|
Name |
Accession |
Description |
Interval |
E-value |
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
4-237 |
2.11e-87 |
|
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: 285.79 E-value: 2.11e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 4 IKANATCGLNGPEMSCKLVEHVpgqpVRNPQCTICDqeSTNEYERHPIEYAIDGTN----RWWQSPSIMNGMvnHYVTIT 79
Cdd:smart00136 20 VTATSTCGEPGPERYCKLVGHT----EQGKKCDYCD--ARNPRRSHPAENLTDGNNpnnpTWWQSEPLSNGP--QNVNLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 80 LDLKQVFQVAYMIIKAAnSPRPGNWILERSIDGTTFEPWQYYAitdTECLTRFNISPRRGPPSYTrDDEVICTSFYSKIQ 159
Cdd:smart00136 92 LDLGKEFHVTYVILKFC-SPRPSLWILERSDFGKTWQPWQYFS---SDCRRTFGRPPRGPITKGN-EDEVICTSEYSDIV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 160 PLENGEIHASLINGRPSAEDP--SPTLLNFTSARYIRLVFQRIRTLNADLMtltlrdprDVDPIVTRRYYYSIKDISVGG 237
Cdd:smart00136 167 PLEGGEIAFSLLEGRPSATDFdnSPVLQEWVTATNIRVRLTRLRTLGDELM--------DDRPEVTRRYYYAISDIAVGG 238
|
|
| Laminin_I super family |
cl26988 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1638-1890 |
9.29e-55 |
|
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: 193.01 E-value: 9.29e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1638 LTTPLPPPYKVLYRFENMTDELKHMLSPQKAPERLLQLADSNLGSLVVEMDQLHSRATKVSADGEQVVDDSDRIHRRAED 1717
Cdd:pfam06008 7 LTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1718 LEKFIKDTLLGAKDLQLKAAELNKTLsrkDGTPDKSLSQMNEEIQAMLEEMRKRQLGRMKITADEEKDLAEELLQKVKRL 1797
Cdd:pfam06008 87 LAEAIKNLIDNIKEINEKVATLGEND---FALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQDLLSRIQTW 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1798 FGDPHQATEDLKAEITKKLSDHDEKLQEAQDLLNEAQLKTRQAGLVANQNLANLTSLERKRAAVSEIKEDVQKVFGESEH 1877
Cdd:pfam06008 164 FQSPQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEETLKTARD 243
|
250
....*....|...
gi 1343941588 1878 LLEEANGLSNSIN 1890
Cdd:pfam06008 244 SLDAANLLLQEID 256
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
1274-1412 |
1.50e-42 |
|
Laminin B (Domain IV);
:
Pssm-ID: 459652 Cd Length: 136 Bit Score: 153.19 E-value: 1.50e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1274 YWLLPEQFTGSMITAYGGQLKYAVYYEARDETGPSSYEPQVIVKGGPNHNMLMFRHITGIQIGQLTRHEIDMTEHEWEFA 1353
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGGGSLNSEPDVILEGNGLRLSYSSPDQPPPDPGQEQTYSVRLHEENWRDS 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1343941588 1354 DGRPMTREDFMDILFHVDYILIKASHGNLMRHSRVSEISLTVAEEGPRsedGEKAHQIE 1412
Cdd:pfam00052 81 DGAPVSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSAVPGGS---GPPASWVE 136
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
532-672 |
3.26e-40 |
|
Laminin B (Domain IV);
:
Pssm-ID: 459652 Cd Length: 136 Bit Score: 146.26 E-value: 3.26e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 532 YWNAPGLYLGNKLTAYGGIVTFTVSYTTDQQVQNAirvTSEPDLIIQGGGMKIIDKRFGQP-VYPSSPSTSHILLLPENF 610
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGGGSL---NSEPDVILEGNGLRLSYSSPDQPpPDPGQEQTYSVRLHEENW 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1343941588 611 lVSETGRPINRRDFLMVLANVTSVMVRASYSTETTAVyRLHSFSMQVASPSGRSERtASAVE 672
Cdd:pfam00052 78 -RDSDGAPVSREDFMMVLANLTAILIRATYSTGSGQV-SLSNVSLDSAVPGGSGPP-ASWVE 136
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2864-2992 |
1.07e-34 |
|
Laminin G domain;
:
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 130.51 E-value: 1.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2864 RTKEQSGLVLYMARINHADFVSIQIKDGQVCLGYDLGRGNISGCVPFSINDGSWHKIRVSRNKQRGVLTVDGLYSKQMTS 2943
Cdd:pfam00054 2 RTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGES 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2944 PNKAD-LLDVVGTLYVGGLPQNYITRRIGPILYSLNGCIRNLKMVGSPVG 2992
Cdd:pfam00054 82 PLGATtDLDVDGPLYVGGLPSLGVKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
3026-3177 |
1.55e-34 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
:
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 130.62 E-value: 1.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 3026 GSYFDGTGYLKAVASYRVGLDVSIALEFRTTRTNGVLLTVSNQD-KDGLGLEIVQGKLLFHVDNGAGRITAEHapdGAGF 3104
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNgGDFLALELEDGRLVLRYDLGSGSLVLSS---KTPL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1343941588 3105 CDGLWHAVTATKLRHKLELEVDGRKSRAESPNARSSTCDTNDPIYVGGYPDGVHQAGLSTKRSFKGCLKNLKI 3177
Cdd:cd00110 78 NDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKV 150
|
|
| Laminin_II super family |
cl05515 |
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 ... |
2091-2210 |
9.09e-34 |
|
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: 127.99 E-value: 9.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2091 VLERLGELNLRLGGLQLNYSQLDDTVSAANQMIQDPEKNIHAAGAKVKELEDEADRLLEKLQPIKMMQDN---LRRNISQ 2167
Cdd:pfam06009 15 VLEQLAPLSQNLENTSEKLSGINRSLEETNELVNDANKALDDAGRSVKKLEELAPDLLDKLKPLKQLEVNsssLSDNISR 94
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1343941588 2168 IKELINQARKQANSIKVSVSSGGDCLRSYRPDIRKGRYNTIIL 2210
Cdd:pfam06009 95 IKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTS 137
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2378-2540 |
1.20e-29 |
|
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: 116.75 E-value: 1.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2378 TVQLDGEGYASVgRPTRWNPNVSTITFKFRTFSSDALLMYMATEDMKDFMSLELSAGKVTVNFDLGSGVGKaVSAKRQ-N 2456
Cdd:cd00110 1 GVSFSGSSYVRL-PTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLV-LSSKTPlN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2457 DGRWKSLTVSRNKKQAIVTiVDidsgiaeDKIVATSQGSATGLNLRENQKIYFGGLPTignySMAARSEVTLKRYAGCLR 2536
Cdd:cd00110 79 DGQWHSVSVERNGRSVTLS-VD-------GERVVESGSPGGSALLNLDGPLYLGGLPE----DLKSPGLPVSPGFVGCIR 146
|
....
gi 1343941588 2537 DIEV 2540
Cdd:cd00110 147 DLKV 150
|
|
| LamG |
smart00282 |
Laminin G domain; |
2207-2349 |
1.92e-29 |
|
Laminin G domain;
:
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 115.51 E-value: 1.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2207 TIILHVKTTTPDNLLFYLGSAKYVDFLALEMRKGKVNFLWDVGSGVGRLEYPSHTIHDGNWHRIEASRNGLNGTISVYPL 2286
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLNDGQWHRVAVERNGRSVTLSVDGG 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1343941588 2287 EgpmagmmptPASANSPAAFTILDVDQNayLFVGGIFNTAKKAEAVKTSTFTGCMGETFLDGK 2349
Cdd:smart00282 81 N---------RVSGESPGGLTILNLDGP--LYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2567-2735 |
1.90e-23 |
|
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: 99.03 E-value: 1.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2567 TVSFSKPGYMELGGLSL-AVDTEISLSFSTLQDNGtILLAVGGstsrqqarnpkrrrrQSGEPYLSVMLNSGSLeVLMFT 2645
Cdd:cd00110 1 GVSFSGSSYVRLPTLPApRTRLSISFSFRTTSPNG-LLLYAGS---------------QNGGDFLALELEDGRL-VLRYD 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2646 RSHSPHRITrrpDQGILNDGREHSLRIERLpGRSFAVQVDEEAKLEAALPNDQPISL--QRLFLGGIPAEVEQTSNKANV 2723
Cdd:cd00110 64 LGSGSLVLS---SKTPLNDGQWHSVSVERN-GRSVTLSVDGERVVESGSPGGSALLNldGPLYLGGLPEDLKSPGLPVSP 139
|
170
....*....|..
gi 1343941588 2724 PFQGCIWNLMVN 2735
Cdd:cd00110 140 GFVGCIRDLKVN 151
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
867-913 |
1.61e-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: 64.30 E-value: 1.61e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1343941588 867 PCQCHINGSLSEVCNKESGQCPCKEDVLGRQCDKCKPSYWWDAEHPG 913
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGG 47
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1055-1098 |
1.94e-11 |
|
Laminin-type epidermal growth factor-like domai;
:
Pssm-ID: 214543 Cd Length: 46 Bit Score: 61.17 E-value: 1.94e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1343941588 1055 CQCS---HVGNNCDANTGQCICPPNTIGERCDRCAPNHWGhDITTGC 1098
Cdd:smart00180 1 CDCDpggSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYG-DGPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1008-1052 |
4.24e-11 |
|
Laminin-type epidermal growth factor-like domai;
:
Pssm-ID: 214543 Cd Length: 46 Bit Score: 60.02 E-value: 4.24e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1343941588 1008 CHCNSFGSKSFDCD-DLGQCRCQPGVSGPKCDRCSRGFFNFQEGGC 1052
Cdd:smart00180 1 CDCDPGGSASGTCDpDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
814-866 |
9.45e-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: 59.29 E-value: 9.45e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1343941588 814 PCNCNYNLdlSVPGSCDPITGQCLkCRQGYGGAACESCADGYYGDAILAKNCQ 866
Cdd:cd00055 1 PCDCNGHG--SLSGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
366-423 |
1.23e-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: 1.23e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1343941588 366 CSCDPHGSVSQSCVADSGQatpsqpagsCWCKEGYGGPQCDRCAVGYKGFPSCERCNC 423
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQ---------CLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1460-1506 |
1.39e-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: 1.39e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1460 CQCSGHSS---TCDPETSICQnCQDNTEGDRCERCMPGFYGVVRGSSDDC 1506
Cdd:pfam00053 1 CDCNPHGSlsdTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1101-1149 |
5.97e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
:
Pssm-ID: 395007 Cd Length: 49 Bit Score: 56.98 E-value: 5.97e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1343941588 1101 CGCNVVGSLSQQCNMNTGCCSCRESFRGEKCDECQIGYRDFPQCIRCEC 1149
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1147-1204 |
6.92e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
:
Pssm-ID: 395007 Cd Length: 49 Bit Score: 56.59 E-value: 6.92e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1343941588 1147 CECSFAGSDSQSCDMErrvcacadqTGKCSCKVNVEGSNCDRCKPDTFGLSARNPLGC 1204
Cdd:pfam00053 1 CDCNPHGSLSDTCDPE---------TGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
706-755 |
9.89e-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: 56.21 E-value: 9.89e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1343941588 706 PCRCHGHAT---QCHEITGHCLdCYHNTAGQYCDTCLPGYYGNATRGSpaDCQ 755
Cdd:cd00055 1 PCDCNGHGSlsgQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGG--GCQ 50
|
|
| SMC_prok_B super family |
cl37069 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1809-2177 |
7.53e-08 |
|
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]
The actual alignment was detected with superfamily member TIGR02168:
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.53 E-value: 7.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1809 KAEITKKLSDHDEKLQEAQDLLNE----------------------AQLKTRQAGLVANQnlanLTSLERKRAAVSEIKE 1866
Cdd:TIGR02168 174 RKETERKLERTRENLDRLEDILNElerqlkslerqaekaerykelkAELRELELALLVLR----LEELREELEELQEELK 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1867 dvqkvfgESEHLLEEangLSNSINEELQDLEEMGRELGPLHDQLDDkvrpLTGGLsdGSLANSVHEAEQHAKELNESAAI 1946
Cdd:TIGR02168 250 -------EAEEELEE---LTAELQELEEKLEELRLEVSELEEEIEE----LQKEL--YALANEISRLEQQKQILRERLAN 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1947 LDN-------ILAEAKNLSFNATAAFHAytnIKDKIDAAEKEAkeakqkasDALELAMGADVPVKEAAKSALQKSQVLLN 2019
Cdd:TIGR02168 314 LERqleeleaQLEELESKLDELAEELAE---LEEKLEELKEEL--------ESLEAELEELEAELEELESRLEELEEQLE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2020 KAKQLENDLRENADSmegLKGRVKAAKDKSKDLlkavNGTIATLNAIPNDTSAKLAATKAVAADANATAIDvlERLGELN 2099
Cdd:TIGR02168 383 TLRSKVAQLELQIAS---LNNEIERLEARLERL----EDRRERLQQEIEELLKKLEEAELKELQAELEELE--EELEELQ 453
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1343941588 2100 LRLGGLQLNYSQLDDTVSAANQMIQDPEKNIHAAGAKVKELEDeadrlleklqpikmMQDNLRRNISQIKELINQARK 2177
Cdd:TIGR02168 454 EELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLER--------------LQENLEGFSEGVKALLKNQSG 517
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
421-467 |
8.80e-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: 50.81 E-value: 8.80e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1343941588 421 CNCSMEGSINtDPCIT---PCVCKENVEGGNCDRCKLGFYNLQHDNPRGC 467
Cdd:pfam00053 1 CDCNPHGSLS-DTCDPetgQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1567-1604 |
5.45e-07 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
:
Pssm-ID: 395007 Cd Length: 49 Bit Score: 48.50 E-value: 5.45e-07
10 20 30
....*....|....*....|....*....|....*...
gi 1343941588 1567 CKCSSWGALAGPCDSVTGQCRCRVGASGTSCDQCMDRH 1604
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGY 38
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
916-953 |
9.86e-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: 47.73 E-value: 9.86e-07
10 20 30
....*....|....*....|....*....|....*....
gi 1343941588 916 PCRCSPRGSIAQRCDPE-GRCTCRPGFAGSRCDQRRPSY 953
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGtGQCECKPNTTGRRCDRCAPGY 39
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
757-812 |
5.51e-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: 45.81 E-value: 5.51e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1343941588 757 CACPlllPSNNFSPTCHLDEGgklVCnRCQMGYTGPRCERCSNGFYGQPDVPGGSC 812
Cdd:pfam00053 1 CDCN---PHGSLSDTCDPETG---QC-LCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
259-286 |
2.39e-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: 43.88 E-value: 2.39e-05
10 20
....*....|....*....|....*...
gi 1343941588 259 CECEHNTCGESCDRCCPGYHQQPWMAGT 286
Cdd:cd00055 21 CECKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1508-1562 |
2.27e-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: 41.19 E-value: 2.27e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1343941588 1508 PCACplpNPENNFSPTCIAEGLddyRCTaCPEGYEGKYCERCATGYHGNPRMPGG 1562
Cdd:cd00055 1 PCDC---NGHGSLSGQCDPGTG---QCE-CKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
4-237 |
2.11e-87 |
|
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: 285.79 E-value: 2.11e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 4 IKANATCGLNGPEMSCKLVEHVpgqpVRNPQCTICDqeSTNEYERHPIEYAIDGTN----RWWQSPSIMNGMvnHYVTIT 79
Cdd:smart00136 20 VTATSTCGEPGPERYCKLVGHT----EQGKKCDYCD--ARNPRRSHPAENLTDGNNpnnpTWWQSEPLSNGP--QNVNLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 80 LDLKQVFQVAYMIIKAAnSPRPGNWILERSIDGTTFEPWQYYAitdTECLTRFNISPRRGPPSYTrDDEVICTSFYSKIQ 159
Cdd:smart00136 92 LDLGKEFHVTYVILKFC-SPRPSLWILERSDFGKTWQPWQYFS---SDCRRTFGRPPRGPITKGN-EDEVICTSEYSDIV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 160 PLENGEIHASLINGRPSAEDP--SPTLLNFTSARYIRLVFQRIRTLNADLMtltlrdprDVDPIVTRRYYYSIKDISVGG 237
Cdd:smart00136 167 PLEGGEIAFSLLEGRPSATDFdnSPVLQEWVTATNIRVRLTRLRTLGDELM--------DDRPEVTRRYYYAISDIAVGG 238
|
|
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
2-237 |
1.55e-82 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 271.38 E-value: 1.55e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2 ADIKANATCGLNGPEMSCKLVEHVPGQpvrnpQCTICDqeSTNEYERHPIEYAIDGTNR----WWQSPSIMngMVNHYVT 77
Cdd:pfam00055 12 REVSATSTCGLNGPERYCILSGLEGGK-----KCFICD--SRDPHNSHPPSNLTDSNNGtnetWWQSETGV--IQYENVN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 78 ITLDLKQVFQVAYMIIKAAnSPRPGNWILERSID-GTTFEPWQYYAitdTECLTRFNISPRrgPPSYTRDDEVICTSFYS 156
Cdd:pfam00055 83 LTLDLGKEFHFTYLILKFK-SPRPAAMVLERSTDfGKTWQPYQYFA---SDCRRTFGRPSG--PSRGIKDDEVICTSEYS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 157 KIQPLENGEIHASLINGRPSAE--DPSPTLLNFTSARYIRLVFQRIRTLNadlmtltlrDPRDVDPIVTRRYYYSIKDIS 234
Cdd:pfam00055 157 DISPLTGGEVIFSTLEGRPSANifDYSPELQDWLTATNIRIRLLRLHTLG---------DELLDDPSVLRKYYYAISDIS 227
|
...
gi 1343941588 235 VGG 237
Cdd:pfam00055 228 VGG 230
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1638-1890 |
9.29e-55 |
|
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: 193.01 E-value: 9.29e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1638 LTTPLPPPYKVLYRFENMTDELKHMLSPQKAPERLLQLADSNLGSLVVEMDQLHSRATKVSADGEQVVDDSDRIHRRAED 1717
Cdd:pfam06008 7 LTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1718 LEKFIKDTLLGAKDLQLKAAELNKTLsrkDGTPDKSLSQMNEEIQAMLEEMRKRQLGRMKITADEEKDLAEELLQKVKRL 1797
Cdd:pfam06008 87 LAEAIKNLIDNIKEINEKVATLGEND---FALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQDLLSRIQTW 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1798 FGDPHQATEDLKAEITKKLSDHDEKLQEAQDLLNEAQLKTRQAGLVANQNLANLTSLERKRAAVSEIKEDVQKVFGESEH 1877
Cdd:pfam06008 164 FQSPQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEETLKTARD 243
|
250
....*....|...
