAPGY 38
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2261-2616 |
1.63e-05 |
|
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: 51.21 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2261 QAGRLLDNTESTLVRAQKLLEivqAVSRALNELASQGfpgnattpsgEQ------LRWALAEVERLLWDMRTRDLGAPQA 2334
Cdd:TIGR02168 176 ETERKLERTRENLDRLEDILN---ELERQLKSLERQA----------EKaerykeLKAELRELELALLVLRLEELREELE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2335 VAEAELAEAQRLMARVQEQLtsfwEENQALATHIRDQLAQYESGLMDLREALNhavNTTREADELNSRNE---ERLREAL 2411
Cdd:TIGR02168 243 ELQEELKEAEEELEELTAEL----QELEEKLEELRLEVSELEEEIEELQKELY---ALANEISRLEQQKQilrERLANLE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2412 QWKQELSQDNATLKATLQAASLTLAHVSELLQGIDKAKEDLEHLAASLDGAWTPLLKRMQAfspasSKVDLVEAAEAHAQ 2491
Cdd:TIGR02168 316 RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEE-----LEEQLETLRSKVAQ 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2492 KLNQLAINLSGIIQgiNQDRFIQRAVEASNAYSSILQAVQAAEDAAGHALRQASrtwemvvqrglaAGARQLLANSSALV 2571
Cdd:TIGR02168 391 LELQIASLNNEIER--LEARLERLEDRRERLQQEIEELLKKLEEAELKELQAEL------------EELEEELEELQEEL 456
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 300798041 2572 ETilgHQERLGLAHGRLQAAGTQLRDVRAKKNQLAAQIQEAQAML 2616
Cdd:TIGR02168 457 ER---LEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQ 498
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2173-2532 |
1.73e-05 |
|
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: 51.21 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2173 VLLLDDLERAGALLPSIREQLR------------GI---NASSTAWARLHRlNASIADLQSKLrsplgphNQTAEQLQTL 2237
Cdd:TIGR02168 625 VLVVDDLDNALELAKKLRPGYRivtldgdlvrpgGVitgGSAKTNSSILER-RREIEELEEKI-------EELEEKIAEL 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2238 EQQSISLQQDTERLGSQATGVQ---DQAGRLLDNTESTLVRA----QKLLEIVQAVSRALNELASQGfpgNATTPSGEQL 2310
Cdd:TIGR02168 697 EKALAELRKELEELEEELEQLRkelEELSRQISALRKDLARLeaevEQLEERIAQLSKELTELEAEI---EELEERLEEA 773
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2311 RWALAEVERllwdmrtrdlgapqavaeaElaeaqrlmarvqeqltsfWEENQALATHIRDQLAQYESGLMDLREALNhav 2390
Cdd:TIGR02168 774 EEELAEAEA-------------------E------------------IEELEAQIEQLKEELKALREALDELRAELT--- 813
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2391 NTTREADELNSRNEERLREALQWKQELSQDNATLK-ATLQAASLTLAhVSELLQGIDKAKEDLEHLAASLDGAWTPLLKR 2469
Cdd:TIGR02168 814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEeLSEDIESLAAE-IEELEELIEELESELEALLNERASLEEALALL 892
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 300798041 2470 MQAFSPASSKV--------DLVEAAEAHAQKLNQLAINLSGIIQGInqDRFIQRaveASNAYSSILQAVQA 2532
Cdd:TIGR02168 893 RSELEELSEELreleskrsELRRELEELREKLAQLELRLEGLEVRI--DNLQER---LSEEYSLTLEEAEA 958
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
2344-2729 |
2.19e-05 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 50.29 E-value: 2.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2344 QRLMARVQEQLTS---FweenqaLATHIRDQLAQYESGLMDLREALnhavnttreadelnsrneERLRealqwkqELSQD 2420
Cdd:COG5278 53 EELLSALLDAETGqrgY------LLTGDESFLEPYEEARAEIDELL------------------AELR-------SLTAD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2421 NATLKATLQA-ASLTLAHVSELLQGIDKAK----EDLEHLAASLDGAwtpllKRMQAFspASSKVDLVEAAEAHAQKLNQ 2495
Cdd:COG5278 102 NPEQQARLDElEALIDQWLAELEQVIALRRagglEAALALVRSGEGK-----ALMDEI--RARLLLLALALAALLLAAAA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2496 LAINLSGIIQGINQDRFIQRAVEASNAYSSILQAVQAAEDAAGHALRQASRTWEMVVQRGLAAGARQLLANSSALVETIL 2575
Cdd:COG5278 175 LLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2576 GHQERLGLAHGRLQAAGTQLRDVRAKKNQLAAQIQEAQAMLAMDTSETSEKIAHAKAVAAEARDTAAHVQSQLQGMQKNV 2655
Cdd:COG5278 255 AALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALA 334
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300798041 2656 ERWQSQLGGLRGQDLSQAERDASSSVSTLEKTLPQLLAKLSHLENRGVHNASLALSANIGRVRKLIAQARSAAN 2729
Cdd:COG5278 335 TALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAA 408
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2976-3102 |
2.34e-05 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 46.54 E-value: 2.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2976 NGIIFFLKQENQ--FLCLAVQDGTLVLLYDFGSGLKRadpLQPPQALtAASKAIQVFLLAgARKRVLVRV---ERATVFS 3050
Cdd:pfam00054 7 SGLLLYNGTQTErdFLALELRDGRLEVSYDLGSGAAV---VRSGDKL-NDGKWHSVELER-NGRSGTLSVdgeARPTGES 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 300798041 3051 V-DQDNELEMADAYYLGGVPPEELppsLRRLFPSGGSVRGCIKGIKALGKYVD 3102
Cdd:pfam00054 82 PlGATTDLDVDGPLYVGGLPSLGV---KKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| TNFRSF16 |
cd13416 |
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 ... |
1844-1914 |
2.50e-05 |
|
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 neurotrophin receptor (p75NTR) or CD271; TNFRSF16 (also known as nerve growth factor receptor (NGFR) or p75 neurotrophin receptor (p75NTR or p75(NTR)), CD271, Gp80-LNGFR) is a common receptor for both neurotrophins and proneurotrophins, and plays a diverse role in many tissues, including the nervous system. It has been shown to be expressed in various types of stem cells and has been used to prospectively isolate stem cells with different degrees of potency. p75NTR owes its signaling to the recruitment of intracellular binding proteins, leading to the activation of different signaling pathways. It binds nerve growth factor (NGF) and the complex can initiate a signaling cascade which has been associated with both neuronal apoptosis and neuronal survival of discrete populations of neurons, depending on the presence or absence of intracellular signaling molecules downstream of p75NTR (e.g. NF-kB, JNK, or p75NTR intracellular death domain). p75NTR can also bind NGF in concert with the neurotrophic tyrosine kinase receptor type 1 (TrkA) protein where it is thought to modulate the formation of the high-affinity neurotrophin binding complex. On melanoma cell, p75NTR is an immunosuppressive factor, induced by interferon (IFN)-gamma, and mediates down-regulation of melanoma antigens. It can interact with the aggregated form of amyloid beta (Abeta) peptides, and plays an important role in etiopathogenesis of Alzheimer's disease by influencing protein tau hyper-phosphorylation. p75(NTR) is involved in the formation and progression of retina diseases; its expression is induced in retinal pigment epithelium (RPE) cells and its knockdown rescues RPE cell proliferation activity and inhibits RPE apoptosis induced by hypoxia. It can therefore be a potential therapeutic target for RPE hypoxia or oxidative stress diseases.
