|
Name |
Accession |
Description |
Interval |
E-value |
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
20-270 |
9.98e-93 |
|
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: 301.20 E-value: 9.98e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 20 QQRGLFPAVLNLASMADITANATCGSMGPEMFCKLVEHVpgqpVRNPQCRICNQRStkPFERHPIEYAIDGTN----RWW 95
Cdd:smart00136 3 RPRSCYPPFVNLAFGREVTATSTCGEPGPERYCKLVGHT----EQGKKCDYCDARN--PRRSHPAENLTDGNNpnnpTWW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 96 QSPSIKNGMeyHYVTITLDLKQVFQIAYVIVKAAnSPRPGNWILERSIDGVTFDPWQYYAitdTECLTRFNINPRTGPPS 175
Cdd:smart00136 77 QSEPLSNGP--QNVNLTLDLGKEFHVTYVILKFC-SPRPSLWILERSDFGKTWQPWQYFS---SDCRRTFGRPPRGPITK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 176 YTrDDEVICTSFYSKIHPLENGEIHTSLINGRPSADDP--SPTLLNFTSARYIRLVFQRIRTLNADLMtltlrdpkDIDP 253
Cdd:smart00136 151 GN-EDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDFdnSPVLQEWVTATNIRVRLTRLRTLGDELM--------DDRP 221
|
250
....*....|....*..
gi 2316002738 254 IVTRRYYYSIKDISVGG 270
Cdd:smart00136 222 EVTRRYYYAISDIAVGG 238
|
|
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
24-270 |
8.90e-87 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 283.70 E-value: 8.90e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 24 LFPAVLNLASMADITANATCGSMGPEMFCKLVEHVPGQpvrnpQCRICNqrSTKPFERHPIEYAIDGTNR----WWQSPS 99
Cdd:pfam00055 1 CYPAFGNLAFGREVSATSTCGLNGPERYCILSGLEGGK-----KCFICD--SRDPHNSHPPSNLTDSNNGtnetWWQSET 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 100 IKngMEYHYVTITLDLKQVFQIAYVIVKAAnSPRPGNWILERSID-GVTFDPWQYYAitdTECLTRFNINPRtgPPSYTR 178
Cdd:pfam00055 74 GV--IQYENVNLTLDLGKEFHFTYLILKFK-SPRPAAMVLERSTDfGKTWQPYQYFA---SDCRRTFGRPSG--PSRGIK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 179 DDEVICTSFYSKIHPLENGEIHTSLINGRPSA--DDPSPTLLNFTSARYIRLVFQRIRTLNADLMTltlrdpkdiDPIVT 256
Cdd:pfam00055 146 DDEVICTSEYSDISPLTGGEVIFSTLEGRPSAniFDYSPELQDWLTATNIRIRLLRLHTLGDELLD---------DPSVL 216
|
250
....*....|....
gi 2316002738 257 RRYYYSIKDISVGG 270
Cdd:pfam00055 217 RKYYYAISDISVGG 230
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1671-1924 |
5.46e-52 |
|
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: 184.92 E-value: 5.46e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1671 LTTPLPPPYKMLYRFENMTEELKHMLSPQKAPERLLQLADSNLGSLVVEMDQLHSRATKVSADGEQVEDDADRIHKRAED 1750
Cdd:pfam06008 7 LTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1751 LEQFIRDTLLGAKDLQSKAAELNQTLsrrDGTPDKSLKEMKEEIQAMLAEMGKRQLGGKKSIAEEEMDLAEELYQKVKRL 1830
Cdd:pfam06008 87 LAEAIKNLIDNIKEINEKVATLGEND---FALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQDLLSRIQTW 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1831 FGDPHQATEDLKAEIKGKLSDHEGKLQEAQDLLHSAQGKMKQAGSLAEQNHANLTGLERKRSAVSAVKQEAQDVLGEGER 1910
Cdd:pfam06008 164 FQSPQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEETLKTARD 243
|
250
....*....|....
gi 2316002738 1911 LLDEANQLSDNINK 1924
Cdd:pfam06008 244 SLDAANLLLQEIDD 257
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
1307-1445 |
2.78e-45 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 160.90 E-value: 2.78e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1307 YWKLPEQFRGSMITAYGGQLKYAVYYEARDETGPSSYEPQVIIKGGPNRSIMMTRHIPGLQIGQLTRHEIDMTEHEWKYA 1386
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGGGSLNSEPDVILEGNGLRLSYSSPDQPPPDPGQEQTYSVRLHEENWRDS 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2316002738 1387 DGRSMTREDFMDILFYVDYILIKASHGNLMRHSRISEISLTVAEEGRPtkeSEKAHQIE 1445
Cdd:pfam00052 81 DGAPVSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSAVPGGS---GPPASWVE 136
|
|
| Laminin_II |
pfam06009 |
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 ... |
2109-2242 |
6.93e-40 |
|
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: 145.71 E-value: 6.93e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2109 TKVVATDANATAIDVLERLGDLNLRLRGLQQNYSELEDTVNAANQMIQDPEKNIHAAGAKVKDLEDEADRLLEKLQPIKK 2188
Cdd:pfam06009 1 SKELAREANETAKEVLEQLAPLSQNLENTSEKLSGINRSLEETNELVNDANKALDDAGRSVKKLEELAPDLLDKLKPLKQ 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2316002738 2189 LQDN---LKRNISQIKELINQARKQANSIKVSVSSGGDCLRSYRPDIRKGRYNTIVL 2242
Cdd:pfam06009 81 LEVNsssLSDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTS 137
|
|
| LamB |
smart00281 |
Laminin B domain; |
1302-1431 |
1.45e-39 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 144.33 E-value: 1.45e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1302 LSEPYYWKLPEQFRGSMITAYGGQLKYAVYYEARDEtGPSSYEPQVIIKGgpNRSIMMTRHIPGLQIGQLTRHEIDMTEH 1381
Cdd:smart00281 1 DNEPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRRG-GTHVSAPDVILEG--NGLRISHPAEGPPLPDELTTVEVRFREE 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1382 EWKYADGRSMTREDFMDILFYVDYILIKASHGNLMRHSRISEISLTVAEE 1431
Cdd:smart00281 78 NWQYYGGRPVTREDLMMVLANLTAILIRATYSQQMAGSRLSDVSLEVAVP 127
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
565-705 |
9.48e-39 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 142.02 E-value: 9.48e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 565 YWNAPGLYLGNKLSAYGGSVVYTVSYTTDQQEQMAirvTSEHDLIIEGGGMKIIDGRFGQP-LYPSSPSTNHIVLLPENF 643
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGGGSL---NSEPDVILEGNGLRLSYSSPDQPpPDPGQEQTYSVRLHEENW 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2316002738 644 lVSGTEQRISRRDFLSVLANVTRVMVRASYSTEPSAVyRLHSFSMQVANPSARGErRASAVE 705
Cdd:pfam00052 78 -RDSDGAPVSREDFMMVLANLTAILIRATYSTGSGQV-SLSNVSLDSAVPGGSGP-PASWVE 136
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
3075-3226 |
1.43e-35 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 133.70 E-value: 1.43e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 3075 GTYFDGTGFLKAVSSYRVGLDVLIELEFRTSRTNGVLLAISNQA-NDGLGLELVQGKLLFHVDNGAGRITAEHMPEgegF 3153
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNgGDFLALELEDGRLVLRYDLGSGSLVLSSKTP---L 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2316002738 3154 CDGQWHAVTANKLRHRVELVVDGKQSQAESPNARSNTCDTNDPIYVGGYPHGVRQAALSTSTSFRGCMRNLKI 3226
Cdd:cd00110 78 NDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKV 150
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2908-3035 |
1.36e-34 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 130.13 E-value: 1.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2908 RTKEESGLVLYMARINHADFVSIQIKDGQVCLGYDLGHGNISGCVPFSINDGNWHKIRVSRVKQRGLLMVDGRYSKQMIS 2987
Cdd:pfam00054 2 RTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGES 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2316002738 2988 PKKAD-LLDVVGMVYVGGLPQNYTTKRIGPILYSINGCIRNLKMVGGPV 3035
Cdd:pfam00054 82 PLGATtDLDVDGPLYVGGLPSLGVKKRRLAISPSFDGCIRDVIVNGKPL 130
|
|
| LamG |
smart00282 |
Laminin G domain; |
3098-3226 |
4.74e-32 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 122.83 E-value: 4.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 3098 IELEFRTSRTNGVLLAI-SNQANDGLGLELVQGKLLFHVDNGAGRITAEHmpEGEGFCDGQWHAVTANKLRHRVELVVDG 3176
Cdd:smart00282 2 ISFSFRTTSPNGLLLYAgSKGGGDYLALELRDGRLVLRYDLGSGPARLTS--DPTPLNDGQWHRVAVERNGRSVTLSVDG 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2316002738 3177 KQSQAESPNARSNTCDTNDPIYVGGYPHGVRQAALSTSTSFRGCMRNLKI 3226
Cdd:smart00282 80 GNRVSGESPGGLTILNLDGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKV 129
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2880-3030 |
6.78e-32 |
|
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: 123.30 E-value: 6.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2880 FGLTRNSHMSFAFDDTKvRERLILEFELRTKEESGLVLYMARINHADFVSIQIKDGQVCLGYDLGHGNISGCVPFSINDG 2959
Cdd:cd00110 2 VSFSGSSYVRLPTLPAP-RTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2316002738 2960 NWHKIRVSRVKQRGLLMVDGRYSKQMISPKKADLLDVVGMVYVGGLPQNYTTKRIgPILYSINGCIRNLKM 3030
Cdd:cd00110 81 QWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGL-PVSPGFVGCIRDLKV 150
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
3102-3226 |
1.21e-31 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 121.37 E-value: 1.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 3102 FRTSRTNGVLLAISNQANDGLGLELVQGKLLFHVDNGAGRITAehMPEGEGFCDGQWHAVTANKLRHRVELVVDGKQSQA 3181
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDFLALELVNGRLVLRYDLGSGPESL--LSSGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVS 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2316002738 3182 ESPNARSNTCDTNDPIYVGGYPHGVRQAALSTSTSFRGCMRNLKI 3226
Cdd:pfam02210 79 SLPPGESLLLNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRV 123
|
|
| LamG |
smart00282 |
Laminin G domain; |
2239-2381 |
1.52e-29 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 115.90 E-value: 1.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2239 TIVLHVKTTTPDNLLFYLGSAKYVDFLALEMRKGKVNFLWDVGSGVGRVEYPHHTIHDGNWHRVEASRNGLNGTISVypl 2318
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLNDGQWHRVAVERNGRSVTLSV--- 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2316002738 2319 EGSmagmmpTPASANSPTAYTILDVDQNayLFVGGILGTVKKAEAVRTTTFTGCMGETFLDGK 2381
Cdd:smart00282 78 DGG------NRVSGESPGGLTILNLDGP--LYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| LamG |
smart00282 |
Laminin G domain; |
2903-3032 |
2.05e-29 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 115.51 E-value: 2.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2903 LEFELRTKEESGLVLYMARINHADFVSIQIKDGQVCLGYDLGHG--NISGcVPFSINDGNWHKIRVSRVKQRGLLMVDGR 2980
Cdd:smart00282 2 ISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGpaRLTS-DPTPLNDGQWHRVAVERNGRSVTLSVDGG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2316002738 2981 YSKQMISPKKADLLDVVGMVYVGGLPQNYTTKRIgPILYSINGCIRNLKMVG 3032
Cdd:smart00282 81 NRVSGESPGGLTILNLDGPLYLGGLPEDLKLPPL-PVTPGFRGCIRNLKVNG 131
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2411-2567 |
3.05e-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: 115.59 E-value: 3.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2411 VQLDGEGYAAVgRPTRWNPNVSTVTFKFRTFSSDALLMYLATEDMKDFMSLELSEGKVKVNFDLGSGVGSAISANRHNDG 2490
Cdd:cd00110 2 VSFSGSSYVRL-PTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2316002738 2491 SWKSLTMSRNKKQATVTVvdiDSSAeekiVATSQGSATGLNLKENQKIYFGGLPTIGNYRSEVTLKRYAGCLREIEV 2567
Cdd:cd00110 81 QWHSVSVERNGRSVTLSV---DGER----VVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKV 150
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2244-2384 |
3.18e-29 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 114.72 E-value: 3.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2244 VKTTTPDNLLFYLGSAKYVDFLALEMRKGKVNFLWDVGSGVGRVEYPhHTIHDGNWHRVEASRNGLNGTISVYPLEgsma 2323
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSG-DKLNDGKWHSVELERNGRSGTLSVDGEA---- 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2316002738 2324 gmmptPASANSPTAYTIlDVDQNAYLFVGGILGTVKKAE-AVRTTTFTGCMGETFLDGKPIG 2384
Cdd:pfam00054 76 -----RPTGESPLGATT-DLDVDGPLYVGGLPSLGVKKRrLAISPSFDGCIRDVIVNGKPLD 131
|
|
| LamB |
smart00281 |
Laminin B domain; |
560-693 |
6.18e-29 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 113.90 E-value: 6.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 560 LGSAYYWNAPGLYLGNKLSAYGGSVVYTVSYTTdqQEQMaiRVTSEHDLIIEGGGMKIIDgRFGQPLYPSSPSTNHIVLL 639
Cdd:smart00281 1 DNEPVYWVAPEQFLGDKVTSYGGKLRYTLSFDG--RRGG--THVSAPDVILEGNGLRISH-PAEGPPLPDELTTVEVRFR 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2316002738 640 PENFLVSGtEQRISRRDFLSVLANVTRVMVRASYStEPSAVYRLHSFSMQVANP 693
Cdd:smart00281 76 EENWQYYG-GRPVTREDLMMVLANLTAILIRATYS-QQMAGSRLSDVSLEVAVP 127
|
|
| LamG |
smart00282 |
Laminin G domain; |
2433-2569 |
1.68e-28 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 112.82 E-value: 1.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2433 TVTFKFRTFSSDALLMYLATEDMKDFMSLELSEGKVKVNFDLGSGVGSAISANRH-NDGSWKSLTMSRNKKQATVTVvdi 2511
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPlNDGQWHRVAVERNGRSVTLSV--- 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2316002738 2512 DSsaEEKIVATSQGSATGLNLKENqkIYFGGLPTIGNYRSEVTLKRYAGCLREIEVSR 2569
Cdd:smart00282 78 DG--GNRVSGESPGGLTILNLDGP--LYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNG 131
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2438-2573 |
6.43e-28 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 110.87 E-value: 6.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2438 FRTFSSDALLMYLATEDMKDFMSLELSEGKVKVNFDLGSGVGSAISANRHNDGSWKSLTMSRNKKQATVTVVDidssaEE 2517
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDG-----EA 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2316002738 2518 KIVATSQGSATGlNLKENQKIYFGGLPTIGNYRS-EVTLKRYAGCLREIEVSRTPYN 2573
Cdd:pfam00054 76 RPTGESPLGATT-DLDVDGPLYVGGLPSLGVKKRrLAISPSFDGCIRDVIVNGKPLD 131
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2220-2379 |
1.40e-26 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 107.89 E-value: 1.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2220 SGGDCLRsYRPDIRKGRYNTIVLHVKTTTPDNLLFYLGSAKYVDFLALEMRKGKVNFLWDVGSGVGRVEYPHHtIHDGNW 2299
Cdd:cd00110 5 SGSSYVR-LPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTP-LNDGQW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2300 HRVEASRNGLNGTISVyplegsmagmmPTPASANSPTAYTILDVDQNAYLFVGGILGTVKKAEAVRTTTFTGCMGETFLD 2379
Cdd:cd00110 83 HSVSVERNGRSVTLSV-----------DGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2594-2768 |
3.10e-21 |
|
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: 92.87 E-value: 3.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2594 TVSFSKPGYMELGGLSL-AVSTEISLSFSTLEDTGtILLAVSGasphsqqarntnlfsskrrrrQSGEPYLSVMLNKGSL 2672
Cdd:cd00110 1 GVSFSGSSYVRLPTLPApRTRLSISFSFRTTSPNG-LLLYAGS---------------------QNGGDFLALELEDGRL 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2673 EVLVFTGSHSPrrVIRRPEQgiLNDGKEHSLRIERLaGRSFAVQVDEEP--KREATLPNDQPISLQRIFLGGIPAEVEQT 2750
Cdd:cd00110 59 VLRYDLGSGSL--VLSSKTP--LNDGQWHSVSVERN-GRSVTLSVDGERvvESGSPGGSALLNLDGPLYLGGLPEDLKSP 133
|
170
....*....|....*...
gi 2316002738 2751 SNRVNVPFQGCIWNLMVN 2768
Cdd:cd00110 134 GLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
2615-2768 |
1.10e-18 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 84.70 E-value: 1.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2615 EISLSFSTLEDTGtILLAVSGASPHsqqarntnlfsskrrrrqsgePYLSVMLNKGSLEVLVFTGSHsprRVIRRPEQGI 2694
Cdd:smart00282 1 SISFSFRTTSPNG-LLLYAGSKGGG---------------------DYLALELRDGRLVLRYDLGSG---PARLTSDPTP 55
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2316002738 2695 LNDGKEHSLRIERLaGRSFAVQVDEEPKREATLPNDQPISL--QRIFLGGIPAEVEQTSNRVNVPFQGCIWNLMVN 2768
Cdd:smart00282 56 LNDGQWHRVAVERN-GRSVTLSVDGGNRVSGESPGGLTILNldGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVN 130
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2656-2768 |
1.67e-14 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 72.73 E-value: 1.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2656 RQSGEPYLSVMLNKGSLEVLVFTGSHsprRVIRRPEQGIlNDGKEHSLRIERLaGRSFAVQVDEE--PKREATLPNDQPI 2733
Cdd:pfam00054 15 TQTERDFLALELRDGRLEVSYDLGSG---AAVVRSGDKL-NDGKWHSVELERN-GRSGTLSVDGEarPTGESPLGATTDL 89
|
90 100 110
....*....|....*....|....*....|....*..
gi 2316002738 2734 SLQR-IFLGGIPAEVEQTSNRVNVP-FQGCIWNLMVN 2768
Cdd:pfam00054 90 DVDGpLYVGGLPSLGVKKRRLAISPsFDGCIRDVIVN 126
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1041-1085 |
9.35e-13 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 64.64 E-value: 9.35e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2316002738 1041 CHCNSFGSKSFDCD-ETGQCRCQPGVTGPKCDRCSRGFFNFQEGGC 1085
Cdd:smart00180 1 CDCDPGGSASGTCDpDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1040-1089 |
1.73e-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: 1.73e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2316002738 1040 PCHCNSFGSKSFDCD-ETGQCRCQPGVTGPKCDRCSRGFFNFQEGGcTPCQ 1089
Cdd:cd00055 1 PCDCNGHGSLSGQCDpGTGQCECKPNTTGRRCDRCAPGYYGLPSQG-GGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
900-944 |
6.86e-12 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 62.37 E-value: 6.86e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2316002738 900 PCQCHTNGSVYEVCNKETGQCPCKENVVGRQCDECMPNCWWDAER 944
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQ 45
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1703-2211 |
7.65e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.51 E-value: 7.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1703 ERLLQLADSNLGSLVVEMDQLHSRATKVSADGEQVEDDADRIHKRAEDLEQFIRDTLLGAKDLQSKAAELNQTLSRRDgt 1782
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELE-- 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1783 pdKSLKEMKEEIQAMLAEmgKRQLGGKKSIAEEEMDLAEELYQKVKRLFGDPHQATEDLKAEIKGKLSDHEGKLQEAQDL 1862
Cdd:COG1196 330 --EELEELEEELEELEEE--LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1863 LHSAQGKMKQAGSLAEQNHANLTGLERKRSAVSAVKQEAQDVLGEGERLLDEANQLSDNINKEIEDLEEMEKELGPLHVQ 1942
Cdd:COG1196 406 EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEE 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1943 LDDKVSRLTSGLSDSLADHVHDAEEHAKQLNESAAILDGILAEAKNLSFNATAAfkaytnikanvdaaekeakaakqrAN 2022
Cdd:COG1196 486 LAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAA------------------------LE 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2023 EALALALGPEVPVKE---AAQGALQKSHRL-------LNQAKQLQNDVKENADSVAGLKGRVKAARDKTKDLLKTVNGtm 2092
Cdd:COG1196 542 AALAAALQNIVVEDDevaAAAIEYLKAAKAgratflpLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLG-- 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2093 ATLSAIPNDTAAKIAATKVVATDANATAIdVLERLGDLNLRLRGLQQNYSELEDTVNAANQMIQDPEKNIHAAGAKVKDL 2172
Cdd:COG1196 620 DTLLGRTLVAARLEAALRRAVTLAGRLRE-VTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEA 698
|
490 500 510
....*....|....*....|....*....|....*....
gi 2316002738 2173 EDEADRLLEKLQPIKKLQDNLKRNISQIKELINQARKQA 2211
Cdd:COG1196 699 LLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREEL 737
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1690-2236 |
9.04e-12 |
|
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: 71.63 E-value: 9.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1690 EELKHMLSPQKAPERLLQLADSNLGSLVVEMDQLHSRATKVSADGEQVEDDADRIHKRAEDLEQFIRDTLLGAKDLQSKA 1769
Cdd:TIGR02168 309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKV 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1770 AELNQTLSRRDGTpdksLKEMKEEIQaMLAEMGKRQlggKKSIAEEEMDLAEELYQKVKRLFGDPHQATEDLKAEikgkL 1849
Cdd:TIGR02168 389 AQLELQIASLNNE----IERLEARLE-RLEDRRERL---QQEIEELLKKLEEAELKELQAELEELEEELEELQEE----L 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1850 SDHEGKLQEAQDLLHSAQGKMKQAGSLAEQNHANLTGLERKRS-------AVSAVKQEAQD------VLGE--------- 1907
Cdd:TIGR02168 457 ERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQEnlegfseGVKALLKNQSGlsgilgVLSElisvdegye 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1908 -------GERL-------LDEANQ-----------------LSDNINKEI-----EDLEEMEKELGPL--HVQLDDKVSR 1949
Cdd:TIGR02168 537 aaieaalGGRLqavvvenLNAAKKaiaflkqnelgrvtflpLDSIKGTEIqgndrEILKNIEGFLGVAkdLVKFDPKLRK 616
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1950 LTSGLSDSL--ADHVHDAEEHAKQLNESAAI--LDGILAEAKNLSFNATAAFKAYT-NIKANVDaaekeakaakqRANEA 2024
Cdd:TIGR02168 617 ALSYLLGGVlvVDDLDNALELAKKLRPGYRIvtLDGDLVRPGGVITGGSAKTNSSIlERRREIE-----------ELEEK 685
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2025 LALALGPEVPVKEAAQGALQKSHRLLNQAKQLQNDVKENADSVAGLKGRVKAAR----------DKTKDLLKTVNGTMAT 2094
Cdd:TIGR02168 686 IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEaeveqleeriAQLSKELTELEAEIEE 765
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2095 LSAIPNDTAAKIAATKVVATDANATAIDVLERLGDLNLRLRGLQQNYSELEDTVNAANQMIQDPEKNIHAAGAKVKDLED 2174
Cdd:TIGR02168 766 LEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEE 845
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2316002738 2175 EADRLLEKLQPIKKLQDNLKRNISQIKELINQARKQANSIKVSVSSGGDCLRSYRPDIRKGR 2236
Cdd:TIGR02168 846 QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE 907
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1041-1088 |
9.70e-12 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 61.99 E-value: 9.70e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2316002738 1041 CHCNSFGSKSFDCD-ETGQCRCQPGVTGPKCDRCSRGFFNFQEGGCTPC 1088
Cdd:pfam00053 1 CDCNPHGSLSDTCDpETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1087-1132 |
1.80e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 61.22 E-value: 1.80e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1087 PCQCSHVG---NNCDANTGQCICPPNTIGERCDRCAPNHWGHDITT-GCK 1132
Cdd:cd00055 1 PCDCNGHGslsGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGgGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1088-1131 |
2.15e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 60.79 E-value: 2.15e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2316002738 1088 CQCS---HVGNNCDANTGQCICPPNTIGERCDRCAPNHWGhDITTGC 1131
Cdd:smart00180 1 CDCDpggSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYG-DGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
847-899 |
2.19e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 61.22 E-value: 2.19e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2316002738 847 PCDCHGNLDLSipGSCDPSTGQCLrCRQGYGGAACDSCADGYYGDAITAKNCQ 899
Cdd:cd00055 1 PCDCNGHGSLS--GQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1088-1131 |
2.43e-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: 2.43e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2316002738 1088 CQCSHVG---NNCDANTGQCICPPNTIGERCDRCAPNHWGHDITTGC 1131
Cdd:pfam00053 1 CDCNPHGslsDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQ 47
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
901-947 |
2.59e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 60.79 E-value: 2.59e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2316002738 901 CQCHTNGSVYEVCNKETGQCPCKENVVGRQCDECMPNcWWDAERQEC 947
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPG-YYGDGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1493-1539 |
2.79e-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: 2.79e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1493 CQCSGHSS---TCDPETSICQnCQDNTEGDRCERCSPGFYGVVRGSPDDC 1539
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. |
1180-1237 |
3.67e-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: 60.44 E-value: 3.67e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2316002738 1180 CECNVSGSDSETCDMErgvcacadrTGKCSCKANVEGHNCDRCKPDTFGLSVRNPLGC 1237
Cdd:pfam00053 1 CDCNPHGSLSDTCDPE---------TGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
901-939 |
5.31e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 60.06 E-value: 5.31e-11
10 20 30
....*....|....*....|....*....|....*....
