|
Name |
Accession |
Description |
Interval |
E-value |
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
22-270 |
6.33e-94 |
|
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: 304.28 E-value: 6.33e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 22 RGLFPAVLNLASMAEISANATCGENGAEMYCKLVEHVpgqpVRNPQCRVCNLRSerPYERHPIEFAIDGTN----RWWQS 97
Cdd:smart00136 5 RSCYPPFVNLAFGREVTATSTCGEPGPERYCKLVGHT----EQGKKCDYCDARN--PRRSHPAENLTDGNNpnnpTWWQS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 98 PSIKNGMdyHYVTITLDLQQVFQIAYVILKAAnSPRPGNWVLERSLDGETFTPWQYFAitdTECITRFNIIPRTGPPAYK 177
Cdd:smart00136 79 EPLSNGP--QNVNLTLDLGKEFHVTYVILKFC-SPRPSLWILERSDFGKTWQPWQYFS---SDCRRTFGRPPRGPITKGN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 178 hDDEVICTSFYSKIHPLENGEIHTSLINGRPSAEDP--SPTLLSFTSARYIRLRFLRIRTLNADLMTLAqndpqsvdPIV 255
Cdd:smart00136 153 -EDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDFdnSPVLQEWVTATNIRVRLTRLRTLGDELMDDR--------PEV 223
|
250
....*....|....*
gi 2196706209 256 TRRYYYSIKDISVGG 270
Cdd:smart00136 224 TRRYYYAISDIAVGG 238
|
|
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
24-270 |
4.66e-90 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 292.95 E-value: 4.66e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 24 LFPAVLNLASMAEISANATCGENGAEMYCKLVEHVPGQpvrnpQCRVCNLRseRPYERHPIEFAIDGTNR----WWQSPS 99
Cdd:pfam00055 1 CYPAFGNLAFGREVSATSTCGLNGPERYCILSGLEGGK-----KCFICDSR--DPHNSHPPSNLTDSNNGtnetWWQSET 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 100 IKngMDYHYVTITLDLQQVFQIAYVILKAAnSPRPGNWVLERSLD-GETFTPWQYFAitdTECITRFNIipRTGPPAYKH 178
Cdd:pfam00055 74 GV--IQYENVNLTLDLGKEFHFTYLILKFK-SPRPAAMVLERSTDfGKTWQPYQYFA---SDCRRTFGR--PSGPSRGIK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 179 DDEVICTSFYSKIHPLENGEIHTSLINGRPSAE--DPSPTLLSFTSARYIRLRFLRIRTLnadlmtlaqNDPQSVDPIVT 256
Cdd:pfam00055 146 DDEVICTSEYSDISPLTGGEVIFSTLEGRPSANifDYSPELQDWLTATNIRIRLLRLHTL---------GDELLDDPSVL 216
|
250
....*....|....
gi 2196706209 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 ... |
1569-1822 |
1.15e-49 |
|
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: 178.38 E-value: 1.15e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1569 LTLPLPPPYGALYRVENMTDELKHMLSPHRAPERLLQLADSNLGSLVTEMDELLSRANKVSADGEQTDSDAERSHKRAQD 1648
Cdd:pfam06008 7 LTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1649 LEQFVKNtllaaeaLRDKARELN---ATLGRRDDGV-EKSVNEMQDEIKAMMNELRSRQLTHPHThTVQEELRAAQDLLL 1724
Cdd:pfam06008 87 LAEAIKN-------LIDNIKEINekvATLGENDFALpSSDLSRMLAEAQRMLGEIRSRDFGTQLQ-NAEAELKAAQDLLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1725 KVQRGFAAPHRVSEELQQEVSSKLRDHDDKLQGAQELLEEAQNNIGNARTLNSDNLRRLEEVQRKRNESSKKKKETEGIL 1804
Cdd:pfam06008 159 RIQTWFQSPQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEETL 238
|
250
....*....|....*...
gi 2196706209 1805 EDGEKILNEANALSDDIN 1822
Cdd:pfam06008 239 KTARDSLDAANLLLQEID 256
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
1211-1349 |
1.16e-46 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 164.75 E-value: 1.16e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1211 YWKLPKQFRGSMITAYGGKLKYTVYYEARDETGHASYEPQVIIRGGATRDKVMIRHMVEPQIGQLTRHEIDMTEHEWKHH 1290
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGGGSLNSEPDVILEGNGLRLSYSSPDQPPPDPGQEQTYSVRLHEENWRDS 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2196706209 1291 DSKPMSREDFMDILFHIENVFIRASHGNVMRQSRISEISLEVAeegRPSVESERAHQIE 1349
Cdd:pfam00052 81 DGAPVSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSA---VPGGSGPPASWVE 136
|
|
| LamB |
smart00281 |
Laminin B domain; |
1206-1335 |
4.94e-43 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 153.96 E-value: 4.94e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1206 LEEPYYWKLPKQFRGSMITAYGGKLKYTVYYEARDEtGHASYEPQVIIRGGATRdkVMIRHMVEPQIGQLTRHEIDMTEH 1285
Cdd:smart00281 1 DNEPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRRG-GTHVSAPDVILEGNGLR--ISHPAEGPPLPDELTTVEVRFREE 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1286 EWKHHDSKPMSREDFMDILFHIENVFIRASHGNVMRQSRISEISLEVAEE 1335
Cdd:smart00281 78 NWQYYGGRPVTREDLMMVLANLTAILIRATYSQQMAGSRLSDVSLEVAVP 127
|
|
| Laminin_II |
pfam06009 |
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 ... |
2009-2145 |
4.04e-41 |
|
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: 149.17 E-value: 4.04e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2009 TKQKASKANDTAIEVLARLKDMNQNLMGLNRNFSTLKDDINKANNLIQDpeKNTIIHAAGAKVKDLEDEAERLLEKLKPI 2088
Cdd:pfam06009 1 SKELAREANETAKEVLEQLAPLSQNLENTSEKLSGINRSLEETNELVND--ANKALDDAGRSVKKLEELAPDLLDKLKPL 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2089 RELQDN---LRKNISQIKELINQARKQANSIKVSVSSGGDCIRTYRPDIKKGRYNTIVLN 2145
Cdd:pfam06009 79 KQLEVNsssLSDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTSL 138
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2952-3101 |
3.34e-36 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 135.62 E-value: 3.34e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2952 GSYFSGTGYAKAVSTYRVGNEVTVALEFRTSTATGVLLGVSGQTMDG-LGIELINGKLLFHADNGVGRVTATSQGAgLCD 3030
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDfLALELEDGRLVLRYDLGSGSLVLSSKTP-LND 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2196706209 3031 GQWHSVTAHKLKHRLELIVDGQKSEAASPDASSASADTNDPVFVGGYPEGLKQFGLTTSAPFKGCMRNIKL 3101
Cdd:cd00110 80 GQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKV 150
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2776-2926 |
5.75e-35 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 131.77 E-value: 5.75e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2776 FGLSRNSHMEFEFDDRKvKNSLIIEFELRTEADSGLVFYMARINHADFATVQVKEGMAHLSFDLGSGNTSVSVPRIINDG 2855
Cdd:cd00110 2 VSFSGSSYVRLPTLPAP-RTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2196706209 2856 HWHKIKVLRDKQRGILTVDGRYIKHTVSPKKADILDVVGKLYVGGLPLNYTTKRIgPVVYSINGCIRNFRM 2926
Cdd:cd00110 81 QWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGL-PVSPGFVGCIRDLKV 150
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2804-2932 |
2.76e-34 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 129.36 E-value: 2.76e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2804 RTEADSGLVFYMARINHADFATVQVKEGMAHLSFDLGSGNTSVSVPRIINDGHWHKIKVLRDKQRGILTVDGRYIKHTVS 2883
Cdd:pfam00054 2 RTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGES 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2884 PKKADI-LDVVGKLYVGGLPLNYTTKRIGPVVYSINGCIRNFRMTNGPQD 2932
Cdd:pfam00054 82 PLGATTdLDVDGPLYVGGLPSLGVKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| LamG |
smart00282 |
Laminin G domain; |
2799-2928 |
4.44e-33 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 125.91 E-value: 4.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2799 IEFELRTEADSGLVFYMARINHADFATVQVKEGMAHLSFDLGSGNTSVSV-PRIINDGHWHKIKVLRDKQRGILTVDGRY 2877
Cdd:smart00282 2 ISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSdPTPLNDGQWHRVAVERNGRSVTLSVDGGN 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2196706209 2878 IKHTVSPKKADILDVVGKLYVGGLPLNYTTKRIgPVVYSINGCIRNFRMTN 2928
Cdd:smart00282 82 RVSGESPGGLTILNLDGPLYLGGLPEDLKLPPL-PVTPGFRGCIRNLKVNG 131
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2312-2469 |
2.16e-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: 124.45 E-value: 2.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2312 VVQFDGDGYAAVSRPtRWNPNASTVTFKFRTFSTSAVLMYLATKDMKDFLSCELSEGRVKVSYDLGSGTGSALSHKRHND 2391
Cdd:cd00110 1 GVSFSGSSYVRLPTL-PAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLND 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2196706209 2392 GRWKSLTMTRSKKKGTLTIlDidtneeEKLFIDSQGGATGLNLKEDERIYFGGLPTIGNYRPEVTQRRYSGCMKDIEV 2469
Cdd:cd00110 80 GQWHSVSVERNGRSVTLSV-D------GERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKV 150
|
|
| LamG |
smart00282 |
Laminin G domain; |
2974-3101 |
7.39e-32 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 122.45 E-value: 7.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2974 TVALEFRTSTATGVLLGV-SGQTMDGLGIELINGKLLFHADNGVGRVTATSQGAGLCDGQWHSVTAHKLKHRLELIVDGQ 3052
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAgSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLNDGQWHRVAVERNGRSVTLSVDGG 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2196706209 3053 KSEAASPDASSASADTNDPVFVGGYPEGLKQFGLTTSAPFKGCMRNIKL 3101
Cdd:smart00282 81 NRVSGESPGGLTILNLDGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKV 129
|
|
| LamG |
smart00282 |
Laminin G domain; |
2335-2471 |
5.88e-31 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 119.75 E-value: 5.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2335 TVTFKFRTFSTSAVLMYLATKDMKDFLSCELSEGRVKVSYDLGSGTGSALSHKRH-NDGRWKSLTMTRSKKKGTLTIldi 2413
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPlNDGQWHRVAVERNGRSVTLSV--- 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2196706209 2414 dtNEEEKLFIDSQGGATGLNLkeDERIYFGGLPTIGNYRPEVTQRRYSGCMKDIEVSR 2471
Cdd:smart00282 78 --DGGNRVSGESPGGLTILNL--DGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNG 131
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2340-2475 |
7.98e-31 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 119.34 E-value: 7.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2340 FRTFSTSAVLMYLATKDMKDFLSCELSEGRVKVSYDLGSGTGSALSHKRHNDGRWKSLTMTRSKKKGTLTIldidtNEEE 2419
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSV-----DGEA 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2196706209 2420 KLFIDSQGGATGlNLKEDERIYFGGLPTIGNY-RPEVTQRRYSGCMKDIEVSRTPYN 2475
Cdd:pfam00054 76 RPTGESPLGATT-DLDVDGPLYVGGLPSLGVKkRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
567-701 |
5.25e-30 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 116.99 E-value: 5.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 567 YWNAPPSYLGNKILAYGGYLTYTISC-TRDELQEIHQGFNVIIEGGGLRLTDRRSEAVPALGLVGvVRRKVPLRAENFRH 645
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYePLPGGGSLNSEPDVILEGNGLRLSYSSPDQPPPDPGQE-QTYSVRLHEENWRD 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2196706209 646 FDSnAAVSKSDIISVLLKVTHLRVRAAHCQLH---SLSSVSMEVASaDSRSGVQARAVE 701
Cdd:pfam00052 80 SDG-APVSREDFMMVLANLTAILIRATYSTGSgqvSLSNVSLDSAV-PGGSGPPASWVE 136
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2979-3101 |
2.23e-28 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 112.13 E-value: 2.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2979 FRTSTATGVLLGVSGQTMDGLGIELINGKLLFHADNGVGRVTATSQGAGLCDGQWHSVTAHKLKHRLELIVDGQKSEAAS 3058
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDFLALELVNGRLVLRYDLGSGPESLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2196706209 3059 PDASSASADTNDPVFVGGYPEGLKQFGLTTSAPFKGCMRNIKL 3101
Cdd:pfam02210 81 PPGESLLLNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRV 123
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2146-2286 |
1.44e-27 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 110.10 E-value: 1.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2146 VKTLAADNLLFYLGSAKFVDFLAIEMRKGK*NFLWDVGSGVGRVEYPDlTINDGNWHRIEASRVGLNGSVSVrplegpkA 2225
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGD-KLNDGKWHSVELERNGRSGTLSV-------D 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2196706209 2226 GIAPTwqSAKSPESYTVlDVDQNAYLFVGGM-LGSVKKADAVKTITFSGCMGETYLDSKPIG 2286
Cdd:pfam00054 73 GEARP--TGESPLGATT-DLDVDGPLYVGGLpSLGVKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| LamG |
smart00282 |
Laminin G domain; |
2141-2283 |
3.39e-27 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 108.97 E-value: 3.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2141 TIVLNVKTLAADNLLFYLGSAKFVDFLAIEMRKGK*NFLWDVGSGVGRVEYPDLTINDGNWHRIEASRVGLNGSVSVRPL 2220
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLNDGQWHRVAVERNGRSVTLSVDGG 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2196706209 2221 EgpkagiaptWQSAKSPESYTVLDVDQNayLFVGGMLGSVKKADAVKTITFSGCMGETYLDSK 2283
Cdd:smart00282 81 N---------RVSGESPGGLTILNLDGP--LYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| LamB |
smart00281 |
Laminin B domain; |
564-688 |
1.03e-25 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 104.65 E-value: 1.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 564 PPYYWNAPPSYLGNKILAYGGYLTYTISCTRDELQEIHQGFNVIIEGGGLRLTdRRSEAVPALGlvGVVRRKVPLRAENF 643
Cdd:smart00281 3 EPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRRGGTHVSAPDVILEGNGLRIS-HPAEGPPLPD--ELTTVEVRFREENW 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2196706209 644 RHFDSNaAVSKSDIISVLLKVTHLRVRA---AHCQLHSLSSVSMEVAS 688
Cdd:smart00281 80 QYYGGR-PVTREDLMMVLANLTAILIRAtysQQMAGSRLSDVSLEVAV 126
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2122-2281 |
1.37e-24 |
|
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: 102.11 E-value: 1.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2122 SGGDCIRtYRPDIKKGRYNTIVLNVKTLAADNLLFYLGSAKFVDFLAIEMRKGK*NFLWDVGSGVGRVEYPDlTINDGNW 2201
Cdd:cd00110 5 SGSSYVR-LPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKT-PLNDGQW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2202 HRIEASRVGLNGSVSVRplegpkagiapTWQSAKSPESYTVLDVDQNAYLFVGGMLGSVKKADAVKTITFSGCMGETYLD 2281
Cdd:cd00110 83 HSVSVERNGRSVTLSVD-----------GERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2496-2670 |
2.89e-23 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 98.26 E-value: 2.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2496 TVSFSRPGYVELNPMVLDI-SSEITLSFSTKKENGIILYGRGglttlthssqsiqnrnlgrkrrQTGEPYVSVQLIKGSL 2574
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRtRLSISFSFRTTSPNGLLLYAGS----------------------QNGGDFLALELEDGRL 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2575 EVLVFSGSKNPRraIRKPdeVILHDGLEHSLRIRRhSGGSFSVQVDEEDRIEQALPNDQPIII--QRLFVGGIPADMAGG 2652
Cdd:cd00110 59 VLRYDLGSGSLV--LSSK--TPLNDGQWHSVSVER-NGRSVTLSVDGERVVESGSPGGSALLNldGPLYLGGLPEDLKSP 133
|
170
....*....|....*...