Pssm-ID: 276921 [Multi-domain] Cd Length: 159 Bit Score: 47.30 E-value: 2.50e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 300798041 1844 ECAPGYYRDTKGlflGRCVPCQchghsdRCLPGSGTCVGCQHNTEgDQCERCRPGFVSSDPSDpASPCVSC 1914
Cdd:cd13416 79 ECAYGYYLDEDS---GTCEPCT------VCPPGQGVVQSCGPNQD-TVCEACPEGTYSDEDSS-TDPCLPC 138
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
2397-2617 |
3.53e-05 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 48.07 E-value: 3.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2397 DELNSRNE---------ERLREALQW---KQELSQDNATLKATLQAASltlahvsellQGIDKAKEDLEHLAASLDGAWT 2464
Cdd:pfam12795 3 DELEKAKLdeaakkkllQDLQQALSLldkIDASKQRAAAYQKALDDAP----------AELRELRQELAALQAKAEAAPK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2465 PLLKRM------QAFSPASSkvDLVEAAEAhAQKLNQLAINLSGIIQGINQDrfIQRAVEASNAYSSILQAVQAAEDAAG 2538
Cdd:pfam12795 73 EILASLsleeleQRLLQTSA--QLQELQNQ-LAQLNSQLIELQTRPERAQQQ--LSEARQRLQQIRNRLNGPAPPGEPLS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2539 HALRQASRTwEMVVQRGLAAGARQLLANSSALVETILGHQERLGLAHGRLQAAGTQLRD-VRAKKNQLAAQIQEAQAMLA 2617
Cdd:pfam12795 148 EAQRWALQA-ELAALKAQIDMLEQELLSNNNRQDLLKARRDLLTLRIQRLEQQLQALQElLNEKRLQEAEQAVAQTEQLA 226
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2782-2906 |
4.25e-05 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 45.77 E-value: 4.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2782 VLYMGSrQATGDYMGVSLRNQKVHWVYRLGeAGPTTLSIDENIGE-QFAAVSIDRTLQfgHMSVTVEKHMVHEIkgdTVA 2860
Cdd:pfam00054 10 LLYNGT-QTERDFLALELRDGRLEVSYDLG-SGAAVVRSGDKLNDgKWHSVELERNGR--SGTLSVDGEARPTG---ESP 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 300798041 2861 PGREGLLNLNPDdfvFYVGGYPSNFTPPEPLRF-PGYLGCIEMDTLN 2906
Cdd:pfam00054 83 LGATTDLDVDGP---LYVGGLPSLGVKKRRLAIsPSFDGCIRDVIVN 126
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2205-2702 |
5.38e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 49.45 E-value: 5.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2205 RLHRLNASIADLQSKLRSPlgpHNQTAEQLQTLEQQSISLQQDTERLGSQATGVQDQAGRLLDNTESTLVRAQKLLEIVQ 2284
Cdd:pfam12128 277 RQEERQETSAELNQLLRTL---DDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQ 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2285 AVSRALNElASQGFPGNATTPSGEQLRWALAEVERLLWDM-RTRDLGAPQAVAEAElaeaQRLMAR-VQEQLTSFW-EEN 2361
Cdd:pfam12128 354 SELENLEE-RLKALTGKHQDVTAKYNRRRSKIKEQNNRDIaGIKDKLAKIREARDR----QLAVAEdDLQALESELrEQL 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2362 QALATHIRDQLAQYESGLMDLREALNHAVNTTREADELNSRNE--ERLREALQW---KQELSQDN-ATLKATLQAASLTL 2435
Cdd:pfam12128 429 EAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDEriERAREEQEAanaEVERLQSElRQARKRRDQASEAL 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2436 ----AHVSELLQGIDKAKEDLEHLAASL-------DGAWTPLLKRMqaFSPA---SSKVDLVEAAEAHAQKLNQLAINLS 2501
Cdd:pfam12128 509 rqasRRLEERQSALDELELQLFPQAGTLlhflrkeAPDWEQSIGKV--ISPEllhRTDLDPEVWDGSVGGELNLYGVKLD 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2502 GIIQGINQDRFIQRAVEAS-NAYSSILQAVQAAEDAAGHALRQASRTWEMVvQRGLAAgARQLLANSSALVETILGHQER 2580
Cdd:pfam12128 587 LKRIDVPEWAASEEELRERlDKAEEALQSAREKQAAAEEQLVQANGELEKA-SREETF-ARTALKNARLDLRRLFDEKQS 664
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2581 LGLA-----HGRLQAAGTQLRDVRAKKNQLAAQIQEAQAMLAMDTSETSEKIAHAKAVAAEARDTA-AHVQSQLQGMQKN 2654
Cdd:pfam12128 665 EKDKknkalAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQlALLKAAIAARRSG 744
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 300798041 2655 VERWQSQLGGLRGQDLSQAERDaSSSVSTLEKTLPQLLAKLSHLENRG 2702
Cdd:pfam12128 745 AKAELKALETWYKRDLASLGVD-PDVIAKLKREIRTLERKIERIAVRR 791
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
362-425 |
5.68e-05 |
|
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: 43.11 E-value: 5.68e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300798041 362 SCNCHGHA---YDCYydpevdrrnasqnldnvyQGGGVCLdCQHHTTGINCERCVPGFYRAPDQPLD 425
Cdd:cd00055 1 PCDCNGHGslsGQCD------------------PGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2204-2482 |
7.88e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.22 E-value: 7.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2204 ARLHRLNASIADLQSKLRSPLGPHNQTAEQLQTLEQQSISLQqdterlgsqatgvqdqagRLLDNTESTLVRAQKLLEIV 2283
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALA------------------RRIRALEQELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2284 QAVSRALNElasqgfpgnattpSGEQLRWALAEVERLLWDMRTRD----LGAPQAVAEaelaeaqrlMARVQEQLTSFWE 2359
Cdd:COG4942 89 EKEIAELRA-------------ELEAQKEELAELLRALYRLGRQPplalLLSPEDFLD---------AVRRLQYLKYLAP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2360 ENQALATHIRDQLAQyesgLMDLREALnhavntTREADELnsrnEERLREALQWKQELSQDNATLKATLQAASLTLAHVS 2439
Cdd:COG4942 147 ARREQAEELRADLAE----LAALRAEL------EAERAEL----EALLAELEEERAALEALKAERQKLLARLEKELAELA 212
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 300798041 2440 ELLQGIDKAKEDLEHLAASLDGAWTPLLKRMQAFSPASSKVDL 2482
Cdd:COG4942 213 AELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKL 255
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
833-871 |
9.33e-05 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 42.34 E-value: 9.33e-05
10 20 30
....*....|....*....|....*....|....*....