gi 2316002738 901 CQCHTNGSVYEVCNKETGQCPCKENVVGRQCDECMPNCW 939
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYY 39
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
739-788 |
8.46e-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: 8.46e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2316002738 739 ACHCHGHAT---QCHEVTGHCLdCSHHTTGPHCDTCLHGYYGNATRGSpaDCQ 788
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. |
740-787 |
3.09e-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: 3.09e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2316002738 740 CHCHGHAT---QCHEVTGHCLdCSHHTTGPHCDTCLHGYYGNATrGSPADC 787
Cdd:pfam00053 1 CDCNPHGSlsdTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPS-DPPQGC 49
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1722-2062 |
5.21e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.85 E-value: 5.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1722 QLHSRATKVSADGEQV-----------EDDADRIHKRAE--DLEQFIrdtllgaKDLQSKAAELNQTLsrrdgtpdKSLK 1788
Cdd:TIGR02168 640 KLRPGYRIVTLDGDLVrpggvitggsaKTNSSILERRREieELEEKI-------EELEEKIAELEKAL--------AELR 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1789 EMKEEIQAMLAEMGKRQLGGKKSIAEEEMDLA--EELYQKVKRLFGDPHQATEDLKAEIKG---KLSDHEGKLQEAQDLL 1863
Cdd:TIGR02168 705 KELEELEEELEQLRKELEELSRQISALRKDLArlEAEVEQLEERIAQLSKELTELEAEIEEleeRLEEAEEELAEAEAEI 784
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1864 HSAQGKMKQAGSLAEQN------------------HANLTGLERKRSAVSAVKQEAQDVLGEGERLLDEANQLSDNINKE 1925
Cdd:TIGR02168 785 EELEAQIEQLKEELKALrealdelraeltllneeaANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEL 864
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1926 IEDLEEMEKELGPLHVQLDDKVSRLTSGLS--DSLADHVHDAEEHAKQLNESAAILDGILAEAKNlsfnataafkAYTNI 2003
Cdd:TIGR02168 865 EELIEELESELEALLNERASLEEALALLRSelEELSEELRELESKRSELRRELEELREKLAQLEL----------RLEGL 934
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2316002738 2004 KANVDaaekeakAAKQRANEALALALGPEVPVKEAAQGALQKSHRllnQAKQLQNDVKE 2062
Cdd:TIGR02168 935 EVRID-------NLQERLSEEYSLTLEEAEALENKIEDDEEEARR---RLKRLENKIKE 983
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
848-903 |
1.19e-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: 1.19e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2316002738 848 CDCHGNLDLSipGSCDPSTGQCLrCRQGYGGAACDSCADGYYGDAITAkncqPCQC 903
Cdd:pfam00053 1 CDCNPHGSLS--DTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSDP----PQGC 49
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1690-2206 |
3.01e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 63.14 E-value: 3.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1690 EELKHMLSPQKapERLLQLADsnlgslvvEMDQLHSRATKVSADGEQVEDDADRIHKRAEDLEQFIRDTLLGAKDLQSKA 1769
Cdd:PRK02224 275 EELAEEVRDLR--ERLEELEE--------ERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEA 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1770 ---AELNQTLSRRDGTPDKSLKEMKEEIQAMLAEMGKRQlgGKKSIAEEEMDLAEELYQKVKRLFGDPHQATEDL---KA 1843
Cdd:PRK02224 345 eslREDADDLEERAEELREEAAELESELEEAREAVEDRR--EEIEELEEEIEELRERFGDAPVDLGNAEDFLEELreeRD 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1844 EIKGKLSDHEGKLQEAQDLLHSAQ-----GKMKQAG-SLAEQNHANltGLERKRSAVSAVKQEAQDVLGEGERLLDEANQ 1917
Cdd:PRK02224 423 ELREREAELEATLRTARERVEEAEalleaGKCPECGqPVEGSPHVE--TIEEDRERVEELEAELEDLEEEVEEVEERLER 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1918 LsdninkeiEDLEEMEKELGplhvQLDDKVSRLTSGLSDSlADHVHDAEEHAKQLNESAAILDgilAEAKNLSFNATAAf 1997
Cdd:PRK02224 501 A--------EDLVEAEDRIE----RLEERREDLEELIAER-RETIEEKRERAEELRERAAELE---AEAEEKREAAAEA- 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1998 kaytnikanvdaaekeakaaKQRANEALAlalgpEVPVKEAAQGALQKSHRLLNQAKQLQNDVKENADSVAGLKGRVKA- 2076
Cdd:PRK02224 564 --------------------EEEAEEARE-----EVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREAl 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2077 --ARDKTKDLLKTVNGTMATLsaipndtAAKIAATKVVATDAN-ATAIDVLERLGDlnlRLRGLQQNYSELEDTVNAANQ 2153
Cdd:PRK02224 619 aeLNDERRERLAEKRERKREL-------EAEFDEARIEEAREDkERAEEYLEQVEE---KLDELREERDDLQAEIGAVEN 688
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2316002738 2154 MIQDPEknihaagakvkDLEDEADRLLEKLQPIKKLQDNL---------------KRNISQIKELINQ 2206
Cdd:PRK02224 689 ELEELE-----------ELRERREALENRVEALEALYDEAeelesmygdlraelrQRNVETLERMLNE 745
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
398-449 |
3.15e-09 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 55.05 E-value: 3.15e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2316002738 398 PCTCDPHGSVSQSCVADSsqatptqpaGSCRCKEGFGGLQCDRCAVGYMGYP 449
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGT---------GQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1493-1540 |
7.04e-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: 7.04e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2316002738 1493 CQCSGHSS---TCDPETSICQnCQDNTEGDRCERCSPGFYGvVRGSPDDCK 1540
Cdd:cd00055 2 CDCNGHGSlsgQCDPGTGQCE-CKPNTTGRRCDRCAPGYYG-LPSQGGGCQ 50
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1703-1987 |
9.25e-09 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 61.77 E-value: 9.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1703 ERLLQLADSNLGSLV----VEMDQLHSRATKvsaDGEQVEDDADRIHKRAEDLEQFIRDTLLGAKD-LQSKAAELNQTLS 1777
Cdd:NF041483 188 ERLAEEARQRLGSEAesarAEAEAILRRARK---DAERLLNAASTQAQEATDHAEQLRSSTAAESDqARRQAAELSRAAE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1778 RRDGTPDKSLKEMKEEIQAMLAEM---GKRQLGGKKSIAEEEMDLAEElyqKVKRLFGDPHQATEDLKAEIKGKLSDHEG 1854
Cdd:NF041483 265 QRMQEAEEALREARAEAEKVVAEAkeaAAKQLASAESANEQRTRTAKE---EIARLVGEATKEAEALKAEAEQALADARA 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1855 klqEAQDLLHSAQGKMKQAGslAEQNHANLTGLERK------------RSAVSAVKQEAQDVLGEGE----RLLDEANQL 1918
Cdd:NF041483 342 ---EAEKLVAEAAEKARTVA--AEDTAAQLAKAARTaeevltkasedaKATTRAAAEEAERIRREAEaeadRLRGEAADQ 416
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2316002738 1919 SDNINKEIEDleeMEKELGPLHVQLDDKVSRLtSGLSDSL-ADHVHDAE--------EHAKQLNESAAILDGILAEAK 1987
Cdd:NF041483 417 AEQLKGAAKD---DTKEYRAKTVELQEEARRL-RGEAEQLrAEAVAEGErirgearrEAVQQIEEAARTAEELLTKAK 490
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
399-456 |
1.22e-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: 1.22e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2316002738 399 CTCDPHGSVSQSCvaDSSQatptqpaGSCRCKEGFGGLQCDRCAVGYMGYPFCQRCNC 456
Cdd:pfam00053 1 CDCNPHGSLSDTC--DPET-------GQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1134-1182 |
1.63e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 52.74 E-value: 1.63e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2316002738 1134 CGCSVIGSVTQQCNVNTGCCLCRDSFRGEKCNECQIGYRDFPQCTQCEC 1182
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1180-1237 |
1.65e-08 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 52.74 E-value: 1.65e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2316002738 1180 CECNVSGSDSETCDMErgvcacadrTGKCSCKANVEGHNCDRCKPDTFGLSvRNPLGC 1237
Cdd:cd00055 2 CDCNGHGSLSGQCDPG---------TGQCECKPNTTGRRCDRCAPGYYGLP-SQGGGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1180-1237 |
2.08e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 52.31 E-value: 2.08e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2316002738 1180 CECNVSGSDSETCDMErgvcacadrTGKCSCKANVEGHNCDRCKPDTFGlsvRNPLGC 1237
Cdd:smart00180 1 CDCDPGGSASGTCDPD---------TGQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
848-891 |
2.13e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 52.31 E-value: 2.13e-08
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2316002738 848 CDCHgnLDLSIPGSCDPSTGQCLrCRQGYGGAACDSCADGYYGD 891
Cdd:smart00180 1 CDCD--PGGSASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD 41
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2035-2289 |
2.50e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 59.15 E-value: 2.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2035 VKEAAQGALQKSHRLLNQAKQLQNDVKENADSVAGLKGRVKAAR---DKTKDLLKTVNGTMATLSAIPNDTAAKIAATKv 2111
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARselEQLEEELEELNEQLQAAQAELAQAQEELESLQ- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2112 vatdanataidvlERLGDLNLRLRGLQQNYSELEDTVNAANQMIQDPEKNIHAAGAKVKDLEDEADRLLEKLQPIKKLQD 2191
Cdd:COG4372 108 -------------EEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2192 NLKRN--ISQIKELINQARKQANSIKVsvssggdcLRSYRPDIRKGRYNTIVLHVKTTTPDNLLFYLGSAKYVDFLALEM 2269
Cdd:COG4372 175 ALSEAeaEQALDELLKEANRNAEKEEE--------LAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEE 246
|
250 260
....*....|....*....|
gi 2316002738 2270 RKGKVNFLWDVGSGVGRVEY 2289
Cdd:COG4372 247 DKEELLEEVILKEIEELELA 266
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
740-782 |
3.83e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 51.93 E-value: 3.83e-08
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2316002738 740 CHCHGHAT-QCHEVTGHCLdCSHHTTGPHCDTCLHGYYGNATRG 782
Cdd:smart00180 3 CDPGGSASgTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1493-1539 |
7.67e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 50.77 E-value: 7.67e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1493 CQCSG---HSSTCDPETSICQnCQDNTEGDRCERCSPGFYGVvrgSPDDC 1539
Cdd:smart00180 1 CDCDPggsASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD---GPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
454-500 |
9.95e-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: 9.95e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2316002738 454 CNCSVEGSTNaDPCIT---PCMCKENVEGENCDRCKLGFYNLQGDNQRGC 500
Cdd:pfam00053 1 CDCNPHGSLS-DTCDPetgQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1751-2084 |
1.33e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 56.83 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1751 LEQFIRDTLLGAKDLQSKAAELNQTLSRRDG---TPDKSLKEMKEEIQAMLAEMGKRQ-----LGGKKSIAEEEMdlaEE 1822
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREeleQLEEELEQARSELEQLEEELEELNeqlqaAQAELAQAQEEL---ES 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1823 LYQKVKRLfgdpHQATEDLKAEIKgKLSDHEGKLQEAQDLLhsaQGKMKQAGSLAEQNHANLTGLERKRSAVSAVKQ--E 1900
Cdd:COG4372 106 LQEEAEEL----QEELEELQKERQ-DLEQQRKQLEAQIAEL---QSEIAEREEELKELEEQLESLQEELAALEQELQalS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1901 AQDVLGEGERLLDEANQlsdNINKEIEDLEEMEKELGPLHVQLDDKVSRLTSGLSDSLADHVHDAEEHAKQLNESAAILD 1980
Cdd:COG4372 178 EAEAEQALDELLKEANR---NAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1981 GILAEAKNLSfnATAAFKAYTNIKANVDAAEKEAKAAKQRANEALALALGPEVPVKEAAQGALQKSHRLLNQAKQLQNDV 2060
Cdd:COG4372 255 VILKEIEELE--LAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELAL 332
|
330 340
....*....|....*....|....
gi 2316002738 2061 KENADSVAGLKGRVKAARDKTKDL 2084
Cdd:COG4372 333 AILLAELADLLQLLLVGLLDNDVL 356
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
399-450 |
1.49e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 50.00 E-value: 1.49e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2316002738 399 CTCDPHGSVSQSCVADSsqatptqpaGSCRCKEGFGGLQCDRCAVGYMGYPF 450
Cdd:smart00180 1 CDCDPGGSASGTCDPDT---------GQCECKPNVTGRRCDRCAPGYYGDGP 43
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
949-986 |
1.59e-07 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 50.05 E-value: 1.59e-07
10 20 30
....*....|....*....|....*....|....*....
gi 2316002738 949 PCRCSPHGSISQRCDVE-GRCICRPGFVGRRCDLRRQGY 986
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGtGQCECKPNTTGRRCDRCAPGY 39
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1600-1637 |
3.24e-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: 49.27 E-value: 3.24e-07
10 20 30
....*....|....*....|....*....|....*...
gi 2316002738 1600 CKCSPWGAWPGPCDPVTGQCRCRVGASGRSCDLCMDRH 1637
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGY 39
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1600-1637 |
4.20e-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: 48.89 E-value: 4.20e-07
10 20 30
....*....|....*....|....*....|....*...
gi 2316002738 1600 CKCSPWGAWPGPCDPVTGQCRCRVGASGRSCDLCMDRH 1637
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGY 38
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1686-1990 |
4.98e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.84 E-value: 4.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1686 ENMTEELKHMLSPQKAPERLLQLADSnlgsLVVEMDQLHSRATKVSAdgEQVEDDADRIHKRAEDLEQFIRDTLLGAKDL 1765
Cdd:PRK03918 344 KKKLKELEKRLEELEERHELYEEAKA----KKEELERLKKRLTGLTP--EKLEKELEELEKAKEEIEEEISKITARIGEL 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1766 QSKAAELNQTLSR------------RDGTPD-----------------KSLKEMKEEIQAMLAEMGK--------RQLGG 1808
Cdd:PRK03918 418 KKEIKELKKAIEElkkakgkcpvcgRELTEEhrkelleeytaelkrieKELKEIEEKERKLRKELRElekvlkkeSELIK 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1809 KKSIAE--------------EEMDLAEELYQKVKRLF----GDPHQATEDLK--AEIKGKLSDHEGKLQEAQDLLHSAQG 1868
Cdd:PRK03918 498 LKELAEqlkeleeklkkynlEELEKKAEEYEKLKEKLiklkGEIKSLKKELEklEELKKKLAELEKKLDELEEELAELLK 577
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1869 KMKQAG-SLAEQNHANLTGLE---RKRSAVSAVKQEAQDVLGEGERLLDEANQLSDNINKEIEDLEEMEKELGPLHVQLD 1944
Cdd:PRK03918 578 ELEELGfESVEELEERLKELEpfyNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYS 657
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1945 D----KVSRLTSGLSDSLADHVHDAEEHAKQLNESAAILDGILAEAKNLS 1990
Cdd:PRK03918 658 EeeyeELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEERE 707
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1600-1637 |
5.34e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 48.46 E-value: 5.34e-07
10 20 30
....*....|....*....|....*....|....*...
gi 2316002738 1600 CKCSPWGAWPGPCDPVTGQCRCRVGASGRSCDLCMDRH 1637
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGY 38
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1785-2080 |
8.18e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.33 E-value: 8.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1785 KSLKEMKEEIQAMLAEMGKRQLGGKKSIAEEEMDLAEELYQkvkrlfgdphQATEDLkAEIKGKLSDHEGKLQEAQDLLH 1864
Cdd:COG1196 216 RELKEELKELEAELLLLKLRELEAELEELEAELEELEAELE----------ELEAEL-AELEAELEELRLELEELELELE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1865 SAQGKMKQAGSLAEQnhanltgLERKRSAVSAVKQEAQDVLGEGERLLDEANQLSDNINKEIEDLEEMEKELGPLHVQLD 1944
Cdd:COG1196 285 EAQAEEYELLAELAR-------LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1945 DKVSRLTSGLSDSLADHVHDAEEHAKQLNESAAILDGILAEAKNLSFNATAAfkaytnikANVDAAEKEAKAAKQRANEA 2024
Cdd:COG1196 358 AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE--------EALLERLERLEEELEELEEA 429
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2316002738 2025 LALALGPEVPVKEAAQGALQKSHRLLNQAKQLQNDVKENADSVAGLKGRVKAARDK 2080
Cdd:COG1196 430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEE 485
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1134-1175 |
8.99e-07 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 48.12 E-value: 8.99e-07
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2316002738 1134 CGCSVIGSVTQQCNVNTGCCLCRDSFRGEKCNECQIGYRDFP 1175
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1745-2211 |
9.98e-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: 54.80 E-value: 9.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1745 HKR--AEDLEQF---IRDTL---LGAKDLQSK----AAELNQTLSRRDGTPDKSLKEMK-------EEIQAMLaEMGKRQ 1805
Cdd:pfam01576 293 QRRdlGEELEALkteLEDTLdttAAQQELRSKreqeVTELKKALEEETRSHEAQLQEMRqkhtqalEELTEQL-EQAKRN 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1806 LGG----KKSIAEEEMDLAEEL--YQKVKrlfGDPHQATEDLKA---EIKGKLSDHEGKLQEAQDLLHSAQGKMKQAGSL 1876
Cdd:pfam01576 372 KANlekaKQALESENAELQAELrtLQQAK---QDSEHKRKKLEGqlqELQARLSESERQRAELAEKLSKLQSELESVSSL 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1877 AEQNHANLTGLERKRSAVSAVKQEAQDVLGEGER-----------LLDEAN-------------------------QLSD 1920
Cdd:pfam01576 449 LNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRqklnlstrlrqLEDERNslqeqleeeeeakrnverqlstlqaQLSD 528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1921 NINK------EIEDLEE----MEKELGPLHVQLDDKVS----------RLTSGLSDSLADhvhdaEEHAKQ----LNESA 1976
Cdd:pfam01576 529 MKKKleedagTLEALEEgkkrLQRELEALTQQLEEKAAaydklektknRLQQELDDLLVD-----LDHQRQlvsnLEKKQ 603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1977 AILDGILAEAKNLSfnataAFKAYTNIKANVDAaekeakaakqRANEALALALGPEVpvkEAAQGA-------------- 2042
Cdd:pfam01576 604 KKFDQMLAEEKAIS-----ARYAEERDRAEAEA----------REKETRALSLARAL---EEALEAkeelertnkqlrae 665
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2043 -----------------LQKSHRLL-NQAKQLQNDVKENADSVAG----------------------LKGRVKAARDKTK 2082
Cdd:pfam01576 666 medlvsskddvgknvheLERSKRALeQQVEEMKTQLEELEDELQAtedaklrlevnmqalkaqferdLQARDEQGEEKRR 745
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2083 DLLKTVNGTMATLSAIPNDTAAKIAATKVvatdanataidvLErlGDLNlrlrglqqnysELEDTVNAANQMIQDPEKNI 2162
Cdd:pfam01576 746 QLVKQVRELEAELEDERKQRAQAVAAKKK------------LE--LDLK-----------ELEAQIDAANKGREEAVKQL 800
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2163 HAAGAKVKDLEDEADRLLEKLQPI--------KKLQdNLKRNISQIKELI---NQARKQA 2211
Cdd:pfam01576 801 KKLQAQMKDLQRELEEARASRDEIlaqskeseKKLK-NLEAELLQLQEDLaasERARRQA 859
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
790-845 |
1.27e-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: 47.73 E-value: 1.27e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2316002738 790 CTCPlnlPSNNFSPTCHLgEEGEllCdQCQPGYTGPRCDRCSNGYYGKPAVPGGSC 845
Cdd:pfam00053 1 CDCN---PHGSLSDTCDP-ETGQ--C-LCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1719-2215 |
1.59e-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: 54.30 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1719 EMDQLHSRATKVSADGEQVEDDADRIHKRAEDLEQFirdtllgaKDLQSKAAELNQT-LSRRDGTPDKSLKEMKEEIQAM 1797
Cdd:TIGR02169 178 ELEEVEENIERLDLIIDEKRQQLERLRREREKAERY--------QALLKEKREYEGYeLLKEKEALERQKEAIERQLASL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1798 LAEMGKRQlggkksiaEEEMDLAEELYQKVKRLfgdphqatEDLKAEIK------------------GKLSDHEGKLQEA 1859
Cdd:TIGR02169 250 EEELEKLT--------EEISELEKRLEEIEQLL--------EELNKKIKdlgeeeqlrvkekigeleAEIASLERSIAEK 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1860 QDLLHSAQGKMKQAGSLAEQNHANLTGLER-------KRSAVSAVKQEAQDVLgegERLLDEANQLS-------DNINKE 1925
Cdd:TIGR02169 314 ERELEDAEERLAKLEAEIDKLLAEIEELEReieeerkRRDKLTEEYAELKEEL---EDLRAELEEVDkefaetrDELKDY 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1926 IEDLEEMEKELGPLHVQLDDKVSRLTSgLSDSLADHVHDAEEHAKQLNESAAILDGILAEAK----NLSFNA---TAAFK 1998
Cdd:TIGR02169 391 REKLEKLKREINELKRELDRLQEELQR-LSEELADLNAAIAGIEAKINELEEEKEDKALEIKkqewKLEQLAadlSKYEQ 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1999 AYTNIKANVDAAEKEAKAAKQR--ANEALALALGPEVPVKEAAQGALQKSHR-LLNQAKQLqNDVKEN---ADSVAGlKG 2072
Cdd:TIGR02169 470 ELYDLKEEYDRVEKELSKLQRElaEAEAQARASEERVRGGRAVEEVLKASIQgVHGTVAQL-GSVGERyatAIEVAA-GN 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2073 RVKAARDKTKD-------LLKTVNGTMAT-------------LSAIPNDTAAKIA-------------------ATKVVA 2113
Cdd:TIGR02169 548 RLNNVVVEDDAvakeaieLLKRRKAGRATflplnkmrderrdLSILSEDGVIGFAvdlvefdpkyepafkyvfgDTLVVE 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2114 TDANATAI-----------DVLERLGDL---NLRLRGLQQNYSELEDTVnaanQMIQDpeknihaagaKVKDLEDEADRL 2179
Cdd:TIGR02169 628 DIEAARRLmgkyrmvtlegELFEKSGAMtggSRAPRGGILFSRSEPAEL----QRLRE----------RLEGLKRELSSL 693
|
570 580 590
....*....|....*....|....*....|....*.
gi 2316002738 2180 LEKLQPIKKLQDNLKRNISQIKELINQARKQANSIK 2215
Cdd:TIGR02169 694 QSELRRIENRLDELSQELSDASRKIGEIEKEIEQLE 729
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
950-980 |
2.34e-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: 46.96 E-value: 2.34e-06
10 20 30
....*....|....*....|....*....|..
gi 2316002738 950 CRCSPHGSISQRCDVE-GRCICRPGFVGRRCD 980
Cdd:pfam00053 1 CDCNPHGSLSDTCDPEtGQCLCKPGVTGRHCD 32
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1742-2215 |
2.59e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.53 E-value: 2.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1742 DRIHKRAEDLEQFIRDtLLGAKDLQS---KAAELNQTLSRRDGTPDKSLKEmKEEIQAMLAEMGKRqLGGK----KSIAE 1814
Cdd:PRK03918 138 DAILESDESREKVVRQ-ILGLDDYENaykNLGEVIKEIKRRIERLEKFIKR-TENIEELIKEKEKE-LEEVlreiNEISS 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1815 EEMDLAEEL------YQKVKRLFGDPHQAtEDLKAEIKGKLSDHEGKLQEAQDLLHSAQGKMK----QAGSLAEqnhanL 1884
Cdd:PRK03918 215 ELPELREELeklekeVKELEELKEEIEEL-EKELESLEGSKRKLEEKIRELEERIEELKKEIEeleeKVKELKE-----L 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1885 TGLERKRSAVSAVKQEAQDVLGEGERLLDEANQLSDNINKEIEDLEEMEKELGPLH---VQLDDKVSRLtsglsdsladh 1961
Cdd:PRK03918 289 KEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKkklKELEKRLEEL----------- 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1962 vhdaEEHAKQLNESAAILDgilaEAKNLSfnatAAFKAYTNIKANvdaaekeakaakqRANEALALAlgpevpvKEAAQG 2041
Cdd:PRK03918 358 ----EERHELYEEAKAKKE----ELERLK----KRLTGLTPEKLE-------------KELEELEKA-------KEEIEE 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2042 ALQKSHRLLNQAKQLQNDVKENADSVAGLKGRVKAAR-----DKTKDLLKTVNGTMATLSAIPNDTAAKIAATKVVATDA 2116
Cdd:PRK03918 406 EISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGrelteEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELREL 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2117 NaTAIDVLERLgdlnLRLRGLQQNYSELEDTVNAANqmIQDPEKNihaagakvkdlEDEADRLLEKLQPIKKLQDNLKRN 2196
Cdd:PRK03918 486 E-KVLKKESEL----IKLKELAEQLKELEEKLKKYN--LEELEKK-----------AEEYEKLKEKLIKLKGEIKSLKKE 547
|
490
....*....|....*....
gi 2316002738 2197 ISQIKELINQARKQANSIK 2215
Cdd:PRK03918 548 LEKLEELKKKLAELEKKLD 566
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1134-1177 |
3.51e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 46.15 E-value: 3.51e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2316002738 1134 CGCSVIGSVTQQCNVNTGCCLCRDSFRGEKCNECQIGY--RDFPQC 1177
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYygDGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
272-319 |
4.67e-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: 45.81 E-value: 4.67e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2316002738 272 CICYGHA---KACPLNTVTkkfsCECEHNTCGESCDRCCPGYHQQPWMAGT 319
Cdd:cd00055 2 CDCNGHGslsGQCDPGTGQ----CECKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
950-986 |
6.45e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 45.38 E-value: 6.45e-06
10 20 30
....*....|....*....|....*....|....*...
gi 2316002738 950 CRCSPHGSISQRCDVE-GRCICRPGFVGRRCDLRRQGY 986
Cdd:smart00180 1 CDCDPGGSASGTCDPDtGQCECKPNVTGRRCDRCAPGY 38
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
453-501 |
1.27e-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: 1.27e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2316002738 453 RCNCSVEGSTNaDPCITP---CMCKENVEGENCDRCKLGFYNLQgDNQRGCE 501
Cdd:cd00055 1 PCDCNGHGSLS-GQCDPGtgqCECKPNTTGRRCDRCAPGYYGLP-SQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
789-846 |
1.62e-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: 44.27 E-value: 1.62e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2316002738 789 PCTCPlnlPSNNFSPTCHlgeEGELLCdQCQPGYTGPRCDRCSNGYYGKPAVPGGsCQ 846
Cdd:cd00055 1 PCDCN---GHGSLSGQCD---PGTGQC-ECKPNTTGRRCDRCAPGYYGLPSQGGG-CQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
790-839 |
1.84e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 44.22 E-value: 1.84e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2316002738 790 CTCPlnlPSNNFSPTCHLgEEGEllCdQCQPGYTGPRCDRCSNGYYGKPA 839
Cdd:smart00180 1 CDCD---PGGSASGTCDP-DTGQ--C-ECKPNVTGRRCDRCAPGYYGDGP 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
454-495 |
2.76e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 43.84 E-value: 2.76e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2316002738 454 CNCSVEGSTNaDPCITP---CMCKENVEGENCDRCKLGFYNLQGD 495
Cdd:smart00180 1 CDCDPGGSAS-GTCDPDtgqCECKPNVTGRRCDRCAPGYYGDGPP 44
|
|
| ClyA-like |
cd21116 |
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ... |
2035-2179 |
1.71e-04 |
|
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including Bacillus cereus HblB, Aeromonas hydrophila AhlB, Bacillus thuringiensis Cry6Aa and similar proteins; This family belongs to the ClyA family of alpha-PFT bacterial toxins. PFTs form the major group of virulence factors in many pathogenic bacteria and in general are critical components of the molecular offensive and defensive machinery of cells in all kingdoms of life. Bacterial PFTs facilitate the takeover of host resources by puncturing holes in the membrane. PFTs can be classified as alpha-PFTs and beta-PFTs depending on the secondary structures of their membrane component. Alpha-PFTs use a ring of amphipathic helices while beta-PFTs use a beta-barrel to construct the pore. Members of this family include the toxins: Bacillus cereus hemolysin binding component B (HblB or HBL-B) of the diarrheal enterotoxin hemolysin BL, Aeromonas hydrophila hemolytic (Ahl) component B (AhlB) of the tripartite AhlABC toxin, Vibrio cholerae cytotoxin motility associated killing factor A (MakA) cytotoxin, Xenorhabdus nematophila alpha-xenorhabdolysin (XaxA), Bacillus thuringiensis crystal 6Aa (Cry6Aa) parasporal crystal (Cry) toxin, and Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA) of the non-hemolytic enterotoxin Nhe, which, despite its name, is hemolytic, among others. In solution, ClyA proteins have an elongated, almost entirely alpha-helical structure, except for a short hydrophobic beta-hairpin known as the beta-tongue. Pore formation by ClyA requires circular oligomerization of the toxin by a sequential mechanism. This, in turn, concentrates the amphipathic helices in the center of the ring-like structure, forming a helical barrel that inserts into the membrane by a wedge-like mechanism. Compared with ClyA, NheA is almost entirely alpha-helical with an enlarged "head" domain, and an enlarged beta-tongue; it has been proposed that NheA could even form beta-barrel pores. Alpha-PFTs with similar structures are increasingly being found in eukaryotes, in particular as components of the immune systems of animals. This family may be distantly related to Escherichia coli alpha-PFT hemolysin E (HlyE, also known as ClyA or SheA).