gi 2196706209 2653 LQRPGRPFEGCIWNLLIN 2670
Cdd:cd00110 134 GLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
2517-2670 |
3.86e-18 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 83.16 E-value: 3.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2517 EITLSFSTKKENGIILYGRGGLTTlthssqsiqnrnlgrkrrqtgePYVSVQLIKGSLEVLVFSGSknpRRAIRKPDEVI 2596
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGG----------------------DYLALELRDGRLVLRYDLGS---GPARLTSDPTP 55
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2196706209 2597 LHDGLEHSLRIRRhSGGSFSVQVDEEDRIEQALPNDQPIII--QRLFVGGIPADMAGGLQRPGRPFEGCIWNLLIN 2670
Cdd:smart00282 56 LNDGQWHRVAVER-NGRSVTLSVDGGNRVSGESPGGLTILNldGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVN 130
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2522-2675 |
2.27e-15 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 75.05 E-value: 2.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2522 FSTKKENGIILYGRgglttlthssqsiqnrnlgrkrRQTGEPYVSVQLIKGSLEVLVFSGSKnpRRAIRKPDEviLHDGL 2601
Cdd:pfam00054 1 FRTTEPSGLLLYNG----------------------TQTERDFLALELRDGRLEVSYDLGSG--AAVVRSGDK--LNDGK 54
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2196706209 2602 EHSLRIRRhSGGSFSVQVDEEDR--IEQALPNDQPIIIQR-LFVGGIPADMAGGLQRP-GRPFEGCIWNLLINTIPMD 2675
Cdd:pfam00054 55 WHSVELER-NGRSGTLSVDGEARptGESPLGATTDLDVDGpLYVGGLPSLGVKKRRLAiSPSFDGCIRDVIVNGKPLD 131
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1607-2121 |
3.54e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 72.79 E-value: 3.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1607 ADSNLGSLVTEMDELLSRANKVSADGEQTDSDAERSHKRAQDLEQFVKNtllaaeaLRDKARELNATLgrrdDGVEKSVN 1686
Cdd:PRK03918 163 AYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINE-------ISSELPELREEL----EKLEKEVK 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1687 EMqDEIKAMMNELRSRQLThphthtVQEELRAAQDLLLKVQRGFAAPHRVSEELQQEV--SSKLRDHDDKLQGAQELLEE 1764
Cdd:PRK03918 232 EL-EELKEEIEELEKELES------LEGSKRKLEEKIRELEERIEELKKEIEELEEKVkeLKELKEKAEEYIKLSEFYEE 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1765 AQNNIGNARTLNSDNLRRLEEVQRKRNESSKKKKETEGILEDGEKILNEANALS------DDINRGTEELEEMKRDLGP- 1837
Cdd:PRK03918 305 YLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEerhelyEEAKAKKEELERLKKRLTGl 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1838 ----LHDQLDYRVSRLAQVVED-DKLKDLVLRAENHAAQLNDSATILD--RSSWPA----------KNLSFNATAAFNAY 1900
Cdd:PRK03918 385 tpekLEKELEELEKAKEEIEEEiSKITARIGELKKEIKELKKAIEELKkaKGKCPVcgrelteehrKELLEEYTAELKRI 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1901 SNIKNYIDEadkaakQAKATATEAVQLatgpRGALKDEAKISLQKSqrLWNEAKNLENvvKDNGDNLGVLQQRLKSADaK 1980
Cdd:PRK03918 465 EKELKEIEE------KERKLRKELREL----EKVLKKESELIKLKE--LAEQLKELEE--KLKKYNLEELEKKAEEYE-K 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1981 NKELLKGLDENLAVLraipNDTAAKLMATKQKASKANDTAIEVLARLKDMNQNLmgLNRNFSTLKDDINKannlIQDPEK 2060
Cdd:PRK03918 530 LKEKLIKLKGEIKSL----KKELEKLEELKKKLAELEKKLDELEEELAELLKEL--EELGFESVEELEER----LKELEP 599
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2196706209 2061 ntiIHAAGAKVKDLEDEAERLLEKLKPIRELQDNLRKNISQIKELINQARKQANSIKVSVS 2121
Cdd:PRK03918 600 ---FYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYS 657
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
945-989 |
4.68e-12 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 62.71 E-value: 4.68e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2196706209 945 CHCNSFGSKSFDC-SESGQCRCQPGVTGQKCDRCSHGHFNFQEGGC 989
Cdd:smart00180 1 CDCDPGGSASGTCdPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1391-1437 |
6.56e-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: 62.37 E-value: 6.56e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1391 CECNGH---SVSCDPDTGVCQnCQHNTEGEKCERCSAGFYGVVRGSPDDC 1437
Cdd:pfam00053 1 CDCNPHgslSDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
944-988 |
1.82e-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: 1.82e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2196706209 944 PCHCNSFGSKSFDC-SESGQCRCQPGVTGQKCDRCSHGHFNFQEGG 988
Cdd:cd00055 1 PCDCNGHGSLSGQCdPGTGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1084-1141 |
2.06e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 61.22 E-value: 2.06e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2196706209 1084 CDCSLSGSNAETCDPEsgvcacaerTGQCSCRMNVEGLRCEMCKFGTFGLSERNPLGC 1141
Cdd:pfam00053 1 CDCNPHGSLSDTCDPE---------TGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
736-784 |
3.79e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 60.45 E-value: 3.79e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2196706209 736 CRCHGHAS---RCDENTGHCLgCEHNTMGPHCDLCSPGYYGDATRGtsHDCR 784
Cdd:cd00055 2 CDCNGHGSlsgQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQG--GGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
897-942 |
8.61e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 59.25 E-value: 8.61e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2196706209 897 CECNSNGSVSEVCNKESGQCQCLQRVLGRACDQCSPGTHMQAGSGC 942
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
945-992 |
1.03e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 58.90 E-value: 1.03e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2196706209 945 CHCNSFGSKSFDC-SESGQCRCQPGVTGQKCDRCSHGHFNFQEGGCTPC 992
Cdd:pfam00053 1 CDCNPHGSLSDTCdPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
736-776 |
1.57e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 58.52 E-value: 1.57e-10
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2196706209 736 CRCHGHAS---RCDENTGHCLgCEHNTMGPHCDLCSPGYYGDAT 776
Cdd:pfam00053 1 CDCNPHGSlsdTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPS 43
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1390-1438 |
1.69e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 58.52 E-value: 1.69e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2196706209 1390 RCECNGH---SVSCDPDTGVCQnCQHNTEGEKCERCSAGFYGvVRGSPDDCK 1438
Cdd:cd00055 1 PCDCNGHgslSGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYG-LPSQGGGCQ 50
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1750-2132 |
1.92e-10 |
|
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: 67.02 E-value: 1.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1750 DHDDKLQGAQELLEEAQNNIGNARTLNSDNLRRLEEVQRKRNES------SKKKKETEGILedgekILNEANALSDDINR 1823
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAeryqalLKEKREYEGYE-----LLKEKEALERQKEA 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1824 GTEELEEMKRDLGPLHDQLDYRVSRLAQVVEDdkLKDLVLR----AENHAAQLNdsatildrsswpAKNLSFNATAAfNA 1899
Cdd:TIGR02169 242 IERQLASLEEELEKLTEEISELEKRLEEIEQL--LEELNKKikdlGEEEQLRVK------------EKIGELEAEIA-SL 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1900 YSNIKNYIDEadkaakqaKATATEAVQLATGPRGALKDEAKiSLQKSQRLWN-EAKNLENVVKDNGDNLGVLQQRLKSAD 1978
Cdd:TIGR02169 307 ERSIAEKERE--------LEDAEERLAKLEAEIDKLLAEIE-ELEREIEEERkRRDKLTEEYAELKEELEDLRAELEEVD 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1979 AKNKELlkgLDENLAVLRAIpNDTAAKLMATKQKASKANDTAIEVLARLKDMNQNLMGlnrnfstLKDDINKannLIQDP 2058
Cdd:TIGR02169 378 KEFAET---RDELKDYREKL-EKLKREINELKRELDRLQEELQRLSEELADLNAAIAG-------IEAKINE---LEEEK 443
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2196706209 2059 EkntiihAAGAKVKDLEDEAERLLEKLKPIRELQDNLRKNISQIKELINQARKQANSIKVSVSSGGDCIRTYRP 2132
Cdd:TIGR02169 444 E------DKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRA 511
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
991-1036 |
2.34e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 58.13 E-value: 2.34e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2196706209 991 PCECSHVG---NNCDPGTGRCLCPLNTVGDRCEKCAPNHWGHD-IATGCK 1036
Cdd:cd00055 1 PCDCNGHGslsGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPsQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
843-895 |
3.35e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 57.75 E-value: 3.35e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2196706209 843 PCSCSGNLDLSvaRSCDPLTGAClHCRRGYAGPNCETCADGYYGDAVGAKNCQ 895
Cdd:cd00055 1 PCDCNGHGSLS--GQCDPGTGQC-ECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
897-945 |
4.61e-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: 57.36 E-value: 4.61e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2196706209 897 CECNSNGSVSEVCNKESGQCQCLQRVLGRACDQCSPGTHMQAGSGCVPC 945
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
992-1035 |
8.05e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 56.59 E-value: 8.05e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2196706209 992 CECSHVG---NNCDPGTGRCLCPLNTVGDRCEKCAPNHWGHDIATGC 1035
Cdd:pfam00053 1 CDCNPHGslsDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQ 47
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
897-943 |
9.94e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 56.21 E-value: 9.94e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2196706209 897 CECNSNGSVSEVCNKESGQCQCLQRVLGRACDQCSPGTHMQA--GSGCV 943
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPsqGGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
992-1035 |
1.18e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.17 E-value: 1.18e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2196706209 992 CECS---HVGNNCDPGTGRCLCPLNTVGDRCEKCAPNHWGhDIATGC 1035
Cdd:smart00180 1 CDCDpggSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYG-DGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
399-456 |
2.23e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 55.44 E-value: 2.23e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2196706209 399 CACDSRGSVSTVCVPddhqategqSAGWCHCKQGYAGEKCDRCAFGYRGFPECRRCNC 456
Cdd:pfam00053 1 CDCNPHGSLSDTCDP---------ETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1498-1533 |
2.79e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 55.05 E-value: 2.79e-09
10 20 30
....*....|....*....|....*....|....*.
gi 2196706209 1498 CECDLVGALPVPCDTHTGACRCRPGATGLKCDRCME 1533
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKP 36
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1038-1086 |
5.22e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 54.28 E-value: 5.22e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2196706209 1038 CGCHVTGAVTQQCNVNTGCCFCRDEFKGEKCNECKLGYRNFPHCVSCDC 1086
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1498-1535 |
7.53e-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: 7.53e-09
10 20 30
....*....|....*....|....*....|....*...
gi 2196706209 1498 CECDLVGALPVPCDTHTGACRCRPGATGLKCDRCMEKH 1535
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGY 39
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1391-1437 |
7.75e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 53.85 E-value: 7.75e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1391 CECNG---HSVSCDPDTGVCQnCQHNTEGEKCERCSAGFYGVvrgSPDDC 1437
Cdd:smart00180 1 CDCDPggsASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD---GPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1498-1535 |
1.03e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 53.47 E-value: 1.03e-08
10 20 30
....*....|....*....|....*....|....*...
gi 2196706209 1498 CECDLVGALPVPCDTHTGACRCRPGATGLKCDRCMEKH 1535
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGY 38
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1084-1141 |
1.06e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 53.47 E-value: 1.06e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2196706209 1084 CDCSLSGSNAETCDPEsgvcacaerTGQCSCRMNVEGLRCEMCKFGTFGlseRNPLGC 1141
Cdd:smart00180 1 CDCDPGGSASGTCDPD---------TGQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1654-2112 |
1.11e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.94 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1654 KNTLLAA------EALRDKARELNATLGRRDDGVEKSVNEMQDEIKAMMNELRS-RQLTHpHTHTVQEELRAAQDLLLKV 1726
Cdd:COG4717 36 KSTLLAFiramllERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEyAELQE-ELEELEEELEELEAELEEL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1727 QRGFAaphRVSEELQ-QEVSSKLRDHDDKLQGAQELLEEAQNNIGNARTLNSDNLRRLEEVQRKRNE-SSKKKKETEGIL 1804
Cdd:COG4717 115 REELE---KLEKLLQlLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEElEELLEQLSLATE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1805 EDGEKILNEANALSDDINRGTEELEEMKRDLGPLHDQLDyrvsRLAQVVEDDKLKDLVLRAENHAAQLNDSATILDRSSW 1884
Cdd:COG4717 192 EELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE----QLENELEAAALEERLKEARLLLLIAAALLALLGLGGS 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1885 PAKNLSFNATAAFNAYSNIKNYIDEADKAAKQAKATATEAVQLATgpRGALKDEAKISLQKSQRLWNEAKNLEnvVKDNG 1964
Cdd:COG4717 268 LLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPA--LEELEEEELEELLAALGLPPDLSPEE--LLELL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1965 DNLGVLQQRLKSADAKNKELLkgLDENLAVLRAIPNDTAAKLMATKQKASKANDTAIEVLARLKDMNQNLMGLNRNFSTL 2044
Cdd:COG4717 344 DRIEELQELLREAEELEEELQ--LEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEEL 421
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2196706209 2045 KDDINKAnnliqdpekntiihaagakvkDLEDEAERLLEKLKPIRELQDNLRKNISQIKELINQARKQ 2112
Cdd:COG4717 422 LEALDEE---------------------ELEEELEELEEELEELEEELEELREELAELEAELEQLEED 468
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1083-1141 |
1.16e-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: 53.13 E-value: 1.16e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2196706209 1083 SCDCSLSGSNAETCDPEsgvcacaerTGQCSCRMNVEGLRCEMCKFGTFGLSERnPLGC 1141
Cdd:cd00055 1 PCDCNGHGSLSGQCDPG---------TGQCECKPNTTGRRCDRCAPGYYGLPSQ-GGGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
398-450 |
1.40e-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: 53.13 E-value: 1.40e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2196706209 398 PCACDSRGSVSTVCVPDDhqateGQsagwCHCKQGYAGEKCDRCAFGYRGFPE 450
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGT-----GQ----CECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
454-500 |
1.85e-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: 1.85e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2196706209 454 CNCSAEGSVNT--DPCQLPCVCKENVEGESCERCKEGYYNLHGDRSSGC 500
Cdd:pfam00053 1 CDCNPHGSLSDtcDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
736-778 |
2.32e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 52.31 E-value: 2.32e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2196706209 736 CRCH--GHASR-CDENTGHCLgCEHNTMGPHCDLCSPGYYGDATRG 778
Cdd:smart00180 1 CDCDpgGSASGtCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
844-887 |
3.61e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 51.93 E-value: 3.61e-08
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2196706209 844 CSCsgNLDLSVARSCDPLTGAClHCRRGYAGPNCETCADGYYGD 887
Cdd:smart00180 1 CDC--DPGGSASGTCDPDTGQC-ECKPNVTGRRCDRCAPGYYGD 41
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
844-890 |
7.13e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 51.20 E-value: 7.13e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2196706209 844 CSCSGNLDLSvaRSCDPLTGAClHCRRGYAGPNCETCADGYYGDAVG 890
Cdd:pfam00053 1 CDCNPHGSLS--DTCDPETGQC-LCKPGVTGRHCDRCKPGYYGLPSD 44
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
399-451 |
9.70e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 50.39 E-value: 9.70e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2196706209 399 CACDSRGSVSTVCVPDDhqateGQsagwCHCKQGYAGEKCDRCAFGYRG--FPEC 451
Cdd:smart00180 1 CDCDPGGSASGTCDPDT-----GQ----CECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1582-1837 |
2.85e-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: 56.60 E-value: 2.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1582 RVENMTDELKHMLSPHRAPERLLQLADSNLGSLVTEMDELLSRANKVSADGEQTDSDAERSHKRAQDLEQFVKNTLLAAE 1661
Cdd:TIGR02168 727 QISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALD 806
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1662 ALRDKARELNATLGRRDDGVEKSVNEMqDEIKAMMNELRSR---------QLTHPHTH--TVQEELRAAQDLLLKVQRGF 1730
Cdd:TIGR02168 807 ELRAELTLLNEEAANLRERLESLERRI-AATERRLEDLEEQieelsedieSLAAEIEEleELIEELESELEALLNERASL 885
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1731 AAPHRVSEELQQEVSSKLRDHDDKLQGAQELLEEAQNNIGNARTlnsdnlrRLEEVQRKRNE-----SSKKKKETEGILE 1805
Cdd:TIGR02168 886 EEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLEL-------RLEGLEVRIDNlqerlSEEYSLTLEEAEA 958
|
250 260 270
....*....|....*....|....*....|..