gi 300798041 833 CRCDVGGALGQGCEPKTGACRCRPNTQGPSCSEPAKDHY 871
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYY 39
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2440-2724 |
9.96e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 9.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2440 ELLQGIDKAKEDLEHLaaslDGAWTPLLKrmqafspASSKVDLVEAAEAHAQKLNQLAINLSGIIQGIN--QDRFIQRAV 2517
Cdd:COG4913 222 DTFEAADALVEHFDDL----ERAHEALED-------AREQIELLEPIRELAERYAAARERLAELEYLRAalRLWFAQRRL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2518 EAsnayssiLQAVQAAEDAAghalrqasrtwemvvQRGLAAGARQLLANSSALVETILG-HQERLGLAHGRLQAAGTQLR 2596
Cdd:COG4913 291 EL-------LEAELEELRAE---------------LARLEAELERLEARLDALREELDElEAQIRGNGGDRLEQLEREIE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2597 DVRAKKNQL---AAQIQEAQAMLAMDTSETSEkiahakavaaeardtaahvqsQLQGMQKNVERWQSQLGGLRGQdLSQA 2673
Cdd:COG4913 349 RLERELEERerrRARLEALLAALGLPLPASAE---------------------EFAALRAEAAALLEALEEELEA-LEEA 406
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 300798041 2674 ERDASSSVSTLEKTLPQLLAKLSHLENRGVhnaslALSANIGRVRKLIAQA 2724
Cdd:COG4913 407 LAEAEAALRDLRRELRELEAEIASLERRKS-----NIPARLLALRDALAEA 452
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2177-2432 |
1.17e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.52 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2177 DDLERAGALLPSIREQLRGINAS-STAWARLHRLNASIADLQSKLrsplgphNQTAEQLQTLEQQsisLQQDTERLGSQA 2255
Cdd:COG3883 23 KELSELQAELEAAQAELDALQAElEELNEEYNELQAELEALQAEI-------DKLQAEIAEAEAE---IEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2256 TGVQDQAGR---------------LLDNTE--STLVRAQKllEIVQAVSRALNELASQGfpgnattpsgEQLRWALAEVE 2318
Cdd:COG3883 93 RALYRSGGSvsyldvllgsesfsdFLDRLSalSKIADADA--DLLEELKADKAELEAKK----------AELEAKLAELE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2319 RLlwdmrtrdlgapqavaeaelaeaQRLMARVQEQLTSFWEENQALATHIRDQLAQYESGLMDLREALNHAVNTTREADE 2398
Cdd:COG3883 161 AL-----------------------KAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
250 260 270
....*....|....*....|....*....|....
gi 300798041 2399 LNSRNEERLREALQWKQELSQDNATLKATLQAAS 2432
Cdd:COG3883 218 AAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGA 251
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2371-2614 |
1.35e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.03 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2371 QLAQYESGLMDLREALNHAVNTTREADELNSRNEERLRE-------------------------ALQWKQELSQ-DNAtl 2424
Cdd:PRK04863 349 KIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAaeeevdelksqladyqqaldvqqtrAIQYQQAVQAlERA-- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2425 KATLQAASLTLAHVSELLQGIdKAKED-----LEHLAASLDGAWTPLLKRMQAFSPASSKVDLVEAAEAH---------- 2489
Cdd:PRK04863 427 KQLCGLPDLTADNAEDWLEEF-QAKEQeateeLLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRSEAWdvarellrrl 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2490 ------AQKLNQLAINLSGIIQGINQDRFIQRAVEASNAYSSilQAVQAAEDAAGHALRQASRtwemvvQRGLAAGARQL 2563
Cdd:PRK04863 506 reqrhlAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLG--KNLDDEDELEQLQEELEAR------LESLSESVSEA 577
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 300798041 2564 LANSSALVEtilgHQERLGLAHGRLQAAGTQLRDVRAKKNQLAAQIQEAQA 2614
Cdd:PRK04863 578 RERRMALRQ----QLEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFE 624
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
2118-2168 |
1.37e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 41.91 E-value: 1.37e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 300798041 2118 CQC-PRGH----CDPHTGRCTCPPGLSGERCDTCsqqhqvpvpgRPGSHGIHCEVC 2168
Cdd:smart00180 1 CDCdPGGSasgtCDPDTGQCECKPNVTGRRCDRC----------APGYYGDGPPGC 46
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2367-2733 |
1.64e-04 |
|
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: 47.74 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2367 HIRDQLAQYESGLMDLREALNHAvnttreadELNSRNEERLREalqWKQELSQdnatLKATLQAASLT--LAHVSELLQG 2444
Cdd:TIGR02168 183 RTRENLDRLEDILNELERQLKSL--------ERQAEKAERYKE---LKAELRE----LELALLVLRLEelREELEELQEE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2445 IDKAKEDLEHLAASLDGAWTPLLKRMQAFSPASSKVDlveaaeaHAQKLNQlaiNLSGIIQGINQD-RFIQRAVEASN-- 2521
Cdd:TIGR02168 248 LKEAEEELEELTAELQELEEKLEELRLEVSELEEEIE-------ELQKELY---ALANEISRLEQQkQILRERLANLErq 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2522 --AYSSILQAVQAAEDAAGHALrqASRTWEMVVQRGLAAGARQLLANSSALVETilghqerlglAHGRLQAAGTQLRDVR 2599
Cdd:TIGR02168 318 leELEAQLEELESKLDELAEEL--AELEEKLEELKEELESLEAELEELEAELEE----------LESRLEELEEQLETLR 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2600 AKKNQLAAQIQEAQAMLamdtsETSEkiahakavaaeardtaahvqSQLQGMQKNVERWQSQLGGLRGQDLSQAERDASS 2679
Cdd:TIGR02168 386 SKVAQLELQIASLNNEI-----ERLE--------------------ARLERLEDRRERLQQEIEELLKKLEEAELKELQA 440
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 300798041 2680 SVSTLEKTLPQLLAKLSHLENRgVHNASLALSANIGRVRKLIAQARSAANKVKV 2733
Cdd:TIGR02168 441 ELEELEEELEELQEELERLEEA-LEELREELEEAEQALDAAERELAQLQARLDS 493
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2176-2459 |