Pssm-ID: 439149 [Multi-domain] Cd Length: 224 Bit Score: 45.87 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2035 VKEAAQGALQKshrLLNQAKQLQNDVKENADSVAGLKgrvkaarDKTKDLLKTVNGTMATLSAIPNDTAAKIAATKVVAT 2114
Cdd:cd21116 85 LIKGDQGAKQQ---LLQGLEALQSQVTKKQTSVTSFI-------NELTTFKNDLDDDSRNLQTDATKAQAQVAVLNALKN 154
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2316002738 2115 ------DANATAIDVLERLGDLnlrLRGLQQNYSELEDTVNAANQMIQDP--EKNIHAAGAKVKDLEDEADRL 2179
Cdd:cd21116 155 qlnslaEQIDAAIDALEKLSND---WQTLDSDIKELITDLEDAESSIDAAflQADLKAAKADWNQLYEQAKSL 224
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1541-1595 |
3.10e-04 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 40.80 E-value: 3.10e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2316002738 1541 PCACpltNPENNFSPTCVaegFDDYRCTaCPEGYEGKYCERCATGYHGNPRMPGG 1595
Cdd:cd00055 1 PCDC---NGHGSLSGQCD---PGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1842-1947 |
4.05e-04 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 42.81 E-value: 4.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1842 KAEIKGKLSDHEGKLQEAQDLLHSAQGKMKQAGSLAEQ--NHANLTGLERKRSAVSAVKQEAqdvlgegERLLDEANQls 1919
Cdd:cd06503 32 EEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEiiEEARKEAEKIKEEILAEAKEEA-------ERILEQAKA-- 102
|
90 100
....*....|....*....|....*....
gi 2316002738 1920 dNINKEIED-LEEMEKELGPLHVQLDDKV 1947
Cdd:cd06503 103 -EIEQEKEKaLAELRKEVADLAVEAAEKI 130
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2047-2214 |
8.38e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.42 E-value: 8.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2047 HRLLNQAKQLQNDVKENADSVAGLKGRVKAARDKTKDLLKTVNGT---MATLSAIPNDTAAKIAAT---KVVATDANATA 2120
Cdd:PRK02224 205 HERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERreeLETLEAEIEDLRETIAETereREELAEEVRDL 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2121 IDVLERLGD------------------LNLRLRGLQQNYSELEDTVNAANQMIQDPEKNIHAAGAKVKDLEDEADRLLEK 2182
Cdd:PRK02224 285 RERLEELEEerddllaeaglddadaeaVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREE 364
|
170 180 190
....*....|....*....|....*....|..
gi 2316002738 2183 LQPIKKLQDNLKRNISQIKELINQARKQANSI 2214
Cdd:PRK02224 365 AAELESELEEAREAVEDRREEIEELEEEIEEL 396
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
292-315 |
9.78e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 39.22 E-value: 9.78e-04
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1719-2212 |
1.51e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 44.43 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1719 EMDQLHSRATKVSADGEQVEDDAdrihkRAEDlEQFIRDTLLGAKDLQSKAAELNQTLSRRDGTPDKSLK-EMKEEIQAM 1797
Cdd:NF041483 576 ELTRLHTEAEERLTAAEEALADA-----RAEA-ERIRREAAEETERLRTEAAERIRTLQAQAEQEAERLRtEAAADASAA 649
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1798 LAEMGKRQLGGKKSIAEEEMDLAEELYQKVKRLFGDPHQATEDLKAEIKGKLS----DHEGKLQEAQDLLHSAQGKMKQA 1873
Cdd:NF041483 650 RAEGENVAVRLRSEAAAEAERLKSEAQESADRVRAEAAAAAERVGTEAAEALAaaqeEAARRRREAEETLGSARAEADQE 729
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1874 GSLAEQNHANLTGLERKRSAvsavkqEAQdvlGEGERLLDEANQLSDNINKEIED-LEEMEKELGPLHVQLDDKVSRLTS 1952
Cdd:NF041483 730 RERAREQSEELLASARKRVE------EAQ---AEAQRLVEEADRRATELVSAAEQtAQQVRDSVAGLQEQAEEEIAGLRS 800
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1953 GlsdslADHVHD-----AEEHAKQLNESA------AILDG--ILAEAKNLSFNATA-AFKAYTNIKANVDAAEKEAKAAK 2018
Cdd:NF041483 801 A-----AEHAAErtrteAQEEADRVRSDAyaererASEDAnrLRREAQEETEAAKAlAERTVSEAIAEAERLRSDASEYA 875
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2019 QR----ANEALAlalgpevpvkEAAQGALQKSHRLLNQAKQLQNDVKENADSVAGlKGRVKAARDKTKdllktvngtmAT 2094
Cdd:NF041483 876 QRvrteASDTLA----------SAEQDAARTRADAREDANRIRSDAAAQADRLIG-EATSEAERLTAE----------AR 934
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2095 LSAIPNDTAAKIAATKVVAtDANATAIDVLERLGDLNLRLRglqqnySELEDTVNAANQMIQdpekNIHAAGAKVK-DLE 2173
Cdd:NF041483 935 AEAERLRDEARAEAERVRA-DAAAQAEQLIAEATGEAERLR------AEAAETVGSAQQHAE----RIRTEAERVKaEAA 1003
|
490 500 510
....*....|....*....|....*....|....*....
gi 2316002738 2174 DEADRLLEKLQpikklqdnlkrniSQIKELINQARKQAN 2212
Cdd:NF041483 1004 AEAERLRTEAR-------------EEADRTLDEARKDAN 1029
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
20-270 |
9.98e-93 |
|
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: 301.20 E-value: 9.98e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 20 QQRGLFPAVLNLASMADITANATCGSMGPEMFCKLVEHVpgqpVRNPQCRICNQRStkPFERHPIEYAIDGTN----RWW 95
Cdd:smart00136 3 RPRSCYPPFVNLAFGREVTATSTCGEPGPERYCKLVGHT----EQGKKCDYCDARN--PRRSHPAENLTDGNNpnnpTWW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 96 QSPSIKNGMeyHYVTITLDLKQVFQIAYVIVKAAnSPRPGNWILERSIDGVTFDPWQYYAitdTECLTRFNINPRTGPPS 175
Cdd:smart00136 77 QSEPLSNGP--QNVNLTLDLGKEFHVTYVILKFC-SPRPSLWILERSDFGKTWQPWQYFS---SDCRRTFGRPPRGPITK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 176 YTrDDEVICTSFYSKIHPLENGEIHTSLINGRPSADDP--SPTLLNFTSARYIRLVFQRIRTLNADLMtltlrdpkDIDP 253
Cdd:smart00136 151 GN-EDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDFdnSPVLQEWVTATNIRVRLTRLRTLGDELM--------DDRP 221
|
250
....*....|....*..
gi 2316002738 254 IVTRRYYYSIKDISVGG 270
Cdd:smart00136 222 EVTRRYYYAISDIAVGG 238
|
|
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
24-270 |
8.90e-87 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 283.70 E-value: 8.90e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 24 LFPAVLNLASMADITANATCGSMGPEMFCKLVEHVPGQpvrnpQCRICNqrSTKPFERHPIEYAIDGTNR----WWQSPS 99
Cdd:pfam00055 1 CYPAFGNLAFGREVSATSTCGLNGPERYCILSGLEGGK-----KCFICD--SRDPHNSHPPSNLTDSNNGtnetWWQSET 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 100 IKngMEYHYVTITLDLKQVFQIAYVIVKAAnSPRPGNWILERSID-GVTFDPWQYYAitdTECLTRFNINPRtgPPSYTR 178
Cdd:pfam00055 74 GV--IQYENVNLTLDLGKEFHFTYLILKFK-SPRPAAMVLERSTDfGKTWQPYQYFA---SDCRRTFGRPSG--PSRGIK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 179 DDEVICTSFYSKIHPLENGEIHTSLINGRPSA--DDPSPTLLNFTSARYIRLVFQRIRTLNADLMTltlrdpkdiDPIVT 256
Cdd:pfam00055 146 DDEVICTSEYSDISPLTGGEVIFSTLEGRPSAniFDYSPELQDWLTATNIRIRLLRLHTLGDELLD---------DPSVL 216
|
250
....*....|....
gi 2316002738 257 RRYYYSIKDISVGG 270
Cdd:pfam00055 217 RKYYYAISDISVGG 230
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1671-1924 |
5.46e-52 |
|
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: 184.92 E-value: 5.46e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1671 LTTPLPPPYKMLYRFENMTEELKHMLSPQKAPERLLQLADSNLGSLVVEMDQLHSRATKVSADGEQVEDDADRIHKRAED 1750
Cdd:pfam06008 7 LTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1751 LEQFIRDTLLGAKDLQSKAAELNQTLsrrDGTPDKSLKEMKEEIQAMLAEMGKRQLGGKKSIAEEEMDLAEELYQKVKRL 1830
Cdd:pfam06008 87 LAEAIKNLIDNIKEINEKVATLGEND---FALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQDLLSRIQTW 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1831 FGDPHQATEDLKAEIKGKLSDHEGKLQEAQDLLHSAQGKMKQAGSLAEQNHANLTGLERKRSAVSAVKQEAQDVLGEGER 1910
Cdd:pfam06008 164 FQSPQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEETLKTARD 243
|
250
....*....|....
gi 2316002738 1911 LLDEANQLSDNINK 1924
Cdd:pfam06008 244 SLDAANLLLQEIDD 257
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
1307-1445 |
2.78e-45 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 160.90 E-value: 2.78e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1307 YWKLPEQFRGSMITAYGGQLKYAVYYEARDETGPSSYEPQVIIKGGPNRSIMMTRHIPGLQIGQLTRHEIDMTEHEWKYA 1386
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGGGSLNSEPDVILEGNGLRLSYSSPDQPPPDPGQEQTYSVRLHEENWRDS 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2316002738 1387 DGRSMTREDFMDILFYVDYILIKASHGNLMRHSRISEISLTVAEEGRPtkeSEKAHQIE 1445
Cdd:pfam00052 81 DGAPVSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSAVPGGS---GPPASWVE 136
|
|
| Laminin_II |
pfam06009 |
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 ... |
2109-2242 |
6.93e-40 |
|
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: 145.71 E-value: 6.93e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2109 TKVVATDANATAIDVLERLGDLNLRLRGLQQNYSELEDTVNAANQMIQDPEKNIHAAGAKVKDLEDEADRLLEKLQPIKK 2188
Cdd:pfam06009 1 SKELAREANETAKEVLEQLAPLSQNLENTSEKLSGINRSLEETNELVNDANKALDDAGRSVKKLEELAPDLLDKLKPLKQ 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2316002738 2189 LQDN---LKRNISQIKELINQARKQANSIKVSVSSGGDCLRSYRPDIRKGRYNTIVL 2242
Cdd:pfam06009 81 LEVNsssLSDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTS 137
|
|
| LamB |
smart00281 |
Laminin B domain; |
1302-1431 |
1.45e-39 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 144.33 E-value: 1.45e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1302 LSEPYYWKLPEQFRGSMITAYGGQLKYAVYYEARDEtGPSSYEPQVIIKGgpNRSIMMTRHIPGLQIGQLTRHEIDMTEH 1381
Cdd:smart00281 1 DNEPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRRG-GTHVSAPDVILEG--NGLRISHPAEGPPLPDELTTVEVRFREE 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1382 EWKYADGRSMTREDFMDILFYVDYILIKASHGNLMRHSRISEISLTVAEE 1431
Cdd:smart00281 78 NWQYYGGRPVTREDLMMVLANLTAILIRATYSQQMAGSRLSDVSLEVAVP 127
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
565-705 |
9.48e-39 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 142.02 E-value: 9.48e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 565 YWNAPGLYLGNKLSAYGGSVVYTVSYTTDQQEQMAirvTSEHDLIIEGGGMKIIDGRFGQP-LYPSSPSTNHIVLLPENF 643
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGGGSL---NSEPDVILEGNGLRLSYSSPDQPpPDPGQEQTYSVRLHEENW 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2316002738 644 lVSGTEQRISRRDFLSVLANVTRVMVRASYSTEPSAVyRLHSFSMQVANPSARGErRASAVE 705
Cdd:pfam00052 78 -RDSDGAPVSREDFMMVLANLTAILIRATYSTGSGQV-SLSNVSLDSAVPGGSGP-PASWVE 136
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
3075-3226 |
1.43e-35 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 133.70 E-value: 1.43e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 3075 GTYFDGTGFLKAVSSYRVGLDVLIELEFRTSRTNGVLLAISNQA-NDGLGLELVQGKLLFHVDNGAGRITAEHMPEgegF 3153
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNgGDFLALELEDGRLVLRYDLGSGSLVLSSKTP---L 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2316002738 3154 CDGQWHAVTANKLRHRVELVVDGKQSQAESPNARSNTCDTNDPIYVGGYPHGVRQAALSTSTSFRGCMRNLKI 3226
Cdd:cd00110 78 NDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKV 150
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2908-3035 |
1.36e-34 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 130.13 E-value: 1.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2908 RTKEESGLVLYMARINHADFVSIQIKDGQVCLGYDLGHGNISGCVPFSINDGNWHKIRVSRVKQRGLLMVDGRYSKQMIS 2987
Cdd:pfam00054 2 RTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGES 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2316002738 2988 PKKAD-LLDVVGMVYVGGLPQNYTTKRIGPILYSINGCIRNLKMVGGPV 3035
Cdd:pfam00054 82 PLGATtDLDVDGPLYVGGLPSLGVKKRRLAISPSFDGCIRDVIVNGKPL 130
|
|
| LamG |
smart00282 |
Laminin G domain; |
3098-3226 |
4.74e-32 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 122.83 E-value: 4.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 3098 IELEFRTSRTNGVLLAI-SNQANDGLGLELVQGKLLFHVDNGAGRITAEHmpEGEGFCDGQWHAVTANKLRHRVELVVDG 3176
Cdd:smart00282 2 ISFSFRTTSPNGLLLYAgSKGGGDYLALELRDGRLVLRYDLGSGPARLTS--DPTPLNDGQWHRVAVERNGRSVTLSVDG 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2316002738 3177 KQSQAESPNARSNTCDTNDPIYVGGYPHGVRQAALSTSTSFRGCMRNLKI 3226
Cdd:smart00282 80 GNRVSGESPGGLTILNLDGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKV 129
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2880-3030 |
6.78e-32 |
|
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: 123.30 E-value: 6.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2880 FGLTRNSHMSFAFDDTKvRERLILEFELRTKEESGLVLYMARINHADFVSIQIKDGQVCLGYDLGHGNISGCVPFSINDG 2959
Cdd:cd00110 2 VSFSGSSYVRLPTLPAP-RTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2316002738 2960 NWHKIRVSRVKQRGLLMVDGRYSKQMISPKKADLLDVVGMVYVGGLPQNYTTKRIgPILYSINGCIRNLKM 3030
Cdd:cd00110 81 QWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGL-PVSPGFVGCIRDLKV 150
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
3102-3226 |
1.21e-31 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 121.37 E-value: 1.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 3102 FRTSRTNGVLLAISNQANDGLGLELVQGKLLFHVDNGAGRITAehMPEGEGFCDGQWHAVTANKLRHRVELVVDGKQSQA 3181
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDFLALELVNGRLVLRYDLGSGPESL--LSSGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVS 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2316002738 3182 ESPNARSNTCDTNDPIYVGGYPHGVRQAALSTSTSFRGCMRNLKI 3226
Cdd:pfam02210 79 SLPPGESLLLNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRV 123
|
|
| LamG |
smart00282 |
Laminin G domain; |
2239-2381 |
1.52e-29 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 115.90 E-value: 1.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2239 TIVLHVKTTTPDNLLFYLGSAKYVDFLALEMRKGKVNFLWDVGSGVGRVEYPHHTIHDGNWHRVEASRNGLNGTISVypl 2318
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLNDGQWHRVAVERNGRSVTLSV--- 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2316002738 2319 EGSmagmmpTPASANSPTAYTILDVDQNayLFVGGILGTVKKAEAVRTTTFTGCMGETFLDGK 2381
Cdd:smart00282 78 DGG------NRVSGESPGGLTILNLDGP--LYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| LamG |
smart00282 |
Laminin G domain; |
2903-3032 |
2.05e-29 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 115.51 E-value: 2.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2903 LEFELRTKEESGLVLYMARINHADFVSIQIKDGQVCLGYDLGHG--NISGcVPFSINDGNWHKIRVSRVKQRGLLMVDGR 2980
Cdd:smart00282 2 ISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGpaRLTS-DPTPLNDGQWHRVAVERNGRSVTLSVDGG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2316002738 2981 YSKQMISPKKADLLDVVGMVYVGGLPQNYTTKRIgPILYSINGCIRNLKMVG 3032
Cdd:smart00282 81 NRVSGESPGGLTILNLDGPLYLGGLPEDLKLPPL-PVTPGFRGCIRNLKVNG 131
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2411-2567 |
3.05e-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: 115.59 E-value: 3.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2411 VQLDGEGYAAVgRPTRWNPNVSTVTFKFRTFSSDALLMYLATEDMKDFMSLELSEGKVKVNFDLGSGVGSAISANRHNDG 2490
Cdd:cd00110 2 VSFSGSSYVRL-PTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2316002738 2491 SWKSLTMSRNKKQATVTVvdiDSSAeekiVATSQGSATGLNLKENQKIYFGGLPTIGNYRSEVTLKRYAGCLREIEV 2567
Cdd:cd00110 81 QWHSVSVERNGRSVTLSV---DGER----VVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKV 150
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2244-2384 |
3.18e-29 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 114.72 E-value: 3.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2244 VKTTTPDNLLFYLGSAKYVDFLALEMRKGKVNFLWDVGSGVGRVEYPhHTIHDGNWHRVEASRNGLNGTISVYPLEgsma 2323
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSG-DKLNDGKWHSVELERNGRSGTLSVDGEA---- 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2316002738 2324 gmmptPASANSPTAYTIlDVDQNAYLFVGGILGTVKKAE-AVRTTTFTGCMGETFLDGKPIG 2384
Cdd:pfam00054 76 -----RPTGESPLGATT-DLDVDGPLYVGGLPSLGVKKRrLAISPSFDGCIRDVIVNGKPLD 131
|
|
| LamB |
smart00281 |
Laminin B domain; |
560-693 |
6.18e-29 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 113.90 E-value: 6.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 560 LGSAYYWNAPGLYLGNKLSAYGGSVVYTVSYTTdqQEQMaiRVTSEHDLIIEGGGMKIIDgRFGQPLYPSSPSTNHIVLL 639
Cdd:smart00281 1 DNEPVYWVAPEQFLGDKVTSYGGKLRYTLSFDG--RRGG--THVSAPDVILEGNGLRISH-PAEGPPLPDELTTVEVRFR 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2316002738 640 PENFLVSGtEQRISRRDFLSVLANVTRVMVRASYStEPSAVYRLHSFSMQVANP 693
Cdd:smart00281 76 EENWQYYG-GRPVTREDLMMVLANLTAILIRATYS-QQMAGSRLSDVSLEVAVP 127
|
|
| LamG |
smart00282 |
Laminin G domain; |
2433-2569 |
1.68e-28 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 112.82 E-value: 1.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2433 TVTFKFRTFSSDALLMYLATEDMKDFMSLELSEGKVKVNFDLGSGVGSAISANRH-NDGSWKSLTMSRNKKQATVTVvdi 2511
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPlNDGQWHRVAVERNGRSVTLSV--- 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2316002738 2512 DSsaEEKIVATSQGSATGLNLKENqkIYFGGLPTIGNYRSEVTLKRYAGCLREIEVSR 2569
Cdd:smart00282 78 DG--GNRVSGESPGGLTILNLDGP--LYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNG 131
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2438-2573 |
6.43e-28 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 110.87 E-value: 6.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2438 FRTFSSDALLMYLATEDMKDFMSLELSEGKVKVNFDLGSGVGSAISANRHNDGSWKSLTMSRNKKQATVTVVDidssaEE 2517
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDG-----EA 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2316002738 2518 KIVATSQGSATGlNLKENQKIYFGGLPTIGNYRS-EVTLKRYAGCLREIEVSRTPYN 2573
Cdd:pfam00054 76 RPTGESPLGATT-DLDVDGPLYVGGLPSLGVKKRrLAISPSFDGCIRDVIVNGKPLD 131
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2220-2379 |
1.40e-26 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 107.89 E-value: 1.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2220 SGGDCLRsYRPDIRKGRYNTIVLHVKTTTPDNLLFYLGSAKYVDFLALEMRKGKVNFLWDVGSGVGRVEYPHHtIHDGNW 2299
Cdd:cd00110 5 SGSSYVR-LPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTP-LNDGQW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2300 HRVEASRNGLNGTISVyplegsmagmmPTPASANSPTAYTILDVDQNAYLFVGGILGTVKKAEAVRTTTFTGCMGETFLD 2379
Cdd:cd00110 83 HSVSVERNGRSVTLSV-----------DGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
3102-3226 |
2.29e-25 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 103.94 E-value: 2.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 3102 FRTSRTNGVLLAISNQAN-DGLGLELVQGKLLFHVDNGAGRITAEHmpeGEGFCDGQWHAVTANKLRHRVELVVDGKQSQ 3180
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTErDFLALELRDGRLEVSYDLGSGAAVVRS---GDKLNDGKWHSVELERNGRSGTLSVDGEARP 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2316002738 3181 -AESPNARSNTCDTNDPIYVGGYP-HGVRQAALSTSTSFRGCMRNLKI 3226
Cdd:pfam00054 78 tGESPLGATTDLDVDGPLYVGGLPsLGVKKRRLAISPSFDGCIRDVIV 125
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2438-2567 |
2.10e-24 |
|
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: 100.96 E-value: 2.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2438 FRTFSSDALLMYLATEDmKDFMSLELSEGKVKVNFDLGSGVGSAISANRH-NDGSWKSLTMSRNKKQATVTVvdidssaE 2516
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGG-SDFLALELVNGRLVLRYDLGSGPESLLSSGKNlNDGQWHSVRVERNGNTLTLSV-------D 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2316002738 2517 EKIVATSQGSATGLNLKENQKIYFGGLPTIGNYRSEVTLKRYAGCLREIEV 2567
Cdd:pfam02210 73 GQTVVSSLPPGESLLLNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRV 123
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2907-3032 |
1.16e-22 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 95.95 E-value: 1.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2907 LRTKEESGLVLYMARINHaDFVSIQIKDGQVCLGYDLGHGNISGCV-PFSINDGNWHKIRVSRVKQRGLLMVDGRYSKQM 2985
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGS-DFLALELVNGRLVLRYDLGSGPESLLSsGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSS 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2316002738 2986 ISPKKADLLDVVGMVYVGGLPQNYTTKRIgPILYSINGCIRNLKMVG 3032
Cdd:pfam02210 80 LPPGESLLLNLNGPLYLGGLPPLLLLPAL-PVRAGFVGCIRDVRVNG 125
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2594-2768 |
3.10e-21 |
|
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: 92.87 E-value: 3.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2594 TVSFSKPGYMELGGLSL-AVSTEISLSFSTLEDTGtILLAVSGasphsqqarntnlfsskrrrrQSGEPYLSVMLNKGSL 2672
Cdd:cd00110 1 GVSFSGSSYVRLPTLPApRTRLSISFSFRTTSPNG-LLLYAGS---------------------QNGGDFLALELEDGRL 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2673 EVLVFTGSHSPrrVIRRPEQgiLNDGKEHSLRIERLaGRSFAVQVDEEP--KREATLPNDQPISLQRIFLGGIPAEVEQT 2750
Cdd:cd00110 59 VLRYDLGSGSL--VLSSKTP--LNDGQWHSVSVERN-GRSVTLSVDGERvvESGSPGGSALLNLDGPLYLGGLPEDLKSP 133
|
170
....*....|....*...
gi 2316002738 2751 SNRVNVPFQGCIWNLMVN 2768
Cdd:cd00110 134 GLPVSPGFVGCIRDLKVN 151
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2244-2381 |
4.09e-21 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 91.33 E-value: 4.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2244 VKTTTPDNLLFYLGSAKYvDFLALEMRKGKVNFLWDVGSGVGRVEYPHHTIHDGNWHRVEASRNGLNGTISVyplEGSMA 2323
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGS-DFLALELVNGRLVLRYDLGSGPESLLSSGKNLNDGQWHSVRVERNGNTLTLSV---DGQTV 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2316002738 2324 GMMPTPASAnsptaytiLDVDQNAYLFVGGILGTVKKAEAVRTTTFTGCMGETFLDGK 2381
Cdd:pfam02210 77 VSSLPPGES--------LLLNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| LamG |
smart00282 |
Laminin G domain; |
2615-2768 |
1.10e-18 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 84.70 E-value: 1.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2615 EISLSFSTLEDTGtILLAVSGASPHsqqarntnlfsskrrrrqsgePYLSVMLNKGSLEVLVFTGSHsprRVIRRPEQGI 2694
Cdd:smart00282 1 SISFSFRTTSPNG-LLLYAGSKGGG---------------------DYLALELRDGRLVLRYDLGSG---PARLTSDPTP 55
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2316002738 2695 LNDGKEHSLRIERLaGRSFAVQVDEEPKREATLPNDQPISL--QRIFLGGIPAEVEQTSNRVNVPFQGCIWNLMVN 2768
Cdd:smart00282 56 LNDGQWHRVAVERN-GRSVTLSVDGGNRVSGESPGGLTILNldGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVN 130
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2656-2768 |
1.67e-14 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 72.73 E-value: 1.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2656 RQSGEPYLSVMLNKGSLEVLVFTGSHsprRVIRRPEQGIlNDGKEHSLRIERLaGRSFAVQVDEE--PKREATLPNDQPI 2733
Cdd:pfam00054 15 TQTERDFLALELRDGRLEVSYDLGSG---AAVVRSGDKL-NDGKWHSVELERN-GRSGTLSVDGEarPTGESPLGATTDL 89
|
90 100 110
....*....|....*....|....*....|....*..
gi 2316002738 2734 SLQR-IFLGGIPAEVEQTSNRVNVP-FQGCIWNLMVN 2768
Cdd:pfam00054 90 DVDGpLYVGGLPSLGVKKRRLAISPsFDGCIRDVIVN 126
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2620-2768 |
1.31e-13 |
|
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: 70.14 E-value: 1.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2620 FSTLEDTGTILLAVSGASPhsqqarntnlfsskrrrrqsgepYLSVMLNKGSLEVLVFTGSHSPR-RVIRRPeqgiLNDG 2698
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSD-----------------------FLALELVNGRLVLRYDLGSGPESlLSSGKN----LNDG 53
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2316002738 2699 KEHSLRIERLaGRSFAVQVDEEPKREATLPNDQPI--SLQRIFLGGIPAEVEQTSNRVNVPFQGCIWNLMVN 2768
Cdd:pfam02210 54 QWHSVRVERN-GNTLTLSVDGQTVVSSLPPGESLLlnLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVN 124
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1041-1085 |
9.35e-13 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 64.64 E-value: 9.35e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2316002738 1041 CHCNSFGSKSFDCD-ETGQCRCQPGVTGPKCDRCSRGFFNFQEGGC 1085
Cdd:smart00180 1 CDCDPGGSASGTCDpDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1040-1089 |
1.73e-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: 1.73e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2316002738 1040 PCHCNSFGSKSFDCD-ETGQCRCQPGVTGPKCDRCSRGFFNFQEGGcTPCQ 1089
Cdd:cd00055 1 PCDCNGHGSLSGQCDpGTGQCECKPNTTGRRCDRCAPGYYGLPSQG-GGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
900-944 |
6.86e-12 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 62.37 E-value: 6.86e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2316002738 900 PCQCHTNGSVYEVCNKETGQCPCKENVVGRQCDECMPNCWWDAER 944
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQ 45
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1703-2211 |
7.65e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.51 E-value: 7.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1703 ERLLQLADSNLGSLVVEMDQLHSRATKVSADGEQVEDDADRIHKRAEDLEQFIRDTLLGAKDLQSKAAELNQTLSRRDgt 1782
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELE-- 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1783 pdKSLKEMKEEIQAMLAEmgKRQLGGKKSIAEEEMDLAEELYQKVKRLFGDPHQATEDLKAEIKGKLSDHEGKLQEAQDL 1862
Cdd:COG1196 330 --EELEELEEELEELEEE--LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1863 LHSAQGKMKQAGSLAEQNHANLTGLERKRSAVSAVKQEAQDVLGEGERLLDEANQLSDNINKEIEDLEEMEKELGPLHVQ 1942
Cdd:COG1196 406 EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEE 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1943 LDDKVSRLTSGLSDSLADHVHDAEEHAKQLNESAAILDGILAEAKNLSFNATAAfkaytnikanvdaaekeakaakqrAN 2022
Cdd:COG1196 486 LAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAA------------------------LE 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2023 EALALALGPEVPVKE---AAQGALQKSHRL-------LNQAKQLQNDVKENADSVAGLKGRVKAARDKTKDLLKTVNGtm 2092
Cdd:COG1196 542 AALAAALQNIVVEDDevaAAAIEYLKAAKAgratflpLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLG-- 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2093 ATLSAIPNDTAAKIAATKVVATDANATAIdVLERLGDLNLRLRGLQQNYSELEDTVNAANQMIQDPEKNIHAAGAKVKDL 2172
Cdd:COG1196 620 DTLLGRTLVAARLEAALRRAVTLAGRLRE-VTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEA 698
|
490 500 510
....*....|....*....|....*....|....*....