gi 2196706209 1806 DGEKILNEANALSDDINRGTEELEEmkrdLGP 1837
Cdd:TIGR02168 959 LENKIEDDEEEARRRLKRLENKIKE----LGP 986
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
454-495 |
3.30e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 49.23 E-value: 3.30e-07
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2196706209 454 CNCSAEGSVNT--DPCQLPCVCKENVEGESCERCKEGYYNLHGD 495
Cdd:smart00180 1 CDCDPGGSASGtcDPDTGQCECKPNVTGRRCDRCAPGYYGDGPP 44
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
453-501 |
3.54e-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: 3.54e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2196706209 453 RCNCSAEGSVNT--DPCQLPCVCKENVEGESCERCKEGYYNLhGDRSSGCE 501
Cdd:cd00055 1 PCDCNGHGSLSGqcDPGTGQCECKPNTTGRRCDRCAPGYYGL-PSQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1037-1079 |
5.89e-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: 48.50 E-value: 5.89e-07
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2196706209 1037 ACGCHVTGAVTQQCNVNTGCCFCRDEFKGEKCNECKLGYRNFP 1079
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1038-1081 |
8.80e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 47.69 E-value: 8.80e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2196706209 1038 CGCHVTGAVTQQCNVNTGCCFCRDEFKGEKCNECKLGY--RNFPHC 1081
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYygDGPPGC 46
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1978-2122 |
2.02e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 52.61 E-value: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1978 DAKNKELlKGLDENLAVLRAIPNDTAAKLMATKQKASKAN---DTAIEVLARLKDMNQNLMGLNRNFSTLKDDINKANNL 2054
Cdd:COG1340 46 DELNAQV-KELREEAQELREKRDELNEKVKELKEERDELNeklNELREELDELRKELAELNKAGGSIDKLRKEIERLEWR 124
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2196706209 2055 IQ----DPEK-NTIIhaagAKVKDLE---DEAERLLEKLKPIRELQ---DNLRKNISQIKELINQARKQANSIKVSVSS 2122
Cdd:COG1340 125 QQtevlSPEEeKELV----EKIKELEkelEKAKKALEKNEKLKELRaelKELRKEAEEIHKKIKELAEEAQELHEEMIE 199
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1604-1874 |
3.64e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.02 E-value: 3.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1604 LQLADSNLgsLVTEMDELLSRANKVSADGEQTDSDAERSHKRAQDLEQfvkntllAAEALRDKARELNATLGRRDDGVEK 1683
Cdd:COG1196 222 LKELEAEL--LLLKLRELEAELEELEAELEELEAELEELEAELAELEA-------ELEELRLELEELELELEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1684 SVNEMQDEIKAM-MNELRSRQLThphthtvQEELRAAQDLLLKVQRGFAAPHRVSE------ELQQEVSSKLRDHDDKLQ 1756
Cdd:COG1196 293 LLAELARLEQDIaRLEERRRELE-------ERLEELEEELAELEEELEELEEELEEleeeleEAEEELEEAEAELAEAEE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1757 GAQELLEEAQNNIGNARTLNSDNLRRLEEVQRKRNESSKKKKETEGILEDGEKILNEANALSDDINRGTEELEEMKRDLg 1836
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL- 444
|
250 260 270
....*....|....*....|....*....|....*...
gi 2196706209 1837 pLHDQLDYRVSRLAQVVEDDKLKDLVLRAENHAAQLND 1874
Cdd:COG1196 445 -EEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
272-319 |
7.93e-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: 45.42 E-value: 7.93e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2196706209 272 CICYGHAkACPLNPNTKKLSCECEHNTCGESCDRCCPGYNQKPWMAGT 319
Cdd:cd00055 2 CDCNGHG-SLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1612-1869 |
8.97e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.60 E-value: 8.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1612 GSLVTEMD--ELLSR----ANKVSADGEQTDSDAERSHKRAQDLEQFVKN--TLLAAEALRDKARELNATLGRRD----- 1678
Cdd:PRK03918 442 GRELTEEHrkELLEEytaeLKRIEKELKEIEEKERKLRKELRELEKVLKKesELIKLKELAEQLKELEEKLKKYNleele 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1679 ------DGVEKSVNEMQDEIKAMMNELRSRQLTHPHTHTVQEELRAAQDLLLKVQR-----GFAAPHRVSEELQQ----- 1742
Cdd:PRK03918 522 kkaeeyEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKeleelGFESVEELEERLKElepfy 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1743 -------EVSSKLRDHDDKLQGAQELLEEAQNNIgnARTLNS--------DNLRRL---EEVQRKRNESSKKKKETEGI- 1803
Cdd:PRK03918 602 neylelkDAEKELEREEKELKKLEEELDKAFEEL--AETEKRleelrkelEELEKKyseEEYEELREEYLELSRELAGLr 679
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2196706209 1804 --LEDGEKILNEANALSDDINRGTEELEEMKRDLGPLHDQLDyRVSRLAQvveddKLKDLVLRAENHA 1869
Cdd:PRK03918 680 aeLEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE-RVEELRE-----KVKKYKALLKERA 741
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1620-1956 |
1.64e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 47.51 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1620 ELLSRANKVSADgeQTDSDAER--SHKRAQD---LEQFVKNTL-----LAAEALRDKAReLNATLGRRDDGVEKSVNEMQ 1689
Cdd:NF041483 75 EQLLRNAQIQAD--QLRADAERelRDARAQTqriLQEHAEHQArlqaeLHTEAVQRRQQ-LDQELAERRQTVESHVNENV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1690 deikAMMNELRSRqlTHPHTHTVQEELRAAQDLLLKVQRgfAAPHRVSEELQQEVSSK------------LRDHDDklqg 1757
Cdd:NF041483 152 ----AWAEQLRAR--TESQARRLLDESRAEAEQALAAAR--AEAERLAEEARQRLGSEaesaraeaeailRRARKD---- 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1758 AQELLE----EAQNNIGNARTLNSDNLRRLEEVQRKRNESSK----KKKETEGILE----DGEKILNEA---------NA 1816
Cdd:NF041483 220 AERLLNaastQAQEATDHAEQLRSSTAAESDQARRQAAELSRaaeqRMQEAEEALRearaEAEKVVAEAkeaaakqlaSA 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1817 LSDDINRGTEELEEMKRDLGPLHDQLDYRVSRLAQVVED-----DKL------KDLVLRAENHAAQLNDSA----TILDR 1881
Cdd:NF041483 300 ESANEQRTRTAKEEIARLVGEATKEAEALKAEAEQALADaraeaEKLvaeaaeKARTVAAEDTAAQLAKAArtaeEVLTK 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1882 SSWPAKNLSfnaTAAFNAYSNIKNYIDeadkaaKQAKATATEAVQLATGPRGALKDEAK------ISLQ-KSQRLWNEAK 1954
Cdd:NF041483 380 ASEDAKATT---RAAAEEAERIRREAE------AEADRLRGEAADQAEQLKGAAKDDTKeyraktVELQeEARRLRGEAE 450
|
..
gi 2196706209 1955 NL 1956
Cdd:NF041483 451 QL 452
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1795-2113 |
2.39e-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: 46.97 E-value: 2.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1795 KKKKETEgiledgeKILNEANalsDDINRGTEELEEMKRDLGPLHDQldyrvSRLAQvveddKLKDlvLRAENHAAQLND 1874
Cdd:TIGR02168 172 ERRKETE-------RKLERTR---ENLDRLEDILNELERQLKSLERQ-----AEKAE-----RYKE--LKAELRELELAL 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1875 SATILD--RSSWPAKNLSFNATAA-FNAYSNIKNYIDEADKAAKQAKATATEAVQLATGPRGALKDE-AKISLQKsQRLW 1950
Cdd:TIGR02168 230 LVLRLEelREELEELQEELKEAEEeLEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEiSRLEQQK-QILR 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1951 NEAKNLENvvkdngdNLGVLQQRLKSADAKNKELLkgldENLAVLRAIPNDTAAKLMATKQKASKANDTAIEVLARLKDM 2030
Cdd:TIGR02168 309 ERLANLER-------QLEELEAQLEELESKLDELA----EELAELEEKLEELKEELESLEAELEELEAELEELESRLEEL 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2031 NQNLMGLNRNFSTLKDDINKANNLIQdpekntiihAAGAKVKDLEDEAERLL-EKLKPIRELQDNLRKNISQIKELINQA 2109
Cdd:TIGR02168 378 EEQLETLRSKVAQLELQIASLNNEIE---------RLEARLERLEDRRERLQqEIEELLKKLEEAELKELQAELEELEEE 448
|
....
gi 2196706209 2110 RKQA 2113
Cdd:TIGR02168 449 LEEL 452
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1598-2115 |
3.75e-04 |
|
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: 46.37 E-value: 3.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1598 RAPERLLQLADSNLGSLVTEMDELLSRANKVSAdgeqtdsdAERSHK----RAQDLEQ-FVKNTLLAAEALRDKARELNA 1672
Cdd:pfam12128 326 ALEDQHGAFLDADIETAAADQEQLPSWQSELEN--------LEERLKaltgKHQDVTAkYNRRRSKIKEQNNRDIAGIKD 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1673 TLGRRDDGVEKSVNEMQDEIKAMMNELRSrQLTHPHTHTVQEELRAAQDL-LLKVQrgFAAPHRVSEEL-QQEVSSKLRD 1750
Cdd:pfam12128 398 KLAKIREARDRQLAVAEDDLQALESELRE-QLEAGKLEFNEEEYRLKSRLgELKLR--LNQATATPELLlQLENFDERIE 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1751 H-DDKLQGAQELLEEAQNNIGNARTLNSDNLRRLEEVQRKRNESSKKKKETEGILEDGEKIL-----NEANALSDDINR- 1823
Cdd:pfam12128 475 RaREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLlhflrKEAPDWEQSIGKv 554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1824 -GTEELeeMKRDLGP-----------------LH-DQLDYRVS---------RLAQVVED-DKLKDLVLRAENHAAQLND 1874
Cdd:pfam12128 555 iSPELL--HRTDLDPevwdgsvggelnlygvkLDlKRIDVPEWaaseeelreRLDKAEEAlQSAREKQAAAEEQLVQANG 632
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1875 SatiLDRSSwpaKNLSFNATAAFNAYSNIKNYIDEADKAAKQAKATATEAVQLATGPRGALKDEAKIsLQKSQRLWNEAK 1954
Cdd:pfam12128 633 E---LEKAS---REETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQ-LDKKHQAWLEEQ 705
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1955 NlenvvkdnGDNLGVLQQRLksadAKNKELLKGLDENLAVLRAIpndtaaklMATKQKASKANDTAIEvlarlKDMNQNL 2034
Cdd:pfam12128 706 K--------EQKREARTEKQ----AYWQVVEGALDAQLALLKAA--------IAARRSGAKAELKALE-----TWYKRDL 760
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2035 MGLN---RNFSTLKDDINKANNLIQDPEKNtiihaaGAKVKDLED--------EAERLLEKLKPI----RELQDNLRKNI 2099
Cdd:pfam12128 761 ASLGvdpDVIAKLKREIRTLERKIERIAVR------RQEVLRYFDwyqetwlqRRPRLATQLSNIeraiSELQQQLARLI 834
|
570
....*....|....*.
gi 2196706209 2100 SQIKELINQARKQANS 2115
Cdd:pfam12128 835 ADTKLRRAKLEMERKA 850
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1439-1493 |
4.37e-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: 40.42 E-value: 4.37e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2196706209 1439 PCACplsNPENNFSPSCVTEgfsDYRCTaCPEGYIGKYCERCATGYHGDPRRAGG 1493
Cdd:cd00055 1 PCDC---NGHGSLSGQCDPG---TGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1738-2147 |
4.39e-04 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 46.36 E-value: 4.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1738 EELQQEVSSKLRDHDDKLQGAQELLEEAQNNIGNArtlnSDNLRRLEEVQRKRNESSKKKKETEGI-----LEDGEKILN 1812
Cdd:PTZ00440 1362 EQIKEEISNKRKEINKYLSNIKSNKEKCDLHVRNA----SRGKDKIDFLNKHEAIEPSNSKEVNIIkitdnINKCKQYSN 1437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1813 EANALSDDINRGTEELEEMKRDLGPLHDQldyrVSRLAQVVEDDKLKDlvlRAENHAAQLNDSATILDRSSwpaKNLSFN 1892
Cdd:PTZ00440 1438 EAMETENKADENNDSIIKYEKEITNILNN----SSILGKKTKLEKKKK---EATNIMDDINGEHSIIKTKL---TKSSEK 1507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1893 ataaFNAYSNIKNYIDEADKAAKQAKATATEAVQLATGP-RGALKDEAKISlQKSQRLWNEAKNLENVVKDNGDNLGVLQ 1971
Cdd:PTZ00440 1508 ----LNQLNEQPNIKREGDVLNNDKSTIAYETIQYNLGRvKHNLLNILNIK-DEIETILNKAQDLMRDISKISKIVENKN 1582
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1972 -QRLKSADAKNKELLkgldENLAVLRAIPNDTAAKLMATKQ---------KASKANdTAIEVLARLKDMNQN-------- 2033
Cdd:PTZ00440 1583 lENLNDKEADYVKYL----DNILKEKQLMEAEYKKLNEIYSdvdniekelKKHKKN-YEIGLLEKVIEINKNiklymdst 1657
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2034 ---LMGLNRNFSTLKD--DINKANnliqdPEKNTIIHAAgaKVKDLEDEAERLLEKL--KPIRELQDNLrkNISQIKELi 2106
Cdd:PTZ00440 1658 kesLNSLVNNFSSLFNnfYLNKYN-----INENLEKYKK--KLNEIYNEFMESYNIIqeKMKEVSNDDV--DYNEAKTL- 1727
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2196706209 2107 nqaRKQANSIKVSVSSGGDCIRTYRPDIKKGRYNTIVLNVK 2147
Cdd:PTZ00440 1728 ---REEAQKEEVNLNNKEEEAKKYLNDIKKQESFRFILYMK 1765
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
292-315 |
8.44e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 39.60 E-value: 8.44e-04
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1952-2117 |
1.13e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.44 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1952 EAKNLENVVKDNGDNLGVLqqRLKSADAKNKELLKGLDENLAVLRaipndtaaKLMATKQKASKANDTAIEVLARLKDMN 2031
Cdd:PRK04778 257 EIQDLKEQIDENLALLEEL--DLDEAEEKNEEIQERIDQLYDILE--------REVKARKYVEKNSDTLPDFLEHAKEQN 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2032 QNLMG----LNRNFS----------TLKDDINKANNLIQDPEKNTiihAAGAKV-KDLEDEAERLLEKLKPIRELQDNLR 2096
Cdd:PRK04778 327 KELKEeidrVKQSYTlneselesvrQLEKQLESLEKQYDEITERI---AEQEIAySELQEELEEILKQLEEIEKEQEKLS 403
|
170 180
....*....|....*....|.