1.81e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2176 LDDLERAGALLPSIREQLRGINASSTAWARLHRLNASIADLQSKLRSpLgphNQTAEQLQTLEQQSISLQQDTERLGSQA 2255
Cdd:COG4913 633 LEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELER-L---DASSDDLAALEEQLEELEAELEELEEEL 708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2256 TGVQDQAGRLldntESTLVRAQKLLEIVQAVSRALNELASQGfpgnattpsgeqLRWALAE-VERLLWDMRTRDLGapqa 2334
Cdd:COG4913 709 DELKGEIGRL----EKELEQAEEELDELQDRLEAAEDLARLE------------LRALLEErFAAALGDAVERELR---- 768
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2335 vaeaelaeaQRLMARVQEQLTSFWEENQALATHIRDQLAQYESGLMDLR---EALNH--AVNTTREADELnSRNEERLRE 2409
Cdd:COG4913 769 ---------ENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDadlESLPEylALLDRLEEDGL-PEYEERFKE 838
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 300798041 2410 ALqwkQELSQDNatlKATLQaasltlahvSELLQGIDKAKEDLEHLAASL 2459
Cdd:COG4913 839 LL---NENSIEF---VADLL---------SKLRRAIREIKERIDPLNDSL 873
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
2174-2443 |
2.66e-04 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 45.37 E-value: 2.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2174 LLLDDLERAGALLPSIREQlrginasstawarlhrlNASIADLQsklrsplgphnqtaEQLQTLEQQSISLQQDTERLGS 2253
Cdd:pfam12795 17 KLLQDLQQALSLLDKIDAS-----------------KQRAAAYQ--------------KALDDAPAELRELRQELAALQA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2254 QAtgvqdqagrllDNTESTLVRAQKLLEIVQAVSRALNELAsqgfpgnattpsgeQLRWALAEVERLLWDMRTRdlgapq 2333
Cdd:pfam12795 66 KA-----------EAAPKEILASLSLEELEQRLLQTSAQLQ--------------ELQNQLAQLNSQLIELQTR------ 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2334 avaeaelaeaqrlMARVQEQLTsfweENQALATHIRDQLAQYESGLMDLREALNHAVNTTREAdeLNSRNEERLREAL-- 2411
Cdd:pfam12795 115 -------------PERAQQQLS----EARQRLQQIRNRLNGPAPPGEPLSEAQRWALQAELAA--LKAQIDMLEQELLsn 175
|
250 260 270
....*....|....*....|....*....|...
gi 300798041 2412 QWKQELSQdnatLKATLQAASLT-LAHVSELLQ 2443
Cdd:pfam12795 176 NNRQDLLK----ARRDLLTLRIQrLEQQLQALQ 204
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
2351-2612 |
2.90e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 47.10 E-value: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2351 QEQ-LTSFWEENQAlATHIRDQLAQYESGLMDLREALNHAVNTTREADELNSRNEERLREALQWKQELSQDNATLKATLQ 2429
Cdd:PRK10246 573 EEQaLTQQWQAVCA-SLNITLQPQDDIQPWLDAQEEHERQLRLLSQRHELQGQIAAHNQQIIQYQQQIEQRQQQLLTALA 651
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2430 AASLTL----AHVSELLQGIDKAK------EDLEHLAASLDgAWTPLLKRMQAFSPASSKVDLVEA---AEAHAQKLNqL 2496
Cdd:PRK10246 652 GYALTLpqedEEASWLATRQQEAQswqqrqNELTALQNRIQ-QLTPLLETLPQSDDLPHSEETVALdnwRQVHEQCLS-L 729
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2497 AINLSGIIQGINQDRfiQRAVEASNAYSSILQAV----QAA------EDAAGHALRQASRTWEMVVQRG--LAAGARQLL 2564
Cdd:PRK10246 730 HSQLQTLQQQDVLEA--QRLQKAQAQFDTALQASvfddQQAflaallDEETLTQLEQLKQNLENQRQQAqtLVTQTAQAL 807
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 300798041 2565 A----------NSSALVETIlghQERLGLAHGRLQAAGT-------QLR---DVRAKKNQLAAQIQEA 2612
Cdd:PRK10246 808 AqhqqhrpdglDLTVTVEQI---QQELAQLAQQLRENTTrqgeirqQLKqdaDNRQQQQALMQQIAQA 872
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
2118-2146 |
3.59e-04 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 40.80 E-value: 3.59e-04
10 20 30
....*....|....*....|....*....|....
gi 300798041 2118 CQCP-----RGHCDPHTGRCTCPPGLSGERCDTC 2146
Cdd:pfam00053 1 CDCNphgslSDTCDPETGQCLCKPGVTGRHCDRC 34
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
2207-2693 |
3.75e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 46.71 E-value: 3.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2207 HRLNASIADLQSKLRSPLGPHNQTAEQLQTLEQQSISLQQDTERLGSQATGVQDQAGRLLDNTESTLVR----------A 2276
Cdd:pfam01576 183 NKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARleeetaqknnA 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2277 QKLLEIVQA-VSRALNELASQgfpgNATTPSGEQLRWALAE-VERL---LWDmrTRDLGAPQavaeaelaeaQRLMARVQ 2351
Cdd:pfam01576 263 LKKIRELEAqISELQEDLESE----RAARNKAEKQRRDLGEeLEALkteLED--TLDTTAAQ----------QELRSKRE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2352 EQLTSfweenqaLATHIRDQLAQYESGLMDLREALNHAVNTTREADELNSRNEERLREAlqwKQELSQDNATLKATLQaa 2431
Cdd:pfam01576 327 QEVTE-------LKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKA---KQALESENAELQAELR-- 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2432 sltlahvseLLQGidkAKEDLEHLAASLDGAwtplLKRMQAFSPASSKVDlVEAAEahaqKLNQLAINLSGIIQGINQ-- 2509
Cdd:pfam01576 395 ---------TLQQ---AKQDSEHKRKKLEGQ----LQELQARLSESERQR-AELAE----KLSKLQSELESVSSLLNEae 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2510 DRFIQRAVEASNAySSILQAVQaaedaaghALRQasrtwEMVVQR-GLAAGARQLLANSSALVETILGHQERLGLAHGRL 2588
Cdd:pfam01576 454 GKNIKLSKDVSSL-ESQLQDTQ--------ELLQ-----EETRQKlNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQL 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2589 QAAGTQLRDVRAKKNQLAAQIQEAQamlamdtsETSEKIahakavaaeARDTAAHVQ------SQLQGMQKNVERWQSQL 2662
Cdd:pfam01576 520 STLQAQLSDMKKKLEEDAGTLEALE--------EGKKRL---------QRELEALTQqleekaAAYDKLEKTKNRLQQEL 582
|
490 500 510
....*....|....*....|....*....|....