gi 1343941588 1878 LLEEANGLSNSIN 1890
Cdd:pfam06008 244 SLDAANLLLQEID 256
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
1274-1412 |
1.50e-42 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 153.19 E-value: 1.50e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1274 YWLLPEQFTGSMITAYGGQLKYAVYYEARDETGPSSYEPQVIVKGGPNHNMLMFRHITGIQIGQLTRHEIDMTEHEWEFA 1353
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGGGSLNSEPDVILEGNGLRLSYSSPDQPPPDPGQEQTYSVRLHEENWRDS 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1343941588 1354 DGRPMTREDFMDILFHVDYILIKASHGNLMRHSRVSEISLTVAEEGPRsedGEKAHQIE 1412
Cdd:pfam00052 81 DGAPVSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSAVPGGS---GPPASWVE 136
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
532-672 |
3.26e-40 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 146.26 E-value: 3.26e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 532 YWNAPGLYLGNKLTAYGGIVTFTVSYTTDQQVQNAirvTSEPDLIIQGGGMKIIDKRFGQP-VYPSSPSTSHILLLPENF 610
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGGGSL---NSEPDVILEGNGLRLSYSSPDQPpPDPGQEQTYSVRLHEENW 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1343941588 611 lVSETGRPINRRDFLMVLANVTSVMVRASYSTETTAVyRLHSFSMQVASPSGRSERtASAVE 672
Cdd:pfam00052 78 -RDSDGAPVSREDFMMVLANLTAILIRATYSTGSGQV-SLSNVSLDSAVPGGSGPP-ASWVE 136
|
|
| LamB |
smart00281 |
Laminin B domain; |
1269-1398 |
1.17e-38 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 141.63 E-value: 1.17e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1269 LSEPFYWLLPEQFTGSMITAYGGQLKYAVYYEARDEtGPSSYEPQVIVKGgpNHNMLMFRHITGIQIGQLTRHEIDMTEH 1348
Cdd:smart00281 1 DNEPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRRG-GTHVSAPDVILEG--NGLRISHPAEGPPLPDELTTVEVRFREE 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1349 EWEFADGRPMTREDFMDILFHVDYILIKASHGNLMRHSRVSEISLTVAEE 1398
Cdd:smart00281 78 NWQYYGGRPVTREDLMMVLANLTAILIRATYSQQMAGSRLSDVSLEVAVP 127
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2864-2992 |
1.07e-34 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 130.51 E-value: 1.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2864 RTKEQSGLVLYMARINHADFVSIQIKDGQVCLGYDLGRGNISGCVPFSINDGSWHKIRVSRNKQRGVLTVDGLYSKQMTS 2943
Cdd:pfam00054 2 RTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGES 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2944 PNKAD-LLDVVGTLYVGGLPQNYITRRIGPILYSLNGCIRNLKMVGSPVG 2992
Cdd:pfam00054 82 PLGATtDLDVDGPLYVGGLPSLGVKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
3026-3177 |
1.55e-34 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 130.62 E-value: 1.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 3026 GSYFDGTGYLKAVASYRVGLDVSIALEFRTTRTNGVLLTVSNQD-KDGLGLEIVQGKLLFHVDNGAGRITAEHapdGAGF 3104
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNgGDFLALELEDGRLVLRYDLGSGSLVLSS---KTPL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1343941588 3105 CDGLWHAVTATKLRHKLELEVDGRKSRAESPNARSSTCDTNDPIYVGGYPDGVHQAGLSTKRSFKGCLKNLKI 3177
Cdd:cd00110 78 NDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKV 150
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2836-2986 |
9.05e-34 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 128.69 E-value: 9.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2836 FGLTKNSHMSFSFDDAKvRERLILEFDLRTKEQSGLVLYMARINHADFVSIQIKDGQVCLGYDLGRGNISGCVPFSINDG 2915
Cdd:cd00110 2 VSFSGSSYVRLPTLPAP-RTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1343941588 2916 SWHKIRVSRNKQRGVLTVDGLYSKQMTSPNKADLLDVVGTLYVGGLPQNYITRRIgPILYSLNGCIRNLKM 2986
Cdd:cd00110 81 QWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGL-PVSPGFVGCIRDLKV 150
|
|
| Laminin_II |
pfam06009 |
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 ... |
2091-2210 |
9.09e-34 |
|
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: 127.99 E-value: 9.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2091 VLERLGELNLRLGGLQLNYSQLDDTVSAANQMIQDPEKNIHAAGAKVKELEDEADRLLEKLQPIKMMQDN---LRRNISQ 2167
Cdd:pfam06009 15 VLEQLAPLSQNLENTSEKLSGINRSLEETNELVNDANKALDDAGRSVKKLEELAPDLLDKLKPLKQLEVNsssLSDNISR 94
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1343941588 2168 IKELINQARKQANSIKVSVSSGGDCLRSYRPDIRKGRYNTIIL 2210
Cdd:pfam06009 95 IKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTS 137
|
|
| LamG |
smart00282 |
Laminin G domain; |
2859-2988 |
2.07e-30 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 118.21 E-value: 2.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2859 LEFDLRTKEQSGLVLYMARINHADFVSIQIKDGQVCLGYDLG--RGNISGcVPFSINDGSWHKIRVSRNKQRGVLTVDGL 2936
Cdd:smart00282 2 ISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGsgPARLTS-DPTPLNDGQWHRVAVERNGRSVTLSVDGG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1343941588 2937 YSKQMTSPNKADLLDVVGTLYVGGLPQNyITRRIGPILYSLNGCIRNLKMVG 2988
Cdd:smart00282 81 NRVSGESPGGLTILNLDGPLYLGGLPED-LKLPPLPVTPGFRGCIRNLKVNG 131
|
|
| LamG |
smart00282 |
Laminin G domain; |
3048-3177 |
2.07e-30 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 118.21 E-value: 2.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 3048 SIALEFRTTRTNGVLL-TVSNQDKDGLGLEIVQGKLLFHVDNGAGRITAEHapDGAGFCDGLWHAVTATKLRHKLELEVD 3126
Cdd:smart00282 1 SISFSFRTTSPNGLLLyAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTS--DPTPLNDGQWHRVAVERNGRSVTLSVD 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1343941588 3127 GRKSRAESPNARSSTCDTNDPIYVGGYPDGVHQAGLSTKRSFKGCLKNLKI 3177
Cdd:smart00282 79 GGNRVSGESPGGLTILNLDGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKV 129
|
|
| LamB |
smart00281 |
Laminin B domain; |
527-660 |
3.34e-30 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 117.36 E-value: 3.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 527 LGSAYYWNAPGLYLGNKLTAYGGIVTFTVSYTTdqqvQNAIRVTSEPDLIIQGGGMKIIDKRFGQPvYPSSPSTSHILLL 606
Cdd:smart00281 1 DNEPVYWVAPEQFLGDKVTSYGGKLRYTLSFDG----RRGGTHVSAPDVILEGNGLRISHPAEGPP-LPDELTTVEVRFR 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1343941588 607 PENFlVSETGRPINRRDFLMVLANVTSVMVRASYSTETTAVYrLHSFSMQVASP 660
Cdd:smart00281 76 EENW-QYYGGRPVTREDLMMVLANLTAILIRATYSQQMAGSR-LSDVSLEVAVP 127
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2378-2540 |
1.20e-29 |
|
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: 116.75 E-value: 1.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2378 TVQLDGEGYASVgRPTRWNPNVSTITFKFRTFSSDALLMYMATEDMKDFMSLELSAGKVTVNFDLGSGVGKaVSAKRQ-N 2456
Cdd:cd00110 1 GVSFSGSSYVRL-PTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLV-LSSKTPlN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2457 DGRWKSLTVSRNKKQAIVTiVDidsgiaeDKIVATSQGSATGLNLRENQKIYFGGLPTignySMAARSEVTLKRYAGCLR 2536
Cdd:cd00110 79 DGQWHSVSVERNGRSVTLS-VD-------GERVVESGSPGGSALLNLDGPLYLGGLPE----DLKSPGLPVSPGFVGCIR 146
|
....
gi 1343941588 2537 DIEV 2540
Cdd:cd00110 147 DLKV 150
|
|
| LamG |
smart00282 |
Laminin G domain; |
2207-2349 |
1.92e-29 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 115.51 E-value: 1.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2207 TIILHVKTTTPDNLLFYLGSAKYVDFLALEMRKGKVNFLWDVGSGVGRLEYPSHTIHDGNWHRIEASRNGLNGTISVYPL 2286
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLNDGQWHRVAVERNGRSVTLSVDGG 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1343941588 2287 EgpmagmmptPASANSPAAFTILDVDQNayLFVGGIFNTAKKAEAVKTSTFTGCMGETFLDGK 2349
Cdd:smart00282 81 N---------RVSGESPGGLTILNLDGP--LYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2212-2352 |
2.00e-28 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 112.41 E-value: 2.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2212 VKTTTPDNLLFYLGSAKYVDFLALEMRKGKVNFLWDVGSGVGRLEYPShTIHDGNWHRIEASRNGLNGTISVYPLEgPMA 2291
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGD-KLNDGKWHSVELERNGRSGTLSVDGEA-RPT 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1343941588 2292 GMMPTPASanspaafTILDVDQNayLFVGGIFNTAKKAE-AVKTSTFTGCMGETFLDGKPIG 2352
Cdd:pfam00054 79 GESPLGAT-------TDLDVDGP--LYVGGLPSLGVKKRrLAISPSFDGCIRDVIVNGKPLD 131
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
3053-3177 |
2.22e-28 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 112.13 E-value: 2.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 3053 FRTTRTNGVLLTVSNQDKDGLGLEIVQGKLLFHVDNGAGRITAEHApdGAGFCDGLWHAVTATKLRHKLELEVDGRKSRA 3132
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDFLALELVNGRLVLRYDLGSGPESLLSS--GKNLNDGQWHSVRVERNGNTLTLSVDGQTVVS 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1343941588 3133 ESPNARSSTCDTNDPIYVGGYPDGVHQAGLSTKRSFKGCLKNLKI 3177
Cdd:pfam02210 79 SLPPGESLLLNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRV 123
|
|
| LamG |
smart00282 |
Laminin G domain; |
2401-2542 |
2.37e-28 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 112.43 E-value: 2.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2401 TITFKFRTFSSDALLMYMATEDMKDFMSLELSAGKVTVNFDLGSGVGKAVSAKRQ-NDGRWKSLTVSRNKKQAIVTiVDi 2479
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPlNDGQWHRVAVERNGRSVTLS-VD- 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1343941588 2480 dsgiAEDKIVATSQGSATGLNLreNQKIYFGGLPTignySMAARSEVTLKRYAGCLRDIEVSR 2542
Cdd:smart00282 79 ----GGNRVSGESPGGLTILNL--DGPLYLGGLPE----DLKLPPLPVTPGFRGCIRNLKVNG 131
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2406-2546 |
1.77e-27 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 109.71 E-value: 1.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2406 FRTFSSDALLMYMATEDMKDFMSLELSAGKVTVNFDLGSGVGKAVSAKRQNDGRWKSLTVSRNKKQAIVTIVDIDSGIAE 2485
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1343941588 2486 DKIVATSQGSATGlnlrenqKIYFGGLPtigNYSMAARSEVTLKRYAGCLRDIEVSRTPYN 2546
Cdd:pfam00054 81 SPLGATTDLDVDG-------PLYVGGLP---SLGVKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2188-2347 |
8.75e-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: 105.58 E-value: 8.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2188 SGGDCLRsYRPDIRKGRYNTIILHVKTTTPDNLLFYLGSAKYVDFLALEMRKGKVNFLWDVGSGVGRLEYPSHtIHDGNW 2267
Cdd:cd00110 5 SGSSYVR-LPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTP-LNDGQW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2268 HRIEASRNGLNGTISVyplegpmagmmPTPASANSPAAFTILDVDQNAYLFVGGIFNTAKKAEAVKTSTFTGCMGETFLD 2347
Cdd:cd00110 83 HSVSVERNGRSVTLSV-----------DGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2567-2735 |
1.90e-23 |
|
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: 99.03 E-value: 1.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2567 TVSFSKPGYMELGGLSL-AVDTEISLSFSTLQDNGtILLAVGGstsrqqarnpkrrrrQSGEPYLSVMLNSGSLeVLMFT 2645
Cdd:cd00110 1 GVSFSGSSYVRLPTLPApRTRLSISFSFRTTSPNG-LLLYAGS---------------QNGGDFLALELEDGRL-VLRYD 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2646 RSHSPHRITrrpDQGILNDGREHSLRIERLpGRSFAVQVDEEAKLEAALPNDQPISL--QRLFLGGIPAEVEQTSNKANV 2723
Cdd:cd00110 64 LGSGSLVLS---SKTPLNDGQWHSVSVERN-GRSVTLSVDGERVVESGSPGGSALLNldGPLYLGGLPEDLKSPGLPVSP 139
|
170
....*....|..
gi 1343941588 2724 PFQGCIWNLMVN 2735
Cdd:cd00110 140 GFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
2588-2735 |
1.26e-19 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 87.39 E-value: 1.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2588 EISLSFSTLQDNGtILLAVGGSTsrqqarnpkrrrrqsGEPYLSVMLNSGSLeVLMFTRSHSPHRITrrPDQGILNDGRE 2667
Cdd:smart00282 1 SISFSFRTTSPNG-LLLYAGSKG---------------GGDYLALELRDGRL-VLRYDLGSGPARLT--SDPTPLNDGQW 61
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2668 HSLRIERLpGRSFAVQVDEEAKLEAALPNDQPISL--QRLFLGGIPAEVEQTSNKANVPFQGCIWNLMVN 2735
Cdd:smart00282 62 HRVAVERN-GRSVTLSVDGGNRVSGESPGGLTILNldGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVN 130
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2593-2735 |
1.17e-14 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 73.12 E-value: 1.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2593 FSTLQDNGTILLAvggstsrqqARNPKRrrrqsgePYLSVMLNSGSLEVLMFTRSHSPHriTRRPDQgiLNDGREHSLRI 2672
Cdd:pfam00054 1 FRTTEPSGLLLYN---------GTQTER-------DFLALELRDGRLEVSYDLGSGAAV--VRSGDK--LNDGKWHSVEL 60
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1343941588 2673 ERLpGRSFAVQVDEEAKL--EAALPNDQPISLQR-LFLGGIPAEVEQTSNKANVP-FQGCIWNLMVN 2735
Cdd:pfam00054 61 ERN-GRSGTLSVDGEARPtgESPLGATTDLDVDGpLYVGGLPSLGVKKRRLAISPsFDGCIRDVIVN 126
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
867-913 |
1.61e-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: 64.30 E-value: 1.61e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1343941588 867 PCQCHINGSLSEVCNKESGQCPCKEDVLGRQCDKCKPSYWWDAEHPG 913
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGG 47
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1055-1098 |
1.94e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 61.17 E-value: 1.94e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1343941588 1055 CQCS---HVGNNCDANTGQCICPPNTIGERCDRCAPNHWGhDITTGC 1098
Cdd:smart00180 1 CDCDpggSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYG-DGPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
868-914 |
2.14e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 60.79 E-value: 2.14e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1343941588 868 CQCHINGSLSEVCNKESGQCPCKEDVLGRQCDKCKPSYwWDAEHPGC 914
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGY-YGDGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1055-1098 |
2.30e-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: 60.83 E-value: 2.30e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1343941588 1055 CQCSHVG---NNCDANTGQCICPPNTIGERCDRCAPNHWGHDITTGC 1098
Cdd:pfam00053 1 CDCNPHGslsDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQ 47
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1008-1052 |
4.24e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 60.02 E-value: 4.24e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1343941588 1008 CHCNSFGSKSFDCD-DLGQCRCQPGVSGPKCDRCSRGFFNFQEGGC 1052
Cdd:smart00180 1 CDCDPGGSASGTCDpDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1054-1099 |
5.01e-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: 60.06 E-value: 5.01e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1054 ACQCSHVG---NNCDANTGQCICPPNTIGERCDRCAPNHWGHDITT-GCK 1099
Cdd:cd00055 1 PCDCNGHGslsGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGgGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1007-1056 |
7.62e-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: 7.62e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1343941588 1007 PCHCNSFGSKSFDCDDL-GQCRCQPGVSGPKCDRCSRGFFNFQEGGcTACQ 1056
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGtGQCECKPNTTGRRCDRCAPGYYGLPSQG-GGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
814-866 |
9.45e-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: 59.29 E-value: 9.45e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1343941588 814 PCNCNYNLdlSVPGSCDPITGQCLkCRQGYGGAACESCADGYYGDAILAKNCQ 866
Cdd:cd00055 1 PCDCNGHG--SLSGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
366-423 |
1.23e-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: 1.23e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1343941588 366 CSCDPHGSVSQSCVADSGQatpsqpagsCWCKEGYGGPQCDRCAVGYKGFPSCERCNC 423
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQ---------CLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1460-1506 |
1.39e-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: 1.39e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1460 CQCSGHSS---TCDPETSICQnCQDNTEGDRCERCMPGFYGVVRGSSDDC 1506
Cdd:pfam00053 1 CDCNPHGSlsdTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
868-919 |
1.56e-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: 1.56e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1343941588 868 CQCHINGSLSEVCNKESGQCPCKEDVLGRQCDKCKPSYWWDaehPGCMPCRC 919
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGL---PSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
366-417 |
2.56e-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: 58.13 E-value: 2.56e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1343941588 366 CSCDPHGSVSQSCVADSGQatpsqpagsCWCKEGYGGPQCDRCAVGYKGFPS 417
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQ---------CECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1008-1055 |
3.10e-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: 57.75 E-value: 3.10e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1343941588 1008 CHCNSFGSKSFDCDDL-GQCRCQPGVSGPKCDRCSRGFFNFQEGGCTAC 1055
Cdd:pfam00053 1 CDCNPHGSLSDTCDPEtGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1101-1149 |
5.97e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 56.98 E-value: 5.97e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1343941588 1101 CGCNVVGSLSQQCNMNTGCCSCRESFRGEKCDECQIGYRDFPQCIRCEC 1149
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1147-1204 |
6.92e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 56.59 E-value: 6.92e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1343941588 1147 CECSFAGSDSQSCDMErrvcacadqTGKCSCKVNVEGSNCDRCKPDTFGLSARNPLGC 1204
Cdd:pfam00053 1 CDCNPHGSLSDTCDPE---------TGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
706-755 |
9.89e-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: 56.21 E-value: 9.89e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1343941588 706 PCRCHGHAT---QCHEITGHCLdCYHNTAGQYCDTCLPGYYGNATRGSpaDCQ 755
Cdd:cd00055 1 PCDCNGHGSlsgQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGG--GCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
707-754 |
1.20e-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: 56.21 E-value: 1.20e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1343941588 707 CRCHGHAT---QCHEITGHCLdCYHNTAGQYCDTCLPGYYGNATrGSPADC 754
Cdd:pfam00053 1 CDCNPHGSlsdTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPS-DPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
366-418 |
1.79e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 55.40 E-value: 1.79e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1343941588 366 CSCDPHGSVSQSCVADSGQatpsqpagsCWCKEGYGGPQCDRCAVGYKG--FPSC 418
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQ---------CECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1460-1497 |
6.80e-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: 53.90 E-value: 6.80e-09
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1343941588 1460 CQCSGHSS---TCDPETSICQnCQDNTEGDRCERCMPGFYG 1497
Cdd:cd00055 2 CDCNGHGSlsgQCDPGTGQCE-CKPNTTGRRCDRCAPGYYG 41
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
815-870 |
1.47e-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: 53.13 E-value: 1.47e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1343941588 815 CNCNYNLdlSVPGSCDPITGQCLkCRQGYGGAACESCADGYYGDAilakNCQPCQC 870
Cdd:pfam00053 1 CDCNPHG--SLSDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLP----SDPPQGC 49
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1642-1955 |
1.85e-08 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 60.36 E-value: 1.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1642 LPPPYKVLYRFENMTDELKHMLspqKAPERLLQLADSNLGSLVVEMDQLHSRATK-VSADGEQVVDDSDRIHRRAEDLEK 1720
Cdd:COG5185 238 FQDPESELEDLAQTSDKLEKLV---EQNTDLRLEKLGENAESSKRLNENANNLIKqFENTKEKIAEYTKSIDIKKATESL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1721 fikdtllgakDLQLKAAELNKTLSRKDGTPDKSLSQMNEEIQ----AMLEEMRKRQLGRMKITADEEKDLAEELLQKVK- 1795
Cdd:COG5185 315 ----------EEQLAAAEAEQELEESKRETETGIQNLTAEIEqgqeSLTENLEAIKEEIENIVGEVELSKSSEELDSFKd 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1796 -------RLFGDPHQATE---DLKAEITKKLSDHDEKLQEAQDLLNEAqlkTRQAGLVANQNLANLTSLERKRAAVSEIK 1865
Cdd:COG5185 385 tiestkeSLDEIPQNQRGyaqEILATLEDTLKAADRQIEELQRQIEQA---TSSNEEVSKLLNELISELNKVMREADEES 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1866 edvqkvfgeSEHLLEEANGLSNSINEELQDLEEMgrelgplHDQLDDKVRPLTGGLSdGSLANSVHEAEQHAKELNESAA 1945
Cdd:COG5185 462 ---------QSRLEEAYDEINRSVRSKKEDLNEE-------LTQIESRVSTLKATLE-KLRAKLERQLEGVRSKLDQVAE 524
|
330
....*....|
gi 1343941588 1946 ILDNILAEAK 1955
Cdd:COG5185 525 SLKDFMRARG 534
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1146-1204 |
2.38e-08 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 52.36 E-value: 2.38e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1343941588 1146 RCECSFAGSDSQSCDMErrvcacadqTGKCSCKVNVEGSNCDRCKPDTFGLsARNPLGC 1204
Cdd:cd00055 1 PCDCNGHGSLSGQCDPG---------TGQCECKPNTTGRRCDRCAPGYYGL-PSQGGGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
815-858 |
2.52e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 52.31 E-value: 2.52e-08
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1343941588 815 CNCNynLDLSVPGSCDPITGQCLkCRQGYGGAACESCADGYYGD 858
Cdd:smart00180 1 CDCD--PGGSASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD 41
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1651-2179 |
4.39e-08 |
|
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: 59.30 E-value: 4.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1651 RFENMTDELKHM------LSPQKAPERLLQLADSnLGSLVVEMDQLHSRATKVSADGEQVVDDSDRIHRRAEDLEKFIKD 1724
Cdd:TIGR02168 214 RYKELKAELRELelallvLRLEELREELEELQEE-LKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1725 TLLGAKDLQLKAAELNKTLsrkdgtpdKSLSQMNEEIQAMLEEMRKRQlgrmKITADEEKDLAEEL--LQKVKRLFGDPH 1802
Cdd:TIGR02168 293 LANEISRLEQQKQILRERL--------ANLERQLEELEAQLEELESKL----DELAEELAELEEKLeeLKEELESLEAEL 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1803 QATEDLKAEITKKLSDHDEKLQEAQDLLNEAQLKTRQAGLVANQNLANLTSLERKRAAVSEIKEDVQKVFGESEhlLEEA 1882
Cdd:TIGR02168 361 EELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE--LKEL 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1883 NGLSNSINEELQDLEEMGRELGPLHDQLDDKVRPLTgglsdgslaNSVHEAEQHAKELNESAAILDNILAEAKNLSFNAT 1962
Cdd:TIGR02168 439 QAELEELEEELEELQEELERLEEALEELREELEEAE---------QALDAAERELAQLQARLDSLERLQENLEGFSEGVK 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1963 AAFHAYTNIKDKIDAAekeakeakqkaSD----------ALELAMGAD-----VPVKEAAKSALQ--------KSQVL-- 2017
Cdd:TIGR02168 510 ALLKNQSGLSGILGVL-----------SElisvdegyeaAIEAALGGRlqavvVENLNAAKKAIAflkqnelgRVTFLpl 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2018 -LNKAKQLENDLRENADSMEGLKGRVKAAKDKSKDLLKAVNGTIATLNAIPNDTSAklaatkavaadanataidvLERLG 2096
Cdd:TIGR02168 579 dSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNA-------------------LELAK 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2097 ELNLR-----LGGLQLN--YSQLDDTVSAANQM------IQDPEKNIHAAGAKVKELEDEADRLLEKLQPIKMMQDNLRR 2163
Cdd:TIGR02168 640 KLRPGyrivtLDGDLVRpgGVITGGSAKTNSSIlerrreIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRK 719
|
570
....*....|....*.