gi 2196706209 2097 KNISQIKELINQARKQANSIK 2117
Cdd:PRK04778 404 EMLQGLRKDELEAREKLERYR 424
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1781-2179 |
1.42e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.74 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1781 RRLEEVQRKRNESSKKKKETEGI-----------LEDGEKILNEANALSDDINRGTEELEEMKRDLGPLHDQLDYRVSRL 1849
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILiaalseqlrkaLFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1850 AQVveDDKLKDLVLRAENHAAQLNdsatildrsswpaknlsfnataafnaysniknyideadkaakqakatateavqlat 1929
Cdd:COG4372 83 EEL--NEQLQAAQAELAQAQEELE-------------------------------------------------------- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1930 gprgALKDEAKISLQKSQRLWNEAKNLENVVKDNGDNLGVLQQRLKSADAKNKELLKGLDENLAVLraipndtaAKLMAT 2009
Cdd:COG4372 105 ----SLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEEL--------AALEQE 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2010 KQKASKANdtAIEVLARL-KDMNQNLMGLNRNFSTLKDDINKANNLIQDPE--KNTIIHAAGAKVKDLEDEAERLLEKLK 2086
Cdd:COG4372 173 LQALSEAE--AEQALDELlKEANRNAEKEEELAEAEKLIESLPRELAEELLeaKDSLEAKLGLALSALLDALELEEDKEE 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2087 PIRELQDNLRKN----ISQIKELINQARKQANSIKVSVSSGGDCIRTYRPDIKKGRYNTIVLNVKTLAADNLLFYLGSAK 2162
Cdd:COG4372 251 LLEEVILKEIEElelaILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLEL 330
|
410
....*....|....*..
gi 2196706209 2163 FVDFLAIEMRKGK*NFL 2179
Cdd:COG4372 331 ALAILLAELADLLQLLL 347
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
786-841 |
2.46e-03 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 38.10 E-value: 2.46e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2196706209 786 CACPLQEPSnnfSPTCHLGEdgeVVCDrCPDGYSGSLCDRCDNGYFGSPRDVGGLC 841
Cdd:pfam00053 1 CDCNPHGSL---SDTCDPET---GQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1601-1815 |
3.76e-03 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 41.66 E-value: 3.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1601 ERLLQLADsNLGSLVTEMDELLSrankvSADGEQTDSDAERSHKRAQDLEQFVKNTLLAAEALRDKARELNATLGRRDDG 1680
Cdd:cd00176 3 QQFLRDAD-ELEAWLSEKEELLS-----STDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1681 VEKSVNEMQ---DEIKAMMNElRSRQLThpHTHTVQEELRAAQDLL--LKVQRGFAAPHRVSEELqQEVSSKLRDHDD-- 1753
Cdd:cd00176 77 IQERLEELNqrwEELRELAEE-RRQRLE--EALDLQQFFRDADDLEqwLEEKEAALASEDLGKDL-ESVEELLKKHKEle 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2196706209 1754 -KLQGAQELLEEAqNNIGNArTLNSDNLRRLEEVQRKRNESSKKKKETEGILEDGEKILNEAN 1815
Cdd:cd00176 153 eELEAHEPRLKSL-NELAEE-LLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
786-834 |
7.89e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 36.52 E-value: 7.89e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2196706209 786 CACPlqePSNNFSPTCHLgEDGevVCdRCPDGYSGSLCDRCDNGYFGSP 834
Cdd:smart00180 1 CDCD---PGGSASGTCDP-DTG--QC-ECKPNVTGRRCDRCAPGYYGDG 42
|
|
| TNFRSF |
cd00185 |
Tumor necrosis factor receptor superfamily (TNFRSF); Members of TNFR superfamily (TNFRSF) ... |
764-845 |
8.02e-03 |
|
Tumor necrosis factor receptor superfamily (TNFRSF); Members of TNFR superfamily (TNFRSF) interactions with TNF superfamily (TNFSF) ligands (TNFL) control key cellular processes such as differentiation, proliferation, apoptosis, and cell growth. Dysregulation of these pathways has been shown to result in a wide range of pathological conditions, including autoimmune diseases, inflammation, cancer, and viral infection. There are 29 very diverse family members of TNFRSF reported in humans: 22 are type I transmembrane receptors (single pass with the N terminus on extracellular side of the cell membrane) and have a clear signal peptide; the remaining 7 members are either type III transmembrane receptors (single pass with the N terminus on extracellular side of the membrane but no signal sequence; TNFR13B, TNFR13C, TNFR17, and XEDAR), or attached to the membrane via a glycosylphosphatidylinositol (GPI) linker (TNFR10C), or secreted as soluble receptors (TNFR11B and TNFR6B). All TNFRs contain relatively short cysteine-rich domains (CRDs) in the ectodomain, and are involved in interaction with the TNF homology domain (THD) of their ligands. TNFRs often have multiple CRDs (between one and six), with the most frequent configurations of three or four copies; most CRDs possess three disulfide bridges, but could have between one and four. Localized or genome-wide duplication and evolution of the TNFRSF members appear to have paralleled the emergence of the adaptive immune system; teleosts (i.e. ray-finned, bony fish), which possess an immune system with B and T cells, possess primary and secondary lymphoid organs, and are capable of adaptive responses to pathogens also display several characteristics that are different from the mammalian immune system, making teleost TNFSF orthologs and paralogs of interest to better understand immune system evolution and the immunological pathways elicited to pathogens.
Pssm-ID: 276900 [Multi-domain] Cd Length: 87 Bit Score: 37.96 E-value: 8.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 764 CDLCSPGYY--GDATRGTSHDCRPCACPLQEPSNNFSPTCHLgedgevvCDRCPDGYSG---------SLCDRCDNGYFG 832
Cdd:cd00185 2 CQRCPPGEYlsSDCTATTDTVCSPCPPGTYSESWNSLSKCLP-------CTTCGGGNQVektpctatdNRCCTCKPGFYC 74
|
90
....*....|...
gi 2196706209 833 SPRDVGGLCRPCS 845
Cdd:cd00185 75 DEGTNVEECKPCT 87
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
22-270 |
6.33e-94 |
|
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: 304.28 E-value: 6.33e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 22 RGLFPAVLNLASMAEISANATCGENGAEMYCKLVEHVpgqpVRNPQCRVCNLRSerPYERHPIEFAIDGTN----RWWQS 97
Cdd:smart00136 5 RSCYPPFVNLAFGREVTATSTCGEPGPERYCKLVGHT----EQGKKCDYCDARN--PRRSHPAENLTDGNNpnnpTWWQS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 98 PSIKNGMdyHYVTITLDLQQVFQIAYVILKAAnSPRPGNWVLERSLDGETFTPWQYFAitdTECITRFNIIPRTGPPAYK 177
Cdd:smart00136 79 EPLSNGP--QNVNLTLDLGKEFHVTYVILKFC-SPRPSLWILERSDFGKTWQPWQYFS---SDCRRTFGRPPRGPITKGN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 178 hDDEVICTSFYSKIHPLENGEIHTSLINGRPSAEDP--SPTLLSFTSARYIRLRFLRIRTLNADLMTLAqndpqsvdPIV 255
Cdd:smart00136 153 -EDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDFdnSPVLQEWVTATNIRVRLTRLRTLGDELMDDR--------PEV 223
|
250
....*....|....*
gi 2196706209 256 TRRYYYSIKDISVGG 270
Cdd:smart00136 224 TRRYYYAISDIAVGG 238
|
|
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
24-270 |
4.66e-90 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 292.95 E-value: 4.66e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 24 LFPAVLNLASMAEISANATCGENGAEMYCKLVEHVPGQpvrnpQCRVCNLRseRPYERHPIEFAIDGTNR----WWQSPS 99
Cdd:pfam00055 1 CYPAFGNLAFGREVSATSTCGLNGPERYCILSGLEGGK-----KCFICDSR--DPHNSHPPSNLTDSNNGtnetWWQSET 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 100 IKngMDYHYVTITLDLQQVFQIAYVILKAAnSPRPGNWVLERSLD-GETFTPWQYFAitdTECITRFNIipRTGPPAYKH 178
Cdd:pfam00055 74 GV--IQYENVNLTLDLGKEFHFTYLILKFK-SPRPAAMVLERSTDfGKTWQPYQYFA---SDCRRTFGR--PSGPSRGIK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 179 DDEVICTSFYSKIHPLENGEIHTSLINGRPSAE--DPSPTLLSFTSARYIRLRFLRIRTLnadlmtlaqNDPQSVDPIVT 256
Cdd:pfam00055 146 DDEVICTSEYSDISPLTGGEVIFSTLEGRPSANifDYSPELQDWLTATNIRIRLLRLHTL---------GDELLDDPSVL 216
|
250
....*....|....
gi 2196706209 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 ... |
1569-1822 |
1.15e-49 |
|
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: 178.38 E-value: 1.15e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1569 LTLPLPPPYGALYRVENMTDELKHMLSPHRAPERLLQLADSNLGSLVTEMDELLSRANKVSADGEQTDSDAERSHKRAQD 1648
Cdd:pfam06008 7 LTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1649 LEQFVKNtllaaeaLRDKARELN---ATLGRRDDGV-EKSVNEMQDEIKAMMNELRSRQLTHPHThTVQEELRAAQDLLL 1724
Cdd:pfam06008 87 LAEAIKN-------LIDNIKEINekvATLGENDFALpSSDLSRMLAEAQRMLGEIRSRDFGTQLQ-NAEAELKAAQDLLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1725 KVQRGFAAPHRVSEELQQEVSSKLRDHDDKLQGAQELLEEAQNNIGNARTLNSDNLRRLEEVQRKRNESSKKKKETEGIL 1804
Cdd:pfam06008 159 RIQTWFQSPQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEETL 238
|
250
....*....|....*...
gi 2196706209 1805 EDGEKILNEANALSDDIN 1822
Cdd:pfam06008 239 KTARDSLDAANLLLQEID 256
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
1211-1349 |
1.16e-46 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 164.75 E-value: 1.16e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1211 YWKLPKQFRGSMITAYGGKLKYTVYYEARDETGHASYEPQVIIRGGATRDKVMIRHMVEPQIGQLTRHEIDMTEHEWKHH 1290
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGGGSLNSEPDVILEGNGLRLSYSSPDQPPPDPGQEQTYSVRLHEENWRDS 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2196706209 1291 DSKPMSREDFMDILFHIENVFIRASHGNVMRQSRISEISLEVAeegRPSVESERAHQIE 1349
Cdd:pfam00052 81 DGAPVSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSA---VPGGSGPPASWVE 136
|
|
| LamB |
smart00281 |
Laminin B domain; |
1206-1335 |
4.94e-43 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 153.96 E-value: 4.94e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1206 LEEPYYWKLPKQFRGSMITAYGGKLKYTVYYEARDEtGHASYEPQVIIRGGATRdkVMIRHMVEPQIGQLTRHEIDMTEH 1285
Cdd:smart00281 1 DNEPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRRG-GTHVSAPDVILEGNGLR--ISHPAEGPPLPDELTTVEVRFREE 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1286 EWKHHDSKPMSREDFMDILFHIENVFIRASHGNVMRQSRISEISLEVAEE 1335
Cdd:smart00281 78 NWQYYGGRPVTREDLMMVLANLTAILIRATYSQQMAGSRLSDVSLEVAVP 127
|
|
| Laminin_II |
pfam06009 |
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 ... |
2009-2145 |
4.04e-41 |
|
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: 149.17 E-value: 4.04e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2009 TKQKASKANDTAIEVLARLKDMNQNLMGLNRNFSTLKDDINKANNLIQDpeKNTIIHAAGAKVKDLEDEAERLLEKLKPI 2088
Cdd:pfam06009 1 SKELAREANETAKEVLEQLAPLSQNLENTSEKLSGINRSLEETNELVND--ANKALDDAGRSVKKLEELAPDLLDKLKPL 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2089 RELQDN---LRKNISQIKELINQARKQANSIKVSVSSGGDCIRTYRPDIKKGRYNTIVLN 2145
Cdd:pfam06009 79 KQLEVNsssLSDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTSL 138
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2952-3101 |
3.34e-36 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 135.62 E-value: 3.34e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2952 GSYFSGTGYAKAVSTYRVGNEVTVALEFRTSTATGVLLGVSGQTMDG-LGIELINGKLLFHADNGVGRVTATSQGAgLCD 3030
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDfLALELEDGRLVLRYDLGSGSLVLSSKTP-LND 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2196706209 3031 GQWHSVTAHKLKHRLELIVDGQKSEAASPDASSASADTNDPVFVGGYPEGLKQFGLTTSAPFKGCMRNIKL 3101
Cdd:cd00110 80 GQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKV 150
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2776-2926 |
5.75e-35 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 131.77 E-value: 5.75e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2776 FGLSRNSHMEFEFDDRKvKNSLIIEFELRTEADSGLVFYMARINHADFATVQVKEGMAHLSFDLGSGNTSVSVPRIINDG 2855
Cdd:cd00110 2 VSFSGSSYVRLPTLPAP-RTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2196706209 2856 HWHKIKVLRDKQRGILTVDGRYIKHTVSPKKADILDVVGKLYVGGLPLNYTTKRIgPVVYSINGCIRNFRM 2926
Cdd:cd00110 81 QWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGL-PVSPGFVGCIRDLKV 150
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2804-2932 |
2.76e-34 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 129.36 E-value: 2.76e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2804 RTEADSGLVFYMARINHADFATVQVKEGMAHLSFDLGSGNTSVSVPRIINDGHWHKIKVLRDKQRGILTVDGRYIKHTVS 2883
Cdd:pfam00054 2 RTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGES 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2884 PKKADI-LDVVGKLYVGGLPLNYTTKRIGPVVYSINGCIRNFRMTNGPQD 2932
Cdd:pfam00054 82 PLGATTdLDVDGPLYVGGLPSLGVKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| LamG |
smart00282 |
Laminin G domain; |
2799-2928 |
4.44e-33 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 125.91 E-value: 4.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2799 IEFELRTEADSGLVFYMARINHADFATVQVKEGMAHLSFDLGSGNTSVSV-PRIINDGHWHKIKVLRDKQRGILTVDGRY 2877
Cdd:smart00282 2 ISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSdPTPLNDGQWHRVAVERNGRSVTLSVDGGN 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2196706209 2878 IKHTVSPKKADILDVVGKLYVGGLPLNYTTKRIgPVVYSINGCIRNFRMTN 2928
Cdd:smart00282 82 RVSGESPGGLTILNLDGPLYLGGLPEDLKLPPL-PVTPGFRGCIRNLKVNG 131
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2312-2469 |
2.16e-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: 124.45 E-value: 2.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2312 VVQFDGDGYAAVSRPtRWNPNASTVTFKFRTFSTSAVLMYLATKDMKDFLSCELSEGRVKVSYDLGSGTGSALSHKRHND 2391
Cdd:cd00110 1 GVSFSGSSYVRLPTL-PAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLND 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2196706209 2392 GRWKSLTMTRSKKKGTLTIlDidtneeEKLFIDSQGGATGLNLKEDERIYFGGLPTIGNYRPEVTQRRYSGCMKDIEV 2469
Cdd:cd00110 80 GQWHSVSVERNGRSVTLSV-D------GERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKV 150
|
|
| LamG |
smart00282 |
Laminin G domain; |
2974-3101 |
7.39e-32 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 122.45 E-value: 7.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2974 TVALEFRTSTATGVLLGV-SGQTMDGLGIELINGKLLFHADNGVGRVTATSQGAGLCDGQWHSVTAHKLKHRLELIVDGQ 3052
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAgSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLNDGQWHRVAVERNGRSVTLSVDGG 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2196706209 3053 KSEAASPDASSASADTNDPVFVGGYPEGLKQFGLTTSAPFKGCMRNIKL 3101