gi 300798041 2663 gglrgQDLSQAERDASSSVSTLEK---TLPQLLA 2693
Cdd:pfam01576 583 -----DDLLVDLDHQRQLVSNLEKkqkKFDQMLA 611
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
2243-2460 |
4.01e-04 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 44.18 E-value: 4.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2243 SLQQDTERLGSQATGVQDQAGRLLDNTESTLVRAQKLLeiVQAVSRALNELASQgfpgnaTTPSGEQLRWAL-AEVERLl 2321
Cdd:pfam01442 1 LLEDSLDELSTYAEELQEQLGPVAQELVDRLEKETEAL--RERLQKDLEEVRAK------LEPYLEELQAKLgQNVEEL- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2322 wdmRTRdLGApqavaeaelaEAQRLMARVQEQLtsfwEEnqalathIRDQLAQYesgLMDLREALNHAVNTTRE-----A 2396
Cdd:pfam01442 72 ---RQR-LEP----------YTEELRKRLNADA----EE-------LQEKLAPY---GEELRERLEQNVDALRArlapyA 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300798041 2397 DELNSRNEERLREalqWKQELSQDNATLKATLQaasltlAHVSELLQgidKAKEDLEHLAASLD 2460
Cdd:pfam01442 124 EELRQKLAERLEE---LKESLAPYAEEVQAQLS------QRLQELRE---KLEPQAEDLREKLD 175
|
|
| HemX |
COG2959 |
Proteobacterial HemX domain, involved in 2-ketogluconate production (unrelated to B. subtilis ... |
2232-2321 |
5.17e-04 |
|
Proteobacterial HemX domain, involved in 2-ketogluconate production (unrelated to B. subtilis HemX, COG0755, no evidence of involvement in heme biosynthesis) [General function prediction only];
Pssm-ID: 442199 [Multi-domain] Cd Length: 361 Bit Score: 45.34 E-value: 5.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2232 EQLQTLEQQSISLQQDTERLGSQATGVQDQAGRLLDNTESTLVRAQKLLEIVQAVSRALNELASQgfpgNATTPSGEQLR 2311
Cdd:COG2959 53 QQLQQQQAELAQLAQQLAALQQQAQELRALAQQLQELLQQLAARLAQLEQRLAELQQQLAALQQL----LQSLSGSSRDD 128
|
90
....*....|
gi 300798041 2312 WALAEVERLL 2321
Cdd:COG2959 129 WLLAEAEYLL 138
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2483-2732 |
5.17e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.16 E-value: 5.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2483 VEAAEahaQKLNQLAINLSGIIQGINQDRFIQRAVEASNAYSSILQAVQAAEDAAGHALRQASRTWEMVVQRGLAAGARQ 2562
Cdd:COG3206 191 LEEAE---AALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQ 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2563 LLANSSALVETILGHQERLGLAHGRLQAAGTQLRDVRAkknQLAAQIQEAQAMLAMDtsetsekiahakavaaeardtAA 2642
Cdd:COG3206 268 LRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRA---QLQQEAQRILASLEAE---------------------LE 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2643 HVQSQLQGMQKNVERWQSQLGGL--RGQDLSQAERDASSSVSTLEktlpQLLAKLShlenrgvhNASLALSANIGRVRkL 2720
Cdd:COG3206 324 ALQAREASLQAQLAQLEARLAELpeLEAELRRLEREVEVARELYE----SLLQRLE--------EARLAEALTVGNVR-V 390
|
250
....*....|..
gi 300798041 2721 IAQARSAANKVK 2732
Cdd:COG3206 391 IDPAVVPLKPVS 402
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
2117-2146 |
6.01e-04 |
|
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: 40.03 E-value: 6.01e-04
10 20 30
....*....|....*....|....*....|....*
gi 300798041 2117 RCQCP-----RGHCDPHTGRCTCPPGLSGERCDTC 2146
Cdd:cd00055 1 PCDCNghgslSGQCDPGTGQCECKPNTTGRRCDRC 35
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
2396-2616 |
6.85e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 45.67 E-value: 6.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2396 ADELNSRNEERLR-EALQWKQELSQDNATLKATLQAaslTLahvsELLQGIDKAKEDLEHLAASLDGAwTPLLKRMQAFS 2474
Cdd:PRK11281 32 NGDLPTEADVQAQlDALNKQKLLEAEDKLVQQDLEQ---TL----ALLDKIDRQKEETEQLKQQLAQA-PAKLRQAQAEL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2475 PASSKVDLVEAAEAHA--------QKLNQLAINLsgiiqginqdrfiQRAVEASNAYSSILQAVQAAEDAAGHALRQAS- 2545
Cdd:PRK11281 104 EALKDDNDEETRETLStlslrqleSRLAQTLDQL-------------QNAQNDLAEYNSQLVSLQTQPERAQAALYANSq 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2546 RTWEM--------VVQRGLAAGARQLLANSSALVETILGHQERLGLAHGRLQAAGTQLRD-VRAKKNQLAAQIQEAQAML 2616
Cdd:PRK11281 171 RLQQIrnllkggkVGGKALRPSQRVLLQAEQALLNAQNDLQRKSLEGNTQLQDLLQKQRDyLTARIQRLEHQLQLLQEAI 250
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2165-2456 |
7.02e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 45.73 E-value: 7.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2165 CEVCDHCVVLlldDLERAGALLPSI--REQLRGINasstawaRLHRLNASIADLQSKLRSPLgphnqtaEQLQTLEQQSI 2242