gi 1343941588 2164 NISQIKELINQARKQA 2179
Cdd:TIGR02168 720 ELEELSRQISALRKDL 735
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1101-1142 |
4.86e-08 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 51.59 E-value: 4.86e-08
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1343941588 1101 CGCNVVGSLSQQCNMNTGCCSCRESFRGEKCDECQIGYRDFP 1142
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1809-2177 |
7.53e-08 |
|
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: 58.53 E-value: 7.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1809 KAEITKKLSDHDEKLQEAQDLLNE----------------------AQLKTRQAGLVANQnlanLTSLERKRAAVSEIKE 1866
Cdd:TIGR02168 174 RKETERKLERTRENLDRLEDILNElerqlkslerqaekaerykelkAELRELELALLVLR----LEELREELEELQEELK 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1867 dvqkvfgESEHLLEEangLSNSINEELQDLEEMGRELGPLHDQLDDkvrpLTGGLsdGSLANSVHEAEQHAKELNESAAI 1946
Cdd:TIGR02168 250 -------EAEEELEE---LTAELQELEEKLEELRLEVSELEEEIEE----LQKEL--YALANEISRLEQQKQILRERLAN 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1947 LDN-------ILAEAKNLSFNATAAFHAytnIKDKIDAAEKEAkeakqkasDALELAMGADVPVKEAAKSALQKSQVLLN 2019
Cdd:TIGR02168 314 LERqleeleaQLEELESKLDELAEELAE---LEEKLEELKEEL--------ESLEAELEELEAELEELESRLEELEEQLE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2020 KAKQLENDLRENADSmegLKGRVKAAKDKSKDLlkavNGTIATLNAIPNDTSAKLAATKAVAADANATAIDvlERLGELN 2099
Cdd:TIGR02168 383 TLRSKVAQLELQIAS---LNNEIERLEARLERL----EDRRERLQQEIEELLKKLEEAELKELQAELEELE--EELEELQ 453
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1343941588 2100 LRLGGLQLNYSQLDDTVSAANQMIQDPEKNIHAAGAKVKELEDeadrlleklqpikmMQDNLRRNISQIKELINQARK 2177
Cdd:TIGR02168 454 EELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLER--------------LQENLEGFSEGVKALLKNQSG 517
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1711-1953 |
8.37e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.15 E-value: 8.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1711 IHRRAEDLEKFIKDTllgaKDLQLKAAELNKTLSRKDG-TPDK------SLSQMNEEIQAMLEEMRKRqLGRMKITADEE 1783
Cdd:PRK03918 350 LEKRLEELEERHELY----EEAKAKKEELERLKKRLTGlTPEKlekeleELEKAKEEIEEEISKITAR-IGELKKEIKEL 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1784 KDLAEELlQKVK-------RLFGDPHQatEDLKAEITKKLSDHDEKLQEAQDLLNEAQ--------LKTRQAGLVANQNL 1848
Cdd:PRK03918 425 KKAIEEL-KKAKgkcpvcgRELTEEHR--KELLEEYTAELKRIEKELKEIEEKERKLRkelrelekVLKKESELIKLKEL 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1849 A-------------NLTSLERKRAAVSEIKEDVQKVFGESEHL---LEEANGLSNS---INEELQDLEEmgrELGPLHDQ 1909
Cdd:PRK03918 502 AeqlkeleeklkkyNLEELEKKAEEYEKLKEKLIKLKGEIKSLkkeLEKLEELKKKlaeLEKKLDELEE---ELAELLKE 578
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1343941588 1910 LDDK----VRPLTGGLSD--------GSLANSVHEAEQHAKELNESAAILDNILAE 1953
Cdd:PRK03918 579 LEELgfesVEELEERLKElepfyneyLELKDAEKELEREEKELKKLEEELDKAFEE 634
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
421-467 |
8.80e-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: 50.81 E-value: 8.80e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1343941588 421 CNCSMEGSINtDPCIT---PCVCKENVEGGNCDRCKLGFYNLQHDNPRGC 467
Cdd:pfam00053 1 CDCNPHGSLS-DTCDPetgQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1686-1955 |
1.01e-07 |
|
chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.16 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1686 EMDQLHSRATKVSADGEQVVDDSDRIHRRAEDLEKFikdtllgaKDLQLKAAELNKT-LSRKDGTPDKSLSQMNEEIQAM 1764
Cdd:TIGR02169 178 ELEEVEENIERLDLIIDEKRQQLERLRREREKAERY--------QALLKEKREYEGYeLLKEKEALERQKEAIERQLASL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1765 LEEMRKRQLGRMKI--TADEEKDLAEELLQKVKRLfGDPHQAT-----EDLKAEITKKLSDHDEKLQEAQDLlnEAQLKT 1837
Cdd:TIGR02169 250 EEELEKLTEEISELekRLEEIEQLLEELNKKIKDL-GEEEQLRvkekiGELEAEIASLERSIAEKERELEDA--EERLAK 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1838 RQAGLvaNQNLANLTSLER-------KRAAVSEIKEDVQKVFGESEHLLEEANGLSNSINEELQD----LEEMGRELGPL 1906
Cdd:TIGR02169 327 LEAEI--DKLLAEIEELEReieeerkRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDyrekLEKLKREINEL 404
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1343941588 1907 ---HDQLDDKVRPLTGGLSDgsLANSVHEAEQhakELNESAAILDNILAEAK 1955
Cdd:TIGR02169 405 kreLDRLQEELQRLSEELAD--LNAAIAGIEA---KINELEEEKEDKALEIK 451
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1147-1204 |
1.12e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 50.39 E-value: 1.12e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1343941588 1147 CECSFAGSDSQSCDMErrvcacadqTGKCSCKVNVEGSNCDRCKPDTFGlsaRNPLGC 1204
Cdd:smart00180 1 CDCDPGGSASGTCDPD---------TGQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1460-1498 |
1.26e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 50.39 E-value: 1.26e-07
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1343941588 1460 CQCSG---HSSTCDPETSICQnCQDNTEGDRCERCMPGFYGV 1498
Cdd:smart00180 1 CDCDPggsASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD 41
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1678-2183 |
1.40e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.77 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1678 SNLGSLVVEMDQLHSRATKVSADGEQVVDDSDRIHRRAEDLEKFIKDTLLGAKDLQLKAAELNKTlsRKDGTPDKSLSQM 1757
Cdd:PRK03918 224 EKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKEL--KEKAEEYIKLSEF 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1758 NEEIQAMLEEMRKRqLGRMKITADEEKDLAEELLQKVKRLfgdphQATEDLKAEITKKLS----DHdEKLQEAQDLLNEA 1833
Cdd:PRK03918 302 YEEYLDELREIEKR-LSRLEEEINGIEERIKELEEKEERL-----EELKKKLKELEKRLEeleeRH-ELYEEAKAKKEEL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1834 Q-LKTRQAGLvanqnlaNLTSLERKRAAVSEIKEDVQKvfgESEHLLEEANGLSNSINEELQDLEEM----------GRE 1902
Cdd:PRK03918 375 ErLKKRLTGL-------TPEKLEKELEELEKAKEEIEE---EISKITARIGELKKEIKELKKAIEELkkakgkcpvcGRE 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1903 LGPLHDQldDKVRPLTGGLSDgsLANSVHEAEQHAKELNESAAILDNILAEAKNLSFNATAAfHAYTNIKDKIDAAEKEA 1982
Cdd:PRK03918 445 LTEEHRK--ELLEEYTAELKR--IEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELA-EQLKELEEKLKKYNLEE 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1983 KEAKQKASDALE---LAMGADVpvkEAAKSALQKSQVLLNKAKQLENDLRENADSMEGLKGRVKAAKDKSkdlLKAVNGT 2059
Cdd:PRK03918 520 LEKKAEEYEKLKeklIKLKGEI---KSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFES---VEELEER 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2060 IATLNAIPN-------------DTSAKLAATKAVAADANATAIDVLERLGELNLRLGGLQLNYSQlDDTVSAANQMIQdP 2126
Cdd:PRK03918 594 LKELEPFYNeylelkdaekeleREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE-EEYEELREEYLE-L 671
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1343941588 2127 EKNIHAAGAKVKELE---DEADRLLEKLQ-------PIKMMQDNLRRNISQIKELINQARKQANSIK 2183
Cdd:PRK03918 672 SRELAGLRAELEELEkrrEEIKKTLEKLKeeleereKAKKELEKLEKALERVEELREKVKKYKALLK 738
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1718-2178 |
2.97e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.31 E-value: 2.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1718 LEKFIKDTLLgaKDLQLKAAELNKTLSRKDGTPDKSLSQMNEEIQAMLEEM--------RKRQLGRMKITADEEKDLAEE 1789
Cdd:COG4717 39 LLAFIRAMLL--ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEeeyaelqeELEELEEELEELEAELEELRE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1790 LLQKVKRL--FGDPHQATEDLKAEI---TKKLSDHDEKLQEAQDLLN-----EAQLKTRQAGLvanQNLANLTSLErKRA 1859
Cdd:COG4717 117 ELEKLEKLlqLLPLYQELEALEAELaelPERLEELEERLEELRELEEeleelEAELAELQEEL---EELLEQLSLA-TEE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1860 AVSEIKEDVQKVFGESEHLLEEANGLSNSINEELQDLEEMGRELgplhdQLDDKVRPLTGGLSDGSLANSVHEAEQHAKE 1939
Cdd:COG4717 193 ELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL-----EAAALEERLKEARLLLLIAAALLALLGLGGS 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1940 LNESAAILDNILAeaknlSFNATAAFHAYTNIKDKIDAAEKEAKEAKQKASDALELAMGADVPVKEAAKSALQKSQV--L 2017
Cdd:COG4717 268 LLSLILTIAGVLF-----LVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELleL 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2018 LNKAKQLENDLRENADSMEGLkgRVKAAKDKSKDLLKAVN-GTIATLNAIpndtsaklaatkavaadanataidvLERLG 2096
Cdd:COG4717 343 LDRIEELQELLREAEELEEEL--QLEELEQEIAALLAEAGvEDEEELRAA-------------------------LEQAE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2097 ElnlrlgglqlnYSQLDDTVSAANQMIQDPEKNIHAAGAKV--KELEDEADRLLEKLQPIKMMQDNLRRNISQIKELINQ 2174
Cdd:COG4717 396 E-----------YQELKEELEELEEQLEELLGELEELLEALdeEELEEELEELEEELEELEEELEELREELAELEAELEQ 464
|
....
gi 1343941588 2175 ARKQ 2178
Cdd:COG4717 465 LEED 468
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1678-2183 |
3.45e-07 |
|
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: 56.34 E-value: 3.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1678 SNLGSLVVEMDQLHSRATKVSAdgeQVVDDSDRIHRRAEDLE-KFIK-----DTLLGAKD------LQLKAaELNKTLSR 1745
Cdd:pfam01576 597 SNLEKKQKKFDQMLAEEKAISA---RYAEERDRAEAEAREKEtRALSlaralEEALEAKEelertnKQLRA-EMEDLVSS 672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1746 KDGTpDKSLSQMNEEIQAM---LEEMRKrQLgrmkitadEEkdLAEELlqkvkrlfgdphQATED-----------LKAE 1811
Cdd:pfam01576 673 KDDV-GKNVHELERSKRALeqqVEEMKT-QL--------EE--LEDEL------------QATEDaklrlevnmqaLKAQ 728
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1812 ITKKLSDHDEKLQEAQDLLNEaQLKTRQAGLVAnqnlanltslERK-RAAVSEIKEDVQKVFGESEHLLEEANglsnsin 1890
Cdd:pfam01576 729 FERDLQARDEQGEEKRRQLVK-QVRELEAELED----------ERKqRAQAVAAKKKLELDLKELEAQIDAAN------- 790
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1891 eelQDLEEMGRELGPLHDQLDDKVRPLTGG-LSDGSLANSVHEAEQHAKELNESAAILDNILAEAKNLSFNATAAfhayt 1969
Cdd:pfam01576 791 ---KGREEAVKQLKKLQAQMKDLQRELEEArASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQE----- 862
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1970 niKDKIdaaekeakeakqkasdALELAMGAdvpvkeAAKSALQKSQVLLN-KAKQLENDLRENADSMEGLKGRVKaakdK 2048
Cdd:pfam01576 863 --RDEL----------------ADEIASGA------SGKSALQDEKRRLEaRIAQLEEELEEEQSNTELLNDRLR----K 914
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2049 SKDLLKAVNGTIATLNAipndTSAKLAATKAVaadanataidvLERLG-ELNLRLgglqlnySQLDDTVSAANQMiqdpe 2127
Cdd:pfam01576 915 STLQVEQLTTELAAERS----TSQKSESARQQ-----------LERQNkELKAKL-------QEMEGTVKSKFKS----- 967
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2128 kNIHAAGAKVKELEDE----------ADRLL----EKLQPIKMMQDNLRRNISQIKElinQARKQANSIK 2183
Cdd:pfam01576 968 -SIAALEAKIAQLEEQleqesrerqaANKLVrrteKKLKEVLLQVEDERRHADQYKD---QAEKGNSRMK 1033
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1101-1144 |
5.01e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 48.46 E-value: 5.01e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1343941588 1101 CGCNVVGSLSQQCNMNTGCCSCRESFRGEKCDECQIGY--RDFPQC 1144
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYygDGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1567-1604 |
5.45e-07 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 48.50 E-value: 5.45e-07
10 20 30
....*....|....*....|....*....|....*...
gi 1343941588 1567 CKCSSWGALAGPCDSVTGQCRCRVGASGTSCDQCMDRH 1604
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGY 38
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1567-1604 |
6.40e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 48.46 E-value: 6.40e-07
10 20 30
....*....|....*....|....*....|....*...
gi 1343941588 1567 CKCSSWGALAGPCDSVTGQCRCRVGASGTSCDQCMDRH 1604
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGY 38
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
916-953 |
9.86e-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: 47.73 E-value: 9.86e-07
10 20 30
....*....|....*....|....*....|....*....
gi 1343941588 916 PCRCSPRGSIAQRCDPE-GRCTCRPGFAGSRCDQRRPSY 953
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGtGQCECKPNTTGRRCDRCAPGY 39
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
707-749 |
1.59e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 47.31 E-value: 1.59e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1343941588 707 CRCH--GHAT-QCHEITGHCLdCYHNTAGQYCDTCLPGYYGNATRG 749
Cdd:smart00180 1 CDCDpgGSASgTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1567-1604 |
2.34e-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: 46.96 E-value: 2.34e-06
10 20 30
....*....|....*....|....*....|....*...
gi 1343941588 1567 CKCSSWGALAGPCDSVTGQCRCRVGASGTSCDQCMDRH 1604
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGY 39
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
917-953 |
2.42e-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: 2.42e-06
10 20 30
....*....|....*....|....*....|....*...
gi 1343941588 917 CRCSPRGSIAQRCDPE-GRCTCRPGFAGSRCDQRRPSY 953
Cdd:pfam00053 1 CDCNPHGSLSDTCDPEtGQCLCKPGVTGRHCDRCKPGY 38
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
917-953 |
3.59e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 46.15 E-value: 3.59e-06
10 20 30
....*....|....*....|....*....|....*...
gi 1343941588 917 CRCSPRGSIAQRCDPE-GRCTCRPGFAGSRCDQRRPSY 953
Cdd:smart00180 1 CDCDPGGSASGTCDPDtGQCECKPNVTGRRCDRCAPGY 38
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
757-812 |
5.51e-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: 45.81 E-value: 5.51e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1343941588 757 CACPlllPSNNFSPTCHLDEGgklVCnRCQMGYTGPRCERCSNGFYGQPDVPGGSC 812
Cdd:pfam00053 1 CDCN---PHGSLSDTCDPETG---QC-LCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1686-1883 |
8.89e-06 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 49.37 E-value: 8.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1686 EMDQLHSRATKVSADGEQVV----DDSDRIHRRAEDLEKfIKDTLLGAkdLQLKAAELNKTLsrkdgtpdkSLSQMNEEI 1761
Cdd:cd00176 48 ELAAHEERVEALNELGEQLIeeghPDAEEIQERLEELNQ-RWEELREL--AEERRQRLEEAL---------DLQQFFRDA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1762 QAMLEEMRK--RQLGRMKITADEEKdlAEELLQKvkrlfgdpHQatedlkaEITKKLSDHDEKLQEAQDLLNEaqlktrq 1839
Cdd:cd00176 116 DDLEQWLEEkeAALASEDLGKDLES--VEELLKK--------HK-------ELEEELEAHEPRLKSLNELAEE------- 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1343941588 1840 agLVANQNLANLTSLERKRAAVSEIKEDVQKVFGESEHLLEEAN 1883
Cdd:cd00176 172 --LLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
756-813 |
1.08e-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: 45.04 E-value: 1.08e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1343941588 756 PCACPlllPSNNFSPTCHLDEGgklVCnRCQMGYTGPRCERCSNGFYGQPDVPGGsCQ 813
Cdd:cd00055 1 PCDCN---GHGSLSGQCDPGTG---QC-ECKPNTTGRRCDRCAPGYYGLPSQGGG-CQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
420-468 |
1.26e-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: 44.65 E-value: 1.26e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1343941588 420 RCNCSMEGSINTDpCITP---CVCKENVEGGNCDRCKLGFYNLQhDNPRGCE 468
Cdd:cd00055 1 PCDCNGHGSLSGQ-CDPGtgqCECKPNTTGRRCDRCAPGYYGLP-SQGGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
757-805 |
1.68e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 44.22 E-value: 1.68e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1343941588 757 CACPlllPSNNFSPTCHLDEGgklVCnRCQMGYTGPRCERCSNGFYGQP 805
Cdd:smart00180 1 CDCD---PGGSASGTCDPDTG---QC-ECKPNVTGRRCDRCAPGYYGDG 42
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
421-467 |
2.10e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 43.84 E-value: 2.10e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1343941588 421 CNCSMEGSINtDPCITP---CVCKENVEGGNCDRCKLGFYNlqhDNPRGC 467
Cdd:smart00180 1 CDCDPGGSAS-GTCDPDtgqCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
259-286 |
2.39e-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: 43.88 E-value: 2.39e-05
10 20
....*....|....*....|....*...
gi 1343941588 259 CECEHNTCGESCDRCCPGYHQQPWMAGT 286
Cdd:cd00055 21 CECKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1508-1562 |
2.27e-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: 41.19 E-value: 2.27e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1343941588 1508 PCACplpNPENNFSPTCIAEGLddyRCTaCPEGYEGKYCERCATGYHGNPRMPGG 1562
Cdd:cd00055 1 PCDC---NGHGSLSGQCDPGTG---QCE-CKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
259-282 |
9.17e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 39.22 E-value: 9.17e-04
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
4-237 |
2.11e-87 |
|
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: 285.79 E-value: 2.11e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 4 IKANATCGLNGPEMSCKLVEHVpgqpVRNPQCTICDqeSTNEYERHPIEYAIDGTN----RWWQSPSIMNGMvnHYVTIT 79
Cdd:smart00136 20 VTATSTCGEPGPERYCKLVGHT----EQGKKCDYCD--ARNPRRSHPAENLTDGNNpnnpTWWQSEPLSNGP--QNVNLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 80 LDLKQVFQVAYMIIKAAnSPRPGNWILERSIDGTTFEPWQYYAitdTECLTRFNISPRRGPPSYTrDDEVICTSFYSKIQ 159
Cdd:smart00136 92 LDLGKEFHVTYVILKFC-SPRPSLWILERSDFGKTWQPWQYFS---SDCRRTFGRPPRGPITKGN-EDEVICTSEYSDIV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 160 PLENGEIHASLINGRPSAEDP--SPTLLNFTSARYIRLVFQRIRTLNADLMtltlrdprDVDPIVTRRYYYSIKDISVGG 237
Cdd:smart00136 167 PLEGGEIAFSLLEGRPSATDFdnSPVLQEWVTATNIRVRLTRLRTLGDELM--------DDRPEVTRRYYYAISDIAVGG 238
|
|
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
2-237 |
1.55e-82 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 271.38 E-value: 1.55e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2 ADIKANATCGLNGPEMSCKLVEHVPGQpvrnpQCTICDqeSTNEYERHPIEYAIDGTNR----WWQSPSIMngMVNHYVT 77
Cdd:pfam00055 12 REVSATSTCGLNGPERYCILSGLEGGK-----KCFICD--SRDPHNSHPPSNLTDSNNGtnetWWQSETGV--IQYENVN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 78 ITLDLKQVFQVAYMIIKAAnSPRPGNWILERSID-GTTFEPWQYYAitdTECLTRFNISPRrgPPSYTRDDEVICTSFYS 156
Cdd:pfam00055 83 LTLDLGKEFHFTYLILKFK-SPRPAAMVLERSTDfGKTWQPYQYFA---SDCRRTFGRPSG--PSRGIKDDEVICTSEYS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 157 KIQPLENGEIHASLINGRPSAE--DPSPTLLNFTSARYIRLVFQRIRTLNadlmtltlrDPRDVDPIVTRRYYYSIKDIS 234
Cdd:pfam00055 157 DISPLTGGEVIFSTLEGRPSANifDYSPELQDWLTATNIRIRLLRLHTLG---------DELLDDPSVLRKYYYAISDIS 227
|
...
gi 1343941588 235 VGG 237
Cdd:pfam00055 228 VGG 230
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1638-1890 |
9.29e-55 |
|
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: 193.01 E-value: 9.29e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1638 LTTPLPPPYKVLYRFENMTDELKHMLSPQKAPERLLQLADSNLGSLVVEMDQLHSRATKVSADGEQVVDDSDRIHRRAED 1717
Cdd:pfam06008 7 LTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1718 LEKFIKDTLLGAKDLQLKAAELNKTLsrkDGTPDKSLSQMNEEIQAMLEEMRKRQLGRMKITADEEKDLAEELLQKVKRL 1797
Cdd:pfam06008 87 LAEAIKNLIDNIKEINEKVATLGEND---FALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQDLLSRIQTW 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1798 FGDPHQATEDLKAEITKKLSDHDEKLQEAQDLLNEAQLKTRQAGLVANQNLANLTSLERKRAAVSEIKEDVQKVFGESEH 1877
Cdd:pfam06008 164 FQSPQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEETLKTARD 243
|
250
....*....|...