Cdd:smart00282 81 NRVSGESPGGLTILNLDGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKV 129
|
|
| LamG |
smart00282 |
Laminin G domain; |
2335-2471 |
5.88e-31 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 119.75 E-value: 5.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2335 TVTFKFRTFSTSAVLMYLATKDMKDFLSCELSEGRVKVSYDLGSGTGSALSHKRH-NDGRWKSLTMTRSKKKGTLTIldi 2413
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPlNDGQWHRVAVERNGRSVTLSV--- 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2196706209 2414 dtNEEEKLFIDSQGGATGLNLkeDERIYFGGLPTIGNYRPEVTQRRYSGCMKDIEVSR 2471
Cdd:smart00282 78 --DGGNRVSGESPGGLTILNL--DGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNG 131
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2340-2475 |
7.98e-31 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 119.34 E-value: 7.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2340 FRTFSTSAVLMYLATKDMKDFLSCELSEGRVKVSYDLGSGTGSALSHKRHNDGRWKSLTMTRSKKKGTLTIldidtNEEE 2419
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSV-----DGEA 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2196706209 2420 KLFIDSQGGATGlNLKEDERIYFGGLPTIGNY-RPEVTQRRYSGCMKDIEVSRTPYN 2475
Cdd:pfam00054 76 RPTGESPLGATT-DLDVDGPLYVGGLPSLGVKkRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
567-701 |
5.25e-30 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 116.99 E-value: 5.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 567 YWNAPPSYLGNKILAYGGYLTYTISC-TRDELQEIHQGFNVIIEGGGLRLTDRRSEAVPALGLVGvVRRKVPLRAENFRH 645
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYePLPGGGSLNSEPDVILEGNGLRLSYSSPDQPPPDPGQE-QTYSVRLHEENWRD 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2196706209 646 FDSnAAVSKSDIISVLLKVTHLRVRAAHCQLH---SLSSVSMEVASaDSRSGVQARAVE 701
Cdd:pfam00052 80 SDG-APVSREDFMMVLANLTAILIRATYSTGSgqvSLSNVSLDSAV-PGGSGPPASWVE 136
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2979-3101 |
2.23e-28 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 112.13 E-value: 2.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2979 FRTSTATGVLLGVSGQTMDGLGIELINGKLLFHADNGVGRVTATSQGAGLCDGQWHSVTAHKLKHRLELIVDGQKSEAAS 3058
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDFLALELVNGRLVLRYDLGSGPESLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2196706209 3059 PDASSASADTNDPVFVGGYPEGLKQFGLTTSAPFKGCMRNIKL 3101
Cdd:pfam02210 81 PPGESLLLNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRV 123
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2146-2286 |
1.44e-27 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 110.10 E-value: 1.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2146 VKTLAADNLLFYLGSAKFVDFLAIEMRKGK*NFLWDVGSGVGRVEYPDlTINDGNWHRIEASRVGLNGSVSVrplegpkA 2225
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGD-KLNDGKWHSVELERNGRSGTLSV-------D 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2196706209 2226 GIAPTwqSAKSPESYTVlDVDQNAYLFVGGM-LGSVKKADAVKTITFSGCMGETYLDSKPIG 2286
Cdd:pfam00054 73 GEARP--TGESPLGATT-DLDVDGPLYVGGLpSLGVKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| LamG |
smart00282 |
Laminin G domain; |
2141-2283 |
3.39e-27 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 108.97 E-value: 3.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2141 TIVLNVKTLAADNLLFYLGSAKFVDFLAIEMRKGK*NFLWDVGSGVGRVEYPDLTINDGNWHRIEASRVGLNGSVSVRPL 2220
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLNDGQWHRVAVERNGRSVTLSVDGG 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2196706209 2221 EgpkagiaptWQSAKSPESYTVLDVDQNayLFVGGMLGSVKKADAVKTITFSGCMGETYLDSK 2283
Cdd:smart00282 81 N---------RVSGESPGGLTILNLDGP--LYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| LamB |
smart00281 |
Laminin B domain; |
564-688 |
1.03e-25 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 104.65 E-value: 1.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 564 PPYYWNAPPSYLGNKILAYGGYLTYTISCTRDELQEIHQGFNVIIEGGGLRLTdRRSEAVPALGlvGVVRRKVPLRAENF 643
Cdd:smart00281 3 EPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRRGGTHVSAPDVILEGNGLRIS-HPAEGPPLPD--ELTTVEVRFREENW 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2196706209 644 RHFDSNaAVSKSDIISVLLKVTHLRVRA---AHCQLHSLSSVSMEVAS 688
Cdd:smart00281 80 QYYGGR-PVTREDLMMVLANLTAILIRAtysQQMAGSRLSDVSLEVAV 126
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2803-2929 |
1.03e-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: 101.73 E-value: 1.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2803 LRTEADSGLVFYMARINHaDFATVQVKEGMAHLSFDLGSGNTSVSVPRI-INDGHWHKIKVLRDKQRGILTVDGRYIKHT 2881
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGS-DFLALELVNGRLVLRYDLGSGPESLLSSGKnLNDGQWHSVRVERNGNTLTLSVDGQTVVSS 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2196706209 2882 VSPKKADILDVVGKLYVGGLPLNYTTKRIgPVVYSINGCIRNFRMtNG 2929
Cdd:pfam02210 80 LPPGESLLLNLNGPLYLGGLPPLLLLPAL-PVRAGFVGCIRDVRV-NG 125
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2122-2281 |
1.37e-24 |
|
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: 102.11 E-value: 1.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2122 SGGDCIRtYRPDIKKGRYNTIVLNVKTLAADNLLFYLGSAKFVDFLAIEMRKGK*NFLWDVGSGVGRVEYPDlTINDGNW 2201
Cdd:cd00110 5 SGSSYVR-LPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKT-PLNDGQW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2202 HRIEASRVGLNGSVSVRplegpkagiapTWQSAKSPESYTVLDVDQNAYLFVGGMLGSVKKADAVKTITFSGCMGETYLD 2281
Cdd:cd00110 83 HSVSVERNGRSVTLSVD-----------GERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2340-2469 |
6.58e-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: 99.42 E-value: 6.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2340 FRTFSTSAVLMYLATKDmKDFLSCELSEGRVKVSYDLGSGTGSALSHKRH-NDGRWKSLTMTRSKKKGTLTILDIDTNEe 2418
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGG-SDFLALELVNGRLVLRYDLGSGPESLLSSGKNlNDGQWHSVRVERNGNTLTLSVDGQTVVS- 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2196706209 2419 eklfidSQGGATGLNLKEDERIYFGGLPTIGNYRPEVTQRRYSGCMKDIEV 2469
Cdd:pfam02210 79 ------SLPPGESLLLNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRV 123
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2496-2670 |
2.89e-23 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 98.26 E-value: 2.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2496 TVSFSRPGYVELNPMVLDI-SSEITLSFSTKKENGIILYGRGglttlthssqsiqnrnlgrkrrQTGEPYVSVQLIKGSL 2574
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRtRLSISFSFRTTSPNGLLLYAGS----------------------QNGGDFLALELEDGRL 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2575 EVLVFSGSKNPRraIRKPdeVILHDGLEHSLRIRRhSGGSFSVQVDEEDRIEQALPNDQPIII--QRLFVGGIPADMAGG 2652
Cdd:cd00110 59 VLRYDLGSGSLV--LSSK--TPLNDGQWHSVSVER-NGRSVTLSVDGERVVESGSPGGSALLNldGPLYLGGLPEDLKSP 133
|
170
....*....|....*...
gi 2196706209 2653 LQRPGRPFEGCIWNLLIN 2670
Cdd:cd00110 134 GLPVSPGFVGCIRDLKVN 151
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2979-3101 |
8.74e-21 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 90.45 E-value: 8.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2979 FRTSTATGVLLGVSGQT-MDGLGIELINGKLLFHADNGVGRVTATSqGAGLCDGQWHSVTAHKLKHRLELIVDG-QKSEA 3056
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTeRDFLALELRDGRLEVSYDLGSGAAVVRS-GDKLNDGKWHSVELERNGRSGTLSVDGeARPTG 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2196706209 3057 ASPDASSASADTNDPVFVGGYPE-GLKQFGLTTSAPFKGCMRNIKL 3101
Cdd:pfam00054 80 ESPLGATTDLDVDGPLYVGGLPSlGVKKRRLAISPSFDGCIRDVIV 125
|
|
| LamG |
smart00282 |
Laminin G domain; |
2517-2670 |
3.86e-18 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 83.16 E-value: 3.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2517 EITLSFSTKKENGIILYGRGGLTTlthssqsiqnrnlgrkrrqtgePYVSVQLIKGSLEVLVFSGSknpRRAIRKPDEVI 2596
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGG----------------------DYLALELRDGRLVLRYDLGS---GPARLTSDPTP 55
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2196706209 2597 LHDGLEHSLRIRRhSGGSFSVQVDEEDRIEQALPNDQPIII--QRLFVGGIPADMAGGLQRPGRPFEGCIWNLLIN 2670
Cdd:smart00282 56 LNDGQWHRVAVER-NGRSVTLSVDGGNRVSGESPGGLTILNldGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVN 130
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2146-2283 |
1.17e-17 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 81.70 E-value: 1.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2146 VKTLAADNLLFYLGSAKfVDFLAIEMRKGK*NFLWDVGSGVGRVEYPDLTINDGNWHRIEASRVGLNGSVSVrplegpka 2225
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGG-SDFLALELVNGRLVLRYDLGSGPESLLSSGKNLNDGQWHSVRVERNGNTLTLSV-------- 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2196706209 2226 giaPTWQSAKSPESYTVLDVDQNAYLFVGGMLGSVKKADAVKTITFSGCMGETYLDSK 2283
Cdd:pfam02210 72 ---DGQTVVSSLPPGESLLLNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2522-2675 |
2.27e-15 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 75.05 E-value: 2.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2522 FSTKKENGIILYGRgglttlthssqsiqnrnlgrkrRQTGEPYVSVQLIKGSLEVLVFSGSKnpRRAIRKPDEviLHDGL 2601
Cdd:pfam00054 1 FRTTEPSGLLLYNG----------------------TQTERDFLALELRDGRLEVSYDLGSG--AAVVRSGDK--LNDGK 54
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2196706209 2602 EHSLRIRRhSGGSFSVQVDEEDR--IEQALPNDQPIIIQR-LFVGGIPADMAGGLQRP-GRPFEGCIWNLLINTIPMD 2675
Cdd:pfam00054 55 WHSVELER-NGRSGTLSVDGEARptGESPLGATTDLDVDGpLYVGGLPSLGVKKRRLAiSPSFDGCIRDVIVNGKPLD 131
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2522-2670 |
8.27e-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: 67.83 E-value: 8.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2522 FSTKKENGIILYGRGGLTtlthssqsiqnrnlgrkrrqtgePYVSVQLIKGSLeVLVFSGSKNPRRAIRKPDEviLHDGL 2601
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGS-----------------------DFLALELVNGRL-VLRYDLGSGPESLLSSGKN--LNDGQ 54
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2196706209 2602 EHSLRIRRHsGGSFSVQVDEEDRIEQALPNDQPIII--QRLFVGGIPADMAGGLQRPGRPFEGCIWNLLIN 2670
Cdd:pfam02210 55 WHSVRVERN-GNTLTLSVDGQTVVSSLPPGESLLLNlnGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVN 124
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1607-2121 |
3.54e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 72.79 E-value: 3.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1607 ADSNLGSLVTEMDELLSRANKVSADGEQTDSDAERSHKRAQDLEQFVKNtllaaeaLRDKARELNATLgrrdDGVEKSVN 1686
Cdd:PRK03918 163 AYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINE-------ISSELPELREEL----EKLEKEVK 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1687 EMqDEIKAMMNELRSRQLThphthtVQEELRAAQDLLLKVQRGFAAPHRVSEELQQEV--SSKLRDHDDKLQGAQELLEE 1764
Cdd:PRK03918 232 EL-EELKEEIEELEKELES------LEGSKRKLEEKIRELEERIEELKKEIEELEEKVkeLKELKEKAEEYIKLSEFYEE 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1765 AQNNIGNARTLNSDNLRRLEEVQRKRNESSKKKKETEGILEDGEKILNEANALS------DDINRGTEELEEMKRDLGP- 1837
Cdd:PRK03918 305 YLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEerhelyEEAKAKKEELERLKKRLTGl 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1838 ----LHDQLDYRVSRLAQVVED-DKLKDLVLRAENHAAQLNDSATILD--RSSWPA----------KNLSFNATAAFNAY 1900
Cdd:PRK03918 385 tpekLEKELEELEKAKEEIEEEiSKITARIGELKKEIKELKKAIEELKkaKGKCPVcgrelteehrKELLEEYTAELKRI 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1901 SNIKNYIDEadkaakQAKATATEAVQLatgpRGALKDEAKISLQKSqrLWNEAKNLENvvKDNGDNLGVLQQRLKSADaK 1980
Cdd:PRK03918 465 EKELKEIEE------KERKLRKELREL----EKVLKKESELIKLKE--LAEQLKELEE--KLKKYNLEELEKKAEEYE-K 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1981 NKELLKGLDENLAVLraipNDTAAKLMATKQKASKANDTAIEVLARLKDMNQNLmgLNRNFSTLKDDINKannlIQDPEK 2060
Cdd:PRK03918 530 LKEKLIKLKGEIKSL----KKELEKLEELKKKLAELEKKLDELEEELAELLKEL--EELGFESVEELEER----LKELEP 599
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2196706209 2061 ntiIHAAGAKVKDLEDEAERLLEKLKPIRELQDNLRKNISQIKELINQARKQANSIKVSVS 2121
Cdd:PRK03918 600 ---FYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYS 657
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
945-989 |
4.68e-12 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 62.71 E-value: 4.68e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2196706209 945 CHCNSFGSKSFDC-SESGQCRCQPGVTGQKCDRCSHGHFNFQEGGC 989
Cdd:smart00180 1 CDCDPGGSASGTCdPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1391-1437 |
6.56e-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: 62.37 E-value: 6.56e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1391 CECNGH---SVSCDPDTGVCQnCQHNTEGEKCERCSAGFYGVVRGSPDDC 1437
Cdd:pfam00053 1 CDCNPHgslSDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
944-988 |
1.82e-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: 1.82e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2196706209 944 PCHCNSFGSKSFDC-SESGQCRCQPGVTGQKCDRCSHGHFNFQEGG 988
Cdd:cd00055 1 PCDCNGHGSLSGQCdPGTGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1084-1141 |
2.06e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 61.22 E-value: 2.06e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2196706209 1084 CDCSLSGSNAETCDPEsgvcacaerTGQCSCRMNVEGLRCEMCKFGTFGLSERNPLGC 1141
Cdd:pfam00053 1 CDCNPHGSLSDTCDPE---------TGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
736-784 |
3.79e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 60.45 E-value: 3.79e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2196706209 736 CRCHGHAS---RCDENTGHCLgCEHNTMGPHCDLCSPGYYGDATRGtsHDCR 784
Cdd:cd00055 2 CDCNGHGSlsgQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQG--GGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
897-942 |
8.61e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 59.25 E-value: 8.61e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2196706209 897 CECNSNGSVSEVCNKESGQCQCLQRVLGRACDQCSPGTHMQAGSGC 942
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