gi 2316002738 2173 EDEADRLLEKLQPIKKLQDNLKRNISQIKELINQARKQA 2211
Cdd:COG1196 699 LLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREEL 737
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1690-2236 |
9.04e-12 |
|
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: 71.63 E-value: 9.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1690 EELKHMLSPQKAPERLLQLADSNLGSLVVEMDQLHSRATKVSADGEQVEDDADRIHKRAEDLEQFIRDTLLGAKDLQSKA 1769
Cdd:TIGR02168 309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKV 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1770 AELNQTLSRRDGTpdksLKEMKEEIQaMLAEMGKRQlggKKSIAEEEMDLAEELYQKVKRLFGDPHQATEDLKAEikgkL 1849
Cdd:TIGR02168 389 AQLELQIASLNNE----IERLEARLE-RLEDRRERL---QQEIEELLKKLEEAELKELQAELEELEEELEELQEE----L 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1850 SDHEGKLQEAQDLLHSAQGKMKQAGSLAEQNHANLTGLERKRS-------AVSAVKQEAQD------VLGE--------- 1907
Cdd:TIGR02168 457 ERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQEnlegfseGVKALLKNQSGlsgilgVLSElisvdegye 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1908 -------GERL-------LDEANQ-----------------LSDNINKEI-----EDLEEMEKELGPL--HVQLDDKVSR 1949
Cdd:TIGR02168 537 aaieaalGGRLqavvvenLNAAKKaiaflkqnelgrvtflpLDSIKGTEIqgndrEILKNIEGFLGVAkdLVKFDPKLRK 616
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1950 LTSGLSDSL--ADHVHDAEEHAKQLNESAAI--LDGILAEAKNLSFNATAAFKAYT-NIKANVDaaekeakaakqRANEA 2024
Cdd:TIGR02168 617 ALSYLLGGVlvVDDLDNALELAKKLRPGYRIvtLDGDLVRPGGVITGGSAKTNSSIlERRREIE-----------ELEEK 685
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2025 LALALGPEVPVKEAAQGALQKSHRLLNQAKQLQNDVKENADSVAGLKGRVKAAR----------DKTKDLLKTVNGTMAT 2094
Cdd:TIGR02168 686 IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEaeveqleeriAQLSKELTELEAEIEE 765
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2095 LSAIPNDTAAKIAATKVVATDANATAIDVLERLGDLNLRLRGLQQNYSELEDTVNAANQMIQDPEKNIHAAGAKVKDLED 2174
Cdd:TIGR02168 766 LEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEE 845
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2316002738 2175 EADRLLEKLQPIKKLQDNLKRNISQIKELINQARKQANSIKVSVSSGGDCLRSYRPDIRKGR 2236
Cdd:TIGR02168 846 QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE 907
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1041-1088 |
9.70e-12 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 61.99 E-value: 9.70e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2316002738 1041 CHCNSFGSKSFDCD-ETGQCRCQPGVTGPKCDRCSRGFFNFQEGGCTPC 1088
Cdd:pfam00053 1 CDCNPHGSLSDTCDpETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1087-1132 |
1.80e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 61.22 E-value: 1.80e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1087 PCQCSHVG---NNCDANTGQCICPPNTIGERCDRCAPNHWGHDITT-GCK 1132
Cdd:cd00055 1 PCDCNGHGslsGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGgGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1088-1131 |
2.15e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 60.79 E-value: 2.15e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2316002738 1088 CQCS---HVGNNCDANTGQCICPPNTIGERCDRCAPNHWGhDITTGC 1131
Cdd:smart00180 1 CDCDpggSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYG-DGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
847-899 |
2.19e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 61.22 E-value: 2.19e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2316002738 847 PCDCHGNLDLSipGSCDPSTGQCLrCRQGYGGAACDSCADGYYGDAITAKNCQ 899
Cdd:cd00055 1 PCDCNGHGSLS--GQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1751-2210 |
2.30e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 69.80 E-value: 2.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1751 LEQFIRDTLLgaKDLQSKAAELNQTLSRRDGTPDKSLKEMKEEIQAMLAEMGK-RQLGGKKSIAEEEMDLAE----ELYQ 1825
Cdd:COG4717 39 LLAFIRAMLL--ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEyAELQEELEELEEELEELEaeleELRE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1826 KVKRL-----FGDPHQATEDLKAEIKGKLSDHEgKLQEAQDLLHSAQGKMKQAGSLAEQNHANLTGLERKRSAvsAVKQE 1900
Cdd:COG4717 117 ELEKLekllqLLPLYQELEALEAELAELPERLE-ELEERLEELRELEEELEELEAELAELQEELEELLEQLSL--ATEEE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1901 AQDVLGEGERLLDEANQLSDNINKEIEDLEEMEKELGPLHVQLddkvsrltsglsdsladHVHDAEEHAKQLNESAAILD 1980
Cdd:COG4717 194 LQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL-----------------EAAALEERLKEARLLLLIAA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1981 GILA------EAKNLSFNATAAFKAYTNIKANVDAAEKEAKAAKQRANEALALAlgpevpvkeAAQGALQKsHRLLNQAK 2054
Cdd:COG4717 257 ALLAllglggSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQAL---------PALEELEE-EELEELLA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2055 QLQNDVKENADSVAGLKGRVKAArdktKDLLKTVNGTMATLSAIPNDTAAKiaatkVVATDANATAIDVLERLGDLNLRL 2134
Cdd:COG4717 327 ALGLPPDLSPEELLELLDRIEEL----QELLREAEELEEELQLEELEQEIA-----ALLAEAGVEDEEELRAALEQAEEY 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2316002738 2135 RGLQQNYSELEDTVNAANqmiqdPEKNIHAAGAKVKDLEDEADRLLEKLQPIKKLQDNLKRNISQIKELINQARKQ 2210
Cdd:COG4717 398 QELKEELEELEEQLEELL-----GELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEED 468
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1088-1131 |
2.43e-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: 2.43e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2316002738 1088 CQCSHVG---NNCDANTGQCICPPNTIGERCDRCAPNHWGHDITTGC 1131
Cdd:pfam00053 1 CDCNPHGslsDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQ 47
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
901-947 |
2.59e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 60.79 E-value: 2.59e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2316002738 901 CQCHTNGSVYEVCNKETGQCPCKENVVGRQCDECMPNcWWDAERQEC 947
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPG-YYGDGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1493-1539 |
2.79e-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: 2.79e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1493 CQCSGHSS---TCDPETSICQnCQDNTEGDRCERCSPGFYGVVRGSPDDC 1539
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. |
1180-1237 |
3.67e-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: 60.44 E-value: 3.67e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2316002738 1180 CECNVSGSDSETCDMErgvcacadrTGKCSCKANVEGHNCDRCKPDTFGLSVRNPLGC 1237
Cdd:pfam00053 1 CDCNPHGSLSDTCDPE---------TGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
901-939 |
5.31e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 60.06 E-value: 5.31e-11
10 20 30
....*....|....*....|....*....|....*....
gi 2316002738 901 CQCHTNGSVYEVCNKETGQCPCKENVVGRQCDECMPNCW 939
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYY 39
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1682-2219 |
7.25e-11 |
|
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: 68.54 E-value: 7.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1682 LYRFENMTEELKHMLSP-----QKApERLL----QLADSNLGSLVVEMDQLHSRATKVSADGEQVEDDADRIHKRAEDLE 1752
Cdd:TIGR02168 188 LDRLEDILNELERQLKSlerqaEKA-ERYKelkaELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1753 QFIRDTLLGAKDLQSKAAELNQTLsrrdgtpdKSLKEMKEEIQAMLAEMGKRQLGGKKSIAEEEMDLAEELYQKvkrlfg 1832
Cdd:TIGR02168 267 EKLEELRLEVSELEEEIEELQKEL--------YALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKL------ 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1833 dphQATEDLKAEIKGKLSDHEGKLQEAQDLLHSAQGKMKQagsLAEQNHANLTGLERKRSAVSAVKQEAQDVLGEGERLL 1912
Cdd:TIGR02168 333 ---DELAEELAELEEKLEELKEELESLEAELEELEAELEE---LESRLEELEEQLETLRSKVAQLELQIASLNNEIERLE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1913 DEANQLSDNINKEIEDLEEMEKELGP-----LHVQLDDKVSRLTSgLSDSLADHVHDAEEHAKQLNESAAILDGILAEAK 1987
Cdd:TIGR02168 407 ARLERLEDRRERLQQEIEELLKKLEEaelkeLQAELEELEEELEE-LQEELERLEEALEELREELEEAEQALDAAERELA 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1988 NLSFNATA------AFKAYTNIKANVDAAEKEAKAAKQRANE----------ALALALGpevpvkEAAQGALQKShrlLN 2051
Cdd:TIGR02168 486 QLQARLDSlerlqeNLEGFSEGVKALLKNQSGLSGILGVLSElisvdegyeaAIEAALG------GRLQAVVVEN---LN 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2052 QAKQLQNDVKENADS-VAGLKGRVKAARDKTKD---LLKTVNGTMATLS-------AIPNDTAAKIAATKVVATDANATA 2120
Cdd:TIGR02168 557 AAKKAIAFLKQNELGrVTFLPLDSIKGTEIQGNdreILKNIEGFLGVAKdlvkfdpKLRKALSYLLGGVLVVDDLDNALE 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2121 IDVLERLGDLNLRLRGlqqnyseleDTVNA----------ANQMIQDPEKNIHAAGAKVKDLEDEADRLLEKLQPIKKLQ 2190
Cdd:TIGR02168 637 LAKKLRPGYRIVTLDG---------DLVRPggvitggsakTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKEL 707
|
570 580
....*....|....*....|....*....
gi 2316002738 2191 DNLKRNISQIKELINQARKQANSIKVSVS 2219
Cdd:TIGR02168 708 EELEEELEQLRKELEELSRQISALRKDLA 736
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
739-788 |
8.46e-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: 8.46e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2316002738 739 ACHCHGHAT---QCHEVTGHCLdCSHHTTGPHCDTCLHGYYGNATRGSpaDCQ 788
Cdd:cd00055 1 PCDCNGHGSlsgQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGG--GCQ 50
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1685-2205 |
2.72e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 66.62 E-value: 2.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1685 FENMTEELKHMLSPQKAPERLLQLADSNLGSLVVEMDQLHSRATKVSADGEQVEDDADRIHKRAEDLEQFIRDtlLGAKD 1764
Cdd:TIGR02168 353 LESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEE--LLKKL 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1765 LQSKAAELNQTLSRrdgtpdksLKEMKEEIQAMLAEMGKRqlggkKSIAEEEMDLAEELYQKVKRlfgDPHQATEDLKAe 1844
Cdd:TIGR02168 431 EEAELKELQAELEE--------LEEELEELQEELERLEEA-----LEELREELEEAEQALDAAER---ELAQLQARLDS- 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1845 IKGKLSDHEGKLQEAQDLLHSAQGKMKQAGSLAEQ-------------------NHANLTGLERKRSAVSAVKQEAQdvl 1905
Cdd:TIGR02168 494 LERLQENLEGFSEGVKALLKNQSGLSGILGVLSELisvdegyeaaieaalggrlQAVVVENLNAAKKAIAFLKQNEL--- 570
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1906 geGERLLDEANQLSDN-IN-KEIEDLEEMEKELGPL--HVQLDDKVSRLTSGLSDSL--ADHVHDAEEHAKQLNESAAI- 1978
Cdd:TIGR02168 571 --GRVTFLPLDSIKGTeIQgNDREILKNIEGFLGVAkdLVKFDPKLRKALSYLLGGVlvVDDLDNALELAKKLRPGYRIv 648
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1979 -LDGIL------------------------------------AEAKNLSFNATAAFKAYTNIKANVDAAEKEAKAAKQRA 2021
Cdd:TIGR02168 649 tLDGDLvrpggvitggsaktnssilerrreieeleekieeleEKIAELEKALAELRKELEELEEELEQLRKELEELSRQI 728
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2022 NEALALALGPEVPVKEAAQGALQKSHRLLNQAKQLQN-----------------DVKENADSVAGLKGRVKAAR---DKT 2081
Cdd:TIGR02168 729 SALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEleerleeaeeelaeaeaEIEELEAQIEQLKEELKALRealDEL 808
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2082 KDLLKTVNGTMATLSAIPNDTAAKIAATKVVATDANATAIDVLERLGDLNLRLRGLQQNYSELEDTVNAA-NQM------ 2154
Cdd:TIGR02168 809 RAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALlNERasleea 888
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 2316002738 2155 -------IQDPEKNIHAAGAKVKDLEDEADRLLEKLQPIKKLQDNLKRNISQIKELIN 2205
Cdd:TIGR02168 889 lallrseLEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLS 946
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
740-787 |
3.09e-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: 3.09e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2316002738 740 CHCHGHAT---QCHEVTGHCLdCSHHTTGPHCDTCLHGYYGNATrGSPADC 787
Cdd:pfam00053 1 CDCNPHGSlsdTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPS-DPPQGC 49
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1722-2062 |
5.21e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.85 E-value: 5.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1722 QLHSRATKVSADGEQV-----------EDDADRIHKRAE--DLEQFIrdtllgaKDLQSKAAELNQTLsrrdgtpdKSLK 1788
Cdd:TIGR02168 640 KLRPGYRIVTLDGDLVrpggvitggsaKTNSSILERRREieELEEKI-------EELEEKIAELEKAL--------AELR 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1789 EMKEEIQAMLAEMGKRQLGGKKSIAEEEMDLA--EELYQKVKRLFGDPHQATEDLKAEIKG---KLSDHEGKLQEAQDLL 1863
Cdd:TIGR02168 705 KELEELEEELEQLRKELEELSRQISALRKDLArlEAEVEQLEERIAQLSKELTELEAEIEEleeRLEEAEEELAEAEAEI 784
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1864 HSAQGKMKQAGSLAEQN------------------HANLTGLERKRSAVSAVKQEAQDVLGEGERLLDEANQLSDNINKE 1925
Cdd:TIGR02168 785 EELEAQIEQLKEELKALrealdelraeltllneeaANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEL 864
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1926 IEDLEEMEKELGPLHVQLDDKVSRLTSGLS--DSLADHVHDAEEHAKQLNESAAILDGILAEAKNlsfnataafkAYTNI 2003
Cdd:TIGR02168 865 EELIEELESELEALLNERASLEEALALLRSelEELSEELRELESKRSELRRELEELREKLAQLEL----------RLEGL 934
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2316002738 2004 KANVDaaekeakAAKQRANEALALALGPEVPVKEAAQGALQKSHRllnQAKQLQNDVKE 2062
Cdd:TIGR02168 935 EVRID-------NLQERLSEEYSLTLEEAEALENKIEDDEEEARR---RLKRLENKIKE 983
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
848-903 |
1.19e-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: 1.19e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2316002738 848 CDCHGNLDLSipGSCDPSTGQCLrCRQGYGGAACDSCADGYYGDAITAkncqPCQC 903
Cdd:pfam00053 1 CDCNPHGSLS--DTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSDP----PQGC 49
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1690-2206 |
3.01e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 63.14 E-value: 3.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1690 EELKHMLSPQKapERLLQLADsnlgslvvEMDQLHSRATKVSADGEQVEDDADRIHKRAEDLEQFIRDTLLGAKDLQSKA 1769
Cdd:PRK02224 275 EELAEEVRDLR--ERLEELEE--------ERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEA 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1770 ---AELNQTLSRRDGTPDKSLKEMKEEIQAMLAEMGKRQlgGKKSIAEEEMDLAEELYQKVKRLFGDPHQATEDL---KA 1843
Cdd:PRK02224 345 eslREDADDLEERAEELREEAAELESELEEAREAVEDRR--EEIEELEEEIEELRERFGDAPVDLGNAEDFLEELreeRD 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1844 EIKGKLSDHEGKLQEAQDLLHSAQ-----GKMKQAG-SLAEQNHANltGLERKRSAVSAVKQEAQDVLGEGERLLDEANQ 1917
Cdd:PRK02224 423 ELREREAELEATLRTARERVEEAEalleaGKCPECGqPVEGSPHVE--TIEEDRERVEELEAELEDLEEEVEEVEERLER 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1918 LsdninkeiEDLEEMEKELGplhvQLDDKVSRLTSGLSDSlADHVHDAEEHAKQLNESAAILDgilAEAKNLSFNATAAf 1997
Cdd:PRK02224 501 A--------EDLVEAEDRIE----RLEERREDLEELIAER-RETIEEKRERAEELRERAAELE---AEAEEKREAAAEA- 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1998 kaytnikanvdaaekeakaaKQRANEALAlalgpEVPVKEAAQGALQKSHRLLNQAKQLQNDVKENADSVAGLKGRVKA- 2076
Cdd:PRK02224 564 --------------------EEEAEEARE-----EVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREAl 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2077 --ARDKTKDLLKTVNGTMATLsaipndtAAKIAATKVVATDAN-ATAIDVLERLGDlnlRLRGLQQNYSELEDTVNAANQ 2153
Cdd:PRK02224 619 aeLNDERRERLAEKRERKREL-------EAEFDEARIEEAREDkERAEEYLEQVEE---KLDELREERDDLQAEIGAVEN 688
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2316002738 2154 MIQDPEknihaagakvkDLEDEADRLLEKLQPIKKLQDNL---------------KRNISQIKELINQ 2206
Cdd:PRK02224 689 ELEELE-----------ELRERREALENRVEALEALYDEAeelesmygdlraelrQRNVETLERMLNE 745
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
398-449 |
3.15e-09 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 55.05 E-value: 3.15e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2316002738 398 PCTCDPHGSVSQSCVADSsqatptqpaGSCRCKEGFGGLQCDRCAVGYMGYP 449
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGT---------GQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1493-1540 |
7.04e-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: 7.04e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2316002738 1493 CQCSGHSS---TCDPETSICQnCQDNTEGDRCERCSPGFYGvVRGSPDDCK 1540
Cdd:cd00055 2 CDCNGHGSlsgQCDPGTGQCE-CKPNTTGRRCDRCAPGYYG-LPSQGGGCQ 50
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1703-1987 |
9.25e-09 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 61.77 E-value: 9.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1703 ERLLQLADSNLGSLV----VEMDQLHSRATKvsaDGEQVEDDADRIHKRAEDLEQFIRDTLLGAKD-LQSKAAELNQTLS 1777
Cdd:NF041483 188 ERLAEEARQRLGSEAesarAEAEAILRRARK---DAERLLNAASTQAQEATDHAEQLRSSTAAESDqARRQAAELSRAAE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1778 RRDGTPDKSLKEMKEEIQAMLAEM---GKRQLGGKKSIAEEEMDLAEElyqKVKRLFGDPHQATEDLKAEIKGKLSDHEG 1854
Cdd:NF041483 265 QRMQEAEEALREARAEAEKVVAEAkeaAAKQLASAESANEQRTRTAKE---EIARLVGEATKEAEALKAEAEQALADARA 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1855 klqEAQDLLHSAQGKMKQAGslAEQNHANLTGLERK------------RSAVSAVKQEAQDVLGEGE----RLLDEANQL 1918
Cdd:NF041483 342 ---EAEKLVAEAAEKARTVA--AEDTAAQLAKAARTaeevltkasedaKATTRAAAEEAERIRREAEaeadRLRGEAADQ 416
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2316002738 1919 SDNINKEIEDleeMEKELGPLHVQLDDKVSRLtSGLSDSL-ADHVHDAE--------EHAKQLNESAAILDGILAEAK 1987
Cdd:NF041483 417 AEQLKGAAKD---DTKEYRAKTVELQEEARRL-RGEAEQLrAEAVAEGErirgearrEAVQQIEEAARTAEELLTKAK 490
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1827-2213 |
9.52e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 61.59 E-value: 9.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1827 VKRLFGDPHQATEDLKAEIKGKlsdhegklqEAQDLlHSAQGKMKQAgsLAEQNhANLTGLERKRSAVSAVKQEAQDVLG 1906
Cdd:PRK02224 178 VERVLSDQRGSLDQLKAQIEEK---------EEKDL-HERLNGLESE--LAELD-EEIERYEEQREQARETRDEADEVLE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1907 EGERLLDEANQLSDNINKEIEDLEEMEKElgplhvqlddkvsrltsglSDSLADHVHDAEEHAKQLNESaaiLDGILAEA 1986
Cdd:PRK02224 245 EHEERREELETLEAEIEDLRETIAETERE-------------------REELAEEVRDLRERLEELEEE---RDDLLAEA 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1987 knlSFNATAAfkaytnikanvdaaekeakaakqranEALALALGPEVPVKEAAQGALQKsHRLlnQAKQLQNDVKENADS 2066
Cdd:PRK02224 303 ---GLDDADA--------------------------EAVEARREELEDRDEELRDRLEE-CRV--AAQAHNEEAESLRED 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2067 VAGLKGRVKAARDKTKDLLKTVNGTMATL----SAIP------NDTAAKIAATKVVATDANATAIDVLERLGDLNLRLRG 2136
Cdd:PRK02224 351 ADDLEERAEELREEAAELESELEEAREAVedrrEEIEeleeeiEELRERFGDAPVDLGNAEDFLEELREERDELREREAE 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2137 LQQNYSELEDTVNAANQMI---------QDPEKNIHAAG------------AKVKDLEDEADRLLEKLQPIKKLQ----- 2190
Cdd:PRK02224 431 LEATLRTARERVEEAEALLeagkcpecgQPVEGSPHVETieedrerveeleAELEDLEEEVEEVEERLERAEDLVeaedr 510
|
410 420
....*....|....*....|....
gi 2316002738 2191 -DNLKRNISQIKELINQARKQANS 2213
Cdd:PRK02224 511 iERLEERREDLEELIAERRETIEE 534
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
399-456 |
1.22e-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: 1.22e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2316002738 399 CTCDPHGSVSQSCvaDSSQatptqpaGSCRCKEGFGGLQCDRCAVGYMGYPFCQRCNC 456
Cdd:pfam00053 1 CDCNPHGSLSDTC--DPET-------GQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1685-2219 |
1.56e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.85 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1685 FENMTEELKHMLSPQKAPERLLQLADSNLGSLVVEMDQLHSRATKVSADGEQVEddadrihKRAEDLEQfirdtllgakd 1764
Cdd:PRK03918 174 IKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLE-------KEVKELEE----------- 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1765 LQSKAAELNQTLSRRDGTPdKSLKEMKEEIQAMLAEMGKRQLGGKKSIAE-EEMDLAEELYQKVKRLFGDphqaTEDLKA 1843
Cdd:PRK03918 236 LKEEIEELEKELESLEGSK-RKLEEKIRELEERIEELKKEIEELEEKVKElKELKEKAEEYIKLSEFYEE----YLDELR 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1844 EIKGKLSDHEGKLQEAQDLLHSAQGKMKQAGSLAEQnhanLTGLERKRSAVSAVKQEAQDVLgegeRLLDEANQLSDNI- 1922
Cdd:PRK03918 311 EIEKRLSRLEEEINGIEERIKELEEKEERLEELKKK----LKELEKRLEELEERHELYEEAK----AKKEELERLKKRLt 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1923 NKEIEDLEEMEKELGPLHVQLDDKVSRLTSGLS--DSLADHVHDA-------------------EEHAKQL-NESAAILD 1980
Cdd:PRK03918 383 GLTPEKLEKELEELEKAKEEIEEEISKITARIGelKKEIKELKKAieelkkakgkcpvcgreltEEHRKELlEEYTAELK 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1981 GILAEAKNLsfnaTAAFKAYTNIKANVDAaekeakaakqranealALALGPEvpvkeaaqgaLQKSHRLLNQAKQLQNDV 2060
Cdd:PRK03918 463 RIEKELKEI----EEKERKLRKELRELEK----------------VLKKESE----------LIKLKELAEQLKELEEKL 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2061 KEnadsvAGLKGRVKAARD--KTKDLLKTVNGTMATLsaipNDTAAKIAATKVVATDANATAIDVLERLGDLNLRLRGLq 2138
Cdd:PRK03918 513 KK-----YNLEELEKKAEEyeKLKEKLIKLKGEIKSL----KKELEKLEELKKKLAELEKKLDELEEELAELLKELEEL- 582
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2139 qNYSELEDTvnaaNQMIQDPEKnIHAAGAKVKDLEDEADRLLEKLqpiKKLQDNLKR---NISQIKELINQARKQANSIK 2215
Cdd:PRK03918 583 -GFESVEEL----EERLKELEP-FYNEYLELKDAEKELEREEKEL---KKLEEELDKafeELAETEKRLEELRKELEELE 653
|
....