gi 1343941588 1878 LLEEANGLSNSIN 1890
Cdd:pfam06008 244 SLDAANLLLQEID 256
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
1274-1412 |
1.50e-42 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 153.19 E-value: 1.50e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1274 YWLLPEQFTGSMITAYGGQLKYAVYYEARDETGPSSYEPQVIVKGGPNHNMLMFRHITGIQIGQLTRHEIDMTEHEWEFA 1353
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGGGSLNSEPDVILEGNGLRLSYSSPDQPPPDPGQEQTYSVRLHEENWRDS 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1343941588 1354 DGRPMTREDFMDILFHVDYILIKASHGNLMRHSRVSEISLTVAEEGPRsedGEKAHQIE 1412
Cdd:pfam00052 81 DGAPVSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSAVPGGS---GPPASWVE 136
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
532-672 |
3.26e-40 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 146.26 E-value: 3.26e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 532 YWNAPGLYLGNKLTAYGGIVTFTVSYTTDQQVQNAirvTSEPDLIIQGGGMKIIDKRFGQP-VYPSSPSTSHILLLPENF 610
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGGGSL---NSEPDVILEGNGLRLSYSSPDQPpPDPGQEQTYSVRLHEENW 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1343941588 611 lVSETGRPINRRDFLMVLANVTSVMVRASYSTETTAVyRLHSFSMQVASPSGRSERtASAVE 672
Cdd:pfam00052 78 -RDSDGAPVSREDFMMVLANLTAILIRATYSTGSGQV-SLSNVSLDSAVPGGSGPP-ASWVE 136
|
|
| LamB |
smart00281 |
Laminin B domain; |
1269-1398 |
1.17e-38 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 141.63 E-value: 1.17e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1269 LSEPFYWLLPEQFTGSMITAYGGQLKYAVYYEARDEtGPSSYEPQVIVKGgpNHNMLMFRHITGIQIGQLTRHEIDMTEH 1348
Cdd:smart00281 1 DNEPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRRG-GTHVSAPDVILEG--NGLRISHPAEGPPLPDELTTVEVRFREE 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1349 EWEFADGRPMTREDFMDILFHVDYILIKASHGNLMRHSRVSEISLTVAEE 1398
Cdd:smart00281 78 NWQYYGGRPVTREDLMMVLANLTAILIRATYSQQMAGSRLSDVSLEVAVP 127
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2864-2992 |
1.07e-34 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 130.51 E-value: 1.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2864 RTKEQSGLVLYMARINHADFVSIQIKDGQVCLGYDLGRGNISGCVPFSINDGSWHKIRVSRNKQRGVLTVDGLYSKQMTS 2943
Cdd:pfam00054 2 RTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGES 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2944 PNKAD-LLDVVGTLYVGGLPQNYITRRIGPILYSLNGCIRNLKMVGSPVG 2992
Cdd:pfam00054 82 PLGATtDLDVDGPLYVGGLPSLGVKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
3026-3177 |
1.55e-34 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 130.62 E-value: 1.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 3026 GSYFDGTGYLKAVASYRVGLDVSIALEFRTTRTNGVLLTVSNQD-KDGLGLEIVQGKLLFHVDNGAGRITAEHapdGAGF 3104
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNgGDFLALELEDGRLVLRYDLGSGSLVLSS---KTPL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1343941588 3105 CDGLWHAVTATKLRHKLELEVDGRKSRAESPNARSSTCDTNDPIYVGGYPDGVHQAGLSTKRSFKGCLKNLKI 3177
Cdd:cd00110 78 NDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKV 150
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2836-2986 |
9.05e-34 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 128.69 E-value: 9.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2836 FGLTKNSHMSFSFDDAKvRERLILEFDLRTKEQSGLVLYMARINHADFVSIQIKDGQVCLGYDLGRGNISGCVPFSINDG 2915
Cdd:cd00110 2 VSFSGSSYVRLPTLPAP-RTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1343941588 2916 SWHKIRVSRNKQRGVLTVDGLYSKQMTSPNKADLLDVVGTLYVGGLPQNYITRRIgPILYSLNGCIRNLKM 2986
Cdd:cd00110 81 QWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGL-PVSPGFVGCIRDLKV 150
|
|
| Laminin_II |
pfam06009 |
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 ... |
2091-2210 |
9.09e-34 |
|
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: 127.99 E-value: 9.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2091 VLERLGELNLRLGGLQLNYSQLDDTVSAANQMIQDPEKNIHAAGAKVKELEDEADRLLEKLQPIKMMQDN---LRRNISQ 2167
Cdd:pfam06009 15 VLEQLAPLSQNLENTSEKLSGINRSLEETNELVNDANKALDDAGRSVKKLEELAPDLLDKLKPLKQLEVNsssLSDNISR 94
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1343941588 2168 IKELINQARKQANSIKVSVSSGGDCLRSYRPDIRKGRYNTIIL 2210
Cdd:pfam06009 95 IKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTS 137
|
|
| LamG |
smart00282 |
Laminin G domain; |
2859-2988 |
2.07e-30 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 118.21 E-value: 2.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2859 LEFDLRTKEQSGLVLYMARINHADFVSIQIKDGQVCLGYDLG--RGNISGcVPFSINDGSWHKIRVSRNKQRGVLTVDGL 2936
Cdd:smart00282 2 ISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGsgPARLTS-DPTPLNDGQWHRVAVERNGRSVTLSVDGG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1343941588 2937 YSKQMTSPNKADLLDVVGTLYVGGLPQNyITRRIGPILYSLNGCIRNLKMVG 2988
Cdd:smart00282 81 NRVSGESPGGLTILNLDGPLYLGGLPED-LKLPPLPVTPGFRGCIRNLKVNG 131
|
|
| LamG |
smart00282 |
Laminin G domain; |
3048-3177 |
2.07e-30 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 118.21 E-value: 2.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 3048 SIALEFRTTRTNGVLL-TVSNQDKDGLGLEIVQGKLLFHVDNGAGRITAEHapDGAGFCDGLWHAVTATKLRHKLELEVD 3126
Cdd:smart00282 1 SISFSFRTTSPNGLLLyAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTS--DPTPLNDGQWHRVAVERNGRSVTLSVD 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1343941588 3127 GRKSRAESPNARSSTCDTNDPIYVGGYPDGVHQAGLSTKRSFKGCLKNLKI 3177
Cdd:smart00282 79 GGNRVSGESPGGLTILNLDGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKV 129
|
|
| LamB |
smart00281 |
Laminin B domain; |
527-660 |
3.34e-30 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 117.36 E-value: 3.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 527 LGSAYYWNAPGLYLGNKLTAYGGIVTFTVSYTTdqqvQNAIRVTSEPDLIIQGGGMKIIDKRFGQPvYPSSPSTSHILLL 606
Cdd:smart00281 1 DNEPVYWVAPEQFLGDKVTSYGGKLRYTLSFDG----RRGGTHVSAPDVILEGNGLRISHPAEGPP-LPDELTTVEVRFR 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1343941588 607 PENFlVSETGRPINRRDFLMVLANVTSVMVRASYSTETTAVYrLHSFSMQVASP 660
Cdd:smart00281 76 EENW-QYYGGRPVTREDLMMVLANLTAILIRATYSQQMAGSR-LSDVSLEVAVP 127
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2378-2540 |
1.20e-29 |
|
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: 116.75 E-value: 1.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2378 TVQLDGEGYASVgRPTRWNPNVSTITFKFRTFSSDALLMYMATEDMKDFMSLELSAGKVTVNFDLGSGVGKaVSAKRQ-N 2456
Cdd:cd00110 1 GVSFSGSSYVRL-PTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLV-LSSKTPlN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2457 DGRWKSLTVSRNKKQAIVTiVDidsgiaeDKIVATSQGSATGLNLRENQKIYFGGLPTignySMAARSEVTLKRYAGCLR 2536
Cdd:cd00110 79 DGQWHSVSVERNGRSVTLS-VD-------GERVVESGSPGGSALLNLDGPLYLGGLPE----DLKSPGLPVSPGFVGCIR 146
|
....
gi 1343941588 2537 DIEV 2540
Cdd:cd00110 147 DLKV 150
|
|
| LamG |
smart00282 |
Laminin G domain; |
2207-2349 |
1.92e-29 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 115.51 E-value: 1.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2207 TIILHVKTTTPDNLLFYLGSAKYVDFLALEMRKGKVNFLWDVGSGVGRLEYPSHTIHDGNWHRIEASRNGLNGTISVYPL 2286
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLNDGQWHRVAVERNGRSVTLSVDGG 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1343941588 2287 EgpmagmmptPASANSPAAFTILDVDQNayLFVGGIFNTAKKAEAVKTSTFTGCMGETFLDGK 2349
Cdd:smart00282 81 N---------RVSGESPGGLTILNLDGP--LYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2212-2352 |
2.00e-28 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 112.41 E-value: 2.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2212 VKTTTPDNLLFYLGSAKYVDFLALEMRKGKVNFLWDVGSGVGRLEYPShTIHDGNWHRIEASRNGLNGTISVYPLEgPMA 2291
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGD-KLNDGKWHSVELERNGRSGTLSVDGEA-RPT 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1343941588 2292 GMMPTPASanspaafTILDVDQNayLFVGGIFNTAKKAE-AVKTSTFTGCMGETFLDGKPIG 2352
Cdd:pfam00054 79 GESPLGAT-------TDLDVDGP--LYVGGLPSLGVKKRrLAISPSFDGCIRDVIVNGKPLD 131
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
3053-3177 |
2.22e-28 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 112.13 E-value: 2.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 3053 FRTTRTNGVLLTVSNQDKDGLGLEIVQGKLLFHVDNGAGRITAEHApdGAGFCDGLWHAVTATKLRHKLELEVDGRKSRA 3132
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDFLALELVNGRLVLRYDLGSGPESLLSS--GKNLNDGQWHSVRVERNGNTLTLSVDGQTVVS 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1343941588 3133 ESPNARSSTCDTNDPIYVGGYPDGVHQAGLSTKRSFKGCLKNLKI 3177
Cdd:pfam02210 79 SLPPGESLLLNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRV 123
|
|
| LamG |
smart00282 |
Laminin G domain; |
2401-2542 |
2.37e-28 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 112.43 E-value: 2.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2401 TITFKFRTFSSDALLMYMATEDMKDFMSLELSAGKVTVNFDLGSGVGKAVSAKRQ-NDGRWKSLTVSRNKKQAIVTiVDi 2479
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPlNDGQWHRVAVERNGRSVTLS-VD- 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1343941588 2480 dsgiAEDKIVATSQGSATGLNLreNQKIYFGGLPTignySMAARSEVTLKRYAGCLRDIEVSR 2542
Cdd:smart00282 79 ----GGNRVSGESPGGLTILNL--DGPLYLGGLPE----DLKLPPLPVTPGFRGCIRNLKVNG 131
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2406-2546 |
1.77e-27 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 109.71 E-value: 1.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2406 FRTFSSDALLMYMATEDMKDFMSLELSAGKVTVNFDLGSGVGKAVSAKRQNDGRWKSLTVSRNKKQAIVTIVDIDSGIAE 2485
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1343941588 2486 DKIVATSQGSATGlnlrenqKIYFGGLPtigNYSMAARSEVTLKRYAGCLRDIEVSRTPYN 2546
Cdd:pfam00054 81 SPLGATTDLDVDG-------PLYVGGLP---SLGVKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
3053-3177 |
6.59e-26 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 105.48 E-value: 6.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 3053 FRTTRTNGVLLTV-SNQDKDGLGLEIVQGKLLFHVDNGAGRITAEHapdGAGFCDGLWHAVTATKLRHKLELEVDGRKS- 3130
Cdd:pfam00054 1 FRTTEPSGLLLYNgTQTERDFLALELRDGRLEVSYDLGSGAAVVRS---GDKLNDGKWHSVELERNGRSGTLSVDGEARp 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1343941588 3131 RAESPNARSSTCDTNDPIYVGGYP-DGVHQAGLSTKRSFKGCLKNLKI 3177
Cdd:pfam00054 78 TGESPLGATTDLDVDGPLYVGGLPsLGVKKRRLAISPSFDGCIRDVIV 125
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2188-2347 |
8.75e-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: 105.58 E-value: 8.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2188 SGGDCLRsYRPDIRKGRYNTIILHVKTTTPDNLLFYLGSAKYVDFLALEMRKGKVNFLWDVGSGVGRLEYPSHtIHDGNW 2267
Cdd:cd00110 5 SGSSYVR-LPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTP-LNDGQW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2268 HRIEASRNGLNGTISVyplegpmagmmPTPASANSPAAFTILDVDQNAYLFVGGIFNTAKKAEAVKTSTFTGCMGETFLD 2347
Cdd:cd00110 83 HSVSVERNGRSVTLSV-----------DGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2863-2988 |
3.97e-25 |
|
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: 102.88 E-value: 3.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2863 LRTKEQSGLVLYMARINHaDFVSIQIKDGQVCLGYDLGRGNISGCV-PFSINDGSWHKIRVSRNKQRGVLTVDGLYSKQM 2941
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGS-DFLALELVNGRLVLRYDLGSGPESLLSsGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSS 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1343941588 2942 TSPNKADLLDVVGTLYVGGLPQNYITRRIgPILYSLNGCIRNLKMVG 2988
Cdd:pfam02210 80 LPPGESLLLNLNGPLYLGGLPPLLLLPAL-PVRAGFVGCIRDVRVNG 125
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2567-2735 |
1.90e-23 |
|
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: 99.03 E-value: 1.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2567 TVSFSKPGYMELGGLSL-AVDTEISLSFSTLQDNGtILLAVGGstsrqqarnpkrrrrQSGEPYLSVMLNSGSLeVLMFT 2645
Cdd:cd00110 1 GVSFSGSSYVRLPTLPApRTRLSISFSFRTTSPNG-LLLYAGS---------------QNGGDFLALELEDGRL-VLRYD 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2646 RSHSPHRITrrpDQGILNDGREHSLRIERLpGRSFAVQVDEEAKLEAALPNDQPISL--QRLFLGGIPAEVEQTSNKANV 2723
Cdd:cd00110 64 LGSGSLVLS---SKTPLNDGQWHSVSVERN-GRSVTLSVDGERVVESGSPGGSALLNldGPLYLGGLPEDLKSPGLPVSP 139
|
170
....*....|..
gi 1343941588 2724 PFQGCIWNLMVN 2735
Cdd:cd00110 140 GFVGCIRDLKVN 151
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2406-2540 |
4.92e-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: 96.72 E-value: 4.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2406 FRTFSSDALLMYMATEDmKDFMSLELSAGKVTVNFDLGSGVGKAVSAKRQ-NDGRWKSLTVSRNKKQAIVTiVDidsgia 2484
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGG-SDFLALELVNGRLVLRYDLGSGPESLLSSGKNlNDGQWHSVRVERNGNTLTLS-VD------ 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1343941588 2485 eDKIVATSQGSATGLNLRENQKIYFGGLPTIGNYSmaarSEVTLKRYAGCLRDIEV 2540
Cdd:pfam02210 73 -GQTVVSSLPPGESLLLNLNGPLYLGGLPPLLLLP----ALPVRAGFVGCIRDVRV 123
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2212-2349 |
2.08e-20 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 89.40 E-value: 2.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2212 VKTTTPDNLLFYLGSAKYvDFLALEMRKGKVNFLWDVGSGVGRLEYPSHTIHDGNWHRIEASRNGLNGTISVYPLegpma 2291
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGS-DFLALELVNGRLVLRYDLGSGPESLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQ----- 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1343941588 2292 gmmpTPASANSPAAFTILDVDQnaYLFVGGIFNTAKKAEAVKTSTFTGCMGETFLDGK 2349
Cdd:pfam02210 75 ----TVVSSLPPGESLLLNLNG--PLYLGGLPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| LamG |
smart00282 |
Laminin G domain; |
2588-2735 |
1.26e-19 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 87.39 E-value: 1.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2588 EISLSFSTLQDNGtILLAVGGSTsrqqarnpkrrrrqsGEPYLSVMLNSGSLeVLMFTRSHSPHRITrrPDQGILNDGRE 2667
Cdd:smart00282 1 SISFSFRTTSPNG-LLLYAGSKG---------------GGDYLALELRDGRL-VLRYDLGSGPARLT--SDPTPLNDGQW 61
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2668 HSLRIERLpGRSFAVQVDEEAKLEAALPNDQPISL--QRLFLGGIPAEVEQTSNKANVPFQGCIWNLMVN 2735
Cdd:smart00282 62 HRVAVERN-GRSVTLSVDGGNRVSGESPGGLTILNldGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVN 130
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2593-2735 |
1.17e-14 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 73.12 E-value: 1.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2593 FSTLQDNGTILLAvggstsrqqARNPKRrrrqsgePYLSVMLNSGSLEVLMFTRSHSPHriTRRPDQgiLNDGREHSLRI 2672
Cdd:pfam00054 1 FRTTEPSGLLLYN---------GTQTER-------DFLALELRDGRLEVSYDLGSGAAV--VRSGDK--LNDGKWHSVEL 60
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1343941588 2673 ERLpGRSFAVQVDEEAKL--EAALPNDQPISLQR-LFLGGIPAEVEQTSNKANVP-FQGCIWNLMVN 2735
Cdd:pfam00054 61 ERN-GRSGTLSVDGEARPtgESPLGATTDLDVDGpLYVGGLPSLGVKKRRLAISPsFDGCIRDVIVN 126
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2593-2735 |
3.02e-14 |
|
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: 71.68 E-value: 3.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2593 FSTLQDNGtILLAVGGSTSrqqarnpkrrrrqsgePYLSVMLNSGSLEVLMftrSHSPHRITRRPDQGILNDGREHSLRI 2672
Cdd:pfam02210 1 FRTRQPNG-LLLYAGGGGS----------------DFLALELVNGRLVLRY---DLGSGPESLLSSGKNLNDGQWHSVRV 60
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1343941588 2673 ERLpGRSFAVQVDEEAKLEAALPNDQPI--SLQRLFLGGIPAEVEQTSNKANVPFQGCIWNLMVN 2735
Cdd:pfam02210 61 ERN-GNTLTLSVDGQTVVSSLPPGESLLlnLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVN 124
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
867-913 |
1.61e-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: 64.30 E-value: 1.61e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1343941588 867 PCQCHINGSLSEVCNKESGQCPCKEDVLGRQCDKCKPSYWWDAEHPG 913
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGG 47
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1055-1098 |
1.94e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 61.17 E-value: 1.94e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1343941588 1055 CQCS---HVGNNCDANTGQCICPPNTIGERCDRCAPNHWGhDITTGC 1098
Cdd:smart00180 1 CDCDpggSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYG-DGPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
868-914 |
2.14e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 60.79 E-value: 2.14e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1343941588 868 CQCHINGSLSEVCNKESGQCPCKEDVLGRQCDKCKPSYwWDAEHPGC 914
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGY-YGDGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1055-1098 |
2.30e-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: 60.83 E-value: 2.30e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1343941588 1055 CQCSHVG---NNCDANTGQCICPPNTIGERCDRCAPNHWGHDITTGC 1098
Cdd:pfam00053 1 CDCNPHGslsDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQ 47
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1008-1052 |
4.24e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 60.02 E-value: 4.24e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1343941588 1008 CHCNSFGSKSFDCD-DLGQCRCQPGVSGPKCDRCSRGFFNFQEGGC 1052
Cdd:smart00180 1 CDCDPGGSASGTCDpDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1054-1099 |
5.01e-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: 60.06 E-value: 5.01e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1054 ACQCSHVG---NNCDANTGQCICPPNTIGERCDRCAPNHWGHDITT-GCK 1099
Cdd:cd00055 1 PCDCNGHGslsGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGgGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1007-1056 |
7.62e-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: 7.62e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1343941588 1007 PCHCNSFGSKSFDCDDL-GQCRCQPGVSGPKCDRCSRGFFNFQEGGcTACQ 1056
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGtGQCECKPNTTGRRCDRCAPGYYGLPSQG-GGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
814-866 |
9.45e-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: 59.29 E-value: 9.45e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1343941588 814 PCNCNYNLdlSVPGSCDPITGQCLkCRQGYGGAACESCADGYYGDAILAKNCQ 866
Cdd:cd00055 1 PCDCNGHG--SLSGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
366-423 |
1.23e-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: 1.23e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1343941588 366 CSCDPHGSVSQSCVADSGQatpsqpagsCWCKEGYGGPQCDRCAVGYKGFPSCERCNC 423
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQ---------CLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1460-1506 |
1.39e-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: 1.39e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1460 CQCSGHSS---TCDPETSICQnCQDNTEGDRCERCMPGFYGVVRGSSDDC 1506
Cdd:pfam00053 1 CDCNPHGSlsdTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
868-919 |
1.56e-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: 1.56e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1343941588 868 CQCHINGSLSEVCNKESGQCPCKEDVLGRQCDKCKPSYWWDaehPGCMPCRC 919
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGL---PSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
366-417 |
2.56e-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: 58.13 E-value: 2.56e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1343941588 366 CSCDPHGSVSQSCVADSGQatpsqpagsCWCKEGYGGPQCDRCAVGYKGFPS 417
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQ---------CECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1008-1055 |
3.10e-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: 57.75 E-value: 3.10e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1343941588 1008 CHCNSFGSKSFDCDDL-GQCRCQPGVSGPKCDRCSRGFFNFQEGGCTAC 1055
Cdd:pfam00053 1 CDCNPHGSLSDTCDPEtGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1101-1149 |
5.97e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 56.98 E-value: 5.97e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1343941588 1101 CGCNVVGSLSQQCNMNTGCCSCRESFRGEKCDECQIGYRDFPQCIRCEC 1149
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1147-1204 |
6.92e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 56.59 E-value: 6.92e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1343941588 1147 CECSFAGSDSQSCDMErrvcacadqTGKCSCKVNVEGSNCDRCKPDTFGLSARNPLGC 1204
Cdd:pfam00053 1 CDCNPHGSLSDTCDPE---------TGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
706-755 |
9.89e-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: 56.21 E-value: 9.89e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1343941588 706 PCRCHGHAT---QCHEITGHCLdCYHNTAGQYCDTCLPGYYGNATRGSpaDCQ 755
Cdd:cd00055 1 PCDCNGHGSlsgQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGG--GCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
707-754 |
1.20e-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: 56.21 E-value: 1.20e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1343941588 707 CRCHGHAT---QCHEITGHCLdCYHNTAGQYCDTCLPGYYGNATrGSPADC 754
Cdd:pfam00053 1 CDCNPHGSlsdTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPS-DPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
366-418 |
1.79e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 55.40 E-value: 1.79e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1343941588 366 CSCDPHGSVSQSCVADSGQatpsqpagsCWCKEGYGGPQCDRCAVGYKG--FPSC 418
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQ---------CECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1670-1956 |
6.77e-09 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 62.06 E-value: 6.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1670 ERLLQLADSNLGSLVVEMDQ------------------LHSRATKVSADGEQ--------------------VVDDSDRI 1711
Cdd:pfam15921 348 EKQLVLANSELTEARTERDQfsqesgnlddqlqklladLHKREKELSLEKEQnkrlwdrdtgnsitidhlrrELDDRNME 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1712 HRRAEDLEKFIKDTLLGAKDLQLKAAE-LNKTLSRkdgtpdksLSQMNEEIQAMLEEMRK--RQLGRMKITADEEKDLAE 1788
Cdd:pfam15921 428 VQRLEALLKAMKSECQGQMERQMAAIQgKNESLEK--------VSSLTAQLESTKEMLRKvvEELTAKKMTLESSERTVS 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1789 ELLQKVKrlfgDPHQATEDLKAEITKKLSDHDEKLQEAQDLLNEAQ-----------LKTRQAGL-----VANQNLANLT 1852
Cdd:pfam15921 500 DLTASLQ----EKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDhlrnvqteceaLKLQMAEKdkvieILRQQIENMT 575
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1853 SL--ERKRAAVSEIKEDVQkvfgesehlleeangLSNSINEELQDLEemgrELGPLHDQLDDKVRPLTGGLSD-----GS 1925
Cdd:pfam15921 576 QLvgQHGRTAGAMQVEKAQ---------------LEKEINDRRLELQ----EFKILKDKKDAKIRELEARVSDlelekVK 636
|
330 340 350
....*....|....*....|....*....|.