Cdd:TIGR00618 504 CPLCGSCIHP---NPARQDIDNPGPltRRMQRGEQ-------TYAQLETSEEDVYHQLTSER-------KQRASLKEQMQ 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2243 SLQQDTERLGSQATGVQDQagrlLDNTESTLVRAQKLLeivQAVSRALNELAsqgfpgnattpsgEQLRWALAEVERLLW 2322
Cdd:TIGR00618 567 EIQQSFSILTQCDNRSKED----IPNLQNITVRLQDLT---EKLSEAEDMLA-------------CEQHALLRKLQPEQD 626
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2323 DMRTRdlgapQAVAEAELAEAQRLMARVQEQLTSFWEENQALATHIRDQLAQY-ESGLMDLREALNHAVNTTREADELNS 2401
Cdd:TIGR00618 627 LQDVR-----LHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELlASRQLALQKMQSEKEQLTYWKEMLAQ 701
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 300798041 2402 RNeERLREALQ-----WK--QELSQDNATLKATLQAASLTLAHVSELLQgiDKAKEDLEHLA 2456
Cdd:TIGR00618 702 CQ-TLLRELEThieeyDRefNEIENASSSLGSDLAAREDALNQSLKELM--HQARTVLKART 760
|
|
| HBM |
pfam16591 |
Helical bimodular sensor domain; The HBM sensor domain has been identified primarily in ... |
2313-2507 |
8.99e-04 |
|
Helical bimodular sensor domain; The HBM sensor domain has been identified primarily in bacterial chemoreceptors but is also present on histidine kinases. characteriztic features of this domain are its size of approximately 250 amino acids and its location in the bacterial periplasm. The McpS chemoreceptor of Pseudomonas putida KT2440 was found to possess an HBM sensor domain and its 3D structure in complex with physiologically relevant ligands has been reported. This domain is composed of 2 long and 4 short helices that form two modules each composed of a 4-helix bundle. The McpS chemoreceptor mediates chemotaxis towards a number of organic acids. Both modules of the McpS HBM domain contain a ligand binding site. Chemo-attractants binds to each of these sites and their binding was shown to trigger a chemotactic response. This domain is primarily found in different proteobacteria but also in archaea. Interestingly, amino acids in both ligand binding sites showed a high degree of conservation suggesting that members of this family sense similar ligands. This domain recognizes Multiple TCA cycle intermediates, citrate and alpha-ketoglutarate (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 435446 [Multi-domain] Cd Length: 246 Bit Score: 43.93 E-value: 8.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2313 ALAEVERLLWDMRT-----RDLGAPQAVAEAELAEAQRLMARVQEQLTSFWE-ENQALATHIRDQLAQYESGLMDLREAL 2386
Cdd:pfam16591 10 DISQLNDTLTDLRIarlqyMLSNGDATAAQAVQKKLDELKQQLQQLKTTFTSpENVRLLQEQLQLIQAYRKSFNELRAAY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2387 NHAVNTTREADElnsrNEERLREAL-----QWKQELSQDNATLkATLQAASLTLAHVSE-------------------LL 2442
Cdd:pfam16591 90 ESRNASRQVMDS----AAERALEAIdqleaEVLQTPEADSRRA-AQYQAISELKRQVQMaryqvrgytftpnedseqaAY 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 300798041 2443 QGIDKAKEDLEHLAASLDGAWTPLLKRMQafSPASSKVDLVEAAEAHAQKLNQLAINLSGIIQGI 2507
Cdd:pfam16591 165 QQLDAALASLDQLRQALAGDPGAALQQLT--SALQGYRDALDTFKAAVAAIEQARQEMTSQGDEI 227
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2231-2535 |
9.21e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 9.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2231 AEQLQTLEQQSISLQQDterlgsqatgvqdqagrlLDNTESTLVRAQKLLEIVQAVSRALNELASQGFpgnattpsgEQL 2310
Cdd:COG4913 609 RAKLAALEAELAELEEE------------------LAEAEERLEALEAELDALQERREALQRLAEYSW---------DEI 661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2311 RWALAEVERllwdmrtrdlgapqavaeaelaeaqrlmARVQEQLTSFWEENQALAThIRDQLAQYESGLMDLREALnhav 2390
Cdd:COG4913 662 DVASAEREI----------------------------AELEAELERLDASSDDLAA-LEEQLEELEAELEELEEEL---- 708
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2391 nttREADELNSRNEERLREALQWKQEL------------SQDNATLKATLQAASLTlAHVSELLQGIDkakEDLEHLAAS 2458
Cdd:COG4913 709 ---DELKGEIGRLEKELEQAEEELDELqdrleaaedlarLELRALLEERFAAALGD-AVERELRENLE---ERIDALRAR 781
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2459 LDGAWTPLLKRMQAFSPA--SSKVDL---VEAAEAHAQKLNQLAINlsGIIQgiNQDRFIQRAVEASNA-----YSSILQ 2528
Cdd:COG4913 782 LNRAEEELERAMRAFNREwpAETADLdadLESLPEYLALLDRLEED--GLPE--YEERFKELLNENSIEfvadlLSKLRR 857
|
....*..