gi 2316002738 2216 VSVS 2219
Cdd:PRK03918 654 KKYS 657
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1134-1182 |
1.63e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 52.74 E-value: 1.63e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2316002738 1134 CGCSVIGSVTQQCNVNTGCCLCRDSFRGEKCNECQIGYRDFPQCTQCEC 1182
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1180-1237 |
1.65e-08 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 52.74 E-value: 1.65e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2316002738 1180 CECNVSGSDSETCDMErgvcacadrTGKCSCKANVEGHNCDRCKPDTFGLSvRNPLGC 1237
Cdd:cd00055 2 CDCNGHGSLSGQCDPG---------TGQCECKPNTTGRRCDRCAPGYYGLP-SQGGGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1180-1237 |
2.08e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 52.31 E-value: 2.08e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2316002738 1180 CECNVSGSDSETCDMErgvcacadrTGKCSCKANVEGHNCDRCKPDTFGlsvRNPLGC 1237
Cdd:smart00180 1 CDCDPGGSASGTCDPD---------TGQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
848-891 |
2.13e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 52.31 E-value: 2.13e-08
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2316002738 848 CDCHgnLDLSIPGSCDPSTGQCLrCRQGYGGAACDSCADGYYGD 891
Cdd:smart00180 1 CDCD--PGGSASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD 41
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2035-2289 |
2.50e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 59.15 E-value: 2.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2035 VKEAAQGALQKSHRLLNQAKQLQNDVKENADSVAGLKGRVKAAR---DKTKDLLKTVNGTMATLSAIPNDTAAKIAATKv 2111
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARselEQLEEELEELNEQLQAAQAELAQAQEELESLQ- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2112 vatdanataidvlERLGDLNLRLRGLQQNYSELEDTVNAANQMIQDPEKNIHAAGAKVKDLEDEADRLLEKLQPIKKLQD 2191
Cdd:COG4372 108 -------------EEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2192 NLKRN--ISQIKELINQARKQANSIKVsvssggdcLRSYRPDIRKGRYNTIVLHVKTTTPDNLLFYLGSAKYVDFLALEM 2269
Cdd:COG4372 175 ALSEAeaEQALDELLKEANRNAEKEEE--------LAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEE 246
|
250 260
....*....|....*....|
gi 2316002738 2270 RKGKVNFLWDVGSGVGRVEY 2289
Cdd:COG4372 247 DKEELLEEVILKEIEELELA 266
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1699-2232 |
3.28e-08 |
|
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: 59.80 E-value: 3.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1699 QKAPERLLQLADSnlgslVVEMDQLHSR--------ATKVSADGE---QVEDDADRIHKRAEDLEQFI------------ 1755
Cdd:pfam01576 15 QKVKERQQKAESE-----LKELEKKHQQlceeknalQEQLQAETElcaEAEEMRARLAARKQELEEILhelesrleeeee 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1756 RDTLLGA--KDLQSKAAELNQTLSRRDG----------TPDKSLKEMKEEIqaMLAEMGKRQLGGKKSIAEEEM-----D 1818
Cdd:pfam01576 90 RSQQLQNekKKMQQHIQDLEEQLDEEEAarqklqlekvTTEAKIKKLEEDI--LLLEDQNSKLSKERKLLEERIseftsN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1819 LAEElYQKVKRLFGDPHQaTEDLKAEIKGKLSDHEGKLQEaqdlLHSAQGKMK-QAGSLAEQnHANLTG-LERKRSAVSA 1896
Cdd:pfam01576 168 LAEE-EEKAKSLSKLKNK-HEAMISDLEERLKKEEKGRQE----LEKAKRKLEgESTDLQEQ-IAELQAqIAELRAQLAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1897 VKQEAQDVLGegeRLLDEANQLSDNINKeiedLEEMEKELGPLHVQLD-DKVSRltsglsdsladhvHDAEEHAKQLNES 1975
Cdd:pfam01576 241 KEEELQAALA---RLEEETAQKNNALKK----IRELEAQISELQEDLEsERAAR-------------NKAEKQRRDLGEE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1976 AAILDGILAEaknlSFNATAAfkaytnikanvdaaekEAKAAKQRANEALAL--ALGPEVPVKEAAQGALQKSHrllNQA 2053
Cdd:pfam01576 301 LEALKTELED----TLDTTAA----------------QQELRSKREQEVTELkkALEEETRSHEAQLQEMRQKH---TQA 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2054 KQLQNDVKENADsvaglkgRVKAARDKTKDLLKTVNGTMA----TLSAIPNDTAAK-------IAATKVVATDANATAID 2122
Cdd:pfam01576 358 LEELTEQLEQAK-------RNKANLEKAKQALESENAELQaelrTLQQAKQDSEHKrkklegqLQELQARLSESERQRAE 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2123 VLERLGDLNLRLRGLQQNYSELEDT-------VNAANQMIQDPEKNIH-------AAGAKVKDLEDEADRLLEKLQPIKK 2188
Cdd:pfam01576 431 LAEKLSKLQSELESVSSLLNEAEGKniklskdVSSLESQLQDTQELLQeetrqklNLSTRLRQLEDERNSLQEQLEEEEE 510
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 2316002738 2189 LQDNLKRNISQIKELINQARKQANSIKVSVSSGGDCLRSYRPDI 2232
Cdd:pfam01576 511 AKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQREL 554
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1706-1936 |
3.30e-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: 59.69 E-value: 3.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1706 LQLADSNLGSLVVEMDQLHSRATKVSADGEQVEDDADRIHKRAEDLEQFIRDTLLGAKDLQSKAAELNQTLSRRDgtpdK 1785
Cdd:TIGR02168 770 LEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLE----E 845
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1786 SLKEMKEEIQAMLAEMGKRQLGGKKsiAEEEMDLAEELYQKVKRLFGDPHQATEDLKAEIK---GKLSDHEGKLQEAQDL 1862
Cdd:TIGR02168 846 QIEELSEDIESLAAEIEELEELIEE--LESELEALLNERASLEEALALLRSELEELSEELReleSKRSELRRELEELREK 923
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1863 LHSAQ---GKMKQ-----AGSLAEQNHANLTGLERKRSAVSAVKQEAQDVLGEGERLLD--------------EANQLSD 1920
Cdd:TIGR02168 924 LAQLElrlEGLEVridnlQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKelgpvnlaaieeyeELKERYD 1003
|
250
....*....|....*.
gi 2316002738 1921 NINKEIEDLEEMEKEL 1936
Cdd:TIGR02168 1004 FLTAQKEDLTEAKETL 1019
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
740-782 |
3.83e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 51.93 E-value: 3.83e-08
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2316002738 740 CHCHGHAT-QCHEVTGHCLdCSHHTTGPHCDTCLHGYYGNATRG 782
Cdd:smart00180 3 CDPGGSASgTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1493-1539 |
7.67e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 50.77 E-value: 7.67e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1493 CQCSG---HSSTCDPETSICQnCQDNTEGDRCERCSPGFYGVvrgSPDDC 1539
Cdd:smart00180 1 CDCDPggsASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD---GPPGC 46
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1710-2214 |
9.63e-08 |
|
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: 58.19 E-value: 9.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1710 DSNLGSLVVEMDQLHSRAT--------KVSADGEQVEDDADRIHKRAEDLEQFIRDTLLGAKDLQSKAAEL--------- 1772
Cdd:pfam05483 189 NNNIEKMILAFEELRVQAEnarlemhfKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLtflleesrd 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1773 --NQtLSRRDGTPDKSLKEMKEEIQAMLAEMGKRQLGGKKSIAEEEMdLAEELYQKVKRLFgdphQATEDLKAEI----K 1846
Cdd:pfam05483 269 kaNQ-LEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKA-LEEDLQIATKTIC----QLTEEKEAQMeelnK 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1847 GK------LSDHEGKLQEAQDLLHSAQGKMkqagslaEQNHANL----TGLERKRSAVSAVK----------QEAQDVLG 1906
Cdd:pfam05483 343 AKaahsfvVTEFEATTCSLEELLRTEQQRL-------EKNEDQLkiitMELQKKSSELEEMTkfknnkevelEELKKILA 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1907 EGERLLDEANQlsdnINKEIEDLEEMEKELgplhvqlddkvsrltSGLSDSLADHVHDAEehaKQLNESAAILDGILAEA 1986
Cdd:pfam05483 416 EDEKLLDEKKQ----FEKIAEELKGKEQEL---------------IFLLQAREKEIHDLE---IQLTAIKTSEEHYLKEV 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1987 KNLSFNATAAFKAYTNIKANVDAAEKEAKAAKQRANEaLALALGPEvpvKEAAQGALQKSHRLLNQAKQLQ--------- 2057
Cdd:pfam05483 474 EDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASD-MTLELKKH---QEDIINCKKQEERMLKQIENLEekemnlrde 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2058 ------------NDVK-------ENADS----VAGLKGRVKAARDKTKDLLKTVNGTMATLSAIPNDTAAKIAATKVVAT 2114
Cdd:pfam05483 550 lesvreefiqkgDEVKckldkseENARSieyeVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENK 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2115 DANATAIDVlerlGDLNLRLRGLQQNYSELEDTVNAANQMIQDPEKNIHAAGAKVKDLEDEAdrllEKLQpiKKLQDNLK 2194
Cdd:pfam05483 630 QLNAYEIKV----NKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEA----VKLQ--KEIDKRCQ 699
|
570 580
....*....|....*....|
gi 2316002738 2195 RNISQIKELINQARKQANSI 2214
Cdd:pfam05483 700 HKIAEMVALMEKHKHQYDKI 719
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
454-500 |
9.95e-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: 9.95e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2316002738 454 CNCSVEGSTNaDPCIT---PCMCKENVEGENCDRCKLGFYNLQGDNQRGC 500
Cdd:pfam00053 1 CDCNPHGSLS-DTCDPetgQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1751-2084 |
1.33e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 56.83 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1751 LEQFIRDTLLGAKDLQSKAAELNQTLSRRDG---TPDKSLKEMKEEIQAMLAEMGKRQ-----LGGKKSIAEEEMdlaEE 1822
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREeleQLEEELEQARSELEQLEEELEELNeqlqaAQAELAQAQEEL---ES 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1823 LYQKVKRLfgdpHQATEDLKAEIKgKLSDHEGKLQEAQDLLhsaQGKMKQAGSLAEQNHANLTGLERKRSAVSAVKQ--E 1900
Cdd:COG4372 106 LQEEAEEL----QEELEELQKERQ-DLEQQRKQLEAQIAEL---QSEIAEREEELKELEEQLESLQEELAALEQELQalS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1901 AQDVLGEGERLLDEANQlsdNINKEIEDLEEMEKELGPLHVQLDDKVSRLTSGLSDSLADHVHDAEEHAKQLNESAAILD 1980
Cdd:COG4372 178 EAEAEQALDELLKEANR---NAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1981 GILAEAKNLSfnATAAFKAYTNIKANVDAAEKEAKAAKQRANEALALALGPEVPVKEAAQGALQKSHRLLNQAKQLQNDV 2060
Cdd:COG4372 255 VILKEIEELE--LAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELAL 332
|
330 340
....*....|....*....|....
gi 2316002738 2061 KENADSVAGLKGRVKAARDKTKDL 2084
Cdd:COG4372 333 AILLAELADLLQLLLVGLLDNDVL 356
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
399-450 |
1.49e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 50.00 E-value: 1.49e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2316002738 399 CTCDPHGSVSQSCVADSsqatptqpaGSCRCKEGFGGLQCDRCAVGYMGYPF 450
Cdd:smart00180 1 CDCDPGGSASGTCDPDT---------GQCECKPNVTGRRCDRCAPGYYGDGP 43
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
949-986 |
1.59e-07 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 50.05 E-value: 1.59e-07
10 20 30
....*....|....*....|....*....|....*....
gi 2316002738 949 PCRCSPHGSISQRCDVE-GRCICRPGFVGRRCDLRRQGY 986
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGtGQCECKPNTTGRRCDRCAPGY 39
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1642-1975 |
1.65e-07 |
|
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: 57.37 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1642 AGIISCDDECSGL-LISDMDRLYRIIT-DVTLTTP--------LPPPYKMLYR---FENMTEELKHMLSPQKAPERLLQL 1708
Cdd:TIGR02168 623 GGVLVVDDLDNALeLAKKLRPGYRIVTlDGDLVRPggvitggsAKTNSSILERrreIEELEEKIEELEEKIAELEKALAE 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1709 ADSNLGSLVVEMDQLHSRATKVSADGEQVEDDADRIHKRAEDLEQFIRDTllgAKDLQSKAAELNQTLSRRDGTPDKsLK 1788
Cdd:TIGR02168 703 LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL---SKELTELEAEIEELEERLEEAEEE-LA 778
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1789 EMKEEIQAMLAEMGKRQlgGKKSIAEEEMDLAEELYQKVKRLFGDPHQATEDLKAEIKGK---LSDHEGKLQEAQDLLHS 1865
Cdd:TIGR02168 779 EAEAEIEELEAQIEQLK--EELKALREALDELRAELTLLNEEAANLRERLESLERRIAATerrLEDLEEQIEELSEDIES 856
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1866 AQGKMKQAGSLAEQNHANLTGLERKRSAVSAV-------KQEAQDVLGEGERLLDEANQLSDNINKEIEDLEEmekELGP 1938
Cdd:TIGR02168 857 LAAEIEELEELIEELESELEALLNERASLEEAlallrseLEELSEELRELESKRSELRRELEELREKLAQLEL---RLEG 933
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2316002738 1939 LHVQLDDKVSRLTSGLSDSLADHV----------HDAEEHAKQLNES 1975
Cdd:TIGR02168 934 LEVRIDNLQERLSEEYSLTLEEAEalenkieddeEEARRRLKRLENK 980
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1735-2215 |
1.70e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.38 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1735 EQVEDDADRIHKRAEDLEQFIRDTLLGAKDLQSKAAELNQTLSRRDGTPDKsLKEMK------EEIQAMLAEMgkRQLgg 1808
Cdd:PRK03918 303 EEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKR-LEELEerhelyEEAKAKKEEL--ERL-- 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1809 KKSIAEEEMDLAEELYQKVKRLFGDPHQATEDLKAEIkGKLSDHEGKLQEAQDLLHSAQGKMKQAGS-LAEQNHANLtgL 1887
Cdd:PRK03918 378 KKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARI-GELKKEIKELKKAIEELKKAKGKCPVCGReLTEEHRKEL--L 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1888 ERKRSAVSAVKQEAQDVLGEGERLLDEAnqlsdninKEIEDLEEMEKELGPLHvqlddkvsrltsglsdSLADHVHDAEE 1967
Cdd:PRK03918 455 EEYTAELKRIEKELKEIEEKERKLRKEL--------RELEKVLKKESELIKLK----------------ELAEQLKELEE 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1968 HAKQLNesaaildgiLAEAKnlsfnatAAFKAYTNIKanvdaaekeakaakQRANEALALALGPEVPVKEAAqgALQKSH 2047
Cdd:PRK03918 511 KLKKYN---------LEELE-------KKAEEYEKLK--------------EKLIKLKGEIKSLKKELEKLE--ELKKKL 558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2048 RLLNQAKQ--------LQNDVKENA-DSVAGLKGRVKAARDKTKDLLKtvngtmatLSAIPND---TAAKIAATKVVATD 2115
Cdd:PRK03918 559 AELEKKLDeleeelaeLLKELEELGfESVEELEERLKELEPFYNEYLE--------LKDAEKElerEEKELKKLEEELDK 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2116 ANATAIDVLERLGDLNLRLRGLQQNYSElEDTVNAANQMIQdPEKNIHAAGAKVKDLE---DEADRLLEKLQ-------P 2185
Cdd:PRK03918 631 AFEELAETEKRLEELRKELEELEKKYSE-EEYEELREEYLE-LSRELAGLRAELEELEkrrEEIKKTLEKLKeeleereK 708
|
490 500 510
....*....|....*....|....*....|
gi 2316002738 2186 IKKLQDNLKRNISQIKELINQARKQANSIK 2215
Cdd:PRK03918 709 AKKELEKLEKALERVEELREKVKKYKALLK 738
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1686-2006 |
2.38e-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: 57.00 E-value: 2.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1686 ENMTEELKHM---LSPQKAPERLLQLADSNLgslvvEMDQLHSRATKVSADGEQVEDDADRIHKRAEDLEQFIRDTLLGA 1762
Cdd:TIGR02169 754 ENVKSELKELearIEELEEDLHKLEEALNDL-----EARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEK 828
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1763 KDLQSKAAELNQtlSRRDgtpdksLKEMKEEIQAMLAEMGKRqlggKKSIAEEEMDLAEELYQKVKRLfgdphqatEDLK 1842
Cdd:TIGR02169 829 EYLEKEIQELQE--QRID------LKEQIKSIEKEIENLNGK----KEELEEELEELEAALRDLESRL--------GDLK 888
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1843 AEIKgklsDHEGKLQEAQDllhsaqgKMKQAGSLAEQNHANLTGLERKRSAVSAVKQEAQDVLGEGERLLDEANQLSDnI 1922
Cdd:TIGR02169 889 KERD----ELEAQLRELER-------KIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLED-V 956
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1923 NKEIEDLEEMEKELGPLHV----QLDDKVSRLtsglsDSLadhvhdAEEHAKQLNESAAILDGI--LAEAKNLSFnataa 1996
Cdd:TIGR02169 957 QAELQRVEEEIRALEPVNMlaiqEYEEVLKRL-----DEL------KEKRAKLEEERKAILERIeeYEKKKREVF----- 1020
|
330
....*....|
gi 2316002738 1997 FKAYTNIKAN 2006
Cdd:TIGR02169 1021 MEAFEAINEN 1030
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1600-1637 |
3.24e-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: 49.27 E-value: 3.24e-07
10 20 30
....*....|....*....|....*....|....*...
gi 2316002738 1600 CKCSPWGAWPGPCDPVTGQCRCRVGASGRSCDLCMDRH 1637
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGY 39
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1600-1637 |
4.20e-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: 48.89 E-value: 4.20e-07
10 20 30
....*....|....*....|....*....|....*...
gi 2316002738 1600 CKCSPWGAWPGPCDPVTGQCRCRVGASGRSCDLCMDRH 1637
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGY 38
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1725-2275 |
4.59e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 56.06 E-value: 4.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1725 SRATKVSADGEQVEDDADRIHKRAEDLEQFIRDTLLGakdlQSKAAELNQTLSRRDgtpdkslkEMKEEIQAMLAEmgkr 1804
Cdd:PRK01156 87 ERRGKGSRREAYIKKDGSIIAEGFDDTTKYIEKNILG----ISKDVFLNSIFVGQG--------EMDSLISGDPAQ---- 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1805 qlggKKSIAEE--EMDLAEELYQKVKRLFgdphqatEDLKAEIKgKLSDHEGKLQEAQDLLHSAQGKMkqagslaEQNHA 1882
Cdd:PRK01156 151 ----RKKILDEilEINSLERNYDKLKDVI-------DMLRAEIS-NIDYLEEKLKSSNLELENIKKQI-------ADDEK 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1883 NLTGLERKRSAVSAVKQEAQDVLGEGERLLDEANQLSDNINKEIEDLEEMEkelgplhvqlddkvSRLTSGLSDSlaDHV 1962
Cdd:PRK01156 212 SHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAE--------------SDLSMELEKN--NYY 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1963 HDAEEHAKQLNESAAILDgilAEAKNLSFNATAAFKAYTNIKANVDAAEKEAKAAKQRANEAlalalgpevpvkEAAQGA 2042
Cdd:PRK01156 276 KELEERHMKIINDPVYKN---RNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVL------------QKDYND 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2043 LQKSHRLLNQAKQLQNDVKENADSVAGLKGRVKAARDKTKDLLKTVNGTMATLSAIPNDTAAKIAATKVVATDANATAID 2122
Cdd:PRK01156 341 YIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQD 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2123 VLERLGDLNLRLRGLQQNYSELEDTVN------------------AANQMIQDPEKNIHAAGAKVKDLEDEADRLLEKLQ 2184
Cdd:PRK01156 421 ISSKVSSLNQRIRALRENLDELSRNMEmlngqsvcpvcgttlgeeKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIV 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2185 PIKKLQDNLkrNISQIKELINQ------ARKQANSIKVSVSSGGDCLRSYrpDIRKGRYNTI---VLHVKTTTPDNLLFY 2255
Cdd:PRK01156 501 DLKKRKEYL--ESEEINKSINEynkiesARADLEDIKIKINELKDKHDKY--EEIKNRYKSLkleDLDSKRTSWLNALAV 576
|
570 580
....*....|....*....|
gi 2316002738 2256 LGSakyVDFLALEMRKGKVN 2275
Cdd:PRK01156 577 ISL---IDIETNRSRSNEIK 593
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1686-1990 |
4.98e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.84 E-value: 4.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1686 ENMTEELKHMLSPQKAPERLLQLADSnlgsLVVEMDQLHSRATKVSAdgEQVEDDADRIHKRAEDLEQFIRDTLLGAKDL 1765
Cdd:PRK03918 344 KKKLKELEKRLEELEERHELYEEAKA----KKEELERLKKRLTGLTP--EKLEKELEELEKAKEEIEEEISKITARIGEL 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1766 QSKAAELNQTLSR------------RDGTPD-----------------KSLKEMKEEIQAMLAEMGK--------RQLGG 1808
Cdd:PRK03918 418 KKEIKELKKAIEElkkakgkcpvcgRELTEEhrkelleeytaelkrieKELKEIEEKERKLRKELRElekvlkkeSELIK 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1809 KKSIAE--------------EEMDLAEELYQKVKRLF----GDPHQATEDLK--AEIKGKLSDHEGKLQEAQDLLHSAQG 1868
Cdd:PRK03918 498 LKELAEqlkeleeklkkynlEELEKKAEEYEKLKEKLiklkGEIKSLKKELEklEELKKKLAELEKKLDELEEELAELLK 577
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1869 KMKQAG-SLAEQNHANLTGLE---RKRSAVSAVKQEAQDVLGEGERLLDEANQLSDNINKEIEDLEEMEKELGPLHVQLD 1944
Cdd:PRK03918 578 ELEELGfESVEELEERLKELEpfyNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYS 657
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1945 D----KVSRLTSGLSDSLADHVHDAEEHAKQLNESAAILDGILAEAKNLS 1990
Cdd:PRK03918 658 EeeyeELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEERE 707
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1685-1936 |
5.15e-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: 55.88 E-value: 5.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1685 FENMTEELKHMLSPQKAPERLLQLADSNLGSLVVE----MDQL------HS------RATKVSADgEQVEDDADRIHKRA 1748
Cdd:pfam05483 298 LEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEkeaqMEELnkakaaHSfvvtefEATTCSLE-ELLRTEQQRLEKNE 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1749 EDLEqfirdtlLGAKDLQSKAAELNQTlsrrdgTPDKSLKEMK-EEIQAMLAEmgKRQLGGKKSIAEEemdLAEELYQKV 1827
Cdd:pfam05483 377 DQLK-------IITMELQKKSSELEEM------TKFKNNKEVElEELKKILAE--DEKLLDEKKQFEK---IAEELKGKE 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1828 KRLFGdPHQATE----DLKAEIKGKLSDHEGKLQEAQDLLHSAQGKMKQAGSLAeqNHANLTGLERKRsavsaVKQEAQD 1903
Cdd:pfam05483 439 QELIF-LLQAREkeihDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELT--AHCDKLLLENKE-----LTQEASD 510
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2316002738 1904 VlgegerLLDEANQLSDNIN---------KEIEDLEEMEKEL 1936
Cdd:pfam05483 511 M------TLELKKHQEDIINckkqeermlKQIENLEEKEMNL 546
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1600-1637 |
5.34e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 48.46 E-value: 5.34e-07
10 20 30
....*....|....*....|....*....|....*...
gi 2316002738 1600 CKCSPWGAWPGPCDPVTGQCRCRVGASGRSCDLCMDRH 1637
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGY 38
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1809-2211 |
6.38e-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: 55.46 E-value: 6.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1809 KKSIAEEEMDLAEElyqKVKRLfgdphQATEDLKAEIKGKLSDHEGKLQEAQDLLHSaqgKMKQAGS-LAEQNHANLTGL 1887
Cdd:TIGR02169 171 KKEKALEELEEVEE---NIERL-----DLIIDEKRQQLERLRREREKAERYQALLKE---KREYEGYeLLKEKEALERQK 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1888 ERKRSAVSAVKQEAQDV---LGEGERLLDEANQLSDNINKEIEDLEEME-----KELGPLHVQLddkvsrltSGLSDSLA 1959
Cdd:TIGR02169 240 EAIERQLASLEEELEKLteeISELEKRLEEIEQLLEELNKKIKDLGEEEqlrvkEKIGELEAEI--------ASLERSIA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1960 DHVHDAEEHAKQLNESAAILDGILAEAKNLSfnataafkaytnikanvdaaekeakaakqRANEALALALgpeVPVKEAA 2039
Cdd:TIGR02169 312 EKERELEDAEERLAKLEAEIDKLLAEIEELE-----------------------------REIEEERKRR---DKLTEEY 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2040 QgALQKSHRLLNQakQLQNDVKENADSVAGLKGRVKAArDKTKDLLKTVNGTMATLSaipnDTAAKIAatkvvatdanat 2119
Cdd:TIGR02169 360 A-ELKEELEDLRA--ELEEVDKEFAETRDELKDYREKL-EKLKREINELKRELDRLQ----EELQRLS------------ 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2120 aidvlERLGDLNLRLRGLQQNYSELEDTVNAANQMIQDPEKNIHAAGAKVKDLEDEADRLLEKLQPIKKLQDNLKRNISQ 2199
Cdd:TIGR02169 420 -----EELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAE 494
|
410
....*....|..