gi 1343941588 1926 LANSVHEAEQHAKELNESAailDNILAEAKN 1956
Cdd:pfam15921 637 LVNAGSERLRAVKDIKQER---DQLLNEVKT 664
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1460-1497 |
6.80e-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: 53.90 E-value: 6.80e-09
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1343941588 1460 CQCSGHSS---TCDPETSICQnCQDNTEGDRCERCMPGFYG 1497
Cdd:cd00055 2 CDCNGHGSlsgQCDPGTGQCE-CKPNTTGRRCDRCAPGYYG 41
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
815-870 |
1.47e-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: 53.13 E-value: 1.47e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1343941588 815 CNCNYNLdlSVPGSCDPITGQCLkCRQGYGGAACESCADGYYGDAilakNCQPCQC 870
Cdd:pfam00053 1 CDCNPHG--SLSDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLP----SDPPQGC 49
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1642-1955 |
1.85e-08 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 60.36 E-value: 1.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1642 LPPPYKVLYRFENMTDELKHMLspqKAPERLLQLADSNLGSLVVEMDQLHSRATK-VSADGEQVVDDSDRIHRRAEDLEK 1720
Cdd:COG5185 238 FQDPESELEDLAQTSDKLEKLV---EQNTDLRLEKLGENAESSKRLNENANNLIKqFENTKEKIAEYTKSIDIKKATESL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1721 fikdtllgakDLQLKAAELNKTLSRKDGTPDKSLSQMNEEIQ----AMLEEMRKRQLGRMKITADEEKDLAEELLQKVK- 1795
Cdd:COG5185 315 ----------EEQLAAAEAEQELEESKRETETGIQNLTAEIEqgqeSLTENLEAIKEEIENIVGEVELSKSSEELDSFKd 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1796 -------RLFGDPHQATE---DLKAEITKKLSDHDEKLQEAQDLLNEAqlkTRQAGLVANQNLANLTSLERKRAAVSEIK 1865
Cdd:COG5185 385 tiestkeSLDEIPQNQRGyaqEILATLEDTLKAADRQIEELQRQIEQA---TSSNEEVSKLLNELISELNKVMREADEES 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1866 edvqkvfgeSEHLLEEANGLSNSINEELQDLEEMgrelgplHDQLDDKVRPLTGGLSdGSLANSVHEAEQHAKELNESAA 1945
Cdd:COG5185 462 ---------QSRLEEAYDEINRSVRSKKEDLNEE-------LTQIESRVSTLKATLE-KLRAKLERQLEGVRSKLDQVAE 524
|
330
....*....|
gi 1343941588 1946 ILDNILAEAK 1955
Cdd:COG5185 525 SLKDFMRARG 534
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1716-1913 |
2.09e-08 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 58.77 E-value: 2.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1716 EDLEKFIKDTLLGAKDLQLKAAELN---KTLSRKDGTPDKSLSQMNEEIQAMLEEMRKR--QLGRMKITADEEKDLAEEL 1790
Cdd:COG1340 11 EELEEKIEELREEIEELKEKRDELNeelKELAEKRDELNAQVKELREEAQELREKRDELneKVKELKEERDELNEKLNEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1791 LQKVKRLF------GDPHQATEDLKAEI--------TKKLSDHDEK--LQEAQDLlnEAQLKTRQAGLVANQNLANL-TS 1853
Cdd:COG1340 91 REELDELRkelaelNKAGGSIDKLRKEIerlewrqqTEVLSPEEEKelVEKIKEL--EKELEKAKKALEKNEKLKELrAE 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1854 LERKRAAVSEIKEDVQKvfgesehLLEEANGLSNSINEELQDLEEMGRELGPLHDQLDDK 1913
Cdd:COG1340 169 LKELRKEAEEIHKKIKE-------LAEEAQELHEEMIELYKEADELRKEADELHKEIVEA 221
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1146-1204 |
2.38e-08 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 52.36 E-value: 2.38e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1343941588 1146 RCECSFAGSDSQSCDMErrvcacadqTGKCSCKVNVEGSNCDRCKPDTFGLsARNPLGC 1204
Cdd:cd00055 1 PCDCNGHGSLSGQCDPG---------TGQCECKPNTTGRRCDRCAPGYYGL-PSQGGGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
815-858 |
2.52e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 52.31 E-value: 2.52e-08
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1343941588 815 CNCNynLDLSVPGSCDPITGQCLkCRQGYGGAACESCADGYYGD 858
Cdd:smart00180 1 CDCD--PGGSASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD 41
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1651-2179 |
4.39e-08 |
|
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: 59.30 E-value: 4.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1651 RFENMTDELKHM------LSPQKAPERLLQLADSnLGSLVVEMDQLHSRATKVSADGEQVVDDSDRIHRRAEDLEKFIKD 1724
Cdd:TIGR02168 214 RYKELKAELRELelallvLRLEELREELEELQEE-LKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1725 TLLGAKDLQLKAAELNKTLsrkdgtpdKSLSQMNEEIQAMLEEMRKRQlgrmKITADEEKDLAEEL--LQKVKRLFGDPH 1802
Cdd:TIGR02168 293 LANEISRLEQQKQILRERL--------ANLERQLEELEAQLEELESKL----DELAEELAELEEKLeeLKEELESLEAEL 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1803 QATEDLKAEITKKLSDHDEKLQEAQDLLNEAQLKTRQAGLVANQNLANLTSLERKRAAVSEIKEDVQKVFGESEhlLEEA 1882
Cdd:TIGR02168 361 EELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE--LKEL 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1883 NGLSNSINEELQDLEEMGRELGPLHDQLDDKVRPLTgglsdgslaNSVHEAEQHAKELNESAAILDNILAEAKNLSFNAT 1962
Cdd:TIGR02168 439 QAELEELEEELEELQEELERLEEALEELREELEEAE---------QALDAAERELAQLQARLDSLERLQENLEGFSEGVK 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1963 AAFHAYTNIKDKIDAAekeakeakqkaSD----------ALELAMGAD-----VPVKEAAKSALQ--------KSQVL-- 2017
Cdd:TIGR02168 510 ALLKNQSGLSGILGVL-----------SElisvdegyeaAIEAALGGRlqavvVENLNAAKKAIAflkqnelgRVTFLpl 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2018 -LNKAKQLENDLRENADSMEGLKGRVKAAKDKSKDLLKAVNGTIATLNAIPNDTSAklaatkavaadanataidvLERLG 2096
Cdd:TIGR02168 579 dSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNA-------------------LELAK 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2097 ELNLR-----LGGLQLN--YSQLDDTVSAANQM------IQDPEKNIHAAGAKVKELEDEADRLLEKLQPIKMMQDNLRR 2163
Cdd:TIGR02168 640 KLRPGyrivtLDGDLVRpgGVITGGSAKTNSSIlerrreIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRK 719
|
570
....*....|....*.
gi 1343941588 2164 NISQIKELINQARKQA 2179
Cdd:TIGR02168 720 ELEELSRQISALRKDL 735
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1101-1142 |
4.86e-08 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 51.59 E-value: 4.86e-08
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1343941588 1101 CGCNVVGSLSQQCNMNTGCCSCRESFRGEKCDECQIGYRDFP 1142
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1809-2177 |
7.53e-08 |
|
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: 58.53 E-value: 7.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1809 KAEITKKLSDHDEKLQEAQDLLNE----------------------AQLKTRQAGLVANQnlanLTSLERKRAAVSEIKE 1866
Cdd:TIGR02168 174 RKETERKLERTRENLDRLEDILNElerqlkslerqaekaerykelkAELRELELALLVLR----LEELREELEELQEELK 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1867 dvqkvfgESEHLLEEangLSNSINEELQDLEEMGRELGPLHDQLDDkvrpLTGGLsdGSLANSVHEAEQHAKELNESAAI 1946
Cdd:TIGR02168 250 -------EAEEELEE---LTAELQELEEKLEELRLEVSELEEEIEE----LQKEL--YALANEISRLEQQKQILRERLAN 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1947 LDN-------ILAEAKNLSFNATAAFHAytnIKDKIDAAEKEAkeakqkasDALELAMGADVPVKEAAKSALQKSQVLLN 2019
Cdd:TIGR02168 314 LERqleeleaQLEELESKLDELAEELAE---LEEKLEELKEEL--------ESLEAELEELEAELEELESRLEELEEQLE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2020 KAKQLENDLRENADSmegLKGRVKAAKDKSKDLlkavNGTIATLNAIPNDTSAKLAATKAVAADANATAIDvlERLGELN 2099
Cdd:TIGR02168 383 TLRSKVAQLELQIAS---LNNEIERLEARLERL----EDRRERLQQEIEELLKKLEEAELKELQAELEELE--EELEELQ 453
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1343941588 2100 LRLGGLQLNYSQLDDTVSAANQMIQDPEKNIHAAGAKVKELEDeadrlleklqpikmMQDNLRRNISQIKELINQARK 2177
Cdd:TIGR02168 454 EELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLER--------------LQENLEGFSEGVKALLKNQSG 517
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1711-1953 |
8.37e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.15 E-value: 8.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1711 IHRRAEDLEKFIKDTllgaKDLQLKAAELNKTLSRKDG-TPDK------SLSQMNEEIQAMLEEMRKRqLGRMKITADEE 1783
Cdd:PRK03918 350 LEKRLEELEERHELY----EEAKAKKEELERLKKRLTGlTPEKlekeleELEKAKEEIEEEISKITAR-IGELKKEIKEL 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1784 KDLAEELlQKVK-------RLFGDPHQatEDLKAEITKKLSDHDEKLQEAQDLLNEAQ--------LKTRQAGLVANQNL 1848
Cdd:PRK03918 425 KKAIEEL-KKAKgkcpvcgRELTEEHR--KELLEEYTAELKRIEKELKEIEEKERKLRkelrelekVLKKESELIKLKEL 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1849 A-------------NLTSLERKRAAVSEIKEDVQKVFGESEHL---LEEANGLSNS---INEELQDLEEmgrELGPLHDQ 1909
Cdd:PRK03918 502 AeqlkeleeklkkyNLEELEKKAEEYEKLKEKLIKLKGEIKSLkkeLEKLEELKKKlaeLEKKLDELEE---ELAELLKE 578
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1343941588 1910 LDDK----VRPLTGGLSD--------GSLANSVHEAEQHAKELNESAAILDNILAE 1953
Cdd:PRK03918 579 LEELgfesVEELEERLKElepfyneyLELKDAEKELEREEKELKKLEEELDKAFEE 634
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1647-2188 |
8.47e-08 |
|
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: 58.53 E-value: 8.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1647 KVLYRFENMTDELKHMLspQKAPERLLQLaDSNLGSLVVEMDQLHSRATKVSADGEQVVDDSDRIHRRAEDLEKFIKDTL 1726
Cdd:TIGR02168 288 KELYALANEISRLEQQK--QILRERLANL-ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1727 LGAKDLQLKAAELNK---TLSRKDGTPDKSLSQMNEEIQAM------LEEMRKRQLGRmkiTADEEKDLAEELLQKVKRL 1797
Cdd:TIGR02168 365 AELEELESRLEELEEqleTLRSKVAQLELQIASLNNEIERLearlerLEDRRERLQQE---IEELLKKLEEAELKELQAE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1798 FGDPHQATEDLKAEitkkLSDHDEKLQEAQDLLNEAQLKTRQAGLVANQNLANLTSLERKRAAVSEIKEDVQKVFGESEH 1877
Cdd:TIGR02168 442 LEELEEELEELQEE----LERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSG 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1878 LLEEANGLSNSIN--------------EELQDL-----------------EEMGR------------------------- 1901
Cdd:TIGR02168 518 LSGILGVLSELISvdegyeaaieaalgGRLQAVvvenlnaakkaiaflkqNELGRvtflpldsikgteiqgndreilkni 597
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1902 --ELGPLHD--QLDDKVRPLTGGLSDGSL-ANSVHEAEQHAKELNESAAI--LD-------------------NILA--- 1952
Cdd:TIGR02168 598 egFLGVAKDlvKFDPKLRKALSYLLGGVLvVDDLDNALELAKKLRPGYRIvtLDgdlvrpggvitggsaktnsSILErrr 677
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1953 EAKNLSFNATAAFHAYTNIKDKIDAAEKEAKEAKQKASDALELAMGADVPVKEAAKS---ALQKSQVLLNKAKQLENDLR 2029
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDlarLEAEVEQLEERIAQLSKELT 757
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2030 ENADSMEGLKGRVkaakDKSKDLLKAVNGTIATLNAIPNDTSaklaatkavaadanataidvlERLGELNLRLGGLQLNY 2109
Cdd:TIGR02168 758 ELEAEIEELEERL----EEAEEELAEAEAEIEELEAQIEQLK---------------------EELKALREALDELRAEL 812
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1343941588 2110 SQLDDTVSAANQMIQDPEKNIHAAGAKVKELEDEADRLLEKLQpikmmqdNLRRNISQIKELINQARKQANSIKVSVSS 2188
Cdd:TIGR02168 813 TLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIE-------SLAAEIEELEELIEELESELEALLNERAS 884
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
421-467 |
8.80e-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: 50.81 E-value: 8.80e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1343941588 421 CNCSMEGSINtDPCIT---PCVCKENVEGGNCDRCKLGFYNLQHDNPRGC 467
Cdd:pfam00053 1 CDCNPHGSLS-DTCDPetgQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1686-1955 |
1.01e-07 |
|
chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.16 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1686 EMDQLHSRATKVSADGEQVVDDSDRIHRRAEDLEKFikdtllgaKDLQLKAAELNKT-LSRKDGTPDKSLSQMNEEIQAM 1764
Cdd:TIGR02169 178 ELEEVEENIERLDLIIDEKRQQLERLRREREKAERY--------QALLKEKREYEGYeLLKEKEALERQKEAIERQLASL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1765 LEEMRKRQLGRMKI--TADEEKDLAEELLQKVKRLfGDPHQAT-----EDLKAEITKKLSDHDEKLQEAQDLlnEAQLKT 1837
Cdd:TIGR02169 250 EEELEKLTEEISELekRLEEIEQLLEELNKKIKDL-GEEEQLRvkekiGELEAEIASLERSIAEKERELEDA--EERLAK 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1838 RQAGLvaNQNLANLTSLER-------KRAAVSEIKEDVQKVFGESEHLLEEANGLSNSINEELQD----LEEMGRELGPL 1906
Cdd:TIGR02169 327 LEAEI--DKLLAEIEELEReieeerkRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDyrekLEKLKREINEL 404
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1343941588 1907 ---HDQLDDKVRPLTGGLSDgsLANSVHEAEQhakELNESAAILDNILAEAK 1955
Cdd:TIGR02169 405 kreLDRLQEELQRLSEELAD--LNAAIAGIEA---KINELEEEKEDKALEIK 451
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1147-1204 |
1.12e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 50.39 E-value: 1.12e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1343941588 1147 CECSFAGSDSQSCDMErrvcacadqTGKCSCKVNVEGSNCDRCKPDTFGlsaRNPLGC 1204
Cdd:smart00180 1 CDCDPGGSASGTCDPD---------TGQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1460-1498 |
1.26e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 50.39 E-value: 1.26e-07
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1343941588 1460 CQCSG---HSSTCDPETSICQnCQDNTEGDRCERCMPGFYGV 1498
Cdd:smart00180 1 CDCDPggsASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD 41
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1678-2183 |
1.40e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.77 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1678 SNLGSLVVEMDQLHSRATKVSADGEQVVDDSDRIHRRAEDLEKFIKDTLLGAKDLQLKAAELNKTlsRKDGTPDKSLSQM 1757
Cdd:PRK03918 224 EKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKEL--KEKAEEYIKLSEF 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1758 NEEIQAMLEEMRKRqLGRMKITADEEKDLAEELLQKVKRLfgdphQATEDLKAEITKKLS----DHdEKLQEAQDLLNEA 1833
Cdd:PRK03918 302 YEEYLDELREIEKR-LSRLEEEINGIEERIKELEEKEERL-----EELKKKLKELEKRLEeleeRH-ELYEEAKAKKEEL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1834 Q-LKTRQAGLvanqnlaNLTSLERKRAAVSEIKEDVQKvfgESEHLLEEANGLSNSINEELQDLEEM----------GRE 1902
Cdd:PRK03918 375 ErLKKRLTGL-------TPEKLEKELEELEKAKEEIEE---EISKITARIGELKKEIKELKKAIEELkkakgkcpvcGRE 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1903 LGPLHDQldDKVRPLTGGLSDgsLANSVHEAEQHAKELNESAAILDNILAEAKNLSFNATAAfHAYTNIKDKIDAAEKEA 1982
Cdd:PRK03918 445 LTEEHRK--ELLEEYTAELKR--IEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELA-EQLKELEEKLKKYNLEE 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1983 KEAKQKASDALE---LAMGADVpvkEAAKSALQKSQVLLNKAKQLENDLRENADSMEGLKGRVKAAKDKSkdlLKAVNGT 2059
Cdd:PRK03918 520 LEKKAEEYEKLKeklIKLKGEI---KSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFES---VEELEER 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2060 IATLNAIPN-------------DTSAKLAATKAVAADANATAIDVLERLGELNLRLGGLQLNYSQlDDTVSAANQMIQdP 2126
Cdd:PRK03918 594 LKELEPFYNeylelkdaekeleREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE-EEYEELREEYLE-L 671
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1343941588 2127 EKNIHAAGAKVKELE---DEADRLLEKLQ-------PIKMMQDNLRRNISQIKELINQARKQANSIK 2183
Cdd:PRK03918 672 SRELAGLRAELEELEkrrEEIKKTLEKLKeeleereKAKKELEKLEKALERVEELREKVKKYKALLK 738
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1718-2178 |
2.97e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.31 E-value: 2.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1718 LEKFIKDTLLgaKDLQLKAAELNKTLSRKDGTPDKSLSQMNEEIQAMLEEM--------RKRQLGRMKITADEEKDLAEE 1789
Cdd:COG4717 39 LLAFIRAMLL--ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEeeyaelqeELEELEEELEELEAELEELRE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1790 LLQKVKRL--FGDPHQATEDLKAEI---TKKLSDHDEKLQEAQDLLN-----EAQLKTRQAGLvanQNLANLTSLErKRA 1859
Cdd:COG4717 117 ELEKLEKLlqLLPLYQELEALEAELaelPERLEELEERLEELRELEEeleelEAELAELQEEL---EELLEQLSLA-TEE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1860 AVSEIKEDVQKVFGESEHLLEEANGLSNSINEELQDLEEMGRELgplhdQLDDKVRPLTGGLSDGSLANSVHEAEQHAKE 1939
Cdd:COG4717 193 ELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL-----EAAALEERLKEARLLLLIAAALLALLGLGGS 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1940 LNESAAILDNILAeaknlSFNATAAFHAYTNIKDKIDAAEKEAKEAKQKASDALELAMGADVPVKEAAKSALQKSQV--L 2017
Cdd:COG4717 268 LLSLILTIAGVLF-----LVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELleL 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2018 LNKAKQLENDLRENADSMEGLkgRVKAAKDKSKDLLKAVN-GTIATLNAIpndtsaklaatkavaadanataidvLERLG 2096
Cdd:COG4717 343 LDRIEELQELLREAEELEEEL--QLEELEQEIAALLAEAGvEDEEELRAA-------------------------LEQAE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2097 ElnlrlgglqlnYSQLDDTVSAANQMIQDPEKNIHAAGAKV--KELEDEADRLLEKLQPIKMMQDNLRRNISQIKELINQ 2174
Cdd:COG4717 396 E-----------YQELKEELEELEEQLEELLGELEELLEALdeEELEEELEELEEELEELEEELEELREELAELEAELEQ 464
|
....