gi 300798041 2529 AVQAAED 2535
Cdd:COG4913 858 AIREIKE 864
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
304-349 |
9.82e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 39.60 E-value: 9.82e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 300798041 304 CVCH--GHAD-VCDakdpsdPFRLQCACQHNTCGGSCDRCCPGFNQQPW 349
Cdd:smart00180 1 CDCDpgGSASgTCD------PDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
2481-2621 |
9.82e-04 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 43.51 E-value: 9.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2481 DLVEAAEAHAQKLNQLAINLsgiiqginqdrfiQRA-VEASNAYSSILQAVQAAEDAAGHALRQASRtWEMVVQRGLAAG 2559
Cdd:pfam04012 15 EGLDKAEDPEKMLEQAIRDM-------------QSElVKARQALAQTIARQKQLERRLEQQTEQAKK-LEEKAQAALTKG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300798041 2560 ----ARQLLANSSALVETILGHQERLGLAH-------GRLQAAGTQLRDVRAKKNQLAAQIQEAQAMLAMDTS 2621
Cdd:pfam04012 81 neelAREALAEKKSLEKQAEALETQLAQQRsaveqlrKQLAALETKIQQLKAKKNLLKARLKAAKAQEAVQTS 153
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2186-2422 |
1.20e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.01 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2186 LPSIREQLRginASSTAWARLhRLNASIADLQSKLrsplgphNQTAEQLQTLEQQSISLQQDTERLGSQATGVQDQAGRL 2265
Cdd:COG3206 184 LPELRKELE---EAEAALEEF-RQKNGLVDLSEEA-------KLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2266 LDNTESTL--VRAQKLLEIVQAVSRALNELASQGFPGNattPSGEQLRWALAEVERLLwdmrtrdlgapqavaeaelaea 2343
Cdd:COG3206 253 PDALPELLqsPVIQQLRAQLAELEAELAELSARYTPNH---PDVIALRAQIAALRAQL---------------------- 307
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300798041 2344 QRLMARVQEQLTSFWEENQALATHIRDQLAQYESGLMDLREALNHAVNTTREADelnsRNEERLREALQWKQELSQDNA 2422
Cdd:COG3206 308 QQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVE----VARELYESLLQRLEEARLAEA 382
|
|
| HAMP |
COG2770 |
HAMP domain [Signal transduction mechanisms]; |
2345-2699 |
1.27e-03 |
|
HAMP domain [Signal transduction mechanisms];
Pssm-ID: 442051 [Multi-domain] Cd Length: 631 Bit Score: 44.72 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2345 RLMArvqeqltsfweenQALATHIRDQLAQYESGLMDLREALNHAVNTTREADELNSRNEERLREALQWKQELSQDNATL 2424
Cdd:COG2770 275 NRMA-------------DSLRESIEEAEEEEELAEAELARLLEALLELLLALLLLLLALLLLAAAALLLELLLLLLLALL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2425 KATLQAASLTLAHVSELLQGIDKAKEDLEHLAASLDGAWTPLLKRMQAFSPASSKVDLVEAAEAHAQKLNQLAINLSGII 2504
Cdd:COG2770 342 LLLLLAADLLLALALAALLLLLALELLLEAELLVLLALEALALEAELAAVLALLAALAAALLLLELALEELVLALLALAL 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2505 QGINQDRFIQRAVEASNAYSSILQAVQAAEDAAGHALRQASRTWEMVVQRGLAAGARQLLANSSALVETILGHQERLGLA 2584
Cdd:COG2770 422 LALAAAAAAAEAAAAALELAAAAIAAAAAAEAEGGLAELEAEELVAAAEALLLLAALLLLAALGALELLLLEEEEEAGAA 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2585 HGRLQAAGTQLRDVRAKKNQLAAQIQEAQAMLAMDTSETSEKIAHAKAVAAEARDTAAHVQSQLQGMQKNVERWQSQLGG 2664
Cdd:COG2770 502 AEELAEELLLLEGLLLLLLLEAEALEVAEELLELEEAALLLAAAAELAALLALLLALAAVEAAALLLAALLLAAVAALLE 581
|
330 340 350
....*....|....*....|....*....|....*
gi 300798041 2665 LRGQDLSQAERDASSSVSTLEKTLPQLLAKLSHLE 2699
Cdd:COG2770 582 LAALLLLLLAAAEALAALELELAAAAEAALAEAEL 616
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
391-420 |
1.50e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 38.83 E-value: 1.50e-03
10 20 30
....*....|....*....|....*....|
gi 300798041 391 YQGGGVCLdCQHHTTGINCERCVPGFYRAP 420
Cdd:smart00180 14 DPDTGQCE-CKPNVTGRRCDRCAPGYYGDG 42
|
|
| VSP |
pfam03302 |
Giardia variant-specific surface protein; |
1842-2147 |
2.12e-03 |
|
Giardia variant-specific surface protein;
Pssm-ID: 146106 [Multi-domain] Cd Length: 397 Bit Score: 43.80 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 1842 CQECAPGYYRDTKGLFLGRCVPCQchghsdrcLPGSGTCVgcqhNTEGDQCERCrpgfVSSDPSDPASPCVscPCPLAVP 1921
Cdd:pfam03302 1 CDECKPGYELSADKTKCTSSAPCK--------TENCKACS----NDKREVCEEC----NSNNYLTPTSQCI--DDCAKIG 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 1922 SNNFADgcilrNGRTQCLCRPGYAG--------ASCERCAPGFFGNplvlGSSCQPCDCSGNGDPNMIFSDC-------- 1985
Cdd:pfam03302 63 NYYYTT-----NANNKKICKECTVAncktcedqGQCQACNDGFYKS----GDACSPCHESCKTCSGGTASDCtecltgka 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 1986 -----DPLTGAC-RGCLRHTTGPRCESCAPGFYGNALlpgnctrcdCSPCGTETCDPQTGRC---------LCKAG-VTG 2049
Cdd:pfam03302 134 lrygnDGTKGTCgEGCTTGTGAGACKTCGLTIDGTSY---------CSECATETEYPQNGVCtstaarataTCKASsVAN 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2050 QRCDHCLEGHfgFEQCQGCHPCA-------CGPAAEGSECNPQTGQCH------------CRPGTTGPQCLECAPGYwgL 2110
Cdd:pfam03302 205 GMCSSCANGY--FRMNGGCYETTkfpgksvCEEANSGGTCQKEAPGYKlnngdlvtcspgCKTCTSNTVCTTCMDGY--V 280
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 300798041 2111 PEKG-CRRCQCPRGHCDPHTGRC-TCPPGL--SGERCDTCS 2147
Cdd:pfam03302 281 KTSDsCTKCDSSCETCTGATTTCkTCATGYykSGTGCVSCT 321
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
304-360 |
2.35e-03 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 38.49 E-value: 2.35e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 300798041 304 CVCHGHADVcdaKDPSDPFRLQCACQHNTCGGSCDRCCPGFNQQPwkpatTDSANEC 360
Cdd:pfam00053 1 CDCNPHGSL---SDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLP-----SDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
363-430 |