gi 2316002738 2200 IKelinqARKQA 2211
Cdd:TIGR02169 495 AE-----AQARA 501
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1785-2080 |
8.18e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.33 E-value: 8.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1785 KSLKEMKEEIQAMLAEMGKRQLGGKKSIAEEEMDLAEELYQkvkrlfgdphQATEDLkAEIKGKLSDHEGKLQEAQDLLH 1864
Cdd:COG1196 216 RELKEELKELEAELLLLKLRELEAELEELEAELEELEAELE----------ELEAEL-AELEAELEELRLELEELELELE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1865 SAQGKMKQAGSLAEQnhanltgLERKRSAVSAVKQEAQDVLGEGERLLDEANQLSDNINKEIEDLEEMEKELGPLHVQLD 1944
Cdd:COG1196 285 EAQAEEYELLAELAR-------LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1945 DKVSRLTSGLSDSLADHVHDAEEHAKQLNESAAILDGILAEAKNLSFNATAAfkaytnikANVDAAEKEAKAAKQRANEA 2024
Cdd:COG1196 358 AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE--------EALLERLERLEEELEELEEA 429
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2316002738 2025 LALALGPEVPVKEAAQGALQKSHRLLNQAKQLQNDVKENADSVAGLKGRVKAARDK 2080
Cdd:COG1196 430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEE 485
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1134-1175 |
8.99e-07 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 48.12 E-value: 8.99e-07
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2316002738 1134 CGCSVIGSVTQQCNVNTGCCLCRDSFRGEKCNECQIGYRDFP 1175
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1745-2211 |
9.98e-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: 54.80 E-value: 9.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1745 HKR--AEDLEQF---IRDTL---LGAKDLQSK----AAELNQTLSRRDGTPDKSLKEMK-------EEIQAMLaEMGKRQ 1805
Cdd:pfam01576 293 QRRdlGEELEALkteLEDTLdttAAQQELRSKreqeVTELKKALEEETRSHEAQLQEMRqkhtqalEELTEQL-EQAKRN 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1806 LGG----KKSIAEEEMDLAEEL--YQKVKrlfGDPHQATEDLKA---EIKGKLSDHEGKLQEAQDLLHSAQGKMKQAGSL 1876
Cdd:pfam01576 372 KANlekaKQALESENAELQAELrtLQQAK---QDSEHKRKKLEGqlqELQARLSESERQRAELAEKLSKLQSELESVSSL 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1877 AEQNHANLTGLERKRSAVSAVKQEAQDVLGEGER-----------LLDEAN-------------------------QLSD 1920
Cdd:pfam01576 449 LNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRqklnlstrlrqLEDERNslqeqleeeeeakrnverqlstlqaQLSD 528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1921 NINK------EIEDLEE----MEKELGPLHVQLDDKVS----------RLTSGLSDSLADhvhdaEEHAKQ----LNESA 1976
Cdd:pfam01576 529 MKKKleedagTLEALEEgkkrLQRELEALTQQLEEKAAaydklektknRLQQELDDLLVD-----LDHQRQlvsnLEKKQ 603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1977 AILDGILAEAKNLSfnataAFKAYTNIKANVDAaekeakaakqRANEALALALGPEVpvkEAAQGA-------------- 2042
Cdd:pfam01576 604 KKFDQMLAEEKAIS-----ARYAEERDRAEAEA----------REKETRALSLARAL---EEALEAkeelertnkqlrae 665
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2043 -----------------LQKSHRLL-NQAKQLQNDVKENADSVAG----------------------LKGRVKAARDKTK 2082
Cdd:pfam01576 666 medlvsskddvgknvheLERSKRALeQQVEEMKTQLEELEDELQAtedaklrlevnmqalkaqferdLQARDEQGEEKRR 745
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2083 DLLKTVNGTMATLSAIPNDTAAKIAATKVvatdanataidvLErlGDLNlrlrglqqnysELEDTVNAANQMIQDPEKNI 2162
Cdd:pfam01576 746 QLVKQVRELEAELEDERKQRAQAVAAKKK------------LE--LDLK-----------ELEAQIDAANKGREEAVKQL 800
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2163 HAAGAKVKDLEDEADRLLEKLQPI--------KKLQdNLKRNISQIKELI---NQARKQA 2211
Cdd:pfam01576 801 KKLQAQMKDLQRELEEARASRDEIlaqskeseKKLK-NLEAELLQLQEDLaasERARRQA 859
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1684-1980 |
1.05e-06 |
|
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: 54.58 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1684 RFENMTEELKHMLSPQKAPERLLQ----LADSNLGS---LVVEMDQLHSRATK-VSADGEQVEDDADRIHKRAEDLEqfi 1755
Cdd:COG5185 237 GFQDPESELEDLAQTSDKLEKLVEqntdLRLEKLGEnaeSSKRLNENANNLIKqFENTKEKIAEYTKSIDIKKATES--- 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1756 rdtllgaKDLQSKAAELNQTLSRRDGTPDKSLKEMKEEIQAMLAEMGKRQlggkKSIAEEEMDLAEELYQ-KVKRLFGDP 1834
Cdd:COG5185 314 -------LEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENL----EAIKEEIENIVGEVELsKSSEELDSF 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1835 HQATEDLKAEIKGKLSDHEGKlqeAQDLLHSAQGKMKQAGSLAEQNHANLTGLERKRSAVSAVKQEAQDVLGEGERLL-D 1913
Cdd:COG5185 383 KDTIESTKESLDEIPQNQRGY---AQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREAdE 459
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2316002738 1914 EANQLSDNINKEIE-DLEEMEKELGPLHVQLDDKVSRLTSGLSDSLADHVHDAEEHAKQLNESAAILD 1980
Cdd:COG5185 460 ESQSRLEEAYDEINrSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLK 527
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
790-845 |
1.27e-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: 47.73 E-value: 1.27e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2316002738 790 CTCPlnlPSNNFSPTCHLgEEGEllCdQCQPGYTGPRCDRCSNGYYGKPAVPGGSC 845
Cdd:pfam00053 1 CDCN---PHGSLSDTCDP-ETGQ--C-LCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1719-2215 |
1.59e-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: 54.30 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1719 EMDQLHSRATKVSADGEQVEDDADRIHKRAEDLEQFirdtllgaKDLQSKAAELNQT-LSRRDGTPDKSLKEMKEEIQAM 1797
Cdd:TIGR02169 178 ELEEVEENIERLDLIIDEKRQQLERLRREREKAERY--------QALLKEKREYEGYeLLKEKEALERQKEAIERQLASL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1798 LAEMGKRQlggkksiaEEEMDLAEELYQKVKRLfgdphqatEDLKAEIK------------------GKLSDHEGKLQEA 1859
Cdd:TIGR02169 250 EEELEKLT--------EEISELEKRLEEIEQLL--------EELNKKIKdlgeeeqlrvkekigeleAEIASLERSIAEK 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1860 QDLLHSAQGKMKQAGSLAEQNHANLTGLER-------KRSAVSAVKQEAQDVLgegERLLDEANQLS-------DNINKE 1925
Cdd:TIGR02169 314 ERELEDAEERLAKLEAEIDKLLAEIEELEReieeerkRRDKLTEEYAELKEEL---EDLRAELEEVDkefaetrDELKDY 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1926 IEDLEEMEKELGPLHVQLDDKVSRLTSgLSDSLADHVHDAEEHAKQLNESAAILDGILAEAK----NLSFNA---TAAFK 1998
Cdd:TIGR02169 391 REKLEKLKREINELKRELDRLQEELQR-LSEELADLNAAIAGIEAKINELEEEKEDKALEIKkqewKLEQLAadlSKYEQ 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1999 AYTNIKANVDAAEKEAKAAKQR--ANEALALALGPEVPVKEAAQGALQKSHR-LLNQAKQLqNDVKEN---ADSVAGlKG 2072
Cdd:TIGR02169 470 ELYDLKEEYDRVEKELSKLQRElaEAEAQARASEERVRGGRAVEEVLKASIQgVHGTVAQL-GSVGERyatAIEVAA-GN 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2073 RVKAARDKTKD-------LLKTVNGTMAT-------------LSAIPNDTAAKIA-------------------ATKVVA 2113
Cdd:TIGR02169 548 RLNNVVVEDDAvakeaieLLKRRKAGRATflplnkmrderrdLSILSEDGVIGFAvdlvefdpkyepafkyvfgDTLVVE 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2114 TDANATAI-----------DVLERLGDL---NLRLRGLQQNYSELEDTVnaanQMIQDpeknihaagaKVKDLEDEADRL 2179
Cdd:TIGR02169 628 DIEAARRLmgkyrmvtlegELFEKSGAMtggSRAPRGGILFSRSEPAEL----QRLRE----------RLEGLKRELSSL 693
|
570 580 590
....*....|....*....|....*....|....*.
gi 2316002738 2180 LEKLQPIKKLQDNLKRNISQIKELINQARKQANSIK 2215
Cdd:TIGR02169 694 QSELRRIENRLDELSQELSDASRKIGEIEKEIEQLE 729
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
950-980 |
2.34e-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: 46.96 E-value: 2.34e-06
10 20 30
....*....|....*....|....*....|..
gi 2316002738 950 CRCSPHGSISQRCDVE-GRCICRPGFVGRRCD 980
Cdd:pfam00053 1 CDCNPHGSLSDTCDPEtGQCLCKPGVTGRHCD 32
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1795-2175 |
2.42e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.60 E-value: 2.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1795 QAMLAEMGKRQLGG-KKSIAEEEMDLAEELYQKVKRLFgdpHQATEDLKaEIKGKLSDHEGKLQEAQDLLHSAQGKMKQa 1873
Cdd:COG4372 10 KARLSLFGLRPKTGiLIAALSEQLRKALFELDKLQEEL---EQLREELE-QAREELEQLEEELEQARSELEQLEEELEE- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1874 gsLAEQnhanltgLERKRSAVSAVKQEAQDVLGEGERLLDEANQLsdniNKEIEDLEEMEKelgplhvQLDDKVSRLTSG 1953
Cdd:COG4372 85 --LNEQ-------LQAAQAELAQAQEELESLQEEAEELQEELEEL----QKERQDLEQQRK-------QLEAQIAELQSE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1954 LSD------SLADHVHDAEEHAKQLNESAAILDGILAEAKNLSFNATAAFKAYTNIKANVDAAEKEAKAAKQRanEALAL 2027
Cdd:COG4372 145 IAEreeelkELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELA--EELLE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2028 ALGPEVPVKEAAQGALQKSHRLLNQAKQLQNDVKENADSVAGLKGRVKaaRDKTKDLLKTVNGTMATLSAIPNDTAAKIA 2107
Cdd:COG4372 223 AKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVE--KDTEEEELEIAALELEALEEAALELKLLAL 300
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2108 ATKVVATDANATAIDVLERLGDL--NLRLRGLQQNYSELEDTVNAANQMIQDPEKNIHAAGAKVKDLEDE 2175
Cdd:COG4372 301 LLNLAALSLIGALEDALLAALLElaKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1742-2215 |
2.59e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.53 E-value: 2.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1742 DRIHKRAEDLEQFIRDtLLGAKDLQS---KAAELNQTLSRRDGTPDKSLKEmKEEIQAMLAEMGKRqLGGK----KSIAE 1814
Cdd:PRK03918 138 DAILESDESREKVVRQ-ILGLDDYENaykNLGEVIKEIKRRIERLEKFIKR-TENIEELIKEKEKE-LEEVlreiNEISS 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1815 EEMDLAEEL------YQKVKRLFGDPHQAtEDLKAEIKGKLSDHEGKLQEAQDLLHSAQGKMK----QAGSLAEqnhanL 1884
Cdd:PRK03918 215 ELPELREELeklekeVKELEELKEEIEEL-EKELESLEGSKRKLEEKIRELEERIEELKKEIEeleeKVKELKE-----L 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1885 TGLERKRSAVSAVKQEAQDVLGEGERLLDEANQLSDNINKEIEDLEEMEKELGPLH---VQLDDKVSRLtsglsdsladh 1961
Cdd:PRK03918 289 KEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKkklKELEKRLEEL----------- 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1962 vhdaEEHAKQLNESAAILDgilaEAKNLSfnatAAFKAYTNIKANvdaaekeakaakqRANEALALAlgpevpvKEAAQG 2041
Cdd:PRK03918 358 ----EERHELYEEAKAKKE----ELERLK----KRLTGLTPEKLE-------------KELEELEKA-------KEEIEE 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2042 ALQKSHRLLNQAKQLQNDVKENADSVAGLKGRVKAAR-----DKTKDLLKTVNGTMATLSAIPNDTAAKIAATKVVATDA 2116
Cdd:PRK03918 406 EISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGrelteEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELREL 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2117 NaTAIDVLERLgdlnLRLRGLQQNYSELEDTVNAANqmIQDPEKNihaagakvkdlEDEADRLLEKLQPIKKLQDNLKRN 2196
Cdd:PRK03918 486 E-KVLKKESEL----IKLKELAEQLKELEEKLKKYN--LEELEKK-----------AEEYEKLKEKLIKLKGEIKSLKKE 547
|
490
....*....|....*....
gi 2316002738 2197 ISQIKELINQARKQANSIK 2215
Cdd:PRK03918 548 LEKLEELKKKLAELEKKLD 566
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1814-2218 |
3.22e-06 |
|
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: 53.26 E-value: 3.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1814 EEEMDLAEELYQKVKrlfgdphqateDLKAEIKGKLSDHEGKLQEAqdllhsaqgkMKQAGSLAEQNHANlTGL----ER 1889
Cdd:pfam01576 4 EEEMQAKEEELQKVK-----------ERQQKAESELKELEKKHQQL----------CEEKNALQEQLQAE-TELcaeaEE 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1890 KRSAVSAVKQEAQDVLGEGERLLDE----ANQLSDN---INKEIEDLEE-MEKELGP---LH---VQLDDKVSRLTSGLS 1955
Cdd:pfam01576 62 MRARLAARKQELEEILHELESRLEEeeerSQQLQNEkkkMQQHIQDLEEqLDEEEAArqkLQlekVTTEAKIKKLEEDIL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1956 dSLADHVHDAEEHAKQLNESAAILDGILAE----AKNLSfnataafkaytnikanvdaaekeakaAKQRANEALALALgp 2031
Cdd:pfam01576 142 -LLEDQNSKLSKERKLLEERISEFTSNLAEeeekAKSLS--------------------------KLKNKHEAMISDL-- 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2032 EVPVKEAAQG--ALQKSHRLLN-QAKQLQNDVKENADSVAGLKGRVKAardKTKDLLktvngtmATLSAIPNDTAAKIAA 2108
Cdd:pfam01576 193 EERLKKEEKGrqELEKAKRKLEgESTDLQEQIAELQAQIAELRAQLAK---KEEELQ-------AALARLEEETAQKNNA 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2109 TKVVaTDANATAIDVLERLG--------------DLNLRLRGLQqnySELEDTVN--AANQMIQdpEKNIHAAGAKVKDL 2172
Cdd:pfam01576 263 LKKI-RELEAQISELQEDLEseraarnkaekqrrDLGEELEALK---TELEDTLDttAAQQELR--SKREQEVTELKKAL 336
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2316002738 2173 EDEAdRLLEklqpiKKLQDNLKRNISQIKELINQArKQANSIKVSV 2218
Cdd:pfam01576 337 EEET-RSHE-----AQLQEMRQKHTQALEELTEQL-EQAKRNKANL 375
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1739-2210 |
3.24e-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: 3.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1739 DDADRIHKRAEDL-EQfiRDTLLGAKDLQSKAAELNQTLSR----RDGTPD----KSLKEMKEEIQAMLAEmgKRQLGGK 1809
Cdd:COG4913 235 DDLERAHEALEDArEQ--IELLEPIRELAERYAAARERLAEleylRAALRLwfaqRRLELLEAELEELRAE--LARLEAE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1810 KSIAEEEMDLAEELYQKVKR-LFGDPHQATEDLKAEIKG---KLSDHEGKLQEAQDLLHSAqgKMKQAGSlAEQNHANLT 1885
Cdd:COG4913 311 LERLEARLDALREELDELEAqIRGNGGDRLEQLEREIERlerELEERERRRARLEALLAAL--GLPLPAS-AEEFAALRA 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1886 GLERKRSAVSAVKQEAQDVLGEGERLLDEANQLSDNINKEIEDLEEMEKELGPLHVQLDDKVSRLTsGLSDS----LADH 1961
Cdd:COG4913 388 EAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEAL-GLDEAelpfVGEL 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1962 VHDAEEHAK-QlnesAAI---LDG----ILAEAKNLsfnatAAFKAY---TNIKANVDAAEKEAKAAKQRANEALALALG 2030
Cdd:COG4913 467 IEVRPEEERwR----GAIervLGGfaltLLVPPEHY-----AAALRWvnrLHLRGRLVYERVRTGLPDPERPRLDPDSLA 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2031 PEVPVKE-AAQGALQkshRLLNQ---------AKQLQND---------VK----------------------ENADSVAG 2069
Cdd:COG4913 538 GKLDFKPhPFRAWLE---AELGRrfdyvcvdsPEELRRHpraitragqVKgngtrhekddrrrirsryvlgfDNRAKLAA 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2070 LKGRVKAARDKtkdlLKTVNGTMATLSAIPNDTAAKIAATKVVAtDANATAIDV-------------LERLGDLNLRLRG 2136
Cdd:COG4913 615 LEAELAELEEE----LAEAEERLEALEAELDALQERREALQRLA-EYSWDEIDVasaereiaeleaeLERLDASSDDLAA 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2137 LQQNYSELEDTVNAANQMIQDPEKNIHAAGAKVKDLEDEADRLLEKLQPI-------------------------KKLQD 2191
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAedlarlelralleerfaaalgdaveRELRE 769
|
570
....*....|....*....
gi 2316002738 2192 NLKRNISQIKELINQARKQ 2210
Cdd:COG4913 770 NLEERIDALRARLNRAEEE 788
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1134-1177 |
3.51e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 46.15 E-value: 3.51e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2316002738 1134 CGCSVIGSVTQQCNVNTGCCLCRDSFRGEKCNECQIGY--RDFPQC 1177
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYygDGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
272-319 |
4.67e-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: 45.81 E-value: 4.67e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2316002738 272 CICYGHA---KACPLNTVTkkfsCECEHNTCGESCDRCCPGYHQQPWMAGT 319
Cdd:cd00055 2 CDCNGHGslsGQCDPGTGQ----CECKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1735-2214 |
5.99e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 52.53 E-value: 5.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1735 EQVEDDA---DRIHKRAEDLEQFIRDTLLGA--KDLQSKAAELNQTLSRRDgTPDKSLKEMKEEIQAMLAEMGKRQlggk 1809
Cdd:pfam12128 204 AILEDDGvvpPKSRLNRQQVEHWIRDIQAIAgiMKIRPEFTKLQQEFNTLE-SAELRLSHLHFGYKSDETLIASRQ---- 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1810 KSIAEEEMDLAEELYQKVKRLfgdphqatEDLKAEIKGKLSDHEGKLQEAQ---DLLHSAQGKMKQAGslAEQNHANLTG 1886
Cdd:pfam12128 279 EERQETSAELNQLLRTLDDQW--------KEKRDELNGELSAADAAVAKDRselEALEDQHGAFLDAD--IETAAADQEQ 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1887 LERKRSAVSAVKQE-------AQDVLGEGERLldEANQLSDNiNKEIEDLEE----MEKELGPLHVQLDDKVSRLTSGLS 1955
Cdd:pfam12128 349 LPSWQSELENLEERlkaltgkHQDVTAKYNRR--RSKIKEQN-NRDIAGIKDklakIREARDRQLAVAEDDLQALESELR 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1956 DSLADHVHDAEEHAKQLNESAAILDGILAEAknlsfnaTAAFKAYTNIKANVDAAEKEAKAAKQR--ANEALALALGPEV 2033
Cdd:pfam12128 426 EQLEAGKLEFNEEEYRLKSRLGELKLRLNQA-------TATPELLLQLENFDERIERAREEQEAAnaEVERLQSELRQAR 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2034 PVKEAAQGALQKSHRLLNQAKQLQNDVKENADSVAGlkgrvkaardktkDLLKTVNGTMATLSaipnDTAAKIAATKVVA 2113
Cdd:pfam12128 499 KRRDQASEALRQASRRLEERQSALDELELQLFPQAG-------------TLLHFLRKEAPDWE----QSIGKVISPELLH 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2114 -TD----ANATAIDVLERLGDLNLRLRGLQQNYS------------ELEDTVNAANQMIQDPEKNIHAAGAKVKDLEDEA 2176
Cdd:pfam12128 562 rTDldpeVWDGSVGGELNLYGVKLDLKRIDVPEWaaseeelrerldKAEEALQSAREKQAAAEEQLVQANGELEKASREE 641
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 2316002738 2177 DRLL-------EKLQPIKKLQDNLKRNISQ-IKELINQARKQANSI 2214
Cdd:pfam12128 642 TFARtalknarLDLRRLFDEKQSEKDKKNKaLAERKDSANERLNSL 687
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
950-986 |
6.45e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 45.38 E-value: 6.45e-06
10 20 30
....*....|....*....|....*....|....*...
gi 2316002738 950 CRCSPHGSISQRCDVE-GRCICRPGFVGRRCDLRRQGY 986
Cdd:smart00180 1 CDCDPGGSASGTCDPDtGQCECKPNVTGRRCDRCAPGY 38
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1703-1986 |
8.11e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 51.43 E-value: 8.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1703 ER--LLQLADSNLGSlvVEMDQLHSRATKVSADGE--QVEDDADRIHKRAEDLEQFIRDTLLGAKDLQSKAAELNQ---T 1775
Cdd:pfam07888 42 ERaeLLQAQEAANRQ--REKEKERYKRDREQWERQrrELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEekdA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1776 LSRRDGTPDKSLKEMKEEIQAMlaemGKRQLggkksiaEEEMDLaEELYQKVKRLFGdphqatedLKAEIKGKLSDHEGK 1855
Cdd:pfam07888 120 LLAQRAAHEARIRELEEDIKTL----TQRVL-------ERETEL-ERMKERAKKAGA--------QRKEEEAERKQLQAK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1856 LQEAQDLLHSAQGKMKQA-GSLAEQNhanlTGLERKRSAVSAVKQeaqdvlgegerLLDEANQlsdninKEIEdLEEMEK 1934
Cdd:pfam07888 180 LQQTEEELRSLSKEFQELrNSLAQRD----TQVLQLQDTITTLTQ-----------KLTTAHR------KEAE-NEALLE 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2316002738 1935 ELGPLHVQL---DDKVSRLTSGLSD--SLADHVHdAEEHAKQLneSAAILDGILAEA 1986
Cdd:pfam07888 238 ELRSLQERLnasERKVEGLGEELSSmaAQRDRTQ-AELHQARL--QAAQLTLQLADA 291
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1719-1936 |
8.82e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.60 E-value: 8.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1719 EMDQLHSRATKVSADGEQVEDDADRIhkraedleqfirdtllgaKDLQSKAAELNqtlsrrdgtpdKSLKEMKEEIQAML 1798
Cdd:PRK03918 526 EYEKLKEKLIKLKGEIKSLKKELEKL------------------EELKKKLAELE-----------KKLDELEEELAELL 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1799 AEMGKRqlgGKKSIAEEEMDLAE--ELYQKVKRLFGDPH--QATEDLKAEIKGKLSDHEGKLQEAQDLLHSAQGKMKQAG 1874
Cdd:PRK03918 577 KELEEL---GFESVEELEERLKElePFYNEYLELKDAEKelEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELE 653
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2316002738 1875 SL-AEQNHANL----TGLERKRSAVSAVKQEAQDVLGEGERLLDEANQLSDNINKEIEDLEEMEKEL 1936
Cdd:PRK03918 654 KKySEEEYEELreeyLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKAL 720
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1709-1920 |
8.96e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.98 E-value: 8.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1709 ADSNLGSLVVEMDQLHSRATKVSADGEQVEDDADRIHKRAEDLEQFIrdtllgaKDLQSKAAELNqtlsrrdgtpdKSLK 1788
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAEL-------EALQAEIDKLQ-----------AEIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1789 EMKEEIQAMLAEMGKR----QLGGK-----------KSIAE--EEMDLAEELYQKVKRLFgdphQATEDLKAEIKGKLSD 1851
Cdd:COG3883 76 EAEAEIEERREELGERaralYRSGGsvsyldvllgsESFSDflDRLSALSKIADADADLL----EELKADKAELEAKKAE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2316002738 1852 HEGKLQEAQDLLHSAQGKMKQAGSLAEQNHANLTGLERKRSAVSAVKQEAQDVLGEGERLLDEANQLSD 1920
Cdd:COG3883 152 LEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAA 220
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1706-2006 |
9.44e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.06 E-value: 9.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1706 LQLADSNLGSLVVEMDQLHSRATKVSADGEQVEDDADRIHKRAEDLEQFIRDTLLGAKDLQSKAAELNQTLSRRdgtpDK 1785
Cdd:COG4372 33 LRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL----QE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1786 SLKEMKEEIQAMLAEMgKRQLGGKKSIAEEEMDLAEELYQKVKRLfgdpHQATEDLkAEIKGKLSDHEGKLQ-------- 1857
Cdd:COG4372 109 EAEELQEELEELQKER-QDLEQQRKQLEAQIAELQSEIAEREEEL----KELEEQL-ESLQEELAALEQELQalseaeae 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1858 -EAQDLLHSAQGKMKQAGSLAEQNHANLTGLERKRSAVSAVKQ--EAQDVLGEGERLLDEANQLSDNINKEIEDLEEMEK 1934
Cdd:COG4372 183 qALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDslEAKLGLALSALLDALELEEDKEELLEEVILKEIEE 262
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2316002738 1935 ELGPLHVQLDDKVSRLTSGLSDSLADHVHDAEEHAKQLNESAAILDGILAEAKNLSFNATAAFKAYTNIKAN 2006
Cdd:COG4372 263 LELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAI 334
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
453-501 |
1.27e-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: 1.27e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2316002738 453 RCNCSVEGSTNaDPCITP---CMCKENVEGENCDRCKLGFYNLQgDNQRGCE 501
Cdd:cd00055 1 PCDCNGHGSLS-GQCDPGtgqCECKPNTTGRRCDRCAPGYYGLP-SQGGGCQ 50
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1672-1974 |
1.29e-05 |
|
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: 50.19 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1672 TTPLPPPYKMlyrfeNMTEELKHMLSPQKAPERLLQLADSNLGSLVVEMDQ-LHSRATKVSADGEQVEDDADRIH-KRAE 1749
Cdd:pfam15905 2 CAPPPGSYDV-----KTSDALKGPVSFEKSQRFRKQKAAESQPNLNNSKDAsTPATARKVKSLELKKKSQKNLKEsKDQK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1750 DLEQFIRDTLLGAKDLQSKAAELNQTLSRRDGTPDKSLKEmKEEIQAMLAEMgKRQL-----------------GGKK-- 1810
Cdd:pfam15905 77 ELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVRE-KTSLSASVASL-EKQLleltrvnellkakfsedGTQKkm 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1811 -SIAEEEMDLAEELYQKVKrlfgdphqatedlkaEIKGKLSDHEGKLQEAQDLLHSAQGKMKQagsLAEQNhanltgler 1889
Cdd:pfam15905 155 sSLSMELMKLRNKLEAKMK---------------EVMAKQEGMEGKLQVTQKNLEHSKGKVAQ---LEEKL--------- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1890 krsavSAVKQEAQDVLGEGERLLDEANQLSDninkEIEDLEEMEKELGPLHVQLDDKVSRLTSgLSDSLADHVHDAEEHA 1969
Cdd:pfam15905 208 -----VSTEKEKIEEKSETEKLLEYITELSC----VSEQVEKYKLDIAQLEELLKEKNDEIES-LKQSLEEKEQELSKQI 277
|
....*
gi 2316002738 1970 KQLNE 1974
Cdd:pfam15905 278 KDLNE 282
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1695-1935 |
1.42e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.15 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1695 MLSPQKAPERLLQLADSNLGSLVVEMDQLHSRATKVSADGEQVEDDADRIHKRAEDLEQFIRDTLLGAKDLQSKAAELNQ 1774
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1775 TLSRRdgtpDKSLKEMKEEIQAMLAEMgkrQLGGKKSIAEEEMDlAEELYQKVKRL--FGDPHQATEDLKAEIKGKLSDh 1852
Cdd:COG4942 91 EIAEL----RAELEAQKEELAELLRAL---YRLGRQPPLALLLS-PEDFLDAVRRLqyLKYLAPARREQAEELRADLAE- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1853 egkLQEAQDLLHSAQGKMKQAGSLAEQNHANLTGL-ERKRSAVSAVKQEAQDVLGEGERLLDEANQLSDNINKEIEDLEE 1931
Cdd:COG4942 162 ---LAALRAELEAERAELEALLAELEEERAALEALkAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
....