gi 1343941588 2175 ARKQ 2178
Cdd:COG4717 465 LEED 468
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1678-2183 |
3.45e-07 |
|
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: 56.34 E-value: 3.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1678 SNLGSLVVEMDQLHSRATKVSAdgeQVVDDSDRIHRRAEDLE-KFIK-----DTLLGAKD------LQLKAaELNKTLSR 1745
Cdd:pfam01576 597 SNLEKKQKKFDQMLAEEKAISA---RYAEERDRAEAEAREKEtRALSlaralEEALEAKEelertnKQLRA-EMEDLVSS 672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1746 KDGTpDKSLSQMNEEIQAM---LEEMRKrQLgrmkitadEEkdLAEELlqkvkrlfgdphQATED-----------LKAE 1811
Cdd:pfam01576 673 KDDV-GKNVHELERSKRALeqqVEEMKT-QL--------EE--LEDEL------------QATEDaklrlevnmqaLKAQ 728
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1812 ITKKLSDHDEKLQEAQDLLNEaQLKTRQAGLVAnqnlanltslERK-RAAVSEIKEDVQKVFGESEHLLEEANglsnsin 1890
Cdd:pfam01576 729 FERDLQARDEQGEEKRRQLVK-QVRELEAELED----------ERKqRAQAVAAKKKLELDLKELEAQIDAAN------- 790
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1891 eelQDLEEMGRELGPLHDQLDDKVRPLTGG-LSDGSLANSVHEAEQHAKELNESAAILDNILAEAKNLSFNATAAfhayt 1969
Cdd:pfam01576 791 ---KGREEAVKQLKKLQAQMKDLQRELEEArASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQE----- 862
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1970 niKDKIdaaekeakeakqkasdALELAMGAdvpvkeAAKSALQKSQVLLN-KAKQLENDLRENADSMEGLKGRVKaakdK 2048
Cdd:pfam01576 863 --RDEL----------------ADEIASGA------SGKSALQDEKRRLEaRIAQLEEELEEEQSNTELLNDRLR----K 914
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2049 SKDLLKAVNGTIATLNAipndTSAKLAATKAVaadanataidvLERLG-ELNLRLgglqlnySQLDDTVSAANQMiqdpe 2127
Cdd:pfam01576 915 STLQVEQLTTELAAERS----TSQKSESARQQ-----------LERQNkELKAKL-------QEMEGTVKSKFKS----- 967
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2128 kNIHAAGAKVKELEDE----------ADRLL----EKLQPIKMMQDNLRRNISQIKElinQARKQANSIK 2183
Cdd:pfam01576 968 -SIAALEAKIAQLEEQleqesrerqaANKLVrrteKKLKEVLLQVEDERRHADQYKD---QAEKGNSRMK 1033
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1731-1965 |
3.58e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 55.29 E-value: 3.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1731 DLQLKAAELNKTLSrkdgtpdKSLSQMNEEIQAMLEEMR--KRQLGRMKitadEEKDLAEELLQKVKRLFgdphQATEDL 1808
Cdd:COG4372 17 GLRPKTGILIAALS-------EQLRKALFELDKLQEELEqlREELEQAR----EELEQLEEELEQARSEL----EQLEEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1809 KAEITKKLSDHDEKLQEAQDLLNEAQLKTRQAGLVANQNLANLTSLERKRAAVSEIKEDVQKVFGESEHLLEEANGLSNS 1888
Cdd:COG4372 82 LEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLES 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1343941588 1889 INEELQDLEEmgrelgplhdqlddKVRPLTGGLSDGSLANSVHEAEQHAKELNESAAILDNILAEAKNLSFNATAAF 1965
Cdd:COG4372 162 LQEELAALEQ--------------ELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAK 224
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1743-1955 |
3.97e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.93 E-value: 3.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1743 LSRKDGTPDKSLSQMN--EEIQAMLEEMRKRQLGRMKITADEEKDLAEELLQKVKRLFGDPHQAtEDLKAEItkklsDHD 1820
Cdd:COG4717 293 LAREKASLGKEAEELQalPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREA-EELEEEL-----QLE 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1821 EKLQEAQDLLNEAQLKTRQAglvANQNLANLTSLERKRAAVSEIKEDVQKVFGESEHLLEEANGlsNSINEELQDLEEMG 1900
Cdd:COG4717 367 ELEQEIAALLAEAGVEDEEE---LRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE--EELEEELEELEEEL 441
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1343941588 1901 RELGPLHDQLDDKVRPLTGGL----SDGSLANSVHEAEQHAKELNE------SAAILDNILAEAK 1955
Cdd:COG4717 442 EELEEELEELREELAELEAELeqleEDGELAELLQELEELKAELRElaeewaALKLALELLEEAR 506
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1696-2200 |
4.08e-07 |
|
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: 56.34 E-value: 4.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1696 KVSADGeQVVDDSDRIHRRAEDLEKFIKDtllgAKDLQLKAAELNKTLSRKDgTPDKSLSQMNEEIQAMLEEMRkrqlGR 1775
Cdd:pfam01576 126 KVTTEA-KIKKLEEDILLLEDQNSKLSKE----RKLLEERISEFTSNLAEEE-EKAKSLSKLKNKHEAMISDLE----ER 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1776 MKitaDEEKDLAEelLQKVKRL----FGDPHQATEDLKAEITK---KLSDHDEKLQEAQDLLNEAQLKTRQAglvanqnL 1848
Cdd:pfam01576 196 LK---KEEKGRQE--LEKAKRKlegeSTDLQEQIAELQAQIAElraQLAKKEEELQAALARLEEETAQKNNA-------L 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1849 ANLTSLErkrAAVSEIKEDVQ-------KVFGESEHLLEEANGL---------SNSINEELQDLEEmgRELGPLHDQLDD 1912
Cdd:pfam01576 264 KKIRELE---AQISELQEDLEseraarnKAEKQRRDLGEELEALkteledtldTTAAQQELRSKRE--QEVTELKKALEE 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1913 KVRpltgglsdgslansVHEAE------QHAKELNEsaaiLDNILAEAKNLSFNATAAFHAYtnikdkidaaekeakeak 1986
Cdd:pfam01576 339 ETR--------------SHEAQlqemrqKHTQALEE----LTEQLEQAKRNKANLEKAKQAL------------------ 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1987 qkASDALELAmgADVPVKEAAKsalQKSQvllNKAKQLENDLRE-NADSMEGLKGRVKAAKDKSKdllkaVNGTIATLNA 2065
Cdd:pfam01576 383 --ESENAELQ--AELRTLQQAK---QDSE---HKRKKLEGQLQElQARLSESERQRAELAEKLSK-----LQSELESVSS 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2066 IPNDTSAKLaatkavaadanataIDVLERLGELNlrlgglqlnySQLDDTvsaaNQMIQDPEKNIHAAGAKVKELEDEAD 2145
Cdd:pfam01576 448 LLNEAEGKN--------------IKLSKDVSSLE----------SQLQDT----QELLQEETRQKLNLSTRLRQLEDERN 499
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1343941588 2146 RLLEKLQPIKMMQDNLRRNISQIKELINQARKQANSIKVSVSSGGDCLRSYRPDI 2200
Cdd:pfam01576 500 SLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQREL 554
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1711-2187 |
4.78e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.84 E-value: 4.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1711 IHRRAEDLEKFIKDT-----LLGA--KDLQLKAAELNK------TLSRKDGTPDKSLSQMnEEIQAMLEEMRKRQLGRMK 1777
Cdd:PRK03918 174 IKRRIERLEKFIKRTenieeLIKEkeKELEEVLREINEisselpELREELEKLEKEVKEL-EELKEEIEELEKELESLEG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1778 ITADEEKDLA-------------EELLQKVKRL------------FGDPHQATEDLKAEITKKLSDHDEKLQEAQDLLNE 1832
Cdd:PRK03918 253 SKRKLEEKIReleerieelkkeiEELEEKVKELkelkekaeeyikLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKE 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1833 AQLKTRQAGLVANQnlanLTSLERKraaVSEIKEDVQKvFGESEHLLEEANGLSNSI-NEELQDLEEMGRELGPLHDQLD 1911
Cdd:PRK03918 333 LEEKEERLEELKKK----LKELEKR---LEELEERHEL-YEEAKAKKEELERLKKRLtGLTPEKLEKELEELEKAKEEIE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1912 DKVRPLTGGLsdGSLANSVHE----------------------AEQHAKEL-NESAAILDNILAEAKNLsfnataafhay 1968
Cdd:PRK03918 405 EEISKITARI--GELKKEIKElkkaieelkkakgkcpvcgrelTEEHRKELlEEYTAELKRIEKELKEI----------- 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1969 TNIKDKIDAAEKEAKEAKQKASDALELAMGADvpVKEAAKSALQKSQV--LLNKAKQLENdLRENADsmeGLKGRVKAAK 2046
Cdd:PRK03918 472 EEKERKLRKELRELEKVLKKESELIKLKELAE--QLKELEEKLKKYNLeeLEKKAEEYEK-LKEKLI---KLKGEIKSLK 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2047 DKSKDlLKAVNGTIATLNaipndtsAKLAatkavaadanataiDVLERLGELNLRLGglQLNYSQLDDTvsaaNQMIQDP 2126
Cdd:PRK03918 546 KELEK-LEELKKKLAELE-------KKLD--------------ELEEELAELLKELE--ELGFESVEEL----EERLKEL 597
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1343941588 2127 EKnIHAAGAKVKELEDEADRLLEKLQPIKMMQDNLRRNISQIKELINQARKQANSIKVSVS 2187
Cdd:PRK03918 598 EP-FYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYS 657
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1101-1144 |
5.01e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 48.46 E-value: 5.01e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1343941588 1101 CGCNVVGSLSQQCNMNTGCCSCRESFRGEKCDECQIGY--RDFPQC 1144
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYygDGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1567-1604 |
5.45e-07 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 48.50 E-value: 5.45e-07
10 20 30
....*....|....*....|....*....|....*...
gi 1343941588 1567 CKCSSWGALAGPCDSVTGQCRCRVGASGTSCDQCMDRH 1604
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGY 38
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1567-1604 |
6.40e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 48.46 E-value: 6.40e-07
10 20 30
....*....|....*....|....*....|....*...
gi 1343941588 1567 CKCSSWGALAGPCDSVTGQCRCRVGASGTSCDQCMDRH 1604
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGY 38
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1652-1960 |
6.42e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 55.50 E-value: 6.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1652 FENMTDELKHMLSPQKAPERLLQLADSNLGSLVVEMDQLHSRATKVSADGEQVVDDSDRIHRRAEDLEKFIKDTLLGAKD 1731
Cdd:pfam05483 298 LEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNED 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1732 -LQLKAAELNKTLSRkdgtpdksLSQM-----NEEIQamLEEMrKRQLGRMKITADEEKD---LAEELLQKVKRLFGdPH 1802
Cdd:pfam05483 378 qLKIITMELQKKSSE--------LEEMtkfknNKEVE--LEEL-KKILAEDEKLLDEKKQfekIAEELKGKEQELIF-LL 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1803 QATE----DLKAEITKKLSDHDEKLQEAQDLLNEAQ-LKTRQAGLVANqnlANLTSLERKRAA------VSEIK---EDV 1868
Cdd:pfam05483 446 QAREkeihDLEIQLTAIKTSEEHYLKEVEDLKTELEkEKLKNIELTAH---CDKLLLENKELTqeasdmTLELKkhqEDI 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1869 QKVFGESEHLLEEANGLSNSINEELQDLEEMGRELGPLHDQLDDKVRPltgglSDGSLANSVHEAEQHAKELNESAAILD 1948
Cdd:pfam05483 523 INCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDK-----SEENARSIEYEVLKKEKQMKILENKCN 597
|
330
....*....|..
gi 1343941588 1949 NILAEAKNLSFN 1960
Cdd:pfam05483 598 NLKKQIENKNKN 609
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1730-2187 |
9.09e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 55.03 E-value: 9.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1730 KDLQLKAAELNKT---LSRKDgTPDKSLSQMNEEIQAMLEEMRKrQLGRMKITADEEKDLAEELLQKVKRLfgdPHQATE 1806
Cdd:TIGR04523 232 DNIEKKQQEINEKtteISNTQ-TQLNQLKDEQNKIKKQLSEKQK-ELEQNNKKIKELEKQLNQLKSEISDL---NNQKEQ 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1807 DLKAEITKKLSDHDEKLQEAQDLLNE-----AQLKTRQAGLVANQNLANLTSLERKRaavsEIKE---DVQKVFGESEHL 1878
Cdd:TIGR04523 307 DWNKELKSELKNQEKKLEEIQNQISQnnkiiSQLNEQISQLKKELTNSESENSEKQR----ELEEkqnEIEKLKKENQSY 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1879 LEEANGLSNSINE---ELQDLEEmgrelgpLHDQLDDKVRpltgglsdgSLANSVHEAEQHAKELneSAAILDNiLAEAK 1955
Cdd:TIGR04523 383 KQEIKNLESQINDlesKIQNQEK-------LNQQKDEQIK---------KLQQEKELLEKEIERL--KETIIKN-NSEIK 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1956 NLSFNATAAFHAYTNIKDKIDAAEKEAkeakqkasDALELAmgadvpVKEAAKSALQKSQVLLNKAKQLENDLRENADsm 2035
Cdd:TIGR04523 444 DLTNQDSVKELIIKNLDNTRESLETQL--------KVLSRS------INKIKQNLEQKQKELKSKEKELKKLNEEKKE-- 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2036 egLKGRVKAAKDKSKDLLKAVNGTIATLNAIPNDTSAKLAATKAVAADANATAIDvlERLGELNLRLGGLQLNYSQLDDT 2115
Cdd:TIGR04523 508 --LEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLE--KEIDEKNKEIEELKQTQKSLKKK 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2116 VSAANQMIQDPEKN-------IHAAGAKVKELEDEAD-------RLLEKLQPIKMMQDNLRRNISQIKELINQAR-KQAN 2180
Cdd:TIGR04523 584 QEEKQELIDQKEKEkkdlikeIEEKEKKISSLEKELEkakkeneKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRnKWPE 663
|
490
....*....|
gi 1343941588 2181 ---SIKVSVS 2187
Cdd:TIGR04523 664 iikKIKESKT 673
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
916-953 |
9.86e-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: 47.73 E-value: 9.86e-07
10 20 30
....*....|....*....|....*....|....*....
gi 1343941588 916 PCRCSPRGSIAQRCDPE-GRCTCRPGFAGSRCDQRRPSY 953
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGtGQCECKPNTTGRRCDRCAPGY 39
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
1731-1891 |
1.11e-06 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 51.83 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1731 DLQLKAAEL---NKTL-----------SRKDGTpDKSLSQM----NEEIQAMLEEMRKRQlgrmkitaDEEKDLAEELLQ 1792
Cdd:pfam15619 22 ELQSKLEELrkeNRLLkrlqkrqekalGKYEGT-ESELPQLiarhNEEVRVLRERLRRLQ--------EKERDLERKLKE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1793 KVKRLFG--DPHQATEDL--------KAEITKKLSDHDEKLQEA----QDLlnEAQLKtrqaglvanqnlanLTSLERKR 1858
Cdd:pfam15619 93 KEAELLRlrDQLKRLEKLsedknlaeREELQKKLEQLEAKLEDKdekiQDL--ERKLE--------------LENKSFRR 156
|
170 180 190
....*....|....*....|....*....|...
gi 1343941588 1859 AAVSEIKEdVQKVFGESEHLLEEANGLSNSINE 1891
Cdd:pfam15619 157 QLAAEKKK-HKEAQEEVKILQEEIERLQQKLKE 188
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1817-2210 |
1.15e-06 |
|
chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 54.69 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1817 SDHDEKLQEAQDLLNEAQLKtrqaglvanqnlanltsLERKRAAVSEIKEDVQKVFGESEHLLE-----------EANGL 1885
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEEN-----------------IERLDLIIDEKRQQLERLRREREKAERyqallkekreyEGYEL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1886 SNSINEELQDLEEMGRELGPLHDQLDDKVRpltgglsdgslansvhEAEQHAKELNESAAILDNILAEAKNLSFNATAAf 1965
Cdd:TIGR02169 229 LKEKEALERQKEAIERQLASLEEELEKLTE----------------EISELEKRLEEIEQLLEELNKKIKDLGEEEQLR- 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1966 haytnIKDKIDAAEKEAKEAKQKASDALElamgadvPVKEAAKSaLQKSQVLLNKAK----QLENDLRENADSMEGLKGR 2041
Cdd:TIGR02169 292 -----VKEKIGELEAEIASLERSIAEKER-------ELEDAEER-LAKLEAEIDKLLaeieELEREIEEERKRRDKLTEE 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2042 VKAAKDKSKDLLKAVnGTIATLNAIPNDTSAKLAatkavaadanataidvlERLGELNLRLGGLQLNYSQLDDTVSAANQ 2121
Cdd:TIGR02169 359 YAELKEELEDLRAEL-EEVDKEFAETRDELKDYR-----------------EKLEKLKREINELKRELDRLQEELQRLSE 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2122 MIQDPEKNIHAAGAKVKELEDEADRLLE-------KLQPIKMMQDNLRRNISQIKELINQARKQANSIKVSVSSGGDCLR 2194
Cdd:TIGR02169 421 ELADLNAAIAGIEAKINELEEEKEDKALeikkqewKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQAR 500
|
410
....*....|....*.
gi 1343941588 2195 SYRPDIRKGRYNTIIL 2210
Cdd:TIGR02169 501 ASEERVRGGRAVEEVL 516
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
707-749 |
1.59e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 47.31 E-value: 1.59e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1343941588 707 CRCH--GHAT-QCHEITGHCLdCYHNTAGQYCDTCLPGYYGNATRG 749
Cdd:smart00180 1 CDCDpgGSASgTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1675-2171 |
2.11e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.89 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1675 LADSNLGSLVVE-----MDQLHSRATKVSADGEQVVDDSDRIHRRAEDLEKFIKDTLLGAKDLQLKAAELNKTLSRKDGT 1749
Cdd:PRK02224 299 LAEAGLDDADAEavearREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREA 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1750 PDKSLSQMnEEIQAMLEEMRKRqLGRMKITADEEKDLAEELLQKVKRLFGDphqatedlKAEITKKLSDHDEKLQEAQDL 1829
Cdd:PRK02224 379 VEDRREEI-EELEEEIEELRER-FGDAPVDLGNAEDFLEELREERDELRER--------EAELEATLRTARERVEEAEAL 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1830 LNEAqlKTRQAGlvanQNLAN---LTSLERKRAAVSEIKEdvqkvfgESEHLLEEANGLSNSInEELQDLEEMGRELGPL 1906
Cdd:PRK02224 449 LEAG--KCPECG----QPVEGsphVETIEEDRERVEELEA-------ELEDLEEEVEEVEERL-ERAEDLVEAEDRIERL 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1907 HDQLDDKVRPLTgglsdgSLANSVHEAEQHAKELNESAAILDNiLAEAKnlsfnataafhaytnikdkidaaekeakeak 1986
Cdd:PRK02224 515 EERREDLEELIA------ERRETIEEKRERAEELRERAAELEA-EAEEK------------------------------- 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1987 qkasdalelamgadvpvKEAAKSALQKSQVLLNKAKQLENDLRENADSMEGLkGRVK---AAKDKSKDLLKAVNGTIATL 2063
Cdd:PRK02224 557 -----------------REAAAEAEEEAEEAREEVAELNSKLAELKERIESL-ERIRtllAAIADAEDEIERLREKREAL 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2064 NAIpNDTSAklaatkavaadanataidvlERLGELNLRLgglqlnySQLDDTVSAAnqmiqdpekNIHAAGAKVKELEDE 2143
Cdd:PRK02224 619 AEL-NDERR--------------------ERLAEKRERK-------RELEAEFDEA---------RIEEAREDKERAEEY 661
|
490 500 510
....*....|....*....|....*....|..
gi 1343941588 2144 ADRLLEKLQPIKMMQDNLRRNI----SQIKEL 2171
Cdd:PRK02224 662 LEQVEEKLDELREERDDLQAEIgaveNELEEL 693
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1567-1604 |
2.34e-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: 46.96 E-value: 2.34e-06
10 20 30
....*....|....*....|....*....|....*...
gi 1343941588 1567 CKCSSWGALAGPCDSVTGQCRCRVGASGTSCDQCMDRH 1604
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGY 39
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
917-953 |
2.42e-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: 2.42e-06
10 20 30
....*....|....*....|....*....|....*...
gi 1343941588 917 CRCSPRGSIAQRCDPE-GRCTCRPGFAGSRCDQRRPSY 953
Cdd:pfam00053 1 CDCNPHGSLSDTCDPEtGQCLCKPGVTGRHCDRCKPGY 38
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1670-1898 |
2.64e-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: 2.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1670 ERLLQLADSNLGSLVVEMDQLHSRATKVSADGEQVVDDSDRIHRRAEDLEKFIkdtllgaKDLQLKAAELNKTLSRKdgt 1749
Cdd:TIGR02168 795 KEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQI-------EELSEDIESLAAEIEEL--- 864
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1750 pDKSLSQMNEEIQAMLEEMRKRQLGRMKITADEEkDLAEELlqkvkrlfgdphqatedlkAEITKKLSDHDEKLQEAQDL 1829
Cdd:TIGR02168 865 -EELIEELESELEALLNERASLEEALALLRSELE-ELSEEL-------------------RELESKRSELRRELEELREK 923
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1830 LNeaQLKTRQAGLvaNQNLANLtsLERKRAAVS----EIKEDVQKVFGESEHLLEEANGLSNSIN----------EELQD 1895
Cdd:TIGR02168 924 LA--QLELRLEGL--EVRIDNL--QERLSEEYSltleEAEALENKIEDDEEEARRRLKRLENKIKelgpvnlaaiEEYEE 997
|
...
gi 1343941588 1896 LEE 1898
Cdd:TIGR02168 998 LKE 1000
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1706-1897 |
2.76e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.38 E-value: 2.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1706 DDSDRIHRRAEDLEKFIkDTLLGAKDLQLKAAELNKTLSR----KDGTPDKSLSQMNEEIQAMLEEMR---KRQLGRMKI 1778
Cdd:COG4913 235 DDLERAHEALEDAREQI-ELLEPIRELAERYAAARERLAEleylRAALRLWFAQRRLELLEAELEELRaelARLEAELER 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1779 TADEEKDLAEELLQKVKRLFGDPHQATEDLKAEItkklSDHDEKLQEAQDLLNEAQLKTRQAGLVANQNLANLTSLERK- 1857
Cdd:COG4913 314 LEARLDALREELDELEAQIRGNGGDRLEQLEREI----ERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEa 389
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1343941588 1858 ---RAAVSEIKEDVQKVFGESEHLLEEANGLSNSINEELQDLE 1897
Cdd:COG4913 390 aalLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1670-1955 |
2.93e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.40 E-value: 2.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1670 ERLLQLADSNLGSLVVEMDQLHSRATKVSADGEQVVDDSDRIHRRAEDLEKFIKDTLLGAKDLQLKAAELNKTLSRkdgt 1749
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAE---- 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1750 pdksLSQMNEEIQAMLEEMRKRQlgrmkITADEEKDLAEELLQKVKrlfgdphQATEDLKAEITKKLSDHDEKLQEAQDL 1829
Cdd:COG1196 328 ----LEEELEELEEELEELEEEL-----EEAEEELEEAEAELAEAE-------EALLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1830 LNEAQLKTRQAGLVANQNLANLTSLERKRAAVSEIKEDVQKVFGESEHLLEEANGLSNSINEELQDLEEMGRELgplhdq 1909
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL------ 465
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1343941588 1910 lddkvrpltggLSDGSLANSVHEAEQHAKELNESAAILDNILAEAK 1955
Cdd:COG1196 466 -----------AELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1753-2186 |
2.98e-06 |
|
chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.53 E-value: 2.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1753 SLSQMNEEIQAMleemrKRQLGRMKITADEEKDLAEELLQKVKrlfgDPHQATEDLKAEItKKLSDHDEKLQEAQdllne 1832
Cdd:TIGR02169 675 ELQRLRERLEGL-----KRELSSLQSELRRIENRLDELSQELS----DASRKIGEIEKEI-EQLEQEEEKLKERL----- 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1833 AQLKTRqaglvanqnlanLTSLERKRAAVSEIKEDVQKVFGESEHLLEEanglsnsINEELQDLEEMgrelgPLHDQLDD 1912
Cdd:TIGR02169 740 EELEED------------LSSLEQEIENVKSELKELEARIEELEEDLHK-------LEEALNDLEAR-----LSHSRIPE 795
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1913 KVRpltgglsdgslansvhEAEQHAKELNESAAILDNILAEAKNLSFNATAAFHAYTNIKDKIDAAekeakeakqkasda 1992
Cdd:TIGR02169 796 IQA----------------ELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDL-------------- 845
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1993 lelamgadvpvkEAAKSALQKSQVLLN--------KAKQLENDLRENADSMEGLKGRVKAAKDKSKDLLKAVNgtiaTLN 2064
Cdd:TIGR02169 846 ------------KEQIKSIEKEIENLNgkkeeleeELEELEAALRDLESRLGDLKKERDELEAQLRELERKIE----ELE 909
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2065 AipndtsaklaatkavaadanatAIDVLE-RLGELNLRLGGLQLNYSQLDDTV------SAANQMIQDPEKNIHAAGAKV 2137
Cdd:TIGR02169 910 A----------------------QIEKKRkRLSELKAKLEALEEELSEIEDPKgedeeiPEEELSLEDVQAELQRVEEEI 967
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1343941588 2138 KELE-------DEADRLLEKLQPIKMMQDNLRRNISQIKELINQARKQANSIKVSV 2186
Cdd:TIGR02169 968 RALEpvnmlaiQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREVFMEA 1023
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
917-953 |
3.59e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 46.15 E-value: 3.59e-06
10 20 30
....*....|....*....|....*....|....*...