945-992 |
1.03e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 58.90 E-value: 1.03e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2196706209 945 CHCNSFGSKSFDC-SESGQCRCQPGVTGQKCDRCSHGHFNFQEGGCTPC 992
Cdd:pfam00053 1 CDCNPHGSLSDTCdPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
736-776 |
1.57e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 58.52 E-value: 1.57e-10
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2196706209 736 CRCHGHAS---RCDENTGHCLgCEHNTMGPHCDLCSPGYYGDAT 776
Cdd:pfam00053 1 CDCNPHGSlsdTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPS 43
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1390-1438 |
1.69e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 58.52 E-value: 1.69e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2196706209 1390 RCECNGH---SVSCDPDTGVCQnCQHNTEGEKCERCSAGFYGvVRGSPDDCK 1438
Cdd:cd00055 1 PCDCNGHgslSGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYG-LPSQGGGCQ 50
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1750-2132 |
1.92e-10 |
|
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: 67.02 E-value: 1.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1750 DHDDKLQGAQELLEEAQNNIGNARTLNSDNLRRLEEVQRKRNES------SKKKKETEGILedgekILNEANALSDDINR 1823
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAeryqalLKEKREYEGYE-----LLKEKEALERQKEA 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1824 GTEELEEMKRDLGPLHDQLDYRVSRLAQVVEDdkLKDLVLR----AENHAAQLNdsatildrsswpAKNLSFNATAAfNA 1899
Cdd:TIGR02169 242 IERQLASLEEELEKLTEEISELEKRLEEIEQL--LEELNKKikdlGEEEQLRVK------------EKIGELEAEIA-SL 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1900 YSNIKNYIDEadkaakqaKATATEAVQLATGPRGALKDEAKiSLQKSQRLWN-EAKNLENVVKDNGDNLGVLQQRLKSAD 1978
Cdd:TIGR02169 307 ERSIAEKERE--------LEDAEERLAKLEAEIDKLLAEIE-ELEREIEEERkRRDKLTEEYAELKEELEDLRAELEEVD 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1979 AKNKELlkgLDENLAVLRAIpNDTAAKLMATKQKASKANDTAIEVLARLKDMNQNLMGlnrnfstLKDDINKannLIQDP 2058
Cdd:TIGR02169 378 KEFAET---RDELKDYREKL-EKLKREINELKRELDRLQEELQRLSEELADLNAAIAG-------IEAKINE---LEEEK 443
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2196706209 2059 EkntiihAAGAKVKDLEDEAERLLEKLKPIRELQDNLRKNISQIKELINQARKQANSIKVSVSSGGDCIRTYRP 2132
Cdd:TIGR02169 444 E------DKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRA 511
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
991-1036 |
2.34e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 58.13 E-value: 2.34e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2196706209 991 PCECSHVG---NNCDPGTGRCLCPLNTVGDRCEKCAPNHWGHD-IATGCK 1036
Cdd:cd00055 1 PCDCNGHGslsGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPsQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
843-895 |
3.35e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 57.75 E-value: 3.35e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2196706209 843 PCSCSGNLDLSvaRSCDPLTGAClHCRRGYAGPNCETCADGYYGDAVGAKNCQ 895
Cdd:cd00055 1 PCDCNGHGSLS--GQCDPGTGQC-ECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
897-945 |
4.61e-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: 57.36 E-value: 4.61e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2196706209 897 CECNSNGSVSEVCNKESGQCQCLQRVLGRACDQCSPGTHMQAGSGCVPC 945
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
992-1035 |
8.05e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 56.59 E-value: 8.05e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2196706209 992 CECSHVG---NNCDPGTGRCLCPLNTVGDRCEKCAPNHWGHDIATGC 1035
Cdd:pfam00053 1 CDCNPHGslsDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQ 47
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
897-943 |
9.94e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 56.21 E-value: 9.94e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2196706209 897 CECNSNGSVSEVCNKESGQCQCLQRVLGRACDQCSPGTHMQA--GSGCV 943
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPsqGGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
992-1035 |
1.18e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.17 E-value: 1.18e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2196706209 992 CECS---HVGNNCDPGTGRCLCPLNTVGDRCEKCAPNHWGhDIATGC 1035
Cdd:smart00180 1 CDCDpggSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYG-DGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
399-456 |
2.23e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 55.44 E-value: 2.23e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2196706209 399 CACDSRGSVSTVCVPddhqategqSAGWCHCKQGYAGEKCDRCAFGYRGFPECRRCNC 456
Cdd:pfam00053 1 CDCNPHGSLSDTCDP---------ETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1649-2129 |
2.36e-09 |
|
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: 63.12 E-value: 2.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1649 LEQFVKNTLLAA-EALRDKARELNAT---LGRRDDGVEKSVNEMQDEIKAMMNELRSRQ-----LTHPHTHTV------Q 1713
Cdd:TIGR04523 194 NKLLKLELLLSNlKKKIQKNKSLESQiseLKKQNNQLKDNIEKKQQEINEKTTEISNTQtqlnqLKDEQNKIKkqlsekQ 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1714 EELRAAQDLL----------------LKVQRgfaaphrvSEELQQEVSSKLRDHDDKLQGAQ-EL---------LEEAQN 1767
Cdd:TIGR04523 274 KELEQNNKKIkelekqlnqlkseisdLNNQK--------EQDWNKELKSELKNQEKKLEEIQnQIsqnnkiisqLNEQIS 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1768 NIGNART-LNSDNLRRLEEVQRKRNESSKKKKETEGILEDGEKILNEANALS---DDINRGTEELEEMKRDLGPLHDQLD 1843
Cdd:TIGR04523 346 QLKKELTnSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLEskiQNQEKLNQQKDEQIKKLQQEKELLE 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1844 YRVSRLAQVVEDDK--LKDLvlraENHAAQLNDSATILDRSSwpaKNLSFNATAAFNAYSNIKNYIDEadkaakqakata 1921
Cdd:TIGR04523 426 KEIERLKETIIKNNseIKDL----TNQDSVKELIIKNLDNTR---ESLETQLKVLSRSINKIKQNLEQ------------ 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1922 teavqlatgprgaLKDEAKISLQKSQRLWNEAKNLENVVKD---NGDNLGVLQQRLKSADAKNKELLKGLDENLAVLrai 1998
Cdd:TIGR04523 487 -------------KQKELKSKEKELKKLNEEKKELEEKVKDltkKISSLKEKIEKLESEKKEKESKISDLEDELNKD--- 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1999 pNDTAAKLMATKQKASKanDTAIEvlaRLKDMNQNLMGLNRNFSTLKDDINKA-NNLIQDPEKNTI-IHAAGAKVKDLED 2076
Cdd:TIGR04523 551 -DFELKKENLEKEIDEK--NKEIE---ELKQTQKSLKKKQEEKQELIDQKEKEkKDLIKEIEEKEKkISSLEKELEKAKK 624
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 2196706209 2077 EAERLLEKLKPIRELQDNLRKNISQIKELINQAR-KQAN---SIKVSVSSGGDCIRT 2129
Cdd:TIGR04523 625 ENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRnKWPEiikKIKESKTKIDDIIEL 681
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1498-1533 |
2.79e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 55.05 E-value: 2.79e-09
10 20 30
....*....|....*....|....*....|....*.
gi 2196706209 1498 CECDLVGALPVPCDTHTGACRCRPGATGLKCDRCME 1533
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKP 36
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1578-2116 |
4.11e-09 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 62.83 E-value: 4.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1578 GALYRVENMTDELKHmlSPHRAPERLLQLADSNLGSLVTEMD-ELLSRANKVSADGEQTDSdaershkraqdleqfVKNT 1656
Cdd:pfam15921 238 GRIFPVEDQLEALKS--ESQNKIELLLQQHQDRIEQLISEHEvEITGLTEKASSARSQANS---------------IQSQ 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1657 LlaaEALRDKARELNATLGRRDDGVEKSVNEMQDEIKammnelRSRQLTHPHTHTVQEELRAAQDLLLKvqrgfAAPHRv 1736
Cdd:pfam15921 301 L---EIIQEQARNQNSMYMRQLSDLESTVSQLRSELR------EAKRMYEDKIEELEKQLVLANSELTE-----ARTER- 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1737 sEELQQEvSSKLRDHDDKL-----QGAQEL-LEEAQN------NIGNARTLnsDNLRR-LE----EVQRKRNESSKKKKE 1799
Cdd:pfam15921 366 -DQFSQE-SGNLDDQLQKLladlhKREKELsLEKEQNkrlwdrDTGNSITI--DHLRReLDdrnmEVQRLEALLKAMKSE 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1800 TEGILEDGEKILNEANALSDDINRGTEELEEMKRdlgplhdqldyrvsRLAQVVEDDKLKDLVLraENHAAQLNDSATIL 1879
Cdd:pfam15921 442 CQGQMERQMAAIQGKNESLEKVSSLTAQLESTKE--------------MLRKVVEELTAKKMTL--ESSERTVSDLTASL 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1880 DRsswpaKNLSFNATAAfnaysniknyideadkaakqakatatEAVQLatgprgalKDEAKISLQKSQRLWNEAKNLENv 1959
Cdd:pfam15921 506 QE-----KERAIEATNA--------------------------EITKL--------RSRVDLKLQELQHLKNEGDHLRN- 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1960 VKDNGDNLgvlqqRLKSADaKNK--ELLKGLDENLAVLRAIPNDTAAKLMATKQKASKA-NDTAIEVlarlkdmnqnlmg 2036
Cdd:pfam15921 546 VQTECEAL-----KLQMAE-KDKviEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEiNDRRLEL------------- 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2037 lnRNFSTLKDdinkannliqdpEKNTIIHAAGAKVKDLEdeaerlLEKLKPIRELQDNLR--KNISQIK-ELINQARKQA 2113
Cdd:pfam15921 607 --QEFKILKD------------KKDAKIRELEARVSDLE------LEKVKLVNAGSERLRavKDIKQERdQLLNEVKTSR 666
|
...
gi 2196706209 2114 NSI 2116
Cdd:pfam15921 667 NEL 669
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1038-1086 |
5.22e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 54.28 E-value: 5.22e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2196706209 1038 CGCHVTGAVTQQCNVNTGCCFCRDEFKGEKCNECKLGYRNFPHCVSCDC 1086
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1639-2121 |
6.05e-09 |
|
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: 62.00 E-value: 6.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1639 AERSHKRAQDLEQfVKNTLLAA--EALRDKARELNATLGRrddgVEKSVNEMQDEIKAM---MNELRSRQlthphtHTVQ 1713
Cdd:TIGR02168 212 AERYKELKAELRE-LELALLVLrlEELREELEELQEELKE----AEEELEELTAELQELeekLEELRLEV------SELE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1714 EELRAAQDLLLKVQrgfaaphrvseELQQEVSSKLRDHDDKLQGAQELLEEAQnnignartlnsdnlRRLEEVQRKRNES 1793
Cdd:TIGR02168 281 EEIEELQKELYALA-----------NEISRLEQQKQILRERLANLERQLEELE--------------AQLEELESKLDEL 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1794 SKKKKETEGILEDgekILNEANALSDDINRGTEELEEMKRDLGPLHDQLDYRVSRLAQVVED-DKLKDLVLRAENHAAQL 1872
Cdd:TIGR02168 336 AEELAELEEKLEE---LKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQiASLNNEIERLEARLERL 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1873 NDSATILDRSSwpAKNLSFNATAAFNAYSNIKNYIDEADKAAKQAKATATEAVQLATGPRGALKDEAKISLQKSQRLWNE 1952
Cdd:TIGR02168 413 EDRRERLQQEI--EELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQAR 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1953 AKNLENV-------------VKDN----GDNLGVLQQRLKSADAKNKELLKGLDENL-AVLraIPNDTAAKLM--ATKQK 2012
Cdd:TIGR02168 491 LDSLERLqenlegfsegvkaLLKNqsglSGILGVLSELISVDEGYEAAIEAALGGRLqAVV--VENLNAAKKAiaFLKQN 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2013 A---------SKANDTAIEVLARLKDMNQ-----------------------------------------NLMGLNRNFS 2042
Cdd:TIGR02168 569 ElgrvtflplDSIKGTEIQGNDREILKNIegflgvakdlvkfdpklrkalsyllggvlvvddldnalelaKKLRPGYRIV 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2043 TLKDDI-----------NKANNLIQDPEKNtiIHAAGAKVKDLEDEAERLLEKLKPIRELQDNLRKNISQIKELINQARK 2111
Cdd:TIGR02168 649 TLDGDLvrpggvitggsAKTNSSILERRRE--IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSR 726
|
570
....*....|
gi 2196706209 2112 QANSIKVSVS 2121
Cdd:TIGR02168 727 QISALRKDLA 736
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1582-2108 |
6.84e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 61.98 E-value: 6.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1582 RVENMTDELKHMLSP----HRAPERLLQLADSnlgsLVTEMDELLSRANKVSADGEQTDSDAERSHKRAQDLEQfvkntl 1657
Cdd:PRK02224 287 RLEELEEERDDLLAEagldDADAEAVEARREE----LEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEE------ 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1658 lAAEALRDKARELNATLgrrdDGVEKSVNEMQDEIKAMMNELrsrqlthphthtvqEELRAAQDlLLKVQRGFAAPHRvs 1737
Cdd:PRK02224 357 -RAEELREEAAELESEL----EEAREAVEDRREEIEELEEEI--------------EELRERFG-DAPVDLGNAEDFL-- 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1738 EELQQEvssklrdHDDKLQGAQEL---LEEAQNNIGNARTLnsdnlrrLEEvqrkrnessKKKKETEGILEDGEkilnEA 1814
Cdd:PRK02224 415 EELREE-------RDELREREAELeatLRTARERVEEAEAL-------LEA---------GKCPECGQPVEGSP----HV 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1815 NALSDDINRgTEELEEMKRDLGPLHDQLDYRVSRLAQVVE--------DDKLKDLVLRAENHAAQLNDSATILDRSSWPA 1886
Cdd:PRK02224 468 ETIEEDRER-VEELEAELEDLEEEVEEVEERLERAEDLVEaedrierlEERREDLEELIAERRETIEEKRERAEELRERA 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1887 KNLSFNATAAFNAYSNIKNYIDEadkaakqakatATEAVQLATGPRGALKDEAkislqksQRLWNEAKNLENvVKDNGDN 1966
Cdd:PRK02224 547 AELEAEAEEKREAAAEAEEEAEE-----------AREEVAELNSKLAELKERI-------ESLERIRTLLAA-IADAEDE 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1967 LGVLQQRLKSADAKN---KELLKGLDENLAVLRAIPNDTA-AKLMATKQKASKANDTAIEVLARLKDMNQNlmglnrnfs 2042
Cdd:PRK02224 608 IERLREKREALAELNderRERLAEKRERKRELEAEFDEARiEEAREDKERAEEYLEQVEEKLDELREERDD--------- 678
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2196706209 2043 tLKDDINKANNLIQDPEKNTIIHAA-GAKVKDLE---DEAERLLEKLkpiRELQDNLRK-NISQIKELINQ 2108
Cdd:PRK02224 679 -LQAEIGAVENELEELEELRERREAlENRVEALEalyDEAEELESMY---GDLRAELRQrNVETLERMLNE 745
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1498-1535 |
7.53e-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: 7.53e-09
10 20 30
....*....|....*....|....*....|....*...
gi 2196706209 1498 CECDLVGALPVPCDTHTGACRCRPGATGLKCDRCMEKH 1535
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGY 39
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1391-1437 |
7.75e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 53.85 E-value: 7.75e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1391 CECNG---HSVSCDPDTGVCQnCQHNTEGEKCERCSAGFYGVvrgSPDDC 1437
Cdd:smart00180 1 CDCDPggsASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD---GPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1498-1535 |
1.03e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 53.47 E-value: 1.03e-08
10 20 30
....*....|....*....|....*....|....*...