gi 2316002738 1932 MEKE 1935
Cdd:COG4942 239 AAER 242
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1784-1996 |
1.59e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.21 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1784 DKSLKEMKEEIQAMLAEMgkrqlggkKSIAEEEMDLAEELYQKVKRLfgdphqatEDLKAEIKgKLsdhEGKLQEAQDLL 1863
Cdd:COG3883 22 QKELSELQAELEAAQAEL--------DALQAELEELNEEYNELQAEL--------EALQAEID-KL---QAEIAEAEAEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1864 HSAQGKMKQAGSLAEQNHANLTGLE------------RKRSAVSAVKQEAQDVLGEGERLLDEANQLSDNINKEIEDLEE 1931
Cdd:COG3883 82 EERREELGERARALYRSGGSVSYLDvllgsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2316002738 1932 MEKELGPLHVQLDDKVSRLtSGLSDSLADHVHDAEEHAKQLNESAAILDGILAEAKNLSFNATAA 1996
Cdd:COG3883 162 LKAELEAAKAELEAQQAEQ-EALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
789-846 |
1.62e-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: 44.27 E-value: 1.62e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2316002738 789 PCTCPlnlPSNNFSPTCHlgeEGELLCdQCQPGYTGPRCDRCSNGYYGKPAVPGGsCQ 846
Cdd:cd00055 1 PCDCN---GHGSLSGQCD---PGTGQC-ECKPNTTGRRCDRCAPGYYGLPSQGGG-CQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
790-839 |
1.84e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 44.22 E-value: 1.84e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2316002738 790 CTCPlnlPSNNFSPTCHLgEEGEllCdQCQPGYTGPRCDRCSNGYYGKPA 839
Cdd:smart00180 1 CDCD---PGGSASGTCDP-DTGQ--C-ECKPNVTGRRCDRCAPGYYGDGP 43
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1814-2204 |
1.94e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.73 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1814 EEEMDLAEELYQKVKRLFGDPHQATEDLK--AEIKGKLSDHEGKLQEAQDLLHSAQGKMKQAGSLaEQNHANLTGLERKR 1891
Cdd:PRK04863 286 EEALELRRELYTSRRQLAAEQYRLVEMARelAELNEAESDLEQDYQAASDHLNLVQTALRQQEKI-ERYQADLEELEERL 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1892 SAVSAVKQEAQDVLGEGERLLDEANQLSDNINKEIED----LEEMEKELGPLH--VQLDDKVSRLtSGLSDSLADHVHD- 1964
Cdd:PRK04863 365 EEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADyqqaLDVQQTRAIQYQqaVQALERAKQL-CGLPDLTADNAEDw 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1965 AEEHAKQLNESAAILDGilAEAK-NLSFNATAAF-KAYtnikanvdaaekeakaakqraneALALALGPEVPVKEAAQGA 2042
Cdd:PRK04863 444 LEEFQAKEQEATEELLS--LEQKlSVAQAAHSQFeQAY-----------------------QLVRKIAGEVSRSEAWDVA 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2043 LQK-----SHRLL-NQAKQLQNDVKEnadsvagLKGRVKAARDKTKdLLKTVNGTmatLSAIPNDtaakiaatkvvATDA 2116
Cdd:PRK04863 499 RELlrrlrEQRHLaEQLQQLRMRLSE-------LEQRLRQQQRAER-LLAEFCKR---LGKNLDD-----------EDEL 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2117 NATAIDVLERLGDLNLRLRGLQQNYSELEDTVNAANQMIQDPEKNI---HAAGAKVKDL-----EDEADR---------L 2179
Cdd:PRK04863 557 EQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARApawLAAQDALARLreqsgEEFEDSqdvteymqqL 636
|
410 420
....*....|....*....|....*
gi 2316002738 2180 LEKLQPIKKLQDNLKRNISQIKELI 2204
Cdd:PRK04863 637 LERERELTVERDELAARKQALDEEI 661
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1680-2008 |
2.40e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.52 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1680 KMLYRFENMTEELKHMLSPQKAPERLLQLADSNLGSLVVEMDQLHSRATKVSADGEQVEDDADRIHKRAEDLEQFIRDTL 1759
Cdd:COG4372 42 KLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1760 LGAKDLQSKAAELNQTLSRRD---GTPDKSLKEMKEEIQAMLAEMGKRQlggkksiAEEEMDLAEELYQKVKRLFGDPHQ 1836
Cdd:COG4372 122 KERQDLEQQRKQLEAQIAELQseiAEREEELKELEEQLESLQEELAALE-------QELQALSEAEAEQALDELLKEANR 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1837 ATEDLKAEIKGKLSDHEGKLQEAQDLLH-SAQGKMKQAGSLAEQNHANLTGLERKRSAVSAVKQEAQDVLGEGERLLD-E 1914
Cdd:COG4372 195 NAEKEEELAEAEKLIESLPRELAEELLEaKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDtE 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1915 ANQLSDNINKEIEDLEEMEKELGPLHVQLDDKVSRLTSGLSDSLADHV-HDAEEHAKQLNESAAILDGILAEAKNLSFNA 1993
Cdd:COG4372 275 EEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLeLAKKLELALAILLAELADLLQLLLVGLLDND 354
|
330
....*....|....*
gi 2316002738 1994 TAAFKAYTNIKANVD 2008
Cdd:COG4372 355 VLELLSKGAEAGVAD 369
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
454-495 |
2.76e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 43.84 E-value: 2.76e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2316002738 454 CNCSVEGSTNaDPCITP---CMCKENVEGENCDRCKLGFYNLQGD 495
Cdd:smart00180 1 CDCDPGGSAS-GTCDPDtgqCECKPNVTGRRCDRCAPGYYGDGPP 44
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1877-2218 |
2.88e-05 |
|
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: 50.07 E-value: 2.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1877 AEQNHANLTGLERKRSAVSAVKQEAQDVLGEGERLLDEANQLSDNINKEIEDLEEMEKELGPLHVQLDDKVSRltsgLSD 1956
Cdd:TIGR02169 676 LQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSS----LEQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1957 SLADHVHDAEEHAKQLNESAAILDGILAEAKNLSfnATAAFKAYTNIKANVDAAEKEAKAAKQRANEALAlALGPEVPVK 2036
Cdd:TIGR02169 752 EIENVKSELKELEARIEELEEDLHKLEEALNDLE--ARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQ-KLNRLTLEK 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2037 EAAQgalQKSHRLLNQAKQLQNDVKENADSVAGLKGRVKAARDKTKDL---LKTVNGTMATLSAIPNDTAAKIAATKVVA 2113
Cdd:TIGR02169 829 EYLE---KEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELeaaLRDLESRLGDLKKERDELEAQLRELERKI 905
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2114 TDANATAIDVLERLGDLNLRLRGLQQNYSELEDTVnaaNQMIQDPE---------KNIHAAGAKVKDLE-------DEAD 2177
Cdd:TIGR02169 906 EELEAQIEKKRKRLSELKAKLEALEEELSEIEDPK---GEDEEIPEeelsledvqAELQRVEEEIRALEpvnmlaiQEYE 982
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2316002738 2178 RLLEKLQPIKKLQDNLKRNISQIKELINQARKQANSIKVSV 2218
Cdd:TIGR02169 983 EVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREVFMEA 1023
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1891-2179 |
4.52e-05 |
|
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: 47.37 E-value: 4.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1891 RSAVSAVKQEAQDvlgeGERLLDEAnqlsdninkeiedLEEMEKELGplhvqlddkvsRLTSGLSDSLADHVhdaeEHAK 1970
Cdd:pfam04012 10 RANIHEGLDKAED----PEKMLEQA-------------IRDMQSELV-----------KARQALAQTIARQK----QLER 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1971 QLNEsaaildgILAEAKNLSFNATAAFKAytnikanvdaaekeakaakqrANEALALAlgpevpvkeaaqgALQKSHRLL 2050
Cdd:pfam04012 58 RLEQ-------QTEQAKKLEEKAQAALTK---------------------GNEELARE-------------ALAEKKSLE 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2051 NQAKQLQNDVKENADSVAGLKGRVKAARDKTKDLLKTVNGTMATLSAIpndtAAKIAATKVVATDANATAIDVLERlgdl 2130
Cdd:pfam04012 97 KQAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKARLKAA----KAQEAVQTSLGSLSTSSATDSFER---- 168
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2316002738 2131 nlrlrgLQQNYSELEDTVNAANQM--IQDPEKNIHAAGAKVKDLEDEADRL 2179
Cdd:pfam04012 169 ------IEEKIEEREARADAAAELasAVDLDAKLEQAGIQMEVSEDVLARL 213
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1711-1990 |
5.78e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.98 E-value: 5.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1711 SNLGSLVVEMDQLHSRATKVSADGEQVEDDADRIHKRAEDLEQfIRDTLLG--------AKDLQSKAAELNQTL----SR 1778
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAE-KRDELNAqvkelreeAQELREKRDELNEKVkelkEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1779 RDGTpDKSLKEMKEEIQAMLAEMGKRQLGGKkSIAEEEMDLAEELYQkvkrlfgdphQATEDLKAEIKGKLSDhegKLQE 1858
Cdd:COG1340 80 RDEL-NEKLNELREELDELRKELAELNKAGG-SIDKLRKEIERLEWR----------QQTEVLSPEEEKELVE---KIKE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1859 AQDLLHSAQGKMKQAGSLAEqnhanltglerKRSAVSAVKQEAQDVLGEGERLLDEANQLSDNINKEIEDLEEMEKELGP 1938
Cdd:COG1340 145 LEKELEKAKKALEKNEKLKE-----------LRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADE 213
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2316002738 1939 LHVQLDDKVSRltsglsdslADHVHDA-EEHAKQLNESAAILDGILAEAKNLS 1990
Cdd:COG1340 214 LHKEIVEAQEK---------ADELHEEiIELQKELRELRKELKKLRKKQRALK 257
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1898-2210 |
7.29e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.78 E-value: 7.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1898 KQEAqdvlgegERLLDEANQlsdNINkEIEDL-EEMEKELGPLHVQ-------------LDDKVSRLtsgLSDSLADHVH 1963
Cdd:COG1196 174 KEEA-------ERKLEATEE---NLE-RLEDIlGELERQLEPLERQaekaeryrelkeeLKELEAEL---LLLKLRELEA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1964 DAEEHAKQLNESAAILDGILAEAKNLSfnataafKAYTNIKANVdaaekeakaakQRANEALALALGPEVPVKEAAQGAL 2043
Cdd:COG1196 240 ELEELEAELEELEAELEELEAELAELE-------AELEELRLEL-----------EELELELEEAQAEEYELLAELARLE 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2044 QKSHRLLNQAKQLQNDVKENADSVAGLKGRVKAARDKTKDLLKTVNGTMATLSAIpndtAAKIAATKVVATDANATAIDV 2123
Cdd:COG1196 302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA----EAELAEAEEALLEAEAELAEA 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2124 LERLGDLNLRLRGLQQNYSELEDTVNAANQMIQDPEKNIHAAGAKVKDLEDEADRLLEKLQPIKKLQDNLKRNISQIKEL 2203
Cdd:COG1196 378 EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457
|
....*..
gi 2316002738 2204 INQARKQ 2210
Cdd:COG1196 458 EEALLEL 464
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1735-1974 |
8.54e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.80 E-value: 8.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1735 EQVEDDADRIHKRAEDLEQfirdtllgAKD-LQSKAAELNQTLSRRD------GTPD---KSLKEMKEEIQAMLAEMGKR 1804
Cdd:PRK04863 386 EAAEEEVDELKSQLADYQQ--------ALDvQQTRAIQYQQAVQALErakqlcGLPDltaDNAEDWLEEFQAKEQEATEE 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1805 --QLGGKKSIAEEEMDLAEELYQKVKRLFG--DPHQATedlkaeikgklsdhegklQEAQDLLHSAQGKMKQAGSLaEQN 1880
Cdd:PRK04863 458 llSLEQKLSVAQAAHSQFEQAYQLVRKIAGevSRSEAW------------------DVARELLRRLREQRHLAEQL-QQL 518
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1881 HANLTGLERKRsavsavkQEAQDVlgegERLLDEANQLSdniNKEIEDLEEMEKELGPLHVQLDDkvsrltsgLSDSLAD 1960
Cdd:PRK04863 519 RMRLSELEQRL-------RQQQRA----ERLLAEFCKRL---GKNLDDEDELEQLQEELEARLES--------LSESVSE 576
|
250
....*....|....
gi 2316002738 1961 HVHDAEEHAKQLNE 1974
Cdd:PRK04863 577 ARERRMALRQQLEQ 590
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1907-2210 |
9.94e-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: 48.51 E-value: 9.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1907 EGERLLDEANqlsDNINKeIED-LEEMEKELGPLHVQLD------DKVSRLTSGLSDSLADHVHDAEEHAKQLNESaail 1979
Cdd:TIGR02168 176 ETERKLERTR---ENLDR-LEDiLNELERQLKSLERQAEkaerykELKAELRELELALLVLRLEELREELEELQEE---- 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1980 dgiLAEAKNLSFNATAAFKAYtnikanvdaaekeakaakqranEALALALGPEVPVKEAAQGALQKshrLLNQAKQLQND 2059
Cdd:TIGR02168 248 ---LKEAEEELEELTAELQEL----------------------EEKLEELRLEVSELEEEIEELQK---ELYALANEISR 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2060 VKENadsvaglKGRVKAARDKTKDLLKTVNGTMAT-------LSAIPNDTAAKIAATKVVATDANATAIDVLERLGDLNL 2132
Cdd:TIGR02168 300 LEQQ-------KQILRERLANLERQLEELEAQLEEleskldeLAEELAELEEKLEELKEELESLEAELEELEAELEELES 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2133 RLRGLQQNYSELEDTVNAANQMIQDPEKNIHAAGAKVKDLEDEADRLL-EKLQPIKKLQDN----LKRNISQIKELINQA 2207
Cdd:TIGR02168 373 RLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQqEIEELLKKLEEAelkeLQAELEELEEELEEL 452
|
...
gi 2316002738 2208 RKQ 2210
Cdd:TIGR02168 453 QEE 455
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1685-2219 |
1.43e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 47.71 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1685 FENMTEELKHMLSPQKAPERLLQLADSNLGSLVVEMDQLHSRATKVSADGEQVEDDADRIHKRAEDLEQFIRDT---LLG 1761
Cdd:TIGR04523 178 LEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTqtqLNQ 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1762 AKD--------LQSKAAELNQTlSRRDGTPDKSLKEMKEEIQAM-------LAEMGKRQLggkKSIAEEEMDLAEELYQK 1826
Cdd:TIGR04523 258 LKDeqnkikkqLSEKQKELEQN-NKKIKELEKQLNQLKSEISDLnnqkeqdWNKELKSEL---KNQEKKLEEIQNQISQN 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1827 VKRLfGDPHQATEDLKAEIKGKLSDHEGKLQEAQDllhsaqgKMKQAGSLAEQNHANLTGLERKRSAVSAVKQEAQDVlg 1906
Cdd:TIGR04523 334 NKII-SQLNEQISQLKKELTNSESENSEKQRELEE-------KQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQ-- 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1907 egerllDEANQLSDNINKEIE-DLEEMEKElgplHVQLDDKVSRLTSGLSDsLADHVHDAEEHAKQLNESAAILDgilae 1985
Cdd:TIGR04523 404 ------EKLNQQKDEQIKKLQqEKELLEKE----IERLKETIIKNNSEIKD-LTNQDSVKELIIKNLDNTRESLE----- 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1986 aKNLSfnataAFKA-YTNIKANVDaaekeakaakqranealalalgpevpvkeaaqgalQKSHRLLNQAKQLQNDVKENA 2064
Cdd:TIGR04523 468 -TQLK-----VLSRsINKIKQNLE-----------------------------------QKQKELKSKEKELKKLNEEKK 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2065 DsvagLKGRVKAARDKTKDLLKTVNGTMATLSAIPNDTAAKiaATKVVATDANATAIDVLERLGDLNLRLRGLQQNYSEL 2144
Cdd:TIGR04523 507 E----LEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDL--EDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSL 580
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2145 EDTVNAANQMIQDPEKN-------IHAAGAKVKDLEDEAD-------RLLEKLQPIKKLQDNLKRNISQIKELINQAR-K 2209
Cdd:TIGR04523 581 KKKQEEKQELIDQKEKEkkdlikeIEEKEKKISSLEKELEkakkeneKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRnK 660
|
570
....*....|...
gi 2316002738 2210 QAN---SIKVSVS 2219
Cdd:TIGR04523 661 WPEiikKIKESKT 673
|
|
| ClyA-like |
cd21116 |
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ... |
2035-2179 |
1.71e-04 |
|
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including Bacillus cereus HblB, Aeromonas hydrophila AhlB, Bacillus thuringiensis Cry6Aa and similar proteins; This family belongs to the ClyA family of alpha-PFT bacterial toxins. PFTs form the major group of virulence factors in many pathogenic bacteria and in general are critical components of the molecular offensive and defensive machinery of cells in all kingdoms of life. Bacterial PFTs facilitate the takeover of host resources by puncturing holes in the membrane. PFTs can be classified as alpha-PFTs and beta-PFTs depending on the secondary structures of their membrane component. Alpha-PFTs use a ring of amphipathic helices while beta-PFTs use a beta-barrel to construct the pore. Members of this family include the toxins: Bacillus cereus hemolysin binding component B (HblB or HBL-B) of the diarrheal enterotoxin hemolysin BL, Aeromonas hydrophila hemolytic (Ahl) component B (AhlB) of the tripartite AhlABC toxin, Vibrio cholerae cytotoxin motility associated killing factor A (MakA) cytotoxin, Xenorhabdus nematophila alpha-xenorhabdolysin (XaxA), Bacillus thuringiensis crystal 6Aa (Cry6Aa) parasporal crystal (Cry) toxin, and Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA) of the non-hemolytic enterotoxin Nhe, which, despite its name, is hemolytic, among others. In solution, ClyA proteins have an elongated, almost entirely alpha-helical structure, except for a short hydrophobic beta-hairpin known as the beta-tongue. Pore formation by ClyA requires circular oligomerization of the toxin by a sequential mechanism. This, in turn, concentrates the amphipathic helices in the center of the ring-like structure, forming a helical barrel that inserts into the membrane by a wedge-like mechanism. Compared with ClyA, NheA is almost entirely alpha-helical with an enlarged "head" domain, and an enlarged beta-tongue; it has been proposed that NheA could even form beta-barrel pores. Alpha-PFTs with similar structures are increasingly being found in eukaryotes, in particular as components of the immune systems of animals. This family may be distantly related to Escherichia coli alpha-PFT hemolysin E (HlyE, also known as ClyA or SheA).
Pssm-ID: 439149 [Multi-domain] Cd Length: 224 Bit Score: 45.87 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2035 VKEAAQGALQKshrLLNQAKQLQNDVKENADSVAGLKgrvkaarDKTKDLLKTVNGTMATLSAIPNDTAAKIAATKVVAT 2114
Cdd:cd21116 85 LIKGDQGAKQQ---LLQGLEALQSQVTKKQTSVTSFI-------NELTTFKNDLDDDSRNLQTDATKAQAQVAVLNALKN 154
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2316002738 2115 ------DANATAIDVLERLGDLnlrLRGLQQNYSELEDTVNAANQMIQDP--EKNIHAAGAKVKDLEDEADRL 2179
Cdd:cd21116 155 qlnslaEQIDAAIDALEKLSND---WQTLDSDIKELITDLEDAESSIDAAflQADLKAAKADWNQLYEQAKSL 224
|
|
| DivIVA |
COG3599 |
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle ... |
1842-1931 |
1.82e-04 |
|
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442818 [Multi-domain] Cd Length: 125 Bit Score: 43.69 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1842 KAEIKGKLSDHEGKLQEAQDLlhsaQGKMKQAGSLAEQnhanlTGLERKRSAvsavKQEAQDVLGE----GERLLDEANQ 1917
Cdd:COG3599 43 NKELKEKLEELEEELEEYREL----EETLQKTLVVAQE-----TAEEVKENA----EKEAELIIKEaeleAEKIIEEAQE 109
|
90
....*....|....
gi 2316002738 1918 LSDNINKEIEDLEE 1931
Cdd:COG3599 110 KARKIVREIEELKR 123
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1785-2180 |
2.29e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 47.25 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1785 KSLKEMKEEiQAMLAEMGKR--QLGGKKSIAEEEMDLAEELYQ----------KVKRLFGDPHQATEDLkAEIKGKLSDH 1852
Cdd:COG3096 296 GARRQLAEE-QYRLVEMAREleELSARESDLEQDYQAASDHLNlvqtalrqqeKIERYQEDLEELTERL-EEQEEVVEEA 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1853 EGKLQEAQDLLHSAQGKMKQAGS-LAEQNHAnLTGLERKrsavsAVK-QEAQDVLGEGERLLDEANQLSDNINKEIEDLE 1930
Cdd:COG3096 374 AEQLAEAEARLEAAEEEVDSLKSqLADYQQA-LDVQQTR-----AIQyQQAVQALEKARALCGLPDLTPENAEDYLAAFR 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1931 EMEKElgplhvqlddkvsrLTSGLSDsLADHVHDAEEHAKQLNESAAILDGILAE--AKNLSFNATAAFKAYTNIKAnvd 2008
Cdd:COG3096 448 AKEQQ--------------ATEEVLE-LEQKLSVADAARRQFEKAYELVCKIAGEveRSQAWQTARELLRRYRSQQA--- 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2009 aaekeakaAKQRAnEALALALGpEVPVKEAAQgalQKSHRLLNQAKQLQNDVKENADSVAGLKGRVKAARDKTKDLLKTV 2088
Cdd:COG3096 510 --------LAQRL-QQLRAQLA-ELEQRLRQQ---QNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEA 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2089 NGTMATLSAIPNDTAAKIAATKVVATdANATAIDVLERLGDlnlrlrglqQNYSELEDT--VNAANQMIQDPEKNI---- 2162
Cdd:COG3096 577 VEQRSELRQQLEQLRARIKELAARAP-AWLAAQDALERLRE---------QSGEALADSqeVTAAMQQLLEREREAtver 646
|
410
....*....|....*....
gi 2316002738 2163 -HAAGAKvKDLEDEADRLL 2180
Cdd:COG3096 647 dELAARK-QALESQIERLS 664
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1785-1967 |
2.87e-04 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 44.18 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1785 KSLKEMKEEIQAMLAEMgkrqlggkksiAEEEMDLAEelyqkvkrlfgdphQATEDLKAEIKGKLSDHEGKLQEAQDLLH 1864
Cdd:pfam01442 7 DELSTYAEELQEQLGPV-----------AQELVDRLE--------------KETEALRERLQKDLEEVRAKLEPYLEELQ 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1865 SA-QGKMKQA----GSLAEQNHANLTG-LERKRSAVSAVKQEAQDVLGEG-----ERLLDEANQLSDNINKEIEDLEEMe 1933
Cdd:pfam01442 62 AKlGQNVEELrqrlEPYTEELRKRLNAdAEELQEKLAPYGEELRERLEQNvdalrARLAPYAEELRQKLAERLEELKES- 140
|
170 180 190
....*....|....*....|....*....|....*...
gi 2316002738 1934 keLGP----LHVQLDDKVSRltsgLSDSLADHVHDAEE 1967
Cdd:pfam01442 141 --LAPyaeeVQAQLSQRLQE----LREKLEPQAEDLRE 172
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2059-2210 |
2.90e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2059 DVKENADSVAGLKGRVKAARDKTKDLLKTVNGTMATLsaipNDTAAKIAATKVVATDANAtAIDVLE-----RLGDLNLR 2133
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEY----NELQAELEALQAEIDKLQA-EIAEAEaeieeRREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2134 LRGLQQN---YSELE------------------DTVNAANQ-MIQDPEKNIHAAGAKVKDLEDEADRLLEKLQPIKKLQD 2191
Cdd:COG3883 92 ARALYRSggsVSYLDvllgsesfsdfldrlsalSKIADADAdLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170
....*....|....*....
gi 2316002738 2192 NLKRNISQIKELINQARKQ 2210
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAE 190
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1541-1595 |
3.10e-04 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 40.80 E-value: 3.10e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2316002738 1541 PCACpltNPENNFSPTCVaegFDDYRCTaCPEGYEGKYCERCATGYHGNPRMPGG 1595
Cdd:cd00055 1 PCDC---NGHGSLSGQCD---PGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| ATP_synt_b |
TIGR01144 |
ATP synthase, F0 subunit b; This model describes the F1/F0 ATP synthase b subunit in bacteria ... |
1837-1947 |
3.90e-04 |
|
ATP synthase, F0 subunit b; This model describes the F1/F0 ATP synthase b subunit in bacteria only. Scoring just below the trusted cutoff are the N-terminal domains of Mycobacterial b/delta fusion proteins and a subunit from an archaeon, Methanosarcina barkeri, in which the ATP synthase homolog differs in architecture and is not experimentally confirmed. This model helps resolve b from the related b' subunit. Within the family is an example from a sodium-translocating rather than proton-translocating ATP synthase. [Energy metabolism, ATP-proton motive force interconversion]
Pssm-ID: 130214 [Multi-domain] Cd Length: 147 Bit Score: 43.55 E-value: 3.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1837 ATEDLKAEIKGKLSDHEGKLQEAQDLLHSAQGKMKQAGSLAEQ--NHANLTGLERKrsavSAVKQEAQDvlgEGERLLDE 1914
Cdd:TIGR01144 23 AIETRQKKIADGLASAERAKKEAALAQKKAQVILKEAKDEAQEiiENANKRGSEIL----EEAKAEARE---EREKIKAQ 95
|
90 100 110
....*....|....*....|....*....|....
gi 2316002738 1915 ANQlsdNINKEIED-LEEMEKELGPLHVQLDDKV 1947
Cdd:TIGR01144 96 ARA---EIEAEKEQaREELRKQVADLSVLGAEKI 126
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1842-1947 |
4.05e-04 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 42.81 E-value: 4.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1842 KAEIKGKLSDHEGKLQEAQDLLHSAQGKMKQAGSLAEQ--NHANLTGLERKRSAVSAVKQEAqdvlgegERLLDEANQls 1919
Cdd:cd06503 32 EEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEiiEEARKEAEKIKEEILAEAKEEA-------ERILEQAKA-- 102
|
90 100
....*....|....*....|....*....
gi 2316002738 1920 dNINKEIED-LEEMEKELGPLHVQLDDKV 1947
Cdd:cd06503 103 -EIEQEKEKaLAELRKEVADLAVEAAEKI 130
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2037-2208 |
4.90e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.78 E-value: 4.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2037 EAAQGALQK---SHRLLN---QAKQLQNDVKENADSVAGLKGRVKAARDKTKDLLKTVNGTMATLSAIPNDTAAKiaatk 2110
Cdd:COG3206 192 EEAEAALEEfrqKNGLVDlseEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQ----- 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2111 vvatdanataiDVLERLGDLNLRLRGLQQNYSELEDTVNAANQMIQDPEKNIHAAGAKVK-DLEDEADRLLEKLQPIKKL 2189
Cdd:COG3206 267 -----------QLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILaSLEAELEALQAREASLQAQ 335
|
170
....*....|....*....
gi 2316002738 2190 QDNLKRNISQIKELINQAR 2208
Cdd:COG3206 336 LAQLEARLAELPELEAELR 354
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1679-2213 |
5.11e-04 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 46.36 E-value: 5.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1679 YKMLYRFENMTEELKHMLSPQKAPERLLQLadsnlgslvvEMDQLHSRATKVSADGEQVEDDADRIH-------KRAEDL 1751
Cdd:PTZ00440 449 DEKINELKKSINQLKTLISIMKSFYDLIIS----------EKDSMDSKEKKESSDSNYQEKVDELLQiinsikeKNNIVN 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1752 EQF--IRDTLLGAKDLQSKAAELNQTLSrrdgTPDKSLKEMKEEiqamlaEMGKRQLggkKSIAEEEMDLAEELYQKVKR 1829
Cdd:PTZ00440 519 NNFknIEDYYITIEGLKNEIEGLIELIK----YYLQSIETLIKD------EKLKRSM---KNDIKNKIKYIEENVDHIKD 585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1830 LF---GDPHQATEDLKAEIKGKLSDHEGKLQEAQDLlhsaQGKMKQ------AGSLAEQNHANLTGLE------RKRSAV 1894
Cdd:PTZ00440 586 IIslnDEIDNIIQQIEELINEALFNKEKFINEKNDL----QEKVKYilnkfyKGDLQELLDELSHFLDdhkylyHEAKSK 661
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1895 SAVKQEAQDVLGEGERL----LDEANQLSDNINKEIEDLEE-----MEKELGPLHV-------QLDDKVSRLTSGLSDSL 1958
Cdd:PTZ00440 662 EDLQTLLNTSKNEYEKLefmkSDNIDNIIKNLKKELQNLLSlkeniIKKQLNNIEQdisnslnQYTIKYNDLKSSIEEYK 741
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1959 ADHVHdAEEHAKQLNEsaaILDGILAEAKNLSFNATAAFKAYTNIKANVDAAekeakaakqranealalalgpevpvkea 2038
Cdd:PTZ00440 742 EEEEK-LEVYKHQIIN---RKNEFILHLYENDKDLPDGKNTYEEFLQYKDTI---------------------------- 789
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2039 aqgaLQKSHRLLNQAKQLQNDVKENadsvaglkgrvkaardktKDLLKTVNGTMATLSaipNDTAAKIAATKvvatdana 2118
Cdd:PTZ00440 790 ----LNKENKISNDINILKENKKNN------------------QDLLNSYNILIQKLE---AHTEKNDEELK-------- 836
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2119 taiDVLERLG--DLNLRLRGLQQNYSELEDTVNAANQMIQDPEKNIHAagakVKDLEDEADRLLEKLQPIkklqDNLKRN 2196
Cdd:PTZ00440 837 ---QLLQKFPteDENLNLKELEKEFNENNQIVDNIIKDIENMNKNINI----IKTLNIAINRSNSNKQLV----EHLLNN 905
|
570
....*....|....*..