gi 1343941588 917 CRCSPRGSIAQRCDPE-GRCTCRPGFAGSRCDQRRPSY 953
Cdd:smart00180 1 CDCDPGGSASGTCDPDtGQCECKPNVTGRRCDRCAPGY 38
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
757-812 |
5.51e-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: 45.81 E-value: 5.51e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1343941588 757 CACPlllPSNNFSPTCHLDEGgklVCnRCQMGYTGPRCERCSNGFYGQPDVPGGSC 812
Cdd:pfam00053 1 CDCN---PHGSLSDTCDPETG---QC-LCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1814-2173 |
5.58e-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: 52.37 E-value: 5.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1814 KKLSDHDEKLQEAQDLLNEAQlKTRQAGLVANQNLANLTS-----LERKRAAVSEIKEDVQKVFGESEHLLEEANGLSNS 1888
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELE-KALAELRKELEELEEELEqlrkeLEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1889 INEELQDLEEMGRELGPLHDQLddkvrpltgglsdgslansvHEAEQHAKELNESaaiLDNILAEAKNLSFNATAAFHAY 1968
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEEL--------------------AEAEAEIEELEAQ---IEQLKEELKALREALDELRAEL 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1969 TNIKDKIdaaekeakeakqkasdalelamgadvpvkeaaksalqksQVLLNKAKQLENDLRENADSMEGLkgrVKAAKDK 2048
Cdd:TIGR02168 813 TLLNEEA---------------------------------------ANLRERLESLERRIAATERRLEDL---EEQIEEL 850
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2049 SKDLLKAvNGTIATLNAIPNDTSAKLaatkavaadanataIDVLERLGELNLRLGGLQLNYSQLDDTvsaanqmiqdpek 2128
Cdd:TIGR02168 851 SEDIESL-AAEIEELEELIEELESEL--------------EALLNERASLEEALALLRSELEELSEE------------- 902
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1343941588 2129 nIHAAGAKVKELEDEADRLLEKLQPIKMMQDNLRRNISQIKELIN 2173
Cdd:TIGR02168 903 -LRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLS 946
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1686-2182 |
7.05e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 52.03 E-value: 7.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1686 EMDQLHSRATKVSADGEQVVDDSDRIHRRAEDLEKFIKdtllgakdlqlKAAELNKTLSRKDGTPDKSLSQMNEEIQAML 1765
Cdd:pfam05483 269 KANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQ-----------RSMSTQKALEEDLQIATKTICQLTEEKEAQM 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1766 EEMRKRQLGRMKITADEEKDLA--EELLQKVKRLFGDPHQATEDLKAEITKKLSDHDE----------KLQEAQDLLNEA 1833
Cdd:pfam05483 338 EELNKAKAAHSFVVTEFEATTCslEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEmtkfknnkevELEELKKILAED 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1834 QL---KTRQAGLVA------NQNLANLtsLERKRAAVSEIKEDVQKVFGESEHLLEEANGLSNSI-NEELQDLeemgrEL 1903
Cdd:pfam05483 418 EKlldEKKQFEKIAeelkgkEQELIFL--LQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELeKEKLKNI-----EL 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1904 GPLHDQLDDKVRPLTGGLSDGSLansvhEAEQHAKELNESAAILDNILAEAKNLSfnataafHAYTNIKDKIDAAEKEAK 1983
Cdd:pfam05483 491 TAHCDKLLLENKELTQEASDMTL-----ELKKHQEDIINCKKQEERMLKQIENLE-------EKEMNLRDELESVREEFI 558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1984 EAKQKASDALELAMGADVPVKEAAKSALQKSQVLLNKAKQLENDLRENADSMEGLKGRVKAAKDKSKDLLKAVNGTIATL 2063
Cdd:pfam05483 559 QKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKV 638
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2064 NaipndtsaklaatkavaadanataidvlerlgELNLRLGGLQLNYSQLDDTVSAANQMIQDPEKNIHAAGAKVKELEDE 2143
Cdd:pfam05483 639 N--------------------------------KLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADE 686
|
490 500 510
....*....|....*....|....*....|....*....
gi 1343941588 2144 AdrllEKLQpiKMMQDNLRRNISQIKELINQARKQANSI 2182
Cdd:pfam05483 687 A----VKLQ--KEIDKRCQHKIAEMVALMEKHKHQYDKI 719
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1686-1883 |
8.89e-06 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 49.37 E-value: 8.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1686 EMDQLHSRATKVSADGEQVV----DDSDRIHRRAEDLEKfIKDTLLGAkdLQLKAAELNKTLsrkdgtpdkSLSQMNEEI 1761
Cdd:cd00176 48 ELAAHEERVEALNELGEQLIeeghPDAEEIQERLEELNQ-RWEELREL--AEERRQRLEEAL---------DLQQFFRDA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1762 QAMLEEMRK--RQLGRMKITADEEKdlAEELLQKvkrlfgdpHQatedlkaEITKKLSDHDEKLQEAQDLLNEaqlktrq 1839
Cdd:cd00176 116 DDLEQWLEEkeAALASEDLGKDLES--VEELLKK--------HK-------ELEEELEAHEPRLKSLNELAEE------- 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1343941588 1840 agLVANQNLANLTSLERKRAAVSEIKEDVQKVFGESEHLLEEAN 1883
Cdd:cd00176 172 --LLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
756-813 |
1.08e-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: 45.04 E-value: 1.08e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1343941588 756 PCACPlllPSNNFSPTCHLDEGgklVCnRCQMGYTGPRCERCSNGFYGQPDVPGGsCQ 813
Cdd:cd00055 1 PCDCN---GHGSLSGQCDPGTG---QC-ECKPNTTGRRCDRCAPGYYGLPSQGGG-CQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
420-468 |
1.26e-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: 44.65 E-value: 1.26e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1343941588 420 RCNCSMEGSINTDpCITP---CVCKENVEGGNCDRCKLGFYNLQhDNPRGCE 468
Cdd:cd00055 1 PCDCNGHGSLSGQ-CDPGtgqCECKPNTTGRRCDRCAPGYYGLP-SQGGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
757-805 |
1.68e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 44.22 E-value: 1.68e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1343941588 757 CACPlllPSNNFSPTCHLDEGgklVCnRCQMGYTGPRCERCSNGFYGQP 805
Cdd:smart00180 1 CDCD---PGGSASGTCDPDTG---QC-ECKPNVTGRRCDRCAPGYYGDG 42
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
421-467 |
2.10e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 43.84 E-value: 2.10e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1343941588 421 CNCSMEGSINtDPCITP---CVCKENVEGGNCDRCKLGFYNlqhDNPRGC 467
Cdd:smart00180 1 CDCDPGGSAS-GTCDPDtgqCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
259-286 |
2.39e-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: 43.88 E-value: 2.39e-05
10 20
....*....|....*....|....*...
gi 1343941588 259 CECEHNTCGESCDRCCPGYHQQPWMAGT 286
Cdd:cd00055 21 CECKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1696-2178 |
3.31e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 50.05 E-value: 3.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1696 KVSADGEQVVDDSDRIHRRAEDLeKFIKDTLL----GAKDLQLKAAELNKTLSrkdgtpDKSLSQMNEEIQAMLEEMRKR 1771
Cdd:TIGR00606 434 EKKGLGRTIELKKEILEKKQEEL-KFVIKELQqlegSSDRILELDQELRKAER------ELSKAEKNSLTETLKKEVKSL 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1772 QLGRMKITADEEKdLAEELLQKvkrlfgDPHQATEDLKAEITKKLSDHDEKLQEAQDllNEAQLKTRQAGLVANQNLANL 1851
Cdd:TIGR00606 507 QNEKADLDRKLRK-LDQEMEQL------NHHTTTRTQMEMLTKDKMDKDEQIRKIKS--RHSDELTSLLGYFPNKKQLED 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1852 TsLERKRAAVSEIKEDVQKVFGEsehlLEEANGLSNSINEELQDLEEmgrELGPLHDQLDDKVRPLTGGLSDGSLANSVH 1931
Cdd:TIGR00606 578 W-LHSKSKEINQTRDRLAKLNKE----LASLEQNKNHINNELESKEE---QLSSYEDKLFDVCGSQDEESDLERLKEEIE 649
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1932 EAEQHAKELNESAAILDNILAEAKNLS----------FNATAAFHAYTN--------IKDKIDAAEKEAKEAKQKASDAL 1993
Cdd:TIGR00606 650 KSSKQRAMLAGATAVYSQFITQLTDENqsccpvcqrvFQTEAELQEFISdlqsklrlAPDKLKSTESELKKKEKRRDEML 729
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1994 ELAMGA----DVPVKEAaKSALQKSQVLLNKAKQLENDLRENadsmEGLKGRVKAAKDKSKDLLKAVnGTIATLNAIPND 2069
Cdd:TIGR00606 730 GLAPGRqsiiDLKEKEI-PELRNKLQKVNRDIQRLKNDIEEQ----ETLLGTIMPEEESAKVCLTDV-TIMERFQMELKD 803
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2070 TSAKLAATKAVAADanataIDVLERLGELNLRLGGLQLNYSQLDDTVSAANQMIQDPEKNIHAAGAKVKELEDEADRLLE 2149
Cdd:TIGR00606 804 VERKIAQQAAKLQG-----SDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGT 878
|
490 500 510
....*....|....*....|....*....|..
gi 1343941588 2150 KLQPIKMMQDNLRRNISQIKEL---INQARKQ 2178
Cdd:TIGR00606 879 NLQRRQQFEEQLVELSTEVQSLireIKDAKEQ 910
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
1707-1882 |
3.96e-05 |
|
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.
Pssm-ID: 403808 [Multi-domain] Cd Length: 142 Bit Score: 46.14 E-value: 3.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1707 DSDRIHRRAEDLEKfikdtllgakdlQLKAAELNKTlsrkdgtpdkslsQMNEEIQAMleeMRKRQLgrmkitADEEKDL 1786
Cdd:pfam12718 8 EAENAQERAEELEE------------KVKELEQENL-------------EKEQEIKSL---THKNQQ------LEEEVEK 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1787 AEELLQKVKRLFGDPHQATEDLKAeITKKLSDHDEKLQEAQDLLNEAQLKTRQAGLVANQnlanltsLERKRAAVSEIKE 1866
Cdd:pfam12718 54 LEEQLKEAKEKAEESEKLKTNNEN-LTRKIQLLEEELEESDKRLKETTEKLRETDVKAEH-------LERKVQALEQERD 125
|
170
....*....|....*.
gi 1343941588 1867 DVQKVFGESEHLLEEA 1882
Cdd:pfam12718 126 EWEKKYEELEEKYKEA 141
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1758-2178 |
4.01e-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: 49.67 E-value: 4.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1758 NEEIQAMLEemRKRQLGRMKITADEEKDLAEELLQKVKRLfgdphqatEDLKAEITKKLSDHDEKLQEAQDLLNEAQLKT 1837
Cdd:TIGR02168 666 AKTNSSILE--RRREIEELEEKIEELEEKIAELEKALAEL--------RKELEELEEELEQLRKELEELSRQISALRKDL 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1838 RQAGLVANQNLANLTSLERKRAAVSEIKEDVQKVFGESEHLLEEANglsnsinEELQDLEEmgrelgplhdqlddkvrpl 1917
Cdd:TIGR02168 736 ARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAE-------AEIEELEA------------------- 789
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1918 tgglsdgslansvhEAEQHAKELNESAAILDNILAEAKNLSFNATAAFHAYTNIKDKIdaaekeakeakqkasDALELAM 1997
Cdd:TIGR02168 790 --------------QIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI---------------AATERRL 840
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1998 GADVPVKEAAKSALQKSQVLLNKAKQLENDLRENADSMEGLKGRVKAAKDKSKDLLKAVNGTIATLNAIPNDTSAKLAAT 2077
Cdd:TIGR02168 841 EDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEEL 920
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2078 KavaadanataidvlERLGELNLRLGGLQLNYSQLDDTVSAANQM-IQDPEKNIHAAGAKVKELEDEADRL---LEKLQP 2153
Cdd:TIGR02168 921 R--------------EKLAQLELRLEGLEVRIDNLQERLSEEYSLtLEEAEALENKIEDDEEEARRRLKRLenkIKELGP 986
|
410 420 430
....*....|....*....|....*....|..
gi 1343941588 2154 IKMM------QDNLRRN-ISQIKELINQARKQ 2178
Cdd:TIGR02168 987 VNLAaieeyeELKERYDfLTAQKEDLTEAKET 1018
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2003-2257 |
4.56e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.75 E-value: 4.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2003 VKEAAKSALQKSQVLLNKAKQLENDLRENADSMEGLKGRVKAAKDKSKDL---LKAVNGTIATLNAIPNDTSAKLAATKA 2079
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLeeeLEELNEQLQAAQAELAQAQEELESLQE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2080 VAADANataidvlERLGELNLRLGGLQLNYSQLDDTVSAANQMIQDPEKNIHAAGAKVKELEDEADRLLEKLQpikmmQD 2159
Cdd:COG4372 109 EAEELQ-------EELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQ-----AL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2160 NLRRNISQIKELINQARKQANSIKVsvssggdcLRSYRPDIRKGRYNTIILHVKTTTPDNLLFYLGSAKYVDFLALEMRK 2239
Cdd:COG4372 177 SEAEAEQALDELLKEANRNAEKEEE--------LAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDK 248
|
250
....*....|....*...
gi 1343941588 2240 GKVNFLWDVGSGVGRLEY 2257
Cdd:COG4372 249 EELLEEVILKEIEELELA 266
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1696-1892 |
7.16e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 7.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1696 KVSADGEQVVDDSDRihRRAEDLEKFIKDTLLGAKDLQLKAAELNKT--LSRKDGTPDKSLSQMNEEiqamlEEMRKRQL 1773
Cdd:PTZ00121 1660 KIKAAEEAKKAEEDK--KKAEEAKKAEEDEKKAAEALKKEAEEAKKAeeLKKKEAEEKKKAEELKKA-----EEENKIKA 1732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1774 GRMKITADEEKDLAEELL------QKVKRLFGDPHQATEDLKAE----ITKKLSDHDEKLQEAQDLLNEaQLKTRQAGLV 1843
Cdd:PTZ00121 1733 EEAKKEAEEDKKKAEEAKkdeeekKKIAHLKKEEEKKAEEIRKEkeavIEEELDEEDEKRRMEVDKKIK-DIFDNFANII 1811
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1343941588 1844 ANQNLANLTSLERKRAAVSEIKEdvqkVFGESEHLLEEANGL------SNSINEE 1892
Cdd:PTZ00121 1812 EGGKEGNLVINDSKEMEDSAIKE----VADSKNMQLEEADAFekhkfnKNNENGE 1862
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1765-2179 |
7.80e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.50 E-value: 7.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1765 LEEMRKR----QLGRMKITADEE---KDLAEELLQKVKRlfgDPHQATEDLK---AEITKKLSDHDEKLQEAQDLLNEAQ 1834
Cdd:PRK02224 164 LEEYRERasdaRLGVERVLSDQRgslDQLKAQIEEKEEK---DLHERLNGLEselAELDEEIERYEEQREQARETRDEAD 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1835 L------KTRQAGLVANQNLANLTS----LERKRAA----VSEIKEDVQKVFGESEHLLEEAnGLSNSINEELQD-LEEM 1899
Cdd:PRK02224 241 EvleeheERREELETLEAEIEDLREtiaeTEREREElaeeVRDLRERLEELEEERDDLLAEA-GLDDADAEAVEArREEL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1900 GRELGPLHDQLDDKVRPLTGGLSDG-SLANSVHEAEQHAKELNESAAILDNILAEAKNlsfnataafhAYTNIKDKIDaa 1978
Cdd:PRK02224 320 EDRDEELRDRLEECRVAAQAHNEEAeSLREDADDLEERAEELREEAAELESELEEARE----------AVEDRREEIE-- 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1979 ekeakeakqkasdALELAMgadvpvkEAAKSALQKSQVLLNKAKQLENDLRENADsmeGLKGRVKAAKDKSKDLLKAVNG 2058
Cdd:PRK02224 388 -------------ELEEEI-------EELRERFGDAPVDLGNAEDFLEELREERD---ELREREAELEATLRTARERVEE 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2059 TIATLNAIPNDTSAKlaatkavaadanataiDV-----LERLGELNLRLGGLQLNYSQLDDTVSAANQMIQDPEKnihaa 2133
Cdd:PRK02224 445 AEALLEAGKCPECGQ----------------PVegsphVETIEEDRERVEELEAELEDLEEEVEEVEERLERAED----- 503
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1343941588 2134 gakVKELEDEADRLLEKLQPIKMMQDNLRRNISQIKELINQARKQA 2179
Cdd:PRK02224 504 ---LVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERA 546
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1650-2182 |
9.55e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 48.51 E-value: 9.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1650 YRFENMTDELKHMLSPQKAPERLLQladSNLGSLVVEMDQLHSRATKVSADGEQVVDDSDRIHRRAEDLEKFIKDTLLGA 1729
Cdd:TIGR01612 744 HIHGEINKDLNKILEDFKNKEKELS---NKINDYAKEKDELNKYKSKISEIKNHYNDQINIDNIKDEDAKQNYDKSKEYI 820
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1730 KDLQLKAAELNKTLSRKDGTPDKSLSQMNEEIQamLEEMRKRQLgrmkitaDEEKDLAEELLQKVkrlfgdphqatedlK 1809
Cdd:TIGR01612 821 KTISIKEDEIFKIINEMKFMKDDFLNKVDKFIN--FENNCKEKI-------DSEHEQFAELTNKI--------------K 877
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1810 AEIT-KKLSDHDEKLQEAQDLLNEAQLKTRQaglvANQNLANLTSLERKRAAVSEIKEDVQKVFGESEHLLEEAN----- 1883
Cdd:TIGR01612 878 AEISdDKLNDYEKKFNDSKSLINEINKSIEE----EYQNINTLKKVDEYIKICENTKESIEKFHNKQNILKEILNknidt 953
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1884 -GLSNSINEELQDleemgrelgPLHDQLDDKVRPLTGGLSDGSLanSVHEAEQhakelNESAAILDNILAeakNLSFNAT 1962
Cdd:TIGR01612 954 iKESNLIEKSYKD---------KFDNTLIDKINELDKAFKDASL--NDYEAKN-----NELIKYFNDLKA---NLGKNKE 1014
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1963 AAFHAYTNIKDKIDAAEKEAKEAKQKASDALELAMGADVpvkeaaksalqksqvlLNKAKQLENDLRENADSMeglkgrv 2042
Cdd:TIGR01612 1015 NMLYHQFDEKEKATNDIEQKIEDANKNIPNIEIAIHTSI----------------YNIIDEIEKEIGKNIELL------- 1071
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2043 kaakdkSKDLLKAVNGTIATLNAIpndtSAKLAATKAVAADANATaidvLERLGELNLRLGGLQLNYSQLDDTVSAANQM 2122
Cdd:TIGR01612 1072 ------NKEILEEAEINITNFNEI----KEKLKHYNFDDFGKEEN----IKYADEINKIKDDIKNLDQKIDHHIKALEEI 1137
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1343941588 2123 IQDPEKNIHAAGAKVKELEDEADRLL--EKLQPIKMMQDNLRRNISQIKELINQARKQANSI 2182
Cdd:TIGR01612 1138 KKKSENYIDEIKAQINDLEDVADKAIsnDDPEEIEKKIENIVTKIDKKKNIYDEIKKLLNEI 1199
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1702-2162 |
1.57e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.62 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1702 EQVVDDSDRIHRRAEDLEKFIKDtllgAKDLQLKAAELNKTLSRKDGTPDKSLSQMNEEIQAMLEEMRKRQLGRMKITAD 1781
Cdd:COG1196 330 EELEELEEELEELEEELEEAEEE----LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1782 EEKdlAEELLQKVKRLfgdpHQATEDLKAEITKKLSDHDEKLQEAQDLLNEAQLKTRQAGLVANQNLANLTSLERKRAAV 1861
Cdd:COG1196 406 EEA--EEALLERLERL----EEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAAL 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1862 SEIKEDVQKVFGESEHLLE---EANGLSNSInEELQDLEEMGRELGPLHDQLDD--KVRPLTGGLSDGSLANSVHEAEQH 1936
Cdd:COG1196 480 AELLEELAEAAARLLLLLEaeaDYEGFLEGV-KAALLLAGLRGLAGAVAVLIGVeaAYEAALEAALAAALQNIVVEDDEV 558
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1937 AKELNESAAilDNILAEAKNLSFNATAAFHAYTNIKDKIDAAEKEAKEAKQKASDALELAMGADVPVKEAAKSALQKSQV 2016
Cdd:COG1196 559 AAAAIEYLK--AAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAAL 636
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2017 LLnkAKQLENDLRENADSMEGLKGRVKAAKDKSKDLLKAvngtIATLNAIPNDTSAKLAATKAVAADANATAIDVLERLG 2096
Cdd:COG1196 637 RR--AVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAA----LLEAEAELEELAERLAEEELELEEALLAEEEEERELA 710
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2097 ELNLRLGGLQLNYSQLDDTVSAANQMIQ-----------DPEKNIHAAGAKVKELEDEADRL---LEKLQPIkmmqdNLR 2162
Cdd:COG1196 711 EAEEERLEEELEEEALEEQLEAEREELLeelleeeelleEEALEELPEPPDLEELERELERLereIEALGPV-----NLL 785
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1508-1562 |
2.27e-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: 41.19 E-value: 2.27e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1343941588 1508 PCACplpNPENNFSPTCIAEGLddyRCTaCPEGYEGKYCERCATGYHGNPRMPGG 1562
Cdd:cd00055 1 PCDC---NGHGSLSGQCDPGTG---QCE-CKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| HAUS-augmin3 |
pfam14932 |
HAUS augmin-like complex subunit 3; This domain is subunit three of the augmin complex found ... |
1782-1941 |
3.97e-04 |
|
HAUS augmin-like complex subunit 3; This domain is subunit three of the augmin complex found from Drosophila to humans. The HAUS-augmin complex is made up of eight subunits. The augmin complex interacts with gamma-TuRC, and attenuation of this interaction severely impairs spindle MT generation. Furthermore, we provide evidence that human augmin plays critical and non-redundant roles in the kinetochore-MT attachment and also central spindle formation during anaphase in human cells.The HAUS complex is required for mitotic spindle assembly and for maintenance of centrosome integrity.