gi 2196706209 1498 CECDLVGALPVPCDTHTGACRCRPGATGLKCDRCMEKH 1535
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGY 38
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1084-1141 |
1.06e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 53.47 E-value: 1.06e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2196706209 1084 CDCSLSGSNAETCDPEsgvcacaerTGQCSCRMNVEGLRCEMCKFGTFGlseRNPLGC 1141
Cdd:smart00180 1 CDCDPGGSASGTCDPD---------TGQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1654-2112 |
1.11e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.94 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1654 KNTLLAA------EALRDKARELNATLGRRDDGVEKSVNEMQDEIKAMMNELRS-RQLTHpHTHTVQEELRAAQDLLLKV 1726
Cdd:COG4717 36 KSTLLAFiramllERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEyAELQE-ELEELEEELEELEAELEEL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1727 QRGFAaphRVSEELQ-QEVSSKLRDHDDKLQGAQELLEEAQNNIGNARTLNSDNLRRLEEVQRKRNE-SSKKKKETEGIL 1804
Cdd:COG4717 115 REELE---KLEKLLQlLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEElEELLEQLSLATE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1805 EDGEKILNEANALSDDINRGTEELEEMKRDLGPLHDQLDyrvsRLAQVVEDDKLKDLVLRAENHAAQLNDSATILDRSSW 1884
Cdd:COG4717 192 EELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE----QLENELEAAALEERLKEARLLLLIAAALLALLGLGGS 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1885 PAKNLSFNATAAFNAYSNIKNYIDEADKAAKQAKATATEAVQLATgpRGALKDEAKISLQKSQRLWNEAKNLEnvVKDNG 1964
Cdd:COG4717 268 LLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPA--LEELEEEELEELLAALGLPPDLSPEE--LLELL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1965 DNLGVLQQRLKSADAKNKELLkgLDENLAVLRAIPNDTAAKLMATKQKASKANDTAIEVLARLKDMNQNLMGLNRNFSTL 2044
Cdd:COG4717 344 DRIEELQELLREAEELEEELQ--LEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEEL 421
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2196706209 2045 KDDINKAnnliqdpekntiihaagakvkDLEDEAERLLEKLKPIRELQDNLRKNISQIKELINQARKQ 2112
Cdd:COG4717 422 LEALDEE---------------------ELEEELEELEEELEELEEELEELREELAELEAELEQLEED 468
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1083-1141 |
1.16e-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: 53.13 E-value: 1.16e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2196706209 1083 SCDCSLSGSNAETCDPEsgvcacaerTGQCSCRMNVEGLRCEMCKFGTFGLSERnPLGC 1141
Cdd:cd00055 1 PCDCNGHGSLSGQCDPG---------TGQCECKPNTTGRRCDRCAPGYYGLPSQ-GGGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
398-450 |
1.40e-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: 53.13 E-value: 1.40e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2196706209 398 PCACDSRGSVSTVCVPDDhqateGQsagwCHCKQGYAGEKCDRCAFGYRGFPE 450
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGT-----GQ----CECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
454-500 |
1.85e-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: 1.85e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2196706209 454 CNCSAEGSVNT--DPCQLPCVCKENVEGESCERCKEGYYNLHGDRSSGC 500
Cdd:pfam00053 1 CDCNPHGSLSDtcDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
736-778 |
2.32e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 52.31 E-value: 2.32e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2196706209 736 CRCH--GHASR-CDENTGHCLgCEHNTMGPHCDLCSPGYYGDATRG 778
Cdd:smart00180 1 CDCDpgGSASGtCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
844-887 |
3.61e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 51.93 E-value: 3.61e-08
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2196706209 844 CSCsgNLDLSVARSCDPLTGAClHCRRGYAGPNCETCADGYYGD 887
Cdd:smart00180 1 CDC--DPGGSASGTCDPDTGQC-ECKPNVTGRRCDRCAPGYYGD 41
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1608-2105 |
3.86e-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: 59.35 E-value: 3.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1608 DSNLGSLVTEMDELLSRAN--------KVSADGEQTDSDAERSHKRAQDLEQFV--------------KNTLLAAEALRD 1665
Cdd:pfam05483 189 NNNIEKMILAFEELRVQAEnarlemhfKLKEDHEKIQHLEEEYKKEINDKEKQVsllliqitekenkmKDLTFLLEESRD 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1666 KARELNATLGRRDDGVeKSVNEMQDEIKAMMNELR-SRQLTHPHTHTVQEELRAAQDLLLKVQRgfaaphrvSEELQQEV 1744
Cdd:pfam05483 269 KANQLEEKTKLQDENL-KELIEKKDHLTKELEDIKmSLQRSMSTQKALEEDLQIATKTICQLTE--------EKEAQMEE 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1745 SSKLR--------DHDDKLQGAQELLEEAQNNIGNartlNSDNLRRLE-EVQRKRNESS-----KKKKETEgiLEDGEKI 1810
Cdd:pfam05483 340 LNKAKaahsfvvtEFEATTCSLEELLRTEQQRLEK----NEDQLKIITmELQKKSSELEemtkfKNNKEVE--LEELKKI 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1811 LNEANALSDDinrgTEELEEMKRDLGPLHDQLDYRVSRLAQVVEDDKLKDLVLRA--ENHAAQLNDSATILDRSSwpAKN 1888
Cdd:pfam05483 414 LAEDEKLLDE----KKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTseEHYLKEVEDLKTELEKEK--LKN 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1889 LSFNATAAFNAYSNiknyideadkaakqakataTEAVQLATGPRGALKDEAK-ISLQKSQ--RLWNEAKNLENVVKDNGD 1965
Cdd:pfam05483 488 IELTAHCDKLLLEN-------------------KELTQEASDMTLELKKHQEdIINCKKQeeRMLKQIENLEEKEMNLRD 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1966 NLGVLQQRLKSadaKNKELLKGLDENLAVLRAIPNDTAAKLMATKQKASKANDTAIEVlarlKDMNQNLMGLNRNFSTLK 2045
Cdd:pfam05483 549 ELESVREEFIQ---KGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQI----ENKNKNIEELHQENKALK 621
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2046 DdinkannliQDPEKNTIIHAAGAKVKDLEDEAERLLEKLKpirELQDNLRKNIsQIKEL 2105
Cdd:pfam05483 622 K---------KGSAENKQLNAYEIKVNKLELELASAKQKFE---EIIDNYQKEI-EDKKI 668
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
844-890 |
7.13e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 51.20 E-value: 7.13e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2196706209 844 CSCSGNLDLSvaRSCDPLTGAClHCRRGYAGPNCETCADGYYGDAVG 890
Cdd:pfam00053 1 CDCNPHGSLS--DTCDPETGQC-LCKPGVTGRHCDRCKPGYYGLPSD 44
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
399-451 |
9.70e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 50.39 E-value: 9.70e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2196706209 399 CACDSRGSVSTVCVPDDhqateGQsagwCHCKQGYAGEKCDRCAFGYRG--FPEC 451
Cdd:smart00180 1 CDCDPGGSASGTCDPDT-----GQ----CECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1658-2048 |
1.20e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 56.83 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1658 LAAEALRDKARELNATLGRRDDGVEKSVNEMQDEIKAMMNELRsrqlthphthTVQEELRAAQDLLLKVQrgfaaphrvs 1737
Cdd:COG4372 13 LSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELE----------QAREELEQLEEELEQAR---------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1738 EELQQeVSSKLRDHDDKLQGAQELLEEAQNNIGNARTLNSDNLRRLEEVQRKRNESSKKKKETEGILEDGEKILNEAnal 1817
Cdd:COG4372 73 SELEQ-LEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAER--- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1818 sddinrgTEELEEMKRDLgplhDQLDYRVSRLAQVVEDDKLKDLVLRAENHAAQLNDSAT---ILDRSSWPAKNLSFNAT 1894
Cdd:COG4372 149 -------EEELKELEEQL----ESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEkeeELAEAEKLIESLPRELA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1895 AAFNAYSNIKNYIDEadkaakqakatatEAVQLATGPRGALKDEAKISLQKSQRLWNEAKNLENVVKDNGDNLGVLQQRL 1974
Cdd:COG4372 218 EELLEAKDSLEAKLG-------------LALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALE 284
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2196706209 1975 KSADAKNKELLKGLDEnLAVLRAIPNDTAAKLMATKQKASKANDTAIEVLARLKDMNQNLMGLNRNFSTLKDDI 2048
Cdd:COG4372 285 LEALEEAALELKLLAL-LLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLE 357
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1685-2114 |
1.58e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 57.34 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1685 VNEMQDEIKAMMNELRSRQLthphthtvqeELRAAQDLLLKvqrgfaaphrvSEELQQEVSSKLrdhddklqgaqELLEE 1764
Cdd:TIGR04523 35 EKQLEKKLKTIKNELKNKEK----------ELKNLDKNLNK-----------DEEKINNSNNKI-----------KILEQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1765 AQNNIGNARTLNSDNLRRLEEVQRKRNESSKKKKETEGILEDG----EKILNEANALSDDINrgteelEEMKRdlgpLHD 1840
Cdd:TIGR04523 83 QIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVElnklEKQKKENKKNIDKFL------TEIKK----KEK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1841 QLDYRVSrlaqvvEDDKLKDLVLRAENHAAQLNDSAtildrsswpaknlsfnataafnaySNIKNYIDEADKaakqakat 1920
Cdd:TIGR04523 153 ELEKLNN------KYNDLKKQKEELENELNLLEKEK------------------------LNIQKNIDKIKN-------- 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1921 ateavQLatgprgaLKDEAKISL-----QKSQRLWNEAKNLENVVKDNGDNLGVLQQRLksaDAKNKELlkgldenlavl 1995
Cdd:TIGR04523 195 -----KL-------LKLELLLSNlkkkiQKNKSLESQISELKKQNNQLKDNIEKKQQEI---NEKTTEI----------- 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1996 raipNDTAAKLMATKQKASKANDTAIEVLARLKDMNQNLMGLNRNFSTLKDDINKANNliqdpEKNTIIHaagakvKDLE 2075
Cdd:TIGR04523 249 ----SNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNN-----QKEQDWN------KELK 313
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2196706209 2076 DEaerLLEKLKPIRELQDNLRKN---ISQIKELINQARKQAN 2114
Cdd:TIGR04523 314 SE---LKNQEKKLEEIQNQISQNnkiISQLNEQISQLKKELT 352
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1582-1837 |
2.85e-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: 56.60 E-value: 2.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1582 RVENMTDELKHMLSPHRAPERLLQLADSNLGSLVTEMDELLSRANKVSADGEQTDSDAERSHKRAQDLEQFVKNTLLAAE 1661
Cdd:TIGR02168 727 QISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALD 806
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1662 ALRDKARELNATLGRRDDGVEKSVNEMqDEIKAMMNELRSR---------QLTHPHTH--TVQEELRAAQDLLLKVQRGF 1730
Cdd:TIGR02168 807 ELRAELTLLNEEAANLRERLESLERRI-AATERRLEDLEEQieelsedieSLAAEIEEleELIEELESELEALLNERASL 885
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1731 AAPHRVSEELQQEVSSKLRDHDDKLQGAQELLEEAQNNIGNARTlnsdnlrRLEEVQRKRNE-----SSKKKKETEGILE 1805
Cdd:TIGR02168 886 EEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLEL-------RLEGLEVRIDNlqerlSEEYSLTLEEAEA 958
|
250 260 270
....*....|....*....|....*....|..
gi 2196706209 1806 DGEKILNEANALSDDINRGTEELEEmkrdLGP 1837
Cdd:TIGR02168 959 LENKIEDDEEEARRRLKRLENKIKE----LGP 986
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
454-495 |
3.30e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 49.23 E-value: 3.30e-07
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2196706209 454 CNCSAEGSVNT--DPCQLPCVCKENVEGESCERCKEGYYNLHGD 495
Cdd:smart00180 1 CDCDPGGSASGtcDPDTGQCECKPNVTGRRCDRCAPGYYGDGPP 44
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
453-501 |
3.54e-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: 3.54e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2196706209 453 RCNCSAEGSVNT--DPCQLPCVCKENVEGESCERCKEGYYNLhGDRSSGCE 501
Cdd:cd00055 1 PCDCNGHGSLSGqcDPGTGQCECKPNTTGRRCDRCAPGYYGL-PSQGGGCQ 50
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1582-2136 |
3.62e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 56.06 E-value: 3.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1582 RVENMTDELKHMLSPHRAPERLLQLADSNLGSLVTEMDELlsraNKVSADGEQTDSDAERSHKRAQDLEQFVKNTLLAAE 1661
Cdd:PRK01156 163 SLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENI----KKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLK 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1662 -------ALRDKARELNATLgRRDDGVEKSVNEMQDEIKAMmnELRSRQLTHPHTHTVQEELRA----AQDLLLKVQ--- 1727
Cdd:PRK01156 239 salnelsSLEDMKNRYESEI-KTAESDLSMELEKNNYYKEL--EERHMKIINDPVYKNRNYINDyfkyKNDIENKKQils 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1728 ------RGFAAPHRVSEELQqevssklRDHDDKLQGAQELlEEAQNNIGNARTLNSDN---LRRLEEVQRKRNESSKKKK 1798
Cdd:PRK01156 316 nidaeiNKYHAIIKKLSVLQ-------KDYNDYIKKKSRY-DDLNNQILELEGYEMDYnsyLKSIESLKKKIEEYSKNIE 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1799 ETEGILEdgeKILNEANALSDDINRgteELEEMKRDLgplhDQLDYRVSRLAQVVedDKLKDLVLRAENHAAQLNDsati 1878
Cdd:PRK01156 388 RMSAFIS---EILKIQEIDPDAIKK---ELNEINVKL----QDISSKVSSLNQRI--RALRENLDELSRNMEMLNG---- 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1879 ldRSSWPAKNLSFNATAA---FNAYSNIKNYIDEADKAAKQakatatEAVQLATGPRGALKDEAKISLQKSQRLWNE--- 1952
Cdd:PRK01156 452 --QSVCPVCGTTLGEEKSnhiINHYNEKKSRLEEKIREIEI------EVKDIDEKIVDLKKRKEYLESEEINKSINEynk 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1953 ----------AKNLENVVKDNGDNLGVLQQRLKSA-----DAKNKELLKGLdenlAVLRAIPNDTAAKlmATKQKASKAN 2017
Cdd:PRK01156 524 iesaradledIKIKINELKDKHDKYEEIKNRYKSLkledlDSKRTSWLNAL----AVISLIDIETNRS--RSNEIKKQLN 597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2018 DtaieVLARLKDMNQNLMGLNR-NFSTLKDDINKANNLiqDPEKNtIIHAAGAKVKDLEDEAERLLEKLKPIRELQDNLR 2096
Cdd:PRK01156 598 D----LESRLQEIEIGFPDDKSyIDKSIREIENEANNL--NNKYN-EIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLK 670
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 2196706209 2097 K---NISQIKELINQARKQANSIKVSVSSGGDCIRTYRPDIKK 2136
Cdd:PRK01156 671 EitsRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINE 713
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1037-1079 |
5.89e-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: 48.50 E-value: 5.89e-07
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2196706209 1037 ACGCHVTGAVTQQCNVNTGCCFCRDEFKGEKCNECKLGYRNFP 1079
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1728-2107 |
8.37e-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: 55.06 E-value: 8.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1728 RGFAAPHRVSEELQ-QEVSSKLRDHDDKLQGAQELLEEAQNNIGNARTLNSDNLRRLEEVQRKRNESSKKKKETEgilED 1806
Cdd:TIGR02168 658 GGVITGGSAKTNSSiLERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALR---KD 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1807 GEKILNEANALSDDINRGTEELEEMKRDLGPLHDQLDYRVSRLAQVveDDKLKDLVLRAENHAAQLNDSATILDrsswpa 1886
Cdd:TIGR02168 735 LARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEA--EAEIEELEAQIEQLKEELKALREALD------ 806
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1887 knlsfnataafnaysniknyideadkaakqakatateavqlatgprgALKDEAKISLQKSQRLWNEAKNLENVVKDNGDN 1966
Cdd:TIGR02168 807 -----------------------------------------------ELRAELTLLNEEAANLRERLESLERRIAATERR 839
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1967 LGVLQQRLKsadaKNKELLKGLDENLAVLRAipndtaaklmatkqKASKANDTAIEVLARLKDMNQNLMGLNRNFSTLKD 2046
Cdd:TIGR02168 840 LEDLEEQIE----ELSEDIESLAAEIEELEE--------------LIEELESELEALLNERASLEEALALLRSELEELSE 901
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2196706209 2047 DINKANNliqdpekntiihaagaKVKDLEDEAERLLEKLKPIRELQDNLRKNISQIKELIN 2107
Cdd:TIGR02168 902 ELRELES----------------KRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLS 946
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1038-1081 |
8.80e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 47.69 E-value: 8.80e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2196706209 1038 CGCHVTGAVTQQCNVNTGCCFCRDEFKGEKCNECKLGY--RNFPHC 1081
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYygDGPPGC 46
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1616-1874 |
1.04e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 54.69 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1616 TEMDELLSRANKVSADGEQTDSDAERSHKRAQDLEqfvkntllaaEALRDKARELNATLGRRDDgVEKSVNEM-QDEIKA 1694
Cdd:TIGR02169 223 YEGYELLKEKEALERQKEAIERQLASLEEELEKLT----------EEISELEKRLEEIEQLLEE-LNKKIKDLgEEEQLR 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1695 MMNELRSrqlthphTHTVQEELRAAQDLLLKVQRGFAAPHRVSEELQQEVSSKLRDHDDKLQGAQELLEEAQNNIGNART 1774
Cdd:TIGR02169 292 VKEKIGE-------LEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1775 LNSDNLRRLEEVQRK----RNESSKKKKETEGILEDGEKILNEANALSDDINRGTEELEEMKRDLGPLHDQLdyrvSRLA 1850
Cdd:TIGR02169 365 ELEDLRAELEEVDKEfaetRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKI----NELE 440
|
250 260
....*....|....*....|....*.