3.62e-03 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 38.10 E-value: 3.62e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 300798041 363 CNCHGHAydcyydpevdrrnasQNLDNVYQGGGVCLdCQHHTTGINCERCVPGFYRapdQPLDSPHVC 430
Cdd:pfam00053 1 CDCNPHG---------------SLSDTCDPETGQCL-CKPGVTGRHCDRCKPGYYG---LPSDPPQGC 49
|
|
| TNFRSF4 |
cd13406 |
Tumor necrosis factor receptor superfamily member 4 (TNFRSF4), also known as CD134 or OXO40; ... |
1984-2070 |
4.36e-03 |
|
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: 40.46 E-value: 4.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 1984 DCDPLTGACRGClRHTTGPRCESCAPGFYGNAL---LPGNCTRCDCSPCGTE--TCDPQTGR-CLCKAGVT-------GQ 2050
Cdd:cd13406 17 ECPPGEGMESRC-TGTQDTVCSPCEPGFYNEAVnyePCKPCTQCNQRSGSEEkqKCTKTSDTvCRCRPGTQpldsykpGV 95
|
90 100
....*....|....*....|
gi 300798041 2051 RCDHCLEGHFGFEQCQGCHP 2070
Cdd:cd13406 96 DCVPCPPGHFSRGDNQACKP 115
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
2596-2750 |
4.45e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 42.34 E-value: 4.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2596 RDVRAKKNQLAAQIQEAQAMLAMDTSETSEKiahakAVAAEARDTAAHVQSQLQGMQKNVERWQSqlggLRGQDL-SQAE 2674
Cdd:COG1566 79 TDLQAALAQAEAQLAAAEAQLARLEAELGAE-----AEIAAAEAQLAAAQAQLDLAQRELERYQA----LYKKGAvSQQE 149
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300798041 2675 RD-ASSSVSTLEKTLPQLLAKLSHLEnrgvhnASLALSANIGRVRKLIAQARSAANKVKVSMKFngrsgVRLRTPRD 2750
Cdd:COG1566 150 LDeARAALDAAQAQLEAAQAQLAQAQ------AGLREEEELAAAQAQVAQAEAALAQAELNLAR-----TTIRAPVD 215
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2372-2701 |
4.94e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.02 E-value: 4.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2372 LAQYESGLMDLREALNHAVNTTREADELNSRNEERLREAlqwkqELSQDnaTLK---ATLQAAsLTLAHVSEL-----LQ 2443
Cdd:COG3096 349 IERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAA-----EEEVD--SLKsqlADYQQA-LDVQQTRAIqyqqaVQ 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2444 GIDKAKEDLEHLAASLDGAwtpllkrmqafspasskVDLVEAAEAHAQKLNQLAINLSgiiqginqdrfiQRAVEASNAY 2523
Cdd:COG3096 421 ALEKARALCGLPDLTPENA-----------------EDYLAAFRAKEQQATEEVLELE------------QKLSVADAAR 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2524 SSILQAVQAAEDAAGHALRqaSRTWEMvvqrglaagARQLLANSSALVetilgHQErlglahGRLQAAGTQLRDVRakkn 2603
Cdd:COG3096 472 RQFEKAYELVCKIAGEVER--SQAWQT---------ARELLRRYRSQQ-----ALA------QRLQQLRAQLAELE---- 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2604 QLAAQIQEAQAMLAmdtsETSEKIahakavaaeardtAAHVQSQLQgmqknVERWQSQLGGLRgQDLSQAERDASSSVST 2683
Cdd:COG3096 526 QRLRQQQNAERLLE----EFCQRI-------------GQQLDAAEE-----LEELLAELEAQL-EELEEQAAEAVEQRSE 582
|
330
....*....|....*...
gi 300798041 2684 LEKTLPQLLAKLSHLENR 2701
Cdd:COG3096 583 LRQQLEQLRARIKELAAR 600
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
2179-2421 |
9.02e-03 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 40.75 E-value: 9.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2179 LERAGALLPSIREQLRGINASSTAWARLHRLNASIADLQSKLRSPLGPHNQTAEQLQTLEQQSISLQQDTERLgsqatgv 2258
Cdd:pfam12795 46 LDDAPAELRELRQELAALQAKAEAAPKEILASLSLEELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERA------- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2259 qdqagrlldntestlvrAQKLLEIVQAVSRALNELASQGFPGNATTPSgeqLRWALaEVERllwdmrtrdlgapqavaea 2338
Cdd:pfam12795 119 -----------------QQQLSEARQRLQQIRNRLNGPAPPGEPLSEA---QRWAL-QAEL------------------- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2339 elaeaQRLMARVQEQltsfweeNQALATH-IRDQLAQYESGLMDLR-EALNHAVNTTREAdeLNSRN----EERLREALQ 2412
Cdd:pfam12795 159 -----AALKAQIDML-------EQELLSNnNRQDLLKARRDLLTLRiQRLEQQLQALQEL--LNEKRlqeaEQAVAQTEQ 224
|
....*....
gi 300798041 2413 WKQELSQDN 2421
Cdd:pfam12795 225 LAEEAAGDH 233
|
|
| GAF |
COG2203 |
GAF domain [Signal transduction mechanisms]; |
2154-2617 |
9.28e-03 |
|
GAF domain [Signal transduction mechanisms];
Pssm-ID: 441805 [Multi-domain] Cd Length: 712 Bit Score: 42.10 E-value: 9.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2154 VPGRPGSHGIHCEVCDHCVVLLLDDLERAGALLPSIREQLRGINASSTAWARLH---RLNASIAdLQSKLrsplgPHNQT 2230
Cdd:COG2203 253 LGRLPLGEGLAGRALRTGEPVVVNDASTDPRFAPSLRELLLALGIRSLLCVPLLvdgRLIGVLA-LYSKE-----PRAFT 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2231 AEQLQTLEQqsislqqdterlgsqatgVQDQAGRLLDNTESTLVRAQKLLEIVQAVSRALNELASQgfpgnattpsgEQL 2310
Cdd:COG2203 327 EEDLELLEA------------------LADQAAIAIERARLYEALEAALAALLQELALLRLLLDLE-----------LTL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2311 RWALAEVERLLWDMRTRDLGAPQAVAEAELAEAQRLMARVQEQLTSFWEENQALATHIRDQLAQYESGLMDLREALNHAV 2390
Cdd:COG2203 378 LRLRQLLLELLLALLLLLSLLGAELLLLLLDAADLSGLLALEGLLLLDLLLLLLLLRRILLLRVLRRLLLGDEEGLVLLL 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2391 NTTREADELNSRNEERLREALQWKQELSQDNATLKATLQAASLTLAHVSELLQGIDKAKEDLEHLAASLDGAWTPLLKRM 2470
Cdd:COG2203 458 ALAELELLEILELLVLLAVILLALALLAALLLLLLLLLALLALSALAVLASLLLALLLLLLLLLLLLLLGLLAALAADLL 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798041 2471 QAFSPASSKVDLVEAAEAHAQKLNQLAINLSGIIQGInQDRFIQRAVEASNAYSSILQAVQAAEDAAGHALRQASRTWEM 2550
Cdd:COG2203 538 LLAAALLEDLLILLLVLLLERELLTLVGVLLLLGLSV-LLIELALALILALALLELLLVAVGDLLLLERDLLLLLVLLVR 616
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300798041 2551 VVQRGLAAGARQLLANSSALVETILGHQERLGLAHGRLQAAGTQLRDVRAKKNQLAAQIQEAQAMLA 2617
Cdd:COG2203 617 LLLELLVVTLELTVLVVLAAVEDSALLLRLALALASLVLLRALLATELDLILDSSLLLGLLLLGALL 683
|
|
| |