Pssm-ID: 464384 [Multi-domain] Cd Length: 261 Bit Score: 45.00 E-value: 3.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1782 EEKDLAEELLQ-KVKRLFGDPHQATEDLKAEItKKLSDHDEKLQ-EAQDLLNEAQLKTRQAGLVanQNLAN-LTSLERKR 1858
Cdd:pfam14932 45 EGAALDEALKTiSAESPGLLNQQDVEALEESL-EEIREATEDLEaELQELQKTKQLKINRLNKL--QAQASsLSQGLRAL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1859 AAVSEIKEdvqkvfGESEHLLEEANGLSNSINEELQDLEEMGRELGPLHDQLDDKVRpltggLSDGSLANSVHEAEQHAK 1938
Cdd:pfam14932 122 VAEEEEAA------KQLEELQEELAALNAKTNNVLQSLQSEVKELASFFSASEPPVF-----LSQLPLEPYLLQEEQFTK 190
|
...
gi 1343941588 1939 ELN 1941
Cdd:pfam14932 191 YLT 193
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1676-1876 |
4.18e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 4.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1676 ADSNLGSLVVEMDQLHSRATKVSADGEQVVDDSDRIHRRAEDLEKFIKDTLLGAKDLQLKAAELNKTLSRKDGTPDKSLS 1755
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1756 QM---------------NEEIQAMLEemrkrQLGRMKITADEEKDLAEELLQKVKRLfgdphqatEDLKAEITKKLSDHD 1820
Cdd:COG3883 94 ALyrsggsvsyldvllgSESFSDFLD-----RLSALSKIADADADLLEELKADKAEL--------EAKKAELEAKLAELE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1343941588 1821 EKLQEAQDLLNEAQLKTRQAGLVANQNLANLTSLERKRAAVSEIKEDVQKVFGESE 1876
Cdd:COG3883 161 ALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1730-1898 |
4.52e-04 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 45.19 E-value: 4.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1730 KDLQLKAAELNKTLSRKDgTPDKSLSQMNEEIQAMLEEMRKR-QLGRMKITADEEKDLAEELLQKVKRLfgdphqATEDL 1808
Cdd:pfam15905 152 KKMSSLSMELMKLRNKLE-AKMKEVMAKQEGMEGKLQVTQKNlEHSKGKVAQLEEKLVSTEKEKIEEKS------ETEKL 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1809 KAEITK------KLSDHDEKLQEAQDLLNEAqlktrqaglvaNQNLANL-TSLERKRAAVSEIKED----VQKVFGESEH 1877
Cdd:pfam15905 225 LEYITElscvseQVEKYKLDIAQLEELLKEK-----------NDEIESLkQSLEEKEQELSKQIKDlnekCKLLESEKEE 293
|
170 180
....*....|....*....|.
gi 1343941588 1878 LLEEANGLSNSINEELQDLEE 1898
Cdd:pfam15905 294 LLREYEEKEQTLNAELEELKE 314
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1753-1915 |
6.52e-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: 43.41 E-value: 6.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1753 SLSQMNEEIQAMLEEMRKrQLGRMkitADEEKDLAEellqkvkrlfgdphQATEDLKAEITKKLSDHDEKLQEAQDLLNE 1832
Cdd:pfam01442 1 LLEDSLDELSTYAEELQE-QLGPV---AQELVDRLE--------------KETEALRERLQKDLEEVRAKLEPYLEELQA 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1833 ----------AQLKTRQAGLVAnQNLANLTSLERKraaVSEIKEDVQKVFGES-----EHLLEEANGLSNSINEELQDLE 1897
Cdd:pfam01442 63 klgqnveelrQRLEPYTEELRK-RLNADAEELQEK---LAPYGEELRERLEQNvdalrARLAPYAEELRQKLAERLEELK 138
|
170
....*....|....*....
gi 1343941588 1898 EMGRELGP-LHDQLDDKVR 1915
Cdd:pfam01442 139 ESLAPYAEeVQAQLSQRLQ 157
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
1759-1912 |
8.52e-04 |
|
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
Pssm-ID: 464788 [Multi-domain] Cd Length: 211 Bit Score: 43.50 E-value: 8.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1759 EEIQAMLEEMRKRQLgRMKITADEEKDL------AEELLQKVKRlfgDPHQA----------TED--LKAEitkklSDHD 1820
Cdd:pfam15665 25 EEIQQILAETREKIL-QYKSKIGEELDLkrriqtLEESLEQHER---MKRQAltefeqykrrVEEreLKAE-----AEHR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1821 EKLQEAQDLLNEAQlKTRQAGLVANQNLANLTSLErKRAAVSEIKEDVQKvfgESEHLLEEANGLSNSINEELQDLEEMG 1900
Cdd:pfam15665 96 QRVVELSREVEEAK-RAFEEKLESFEQLQAQFEQE-KRKALEELRAKHRQ---EIQELLTTQRAQSASSLAEQEKLEELH 170
|
170
....*....|...
gi 1343941588 1901 R-ELGPLHDQLDD 1912
Cdd:pfam15665 171 KaELESLRKEVED 183
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1688-1870 |
8.59e-04 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 44.28 E-value: 8.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1688 DQLHSRATKVSADGEQVVDDsdrihrraedLEKFIKDTLLGAKDLQLKAAELNKTLSRKDGT-PDKSLSQMNEEIQAMLE 1766
Cdd:cd22656 124 DDLLKEAKKYQDKAAKVVDK----------LTDFENQTEKDQTALETLEKALKDLLTDEGGAiARKEIKDLQKELEKLNE 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1767 EMRKRQLGRMKITADEEKDLAEElLQKVKRLFGDPHQATEDLKaEITKKLS---DHDEKLQEAQDLLNeAQLKTRQAGL- 1842
Cdd:cd22656 194 EYAAKLKAKIDELKALIADDEAK-LAAALRLIADLTAADTDLD-NLLALIGpaiPALEKLQGAWQAIA-TDLDSLKDLLe 270
|
170 180 190
....*....|....*....|....*....|..
gi 1343941588 1843 --VANQNLANLTSLERKRAAVS--EIKEDVQK 1870
Cdd:cd22656 271 ddISKIPAAILAKLELEKAIEKwnELAEKADK 302
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
259-282 |
9.17e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 39.22 E-value: 9.17e-04
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1710-1976 |
1.42e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 44.07 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1710 RIHRRAEDLEKFiKDTLlgaKDLQLkAAELNKTlsrkdgtpdKSLSqMNEEIQAMLEEMRKRQLgrmKITADE----EKD 1785
Cdd:pfam06160 7 KIYKEIDELEER-KNEL---MNLPV-QEELSKV---------KKLN-LTGETQEKFEEWRKKWD---DIVTKSlpdiEEL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1786 L--AEELLQKVKrlFgdpHQATEDLKaEITKKLSDHDEKLQEAQDLLNEaqlktrqaglvanqnlanLTSLERK-RAAVS 1862
Cdd:pfam06160 69 LfeAEELNDKYR--F---KKAKKALD-EIEELLDDIEEDIKQILEELDE------------------LLESEEKnREEVE 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1863 EIKEDVQKV----------FGESEHLLE-----------------------EANGLSNSINEELQDLEEMGRELGPLHDQ 1909
Cdd:pfam06160 125 ELKDKYRELrktllanrfsYGPAIDELEkqlaeieeefsqfeeltesgdylEAREVLEKLEEETDALEELMEDIPPLYEE 204
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1343941588 1910 LD----DKVRPLTGGLSDGSLANSVHEAEQHAKELNESAAILDNILAEAKNLSFNATAAfhAYTNIKDKID 1976
Cdd:pfam06160 205 LKtelpDQLEELKEGYREMEEEGYALEHLNVDKEIQQLEEQLEENLALLENLELDEAEE--ALEEIEERID 273
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1670-1836 |
1.44e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.99 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1670 ERLLQLA--DSNLGSLVVEMDQLHSRATKVSADGEQVVDDSDRIHRRAEDLEKFIKDTLLGAKDLQLKAAELNKTLSRkd 1747
Cdd:COG1579 7 RALLDLQelDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGN-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1748 GTPDKSLSQMNEEIQAM---LEEMRKRQLGRMKI--TADEEKDLAEELLQKVKRLFGDPHQATEDLKAEITKKLSDHDEK 1822
Cdd:COG1579 85 VRNNKEYEALQKEIESLkrrISDLEDEILELMERieELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
170
....*....|....
gi 1343941588 1823 LQEAQDLLNEAQLK 1836
Cdd:COG1579 165 REELAAKIPPELLA 178
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1760-2063 |
1.59e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.16 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1760 EIQAMLEEMRKRQLGRMKITADEEKDLAEELLQkvkrlfgdphqATEDLKAEITKKLSDHDEKLQEAQDLLNEAQLKTRQ 1839
Cdd:COG1196 217 ELKEELKELEAELLLLKLRELEAELEELEAELE-----------ELEAELEELEAELAELEAELEELRLELEELELELEE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1840 AGLVANQNLANLTSLERKRAAVSEIKEDVQKVFGESEHLLEEANGLSNSINEELQDLEEMGRELGPLHDQLDDKVRPLTG 1919
Cdd:COG1196 286 AQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1920 GLSD----------------GSLANSVHEAEQHAKELNESAAILDNILAEAKNLSFNATAAFHAYTNIKDKIDAAEKEAK 1983
Cdd:COG1196 366 ALLEaeaelaeaeeeleelaEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1984 EAKQKASDALELAMGADVPVKEA------AKSALQKSQVLLNKAKQLENDLRENADSMEGLKGRVKAAKDksKDLLKAVN 2057
Cdd:COG1196 446 EAAEEEAELEEEEEALLELLAELleeaalLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALL--LAGLRGLA 523
|
....*.
gi 1343941588 2058 GTIATL 2063
Cdd:COG1196 524 GAVAVL 529
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1657-2184 |
2.28e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.74 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1657 DELKHMLSPQKAPERLLQLADSNLGSLVVEMDQLH-----------SRATKVSADGEQVVDDSDRIHRRAEDLEKFIKDT 1725
Cdd:PRK01156 41 DAIRFALFTDKRTEKIEDMIKKGKNNLEVELEFRIgghvyqirrsiERRGKGSRREAYIKKDGSIIAEGFDDTTKYIEKN 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1726 LLG-AKDLQLkaaelNKTLSRKdGTPDKSLSQMNEEIQAMLEEMRkrQLGRMKITADEEKDLAEELLQKVKRL--FGDPH 1802
Cdd:PRK01156 121 ILGiSKDVFL-----NSIFVGQ-GEMDSLISGDPAQRKKILDEIL--EINSLERNYDKLKDVIDMLRAEISNIdyLEEKL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1803 QATEDLKAEITKKLSDHDEK----LQEAQDLLNEAQLKTRQAGLvANQNLANLTSLERKraaVSEIKEDVQKVFGESEHL 1878
Cdd:PRK01156 193 KSSNLELENIKKQIADDEKShsitLKEIERLSIEYNNAMDDYNN-LKSALNELSSLEDM---KNRYESEIKTAESDLSME 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1879 LEEANGLSnSINEELQDLE--------EMGRELGPLHDQLDDKVRPLTGglSDGSLaNSVHEAEQHAKELNESAAI---- 1946
Cdd:PRK01156 269 LEKNNYYK-ELEERHMKIIndpvyknrNYINDYFKYKNDIENKKQILSN--IDAEI-NKYHAIIKKLSVLQKDYNDyikk 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1947 ------LDNILAEAKNLSFNATAAFHAYTNIKDKIDAAEKEAKEAKQKASDALELA-MGADVPVKEAA--KSALQKSQVL 2017
Cdd:PRK01156 345 ksryddLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQeIDPDAIKKELNeiNVKLQDISSK 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2018 LNKAKQLENDLRENAD----SMEGLKGRVKA-------AKDKSKDLLKAVNGTIATLNAIPNdtsaKLAATKAVAADANA 2086
Cdd:PRK01156 425 VSSLNQRIRALRENLDelsrNMEMLNGQSVCpvcgttlGEEKSNHIINHYNEKKSRLEEKIR----EIEIEVKDIDEKIV 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 2087 TAIDVLERLGELNLRlgglqlNYSQLDDTVSAANQMIQDPEKNIhaagAKVKELEDEADRLLEKLQPIKMMQ-------- 2158
Cdd:PRK01156 501 DLKKRKEYLESEEIN------KSINEYNKIESARADLEDIKIKI----NELKDKHDKYEEIKNRYKSLKLEDldskrtsw 570
|
570 580 590
....*....|....*....|....*....|....*...
gi 1343941588 2159 ------------DNLRRNISQIKELINQARKQANSIKV 2184
Cdd:PRK01156 571 lnalavislidiETNRSRSNEIKKQLNDLESRLQEIEI 608
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1737-1920 |
2.90e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 41.73 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1737 AELNKTLSR-KDgtPDKSLSQMNEEIQAMLEEMR-------------KRQLGRMK-------------ITADEEkDLAEE 1789
Cdd:COG1842 12 ANINALLDKaED--PEKMLDQAIRDMEEDLVEARqalaqvianqkrlERQLEELEaeaekweekarlaLEKGRE-DLARE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1790 LLQKVKRLfgdpHQATEDLKAEITkKLSDHDEKLQEAQDLLNE--AQLKTRQAGLVANQNLANLTslERKRAAVSEIKED 1867
Cdd:COG1842 89 ALERKAEL----EAQAEALEAQLA-QLEEQVEKLKEALRQLESklEELKAKKDTLKARAKAAKAQ--EKVNEALSGIDSD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1343941588 1868 vqkvfgESEHLLEEANglsNSInEELQDLEEMGRELGPlHDQLDDKVRPLTGG 1920
Cdd:COG1842 162 ------DATSALERME---EKI-EEMEARAEAAAELAA-GDSLDDELAELEAD 203
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1757-1898 |
3.31e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.83 E-value: 3.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1757 MNEEIQAMLE----EMRKRQLGRMKITADEEKDLAEELLQKVKRLFGDPHQATEDLKAEITKK---LSDHDEKLQEAQDL 1829
Cdd:COG1579 2 MPEDLRALLDlqelDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLeleIEEVEARIKKYEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1830 LNEAQlKTRQAglvanQNLAN-LTSLERKRA-------AVSEIKEDVQKVFGESEHLLEEA----NGLSNSINEELQDLE 1897
Cdd:COG1579 82 LGNVR-NNKEY-----EALQKeIESLKRRISdledeilELMERIEELEEELAELEAELAELeaelEEKKAELDEELAELE 155
|
.
gi 1343941588 1898 E 1898
Cdd:COG1579 156 A 156
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1768-1976 |
4.20e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 42.90 E-value: 4.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1768 MRKRQlgRMKITADEEK-------DLAEELlQKVKRL---------FGDPHQATEDLkaeITKKLSDHDEKLQEAQDLLN 1831
Cdd:PRK04778 23 LRKRN--YKRIDELEERkqelenlPVNDEL-EKVKKLnltgqseekFEEWRQKWDEI---VTNSLPDIEEQLFEAEELND 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1832 --------------EAQLKTRQAGLVA-NQNLANLTSLERK-RAAVSEIKEDVQKV----------FGESEHLLE----- 1880
Cdd:PRK04778 97 kfrfrkakheineiESLLDLIEEDIEQiLEELQELLESEEKnREEVEQLKDLYRELrksllanrfsFGPALDELEkqlen 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1881 ------------------EANGLSNSINEELQDLEEMGRELGPLH--------DQLDDkvrpltggLSDG----SLANSV 1930
Cdd:PRK04778 177 leeefsqfveltesgdyvEAREILDQLEEELAALEQIMEEIPELLkelqtelpDQLQE--------LKAGyrelVEEGYH 248
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1343941588 1931 HEAEQHAKELNESAAILDNILAEAKNLSFNATAAfhAYTNIKDKID 1976
Cdd:PRK04778 249 LDHLDIEKEIQDLKEQIDENLALLEELDLDEAEE--KNEEIQERID 292
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1808-1976 |
5.29e-03 |
|
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: 41.20 E-value: 5.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1808 LKAEITKKLsdhdEKLQEAQDLLN----EAQLKTRQAGLVANQNLANLTSLERKRAAVSEIKEDVQKvfgESEHLLEEAN 1883
Cdd:pfam04012 9 VRANIHEGL----DKAEDPEKMLEqairDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEE---KAQAALTKGN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1884 -GLSNSINEELQDLEEMGRELGPLHDQLDDKVRPLTGGLSDgsLANSVHEAEQHAKEL--NESAAI----LDNILAEAKN 1956
Cdd:pfam04012 82 eELAREALAEKKSLEKQAEALETQLAQQRSAVEQLRKQLAA--LETKIQQLKAKKNLLkaRLKAAKaqeaVQTSLGSLST 159
|
170 180
....*....|....*....|
gi 1343941588 1957 LSfnATAAFHaytNIKDKID 1976
Cdd:pfam04012 160 SS--ATDSFE---RIEEKIE 174
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1759-1932 |
5.39e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.64 E-value: 5.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1759 EEIQAMLEEMRkRQLGRMKitaDEEKDLAEEL------LQKVK---RLFGDPHQATEDLkAEITKKLSDHDEKLQEAQDL 1829
Cdd:PRK04863 303 AAEQYRLVEMA-RELAELN---EAESDLEQDYqaasdhLNLVQtalRQQEKIERYQADL-EELEERLEEQNEVVEEADEQ 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1830 LNEAQlktrqaglvanqnlanltslERKRAAVSEIKE------DVQKVFGESE----------HLLEEANGLSNSINEEL 1893
Cdd:PRK04863 378 QEENE--------------------ARAEAAEEEVDElksqlaDYQQALDVQQtraiqyqqavQALERAKQLCGLPDLTA 437
|
170 180 190
....*....|....*....|....*....|....*....
gi 1343941588 1894 QDLEEMGRELGPLHDQLDDKVRPLTGGLSDGSLANSVHE 1932
Cdd:PRK04863 438 DNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFE 476
|
|
| VSP |
pfam03302 |
Giardia variant-specific surface protein; |
1425-1618 |
7.39e-03 |
|
Giardia variant-specific surface protein;
Pssm-ID: 146106 [Multi-domain] Cd Length: 397 Bit Score: 41.49 E-value: 7.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1425 CEECAAGFYRLRTGSAGSSSAARVPTAAGMGSCVQCQCSGHSSTCDPETSIC--QNCQDNTEGDRCERCmpgfyGVVRGS 1502
Cdd:pfam03302 93 CQACNDGFYKSGDACSPCHESCKTCSGGTASDCTECLTGKALRYGNDGTKGTcgEGCTTGTGAGACKTC-----GLTIDG 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1503 SDDCKPCACPLPNPENNF--------SPTCIAEGLDDYRCTACPEGYEgkyceRCATGYHGNPRMPGGR-CEE------C 1567
Cdd:pfam03302 168 TSYCSECATETEYPQNGVctstaaraTATCKASSVANGMCSSCANGYF-----RMNGGCYETTKFPGKSvCEEansggtC 242
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1343941588 1568 KCSSWGALAGPCDSVTGQCRCRVGASGTSCDQCMDRHVCGPAGIISCDDEC 1618
Cdd:pfam03302 243 QKEAPGYKLNNGDLVTCSPGCKTCTSNTVCTTCMDGYVKTSDSCTKCDSSC 293
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1688-1898 |
7.81e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.05 E-value: 7.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1688 DQLHSRATKVSAD---GEQVVDDSDRIHRRAEDLEKfikdtllgAKDLQLKAAELNKT---LSRKDGTPDKSlsqmnEEI 1761
Cdd:PTZ00121 1357 DEAEAAEEKAEAAekkKEEAKKKADAAKKKAEEKKK--------ADEAKKKAEEDKKKadeLKKAAAAKKKA-----DEA 1423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343941588 1762 QAMLEEMRKRQLGRMKItadEEKDLAEELLQKV---KRLFGDPHQATEDLKAEITKKLSDHDEKLQEAQDLLNEAQLKTR 1838
Cdd:PTZ00121 1424 KKKAEEKKKADEAKKKA---EEAKKADEAKKKAeeaKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKAD 1500
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1343941588 1839 QA--GLVANQNLANLTSLERKRAAvSEIKEDVQKVFGESEHLLEE---ANGLSNSinEELQDLEE 1898
Cdd:PTZ00121 1501 EAkkAAEAKKKADEAKKAEEAKKA-DEAKKAEEAKKADEAKKAEEkkkADELKKA--EELKKAEE 1562
|
|
| |