gi 2316002738 2197 ISQIKELINQARKQANS 2213
Cdd:PTZ00440 906 KIDLKNKLEQHMKIINT 922
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1684-1849 |
6.13e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.82 E-value: 6.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1684 RFENMTEELKhmlspqKAPERLLQLADSnLGSLVVEMDQLHSRATKVSADGEQVEDDADRIHKRAEDLEQFIRDTLLGAK 1763
Cdd:TIGR02168 839 RLEDLEEQIE------ELSEDIESLAAE-IEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRS 911
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1764 DLQSKAAELNQTLSrrdgtpdkSLKEMKEEIQAMLAEMgkrqlggKKSIAEEEMDLAEELYQKVKRLFGDPHQATEDLKa 1843
Cdd:TIGR02168 912 ELRRELEELREKLA--------QLELRLEGLEVRIDNL-------QERLSEEYSLTLEEAEALENKIEDDEEEARRRLK- 975
|
....*.
gi 2316002738 1844 EIKGKL 1849
Cdd:TIGR02168 976 RLENKI 981
|
|
| YydB |
COG5293 |
Uncharacterized conserved protein YydD, contains DUF2326 domain [Function unknown]; |
1715-1974 |
6.57e-04 |
|
Uncharacterized conserved protein YydD, contains DUF2326 domain [Function unknown];
Pssm-ID: 444096 [Multi-domain] Cd Length: 572 Bit Score: 45.32 E-value: 6.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1715 SLVVEMDQLHSRATKVSADGEQVEDDADR-IHKRAEDLEQFIrdtllgaKDLQSKAAELNQTLSRRDGTP-DKSLKEMKE 1792
Cdd:COG5293 181 DLAAEKYELKEEIKELKKLRKALKDELIGsVVKSISELRAEI-------LELEEEIEKLEKDLEKFDVAEnYEELEKELD 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1793 EIQAMLAEMG------KRQLGGKKSIAEEEMDL----AEELYQKVKRLFGDphQATEDL------KAEIKGKLSDH-EGK 1855
Cdd:COG5293 254 ELKREINELRneryslERRLKKIERSLEEEIDIdpdeLEKLYEEAGVFFPD--QVKKRFeeveafHKSIVENRREYlEEE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1856 LQEAQDLLHSAQGKMKQagslaeqnhanltgLERKRSAVSAVKQEaqdvlgegERLLDEANQLSDNINKEIEDLEEMEKE 1935
Cdd:COG5293 332 IAELEAELEELEAELAE--------------LGKERAELLSLLDS--------KGALDKYKELQEELAELEAELEELESR 389
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2316002738 1936 LGPLHvQLDDKVSRLTSGLSD---SLADHVHDAEEHAKQLNE 1974
Cdd:COG5293 390 LEKLQ-ELEDEIRELKEERAElkeEIESDIEERKELLDEINK 430
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1680-2225 |
7.03e-04 |
|
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: 45.42 E-value: 7.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1680 KMLYRFENMTEELKHMlspQKAPERLLqladSNLGSLVVEMDQLHSRATKVSADGEQVEDDADRIHKRAE----DLEQFI 1755
Cdd:TIGR00606 238 EIVKSYENELDPLKNR---LKEIEHNL----SKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDeqlnDLYHNH 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1756 RDTLlgakdlQSKAAELNQtLSRRDGTPDKSLKEMKEEIQAMLAEMGKRQLGGKK----SIAEEEMDLAEELYQKVKRLF 1831
Cdd:TIGR00606 311 QRTV------REKERELVD-CQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRhqehIRARDSLIQSLATRLELDGFE 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1832 GDPHQATEdLKAEIKGKLSDHEGKLQEAQDLLHSAQGKMKQAGSLAEQNHANLTGLERKRSAVSAVKQEAQDVLGEGERL 1911
Cdd:TIGR00606 384 RGPFSERQ-IKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKE 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1912 LDEANQLSDNINKEIEDLEEMEKELGPLhvqldDKVSRLTSGLSD--SLADHVHDAEEHAKQLNESAAILDGILAEAKNL 1989
Cdd:TIGR00606 463 LQQLEGSSDRILELDQELRKAERELSKA-----EKNSLTETLKKEvkSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQM 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1990 SFNATAAFKAYTNIKANvdaaekeakaAKQRANEALALAlgPEVPVKEAAQGALQKSHRLLNQAKQLQNDVKENADSVAG 2069
Cdd:TIGR00606 538 EMLTKDKMDKDEQIRKI----------KSRHSDELTSLL--GYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQ 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2070 LKGRV-KAARDKTKDLLK------TVNGTMATLSAIPN----------DTAAKIAATKVVA------TDANATAIDVLER 2126
Cdd:TIGR00606 606 NKNHInNELESKEEQLSSyedklfDVCGSQDEESDLERlkeeieksskQRAMLAGATAVYSqfitqlTDENQSCCPVCQR 685
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2127 L----GDLNLRLRGLQQNYSELEDTVNAANQMIQDPEKNIHAAGAKVKDLEDEADRLLEKLQPIKKLQDNLKRNISQIKE 2202
Cdd:TIGR00606 686 VfqteAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKN 765
|
570 580
....*....|....*....|...
gi 2316002738 2203 LINQARKQANSIKVSVSSGGDCL 2225
Cdd:TIGR00606 766 DIEEQETLLGTIMPEEESAKVCL 788
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1789-2086 |
7.14e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.52 E-value: 7.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1789 EMKEEIQAMLAEmgkrqLGGKKSIAEEEmdlAEELYQKVKRLFgdphQATEDLKAEIKGKLSDHEGKLQEAQDLLhsaqg 1868
Cdd:COG1340 1 SKTDELSSSLEE-----LEEKIEELREE---IEELKEKRDELN----EELKELAEKRDELNAQVKELREEAQELR----- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1869 kmkqagSLAEQNHANLTGLERKRSAVSAVKQEAQDVLGEGERLLDEANQLS---DNINKEIEDLEEM--------EKElg 1937
Cdd:COG1340 64 ------EKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGgsiDKLRKEIERLEWRqqtevlspEEE-- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1938 plhVQLDDKVSRLTSGLsdsladhvhdaeEHAKQLNESAAILDGILAEAKNLSFNATAAFKAYTNIKANVDAAEKEAKAA 2017
Cdd:COG1340 136 ---KELVEKIKELEKEL------------EKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIEL 200
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2316002738 2018 KQRANEalalaLGPEV-PVKEAAQGALQKSHRLLNQAKQLQNDVKENADSVAGLKGRVKAA-RDKTKDLLK 2086
Cdd:COG1340 201 YKEADE-----LRKEAdELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALkREKEKEELE 266
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1885-2120 |
7.14e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 7.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1885 TGLERKRSAVSAVKQEAQDVLGEGERLLDEANQLSDNINKEIEDLEEMEKELGPLHVQLDDKVSRLTSgLSDSLADHVHD 1964
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEE-RREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1965 AEEHAKQLNESAAILdgilaEAKNLSfNATAAFKAYTNIKANvDAAEKEAKAAKQRANEALALALgpevpvkEAAQGALQ 2044
Cdd:COG3883 95 LYRSGGSVSYLDVLL-----GSESFS-DFLDRLSALSKIADA-DADLLEELKADKAELEAKKAEL-------EAKLAELE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2316002738 2045 KSHRLLNQAK-QLQNDVKENADSVAGLKGRVKAARDKTKDLLKTVNGTMATLSAIPNDTAAKIAATKVVATDANATA 2120
Cdd:COG3883 161 ALKAELEAAKaELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAA 237
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1703-1919 |
8.34e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 8.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1703 ERLLQLADSNLGSLVVEMDQLHSRATKVSADGEQVEDDADRIHKRAEDLEQFIrdtllgaKDLQSKAAELNQTLSRRDGT 1782
Cdd:COG3883 29 QAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEI-------EERREELGERARALYRSGGS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1783 PD--------KSLKEMKEEIQAMlaemgkrqlggkKSIAEEEMDLAEELYQKVKRLfgdphqatEDLKAEIKGKLSDHEG 1854
Cdd:COG3883 102 VSyldvllgsESFSDFLDRLSAL------------SKIADADADLLEELKADKAEL--------EAKKAELEAKLAELEA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2316002738 1855 KLQEAQDLLHSAQGKMKQAGSLAEQNHANLTGLERKRSAVSAVKQEAQDVLGEGERLLDEANQLS 1919
Cdd:COG3883 162 LKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2047-2214 |
8.38e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.42 E-value: 8.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2047 HRLLNQAKQLQNDVKENADSVAGLKGRVKAARDKTKDLLKTVNGT---MATLSAIPNDTAAKIAAT---KVVATDANATA 2120
Cdd:PRK02224 205 HERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERreeLETLEAEIEDLRETIAETereREELAEEVRDL 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2121 IDVLERLGD------------------LNLRLRGLQQNYSELEDTVNAANQMIQDPEKNIHAAGAKVKDLEDEADRLLEK 2182
Cdd:PRK02224 285 RERLEELEEerddllaeaglddadaeaVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREE 364
|
170 180 190
....*....|....*....|....*....|..
gi 2316002738 2183 LQPIKKLQDNLKRNISQIKELINQARKQANSI 2214
Cdd:PRK02224 365 AAELESELEEAREAVEDRREEIEELEEEIEEL 396
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
292-315 |
9.78e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 39.22 E-value: 9.78e-04
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2119-2215 |
1.15e-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: 43.37 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2119 TAIDVLE-RLGDLNLRLRGLQQNYSELEDTVNAANQMIQDPEKNIHAAGAKVKDLEDEADRLLEKLQPIKK------LQ- 2190
Cdd:COG1579 17 SELDRLEhRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNnkeyeaLQk 96
|
90 100
....*....|....*....|....*..
gi 2316002738 2191 --DNLKRNISQIKELINQARKQANSIK 2215
Cdd:COG1579 97 eiESLKRRISDLEDEILELMERIEELE 123
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1703-1860 |
1.24e-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: 43.37 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1703 ERLLQLA--DSNLGSLVVEMDQLHSRATKVSADGEQVEDDADRIHKRAEDLEQFIRDTLLGAKDLQSKAAELNQTLSRrd 1780
Cdd:COG1579 7 RALLDLQelDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGN-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1781 GTPDKSLKEMKEEIQAMLAEMGK-----RQLGGKKSIAEEEMDLAEELYQKVKRLFgdphqatEDLKAEIKGKLSDHEGK 1855
Cdd:COG1579 85 VRNNKEYEALQKEIESLKRRISDledeiLELMERIEELEEELAELEAELAELEAEL-------EEKKAELDEELAELEAE 157
|
....*
gi 2316002738 1856 LQEAQ 1860
Cdd:COG1579 158 LEELE 162
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1694-1937 |
1.25e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1694 HMLSPQKAPERLLQLADsnlgslvvEMDQL---HSRATKVSadgEQVE------DDADRIHKRAEDLEQF--IRDTL--- 1759
Cdd:COG4913 216 YMLEEPDTFEAADALVE--------HFDDLeraHEALEDAR---EQIEllepirELAERYAAARERLAELeyLRAALrlw 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1760 -------LGAKDLQSKAAELNQTLSRRDGTpDKSLKEMKEEIQAMLAEMgkRQLGG-KKSIAEEEMDLAEELYQKVKRLF 1831
Cdd:COG4913 285 faqrrleLLEAELEELRAELARLEAELERL-EARLDALREELDELEAQI--RGNGGdRLEQLEREIERLERELEERERRR 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1832 GDPHQATEDLKAEIKGKLSDHEGKLQEAQDLLHsaqgkmkQAGSLAEQNHANLTGLERKRsavSAVKQEAQDVLGEGERL 1911
Cdd:COG4913 362 ARLEALLAALGLPLPASAEEFAALRAEAAALLE-------ALEEELEALEEALAEAEAAL---RDLRRELRELEAEIASL 431
|
250 260
....*....|....*....|....*..
gi 2316002738 1912 ldEANQlsDNINKEIEDL-EEMEKELG 1937
Cdd:COG4913 432 --ERRK--SNIPARLLALrDALAEALG 454
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1690-1934 |
1.34e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.51 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1690 EELKHMLSpqkapeRLLQLADSNLGSLVVEMDQLHSRatkvSADGEQVEDDADRI---HKRAEDLEQFIRDTLLGakDLQ 1766
Cdd:PRK01156 497 EKIVDLKK------RKEYLESEEINKSINEYNKIESA----RADLEDIKIKINELkdkHDKYEEIKNRYKSLKLE--DLD 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1767 SKAAELNQTLSRRDGTPDKSLKEMKEEIQAMLAEMGKR-----------QLGGKKSIA--EEEMDLAEELY---QKVKRL 1830
Cdd:PRK01156 565 SKRTSWLNALAVISLIDIETNRSRSNEIKKQLNDLESRlqeieigfpddKSYIDKSIReiENEANNLNNKYneiQENKIL 644
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1831 FGDPHQATEDLKAEIKGKlSDHEGKLQEAQDLLHSAQGKMKQAGSLAEQNHANLTGLERKRsavsavkqeaqdvlgegER 1910
Cdd:PRK01156 645 IEKLRGKIDNYKKQIAEI-DSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTI-----------------EI 706
|
250 260
....*....|....*....|....
gi 2316002738 1911 LLDEANQLSDNINKEIEDLEEMEK 1934
Cdd:PRK01156 707 LRTRINELSDRINDINETLESMKK 730
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2119-2217 |
1.36e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.75 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2119 TAIDVL-ERLGDLNLRLRGLQQNYSELEDTVNAANQMIQDPEKNIHAAGAKVKDLEDEA-------DRLLEKLQPIKKLQ 2190
Cdd:COG1340 1 SKTDELsSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAqelrekrDELNEKVKELKEER 80
|
90 100
....*....|....*....|....*..
gi 2316002738 2191 DNLKRNISQIKELINQARKQANSIKVS 2217
Cdd:COG1340 81 DELNEKLNELREELDELRKELAELNKA 107
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1768-2210 |
1.51e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1768 KAAEL-NQTLSrrdGTPDKSL-----------KEMKEEIQAMLAEMgkRQLGGkksiAEEEMDLAEElyqKVKRLfgDP- 1834
Cdd:COG4913 192 KALRLlHKTQS---FKPIGDLddfvreymleePDTFEAADALVEHF--DDLER----AHEALEDARE---QIELL--EPi 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1835 ---HQATEDLKAEIkgklsdheGKLQEAQDLLHS--AQGKMKQAGSLAEQNHANLTGLERKRSAVSAVKQEAQDVLGEGE 1909
Cdd:COG4913 258 relAERYAAARERL--------AELEYLRAALRLwfAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1910 RLLDEA--NQLsDNINKEIEDLEEMEKELGPLHVQLDDKVSRLtsGLSDSLadhvhDAEEHAKQLNESAAILDGILAEAK 1987
Cdd:COG4913 330 AQIRGNggDRL-EQLEREIERLERELEERERRRARLEALLAAL--GLPLPA-----SAEEFAALRAEAAALLEALEEELE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1988 NLSFNATAAFKAYTNIKANVDAAEKEAKAAKQRAN----------EALALALGP---EVP-------VKE-------AAQ 2040
Cdd:COG4913 402 ALEEALAEAEAALRDLRRELRELEAEIASLERRKSniparllalrDALAEALGLdeaELPfvgelieVRPeeerwrgAIE 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2041 GAL------------------------QKSHRL----LNQAKQLQNDVKENADSVAG-LKGRVKAARDKTKDLLK----- 2086
Cdd:COG4913 482 RVLggfaltllvppehyaaalrwvnrlHLRGRLvyerVRTGLPDPERPRLDPDSLAGkLDFKPHPFRAWLEAELGrrfdy 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2087 ----------------TVNGTMATLSA---------------IPNDTAAKIAATKVVATDANATAIDVLERLGDLNLRLR 2135
Cdd:COG4913 562 vcvdspeelrrhpraiTRAGQVKGNGTrhekddrrrirsryvLGFDNRAKLAALEAELAELEEELAEAEERLEALEAELD 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2136 GLQQ---------NYSELEDTVNAANQMIQDPE---KNIHAAGAKVKDLEDEADRLLEKLQPIKKLQDNLKRNISQIKEL 2203
Cdd:COG4913 642 ALQErrealqrlaEYSWDEIDVASAEREIAELEaelERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKE 721
|
....*..
gi 2316002738 2204 INQARKQ 2210
Cdd:COG4913 722 LEQAEEE 728
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1719-2212 |
1.51e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 44.43 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1719 EMDQLHSRATKVSADGEQVEDDAdrihkRAEDlEQFIRDTLLGAKDLQSKAAELNQTLSRRDGTPDKSLK-EMKEEIQAM 1797
Cdd:NF041483 576 ELTRLHTEAEERLTAAEEALADA-----RAEA-ERIRREAAEETERLRTEAAERIRTLQAQAEQEAERLRtEAAADASAA 649
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1798 LAEMGKRQLGGKKSIAEEEMDLAEELYQKVKRLFGDPHQATEDLKAEIKGKLS----DHEGKLQEAQDLLHSAQGKMKQA 1873
Cdd:NF041483 650 RAEGENVAVRLRSEAAAEAERLKSEAQESADRVRAEAAAAAERVGTEAAEALAaaqeEAARRRREAEETLGSARAEADQE 729
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1874 GSLAEQNHANLTGLERKRSAvsavkqEAQdvlGEGERLLDEANQLSDNINKEIED-LEEMEKELGPLHVQLDDKVSRLTS 1952
Cdd:NF041483 730 RERAREQSEELLASARKRVE------EAQ---AEAQRLVEEADRRATELVSAAEQtAQQVRDSVAGLQEQAEEEIAGLRS 800
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1953 GlsdslADHVHD-----AEEHAKQLNESA------AILDG--ILAEAKNLSFNATA-AFKAYTNIKANVDAAEKEAKAAK 2018
Cdd:NF041483 801 A-----AEHAAErtrteAQEEADRVRSDAyaererASEDAnrLRREAQEETEAAKAlAERTVSEAIAEAERLRSDASEYA 875
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2019 QR----ANEALAlalgpevpvkEAAQGALQKSHRLLNQAKQLQNDVKENADSVAGlKGRVKAARDKTKdllktvngtmAT 2094
Cdd:NF041483 876 QRvrteASDTLA----------SAEQDAARTRADAREDANRIRSDAAAQADRLIG-EATSEAERLTAE----------AR 934
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2095 LSAIPNDTAAKIAATKVVAtDANATAIDVLERLGDLNLRLRglqqnySELEDTVNAANQMIQdpekNIHAAGAKVK-DLE 2173
Cdd:NF041483 935 AEAERLRDEARAEAERVRA-DAAAQAEQLIAEATGEAERLR------AEAAETVGSAQQHAE----RIRTEAERVKaEAA 1003
|
490 500 510
....*....|....*....|....*....|....*....
gi 2316002738 2174 DEADRLLEKLQpikklqdnlkrniSQIKELINQARKQAN 2212
Cdd:NF041483 1004 AEAERLRTEAR-------------EEADRTLDEARKDAN 1029
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2044-2215 |
1.55e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.36 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2044 QKSHRLLNQAKQLQNDVKENADSVAGLKGRVKAARDKTKDLLKTVN---GTMATLSAIPNDTAA---KIAA------TKV 2111
Cdd:COG1340 50 AQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDelrKELAELNKAGGSIDKlrkEIERlewrqqTEV 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2112 VATDANataIDVLERLGDLNLRLRGLQQNYSELEDTVNAANQmIQDPEKNIHAAGAKVKDLEDEADRLLEKLQPIKKLQD 2191
Cdd:COG1340 130 LSPEEE---KELVEKIKELEKELEKAKKALEKNEKLKELRAE-LKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEAD 205
|
170 180
....*....|....*....|....
gi 2316002738 2192 NLKRNISQIKELINQARKQANSIK 2215
Cdd:COG1340 206 ELRKEADELHKEIVEAQEKADELH 229
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2037-2220 |
2.09e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2037 EAAQGALQKshrLLNQAKQLQNDVKENADSVAGLKGRVKAARDKTKDLLKTV---NGTMATLSAI-----PNDTAAKIAA 2108
Cdd:COG3883 47 EELNEEYNE---LQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALyrsGGSVSYLDVLlgsesFSDFLDRLSA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2109 TKVVaTDANATAIDVLERLGDlnlrlrglqqnysELEDTVNAANQMIQDPEKNIHAAGAKVKDLEDEADrllEKLQPIKK 2188
Cdd:COG3883 124 LSKI-ADADADLLEELKADKA-------------ELEAKKAELEAKLAELEALKAELEAAKAELEAQQA---EQEALLAQ 186
|
170 180 190
....*....|....*....|....*....|..
gi 2316002738 2189 LQDNLKRNISQIKELINQARKQANSIKVSVSS 2220
Cdd:COG3883 187 LSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1836-2006 |
2.62e-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: 42.22 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1836 QATEDLKAEIKGKLSDHEGKLQEAQDLLHSAQGKMKQAGSLAEQNHANLTGLERKRSAVSAVKQEAQDVLGEGeRLLDEA 1915
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV-RNNKEY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1916 NQLS---DNINKEIEDLEEMEKELGPLHVQLDDKVSRLTSGLSDSLADHVHDAEEHAKQLNESAAILDGILAEAKNL--S 1990
Cdd:COG1579 92 EALQkeiESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELaaK 171
|
170
....*....|....*.
gi 2316002738 1991 FNAtAAFKAYTNIKAN 2006
Cdd:COG1579 172 IPP-ELLALYERIRKR 186
|
|
| FlgK |
COG1256 |
Flagellar hook-associated protein FlgK [Cell motility]; |
2092-2183 |
2.91e-03 |
|
Flagellar hook-associated protein FlgK [Cell motility];
Pssm-ID: 440868 [Multi-domain] Cd Length: 479 Bit Score: 43.33 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2092 MATLSAIPNDTAAKiaatKVVATDANATAidvlERLGDLNLRLRGLQQN-YSELEDTVNAANQMIQDPEK------NIHA 2164
Cdd:COG1256 119 LQELASNPESSAAR----QAVLEAAQALA----DRFNSLSSQLQDLRADaDSQIASTVDEINSLLSQIADlnkqivKAEA 190
|
90
....*....|....*....
gi 2316002738 2165 AGAKVKDLEDEADRLLEKL 2183
Cdd:COG1256 191 GGQDANDLLDQRDQLLDEL 209
|
|
| TNFRSF6_teleost |
cd13423 |
Tumor necrosis factor receptor superfamily member 6 (TNFRSF6) in teleosts; also known as fas ... |
804-901 |
3.58e-03 |
|
Tumor necrosis factor receptor superfamily member 6 (TNFRSF6) in teleosts; also known as fas cell surface death receptor (FasR); This subfamily of TNFRSF6 (also known as fas cell surface death receptor (FasR) or Fas; APT1; CD95; FAS1; APO-1; FASTM; ALPS1A) is found in teleosts. It contains a death domain and plays a central role in the physiological regulation of programmed cell death. In humans, it has been implicated in the pathogenesis of various malignancies and diseases of the immune system. The receptor interactions with the Fas ligand (FasL), allowing the formation of a death-inducing signaling complex that includes Fas-associated death domain protein (FADD), caspase 8, and caspase 10; autoproteolytic processing of the caspases in the complex triggers a downstream caspase cascade, leading to apoptosis. This receptor has also been shown to activate NF-kappaB, MAPK3/ERK1, and MAPK8/JNK, and is involved in transducing the proliferating signals in normal diploid fibroblast and T cells. In channel catfish and the Japanese rice fish, medaka, homologs of Fas receptor (FasR), as well as FADD and caspase 8, have been identified and characterized, and likely constitute the teleost equivalent of the death-inducing signaling complex (DISC). FasL/FasR are involved in the initiation of apoptosis and suggest that mechanisms of cell-mediated cytotoxicity in teleosts are similar to those used by mammals; presumably, the mechanism of apoptosis induction via death receptors was evolutionarily established during the appearance of vertebrates.
Pssm-ID: 276928 [Multi-domain] Cd Length: 103 Bit Score: 39.33 E-value: 3.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 804 TCHLGEEGELLCDQCQPGYTGPRCDRCSNGYYGKPAVPGGSCQPCD-CHGNLDLSIPGSCDPSTGQCLRCRQGYggaACD 882
Cdd:cd13423 13 TCCLCPAGQHVEKHCTNNGTDGECEACEDGTYNSHPNSLDSCEPCTsCDPNANLEVEERCTPSSDTVCRCKEGH---YCD 89
|
90
....*....|....*....
gi 2316002738 883 SCAdgyygdaiTAKNCQPC 901
Cdd:cd13423 90 KGE--------ECKVCYPC 100
|
|
| PRK07352 |
PRK07352 |
F0F1 ATP synthase subunit B; Validated |
1839-1914 |
4.99e-03 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180941 [Multi-domain] Cd Length: 174 Bit Score: 40.71 E-value: 4.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1839 EDLKAEIKGKLSDHEGKLQEAQDLLHSAQGKMKQAGSLAEQNHAN---------LTGLERKRSAVSAVKQEA-QDVLGEG 1908
Cdd:PRK07352 49 EERREAILQALKEAEERLRQAAQALAEAQQKLAQAQQEAERIRADakaraeairAEIEKQAIEDMARLKQTAaADLSAEQ 128
|
....*.
gi 2316002738 1909 ERLLDE 1914
Cdd:PRK07352 129 ERVIAQ 134
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1784-2199 |
5.04e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 42.90 E-value: 5.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1784 DKSLKEMKEEIQAMLAEMGKRQLGGKKSIAEEEMdlaEELYQKVKRLFGDPH--QATEDLKaEIKGKLSDHEGKLQEAQD 1861
Cdd:PTZ00440 1200 DQVKKNMSKERNDHLTTFEYNAYYDKATASYENI---EELTTEAKGLKGEANrsTNVDELK-EIKLQVFSYLQQVIKENN 1275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1862 LLHSAQGKMKQAGSLAEQNHanltgLERKRSAVSAVKQEAQDVLGEGERLLDEANQLSDNINKEIEDLEEMEKelgPLHV 1941
Cdd:PTZ00440 1276 KMENALHEIKNMYEFLISID-----SEKILKEILNSTKKAEEFSNDAKKELEKTDNLIKQVEAKIEQAKEHKN---KIYG 1347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 1942 QLDDKvsrltsglsdSLADHVHDAEEHAKQLNESAAILDGILAEAKNLSFNATAAFKAYTNIKANVDAAEKeakaakqra 2021
Cdd:PTZ00440 1348 SLEDK----------QIDDEIKKIEQIKEEISNKRKEINKYLSNIKSNKEKCDLHVRNASRGKDKIDFLNK--------- 1408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2022 NEALALALGPEVPVKEaAQGALQKSHRLLNQAKQLQNDVKENADSVaglkgrVKAARDKTKDLLKTVNGTMATLSAIPND 2101
Cdd:PTZ00440 1409 HEAIEPSNSKEVNIIK-ITDNINKCKQYSNEAMETENKADENNDSI------IKYEKEITNILNNSSILGKKTKLEKKKK 1481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316002738 2102 TAAKIaatkvvATDANATAIDVLERLGDLNLRLRGL--QQNYSELEDTVN-----AANQMIQDPEKNIHAAGAKVKDLED 2174
Cdd:PTZ00440 1482 EATNI------MDDINGEHSIIKTKLTKSSEKLNQLneQPNIKREGDVLNndkstIAYETIQYNLGRVKHNLLNILNIKD 1555
|
410 420
....*....|....*....|....*....
gi 2316002738 2175 EADRLLEK----LQPIKKLQDNLKRNISQ 2199
Cdd:PTZ00440 1556 EIETILNKaqdlMRDISKISKIVENKNLE 1584
|
|
| |