gi 2196706209 1851 QVVED--DKLKDLVLRAENHAAQLND 1874
Cdd:TIGR02169 441 EEKEDkaLEIKKQEWKLEQLAADLSK 466
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1978-2122 |
2.02e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 52.61 E-value: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1978 DAKNKELlKGLDENLAVLRAIPNDTAAKLMATKQKASKAN---DTAIEVLARLKDMNQNLMGLNRNFSTLKDDINKANNL 2054
Cdd:COG1340 46 DELNAQV-KELREEAQELREKRDELNEKVKELKEERDELNeklNELREELDELRKELAELNKAGGSIDKLRKEIERLEWR 124
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2196706209 2055 IQ----DPEK-NTIIhaagAKVKDLE---DEAERLLEKLKPIRELQ---DNLRKNISQIKELINQARKQANSIKVSVSS 2122
Cdd:COG1340 125 QQtevlSPEEeKELV----EKIKELEkelEKAKKALEKNEKLKELRaelKELRKEAEEIHKKIKELAEEAQELHEEMIE 199
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1581-1882 |
3.41e-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: 53.30 E-value: 3.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1581 YRVENMTDELKHML-SPHRAPERLLQLADSNlgSLVTEMDELLSRANK---------VSADG--EQTDSDAERSHKRAQD 1648
Cdd:pfam12128 440 YRLKSRLGELKLRLnQATATPELLLQLENFD--ERIERAREEQEAANAeverlqselRQARKrrDQASEALRQASRRLEE 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1649 LEQF---VKNTLLAA-----EALRDKARELNATLGR--------RDDgVEKSVNEMQ--DEIKAMMNELRSRQLTHPHTH 1710
Cdd:pfam12128 518 RQSAldeLELQLFPQagtllHFLRKEAPDWEQSIGKvispellhRTD-LDPEVWDGSvgGELNLYGVKLDLKRIDVPEWA 596
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1711 TVQEELRAAQDlllKVQRGFAAPHrvseELQQEVSSKLRDHDDKLQGAQELLEEAQNNIGNARtlnsDNLRRL----EEV 1786
Cdd:pfam12128 597 ASEEELRERLD---KAEEALQSAR----EKQAAAEEQLVQANGELEKASREETFARTALKNAR----LDLRRLfdekQSE 665
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1787 QRKRNESSKKKKETEGilEDGEKILNEANALSDDINRGTEELEEMKRDLgplhdqldyRVSRLA--QVVE---DDKLKDL 1861
Cdd:pfam12128 666 KDKKNKALAERKDSAN--ERLNSLEAQLKQLDKKHQAWLEEQKEQKREA---------RTEKQAywQVVEgalDAQLALL 734
|
330 340
....*....|....*....|....*
gi 2196706209 1862 V----LRAENHAAQLNDSATILDRS 1882
Cdd:pfam12128 735 KaaiaARRSGAKAELKALETWYKRD 759
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1604-1874 |
3.64e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.02 E-value: 3.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1604 LQLADSNLgsLVTEMDELLSRANKVSADGEQTDSDAERSHKRAQDLEQfvkntllAAEALRDKARELNATLGRRDDGVEK 1683
Cdd:COG1196 222 LKELEAEL--LLLKLRELEAELEELEAELEELEAELEELEAELAELEA-------ELEELRLELEELELELEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1684 SVNEMQDEIKAM-MNELRSRQLThphthtvQEELRAAQDLLLKVQRGFAAPHRVSE------ELQQEVSSKLRDHDDKLQ 1756
Cdd:COG1196 293 LLAELARLEQDIaRLEERRRELE-------ERLEELEEELAELEEELEELEEELEEleeeleEAEEELEEAEAELAEAEE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1757 GAQELLEEAQNNIGNARTLNSDNLRRLEEVQRKRNESSKKKKETEGILEDGEKILNEANALSDDINRGTEELEEMKRDLg 1836
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL- 444
|
250 260 270
....*....|....*....|....*....|....*...
gi 2196706209 1837 pLHDQLDYRVSRLAQVVEDDKLKDLVLRAENHAAQLND 1874
Cdd:COG1196 445 -EEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1580-1833 |
3.93e-06 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 52.72 E-value: 3.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1580 LYRVENMTDELKHMLSphRAPERLLQL-ADSNLGSL-VTEMDELLsrANKVSADG-EQTDSDAERSHKRAQDLeQFVKNT 1656
Cdd:pfam05701 72 LESTKRLIEELKLNLE--RAQTEEAQAkQDSELAKLrVEEMEQGI--ADEASVAAkAQLEVAKARHAAAVAEL-KSVKEE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1657 L---------LAAEalRD----KARElnATLGRRDdgVEKSVNEMQDEIKAMMNELRSRQLTHphtHTVQEE-LRAA--- 1719
Cdd:pfam05701 147 LeslrkeyasLVSE--RDiaikRAEE--AVSASKE--IEKTVEELTIELIATKESLESAHAAH---LEAEEHrIGAAlar 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1720 -QDLL-----LKvqrgfaaphRVSEELQ---QEVSSKlRDHDDKLQGAQELLEEAQNNIgNARTLNSDNLRRLEEVQRKR 1790
Cdd:pfam05701 218 eQDKLnwekeLK---------QAEEELQrlnQQLLSA-KDLKSKLETASALLLDLKAEL-AAYMESKLKEEADGEGNEKK 286
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2196706209 1791 NESS------KKKKETEGILEDGEKILNEANA-------LSDDINRGTEELEEMKR 1833
Cdd:pfam05701 287 TSTSiqaalaSAKKELEEVKANIEKAKDEVNClrvaaasLRSELEKEKAELASLRQ 342
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1619-2154 |
5.71e-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: 52.48 E-value: 5.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1619 DELLSRANKVSADGEQTDSDAERSHkrAQDLEQfvKNTL---LAAEA-LRDKARELNATLGRRDDGVEKSVNEMQDEIKA 1694
Cdd:pfam01576 11 EEELQKVKERQQKAESELKELEKKH--QQLCEE--KNALqeqLQAETeLCAEAEEMRARLAARKQELEEILHELESRLEE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1695 mmNELRSRQLT------HPHTHTVQEELRAAQDLLLKVQRgfaapHRVSEE-----LQQEVSSkLRDHDDKLQGAQELLE 1763
Cdd:pfam01576 87 --EEERSQQLQnekkkmQQHIQDLEEQLDEEEAARQKLQL-----EKVTTEakikkLEEDILL-LEDQNSKLSKERKLLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1764 EAQNNIgnartlnSDNLRrlEEVQRKRNESSKKKKETEGILEDGEKILNEAnalsddinRGTEELEEMKRDL----GPLH 1839
Cdd:pfam01576 159 ERISEF-------TSNLA--EEEEKAKSLSKLKNKHEAMISDLEERLKKEE--------KGRQELEKAKRKLegesTDLQ 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1840 DQldyrVSRL-AQVVE--------DDKLKDLVLRAENHAAQLNdsatildrsswpaknlsfnatAAFNAYSNIKNYIDEa 1910
Cdd:pfam01576 222 EQ----IAELqAQIAElraqlakkEEELQAALARLEEETAQKN---------------------NALKKIRELEAQISE- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1911 dkaakqakatATEAVQLATGPRG--------------ALKDEAKISL-----------QKSQRLWNEAKNLENVVKDNGD 1965
Cdd:pfam01576 276 ----------LQEDLESERAARNkaekqrrdlgeeleALKTELEDTLdttaaqqelrsKREQEVTELKKALEEETRSHEA 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1966 NLGVLQQ-----------------RLKSADAKNKELLKGLDENLAV-LRAIpndTAAKlMATKQKASKANDTAIEVLARL 2027
Cdd:pfam01576 346 QLQEMRQkhtqaleelteqleqakRNKANLEKAKQALESENAELQAeLRTL---QQAK-QDSEHKRKKLEGQLQELQARL 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2028 KDMNQNLMGLNRNFSTLKDDINKANNLIQDPEKNTI------------IH--------------AAGAKVKDLEDEAERL 2081
Cdd:pfam01576 422 SESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIklskdvsslesqLQdtqellqeetrqklNLSTRLRQLEDERNSL 501
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2196706209 2082 LEKLKPIRELQDNLRKNISQIKELINQARKQANSIKVSVSSGGDCIRTYRPDIKKGrynTIVLNVKTLAADNL 2154
Cdd:pfam01576 502 QEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEAL---TQQLEEKAAAYDKL 571
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
272-319 |
7.93e-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: 45.42 E-value: 7.93e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2196706209 272 CICYGHAkACPLNPNTKKLSCECEHNTCGESCDRCCPGYNQKPWMAGT 319
Cdd:cd00055 2 CDCNGHG-SLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1607-1873 |
8.21e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.98 E-value: 8.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1607 ADSNLGSLVTEMDELLSRANKVSADGEQTDSDAERSHKRAQDLEQFVKNTLLAAEALRDKARELNATLGRRDDGVEKsVN 1686
Cdd:TIGR02168 668 TNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ-LE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1687 EMQDEIKAMMNELrsrqlthphthtvQEELRAAQDLLLKVQRGFAAPHRVSEELQQEV---SSKLRDHDDKLQGAQELLE 1763
Cdd:TIGR02168 747 ERIAQLSKELTEL-------------EAEIEELEERLEEAEEELAEAEAEIEELEAQIeqlKEELKALREALDELRAELT 813
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1764 EAQNNIGNARTLNSDNLRRLEEVQRKRNESSKKKKETEGILEDGEKILNEA----NALSDDINRGTEELEEMKRDLGPLH 1839
Cdd:TIGR02168 814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELeeliEELESELEALLNERASLEEALALLR 893
|
250 260 270
....*....|....*....|....*....|....*
gi 2196706209 1840 DQLDYRVSRLAQVVED-DKLKDLVLRAENHAAQLN 1873
Cdd:TIGR02168 894 SELEELSEELRELESKrSELRRELEELREKLAQLE 928
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1612-1869 |
8.97e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.60 E-value: 8.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1612 GSLVTEMD--ELLSR----ANKVSADGEQTDSDAERSHKRAQDLEQFVKN--TLLAAEALRDKARELNATLGRRD----- 1678
Cdd:PRK03918 442 GRELTEEHrkELLEEytaeLKRIEKELKEIEEKERKLRKELRELEKVLKKesELIKLKELAEQLKELEEKLKKYNleele 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1679 ------DGVEKSVNEMQDEIKAMMNELRSRQLTHPHTHTVQEELRAAQDLLLKVQR-----GFAAPHRVSEELQQ----- 1742
Cdd:PRK03918 522 kkaeeyEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKeleelGFESVEELEERLKElepfy 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1743 -------EVSSKLRDHDDKLQGAQELLEEAQNNIgnARTLNS--------DNLRRL---EEVQRKRNESSKKKKETEGI- 1803
Cdd:PRK03918 602 neylelkDAEKELEREEKELKKLEEELDKAFEEL--AETEKRleelrkelEELEKKyseEEYEELREEYLELSRELAGLr 679
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2196706209 1804 --LEDGEKILNEANALSDDINRGTEELEEMKRDLGPLHDQLDyRVSRLAQvveddKLKDLVLRAENHA 1869
Cdd:PRK03918 680 aeLEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE-RVEELRE-----KVKKYKALLKERA 741
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
1939-2085 |
1.01e-05 |
|
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.
Pssm-ID: 427715 [Multi-domain] Cd Length: 360 Bit Score: 50.85 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1939 AKISLQksQRLWNEA-KNLENVVKDNGDNLGVLQQRLKSADAKNKELLKGLDENLAVLRAIPNDTAAKLMATKQK----- 2012
Cdd:pfam04108 31 AKIAFL--RRGLSVQlANLEKVREGLEKVLNELKKDFKQLLKDLDAALERLEETLDKLRNTPVEPALPPGEEKQKtlldf 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2196706209 2013 -----ASKANDTAIEVLARLKDMNQNLMGLNRNFSTLKDDINKA-NNLIQDPEKNTIIHAAGAKVKDLEDEAERLLEKL 2085
Cdd:pfam04108 109 idedsVEILRDALKELIDELQAAQESLDSDLKRFDDDLRDLQKElESLSSPSESISLIPTLLKELESLEEEMASLLESL 187
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1762-2148 |
1.02e-05 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 51.76 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1762 LEEAQNNIGNART-LNSDNLRRLEEvqrkrnESSKKKKETEGILEDGEKILNEANALSDDINRGTEELEEMK-RDLGPL- 1838
Cdd:PTZ00440 1277 MENALHEIKNMYEfLISIDSEKILK------EILNSTKKAEEFSNDAKKELEKTDNLIKQVEAKIEQAKEHKnKIYGSLe 1350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1839 HDQLDYRVSRLAQVVED---------DKLKDLVLRAENHAAQLNDSATILDRSSWPAKN--LSFNATAAFNAySNIKNYI 1907
Cdd:PTZ00440 1351 DKQIDDEIKKIEQIKEEisnkrkeinKYLSNIKSNKEKCDLHVRNASRGKDKIDFLNKHeaIEPSNSKEVNI-IKITDNI 1429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1908 DEADKAAKQAKATateAVQLATGPRGALKDEAKIS--LQKSQRLWNEAKnLENVVKDNGDNLGvlqqRLKSADAKNKELL 1985
Cdd:PTZ00440 1430 NKCKQYSNEAMET---ENKADENNDSIIKYEKEITniLNNSSILGKKTK-LEKKKKEATNIMD----DINGEHSIIKTKL 1501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1986 KGLDENLAVLRAIPNDTAAKLMATKQKASKANDTAIEVLARLKdmnQNLMGLNRnfstLKDDI----NKANNLIQDpekn 2061
Cdd:PTZ00440 1502 TKSSEKLNQLNEQPNIKREGDVLNNDKSTIAYETIQYNLGRVK---HNLLNILN----IKDEIetilNKAQDLMRD---- 1570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2062 tiihaagakVKDLEDEAERL-LEKLKPIRELQDNLRKNISQIKELINQARKQANSIKVSVSSGGDCIRTYRPDIKKGRYN 2140
Cdd:PTZ00440 1571 ---------ISKISKIVENKnLENLNDKEADYVKYLDNILKEKQLMEAEYKKLNEIYSDVDNIEKELKKHKKNYEIGLLE 1641
|
....*...
gi 2196706209 2141 TIVLNVKT 2148
Cdd:PTZ00440 1642 KVIEINKN 1649
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1604-1909 |
1.14e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 50.67 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1604 LQLADSNLGSLVTEMDELLSRANKVSADGEQTDSDAERSHKRAQDLEqfvkntllaaEALRDKARELNATLGRRDDGVE- 1682
Cdd:COG4372 33 LRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLE----------EELEELNEQLQAAQAELAQAQEe 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1683 -KSVNEMQDEIKAMMNELRSRQlthphtHTVQEELRAAQDLLLKVQRGFAAPHRVSEELQQEVSSkLRDHDDKL------ 1755
Cdd:COG4372 103 lESLQEEAEELQEELEELQKER------QDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLES-LQEELAALeqelqa 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1756 -------QGAQELLEEAQNNIGNARTLNSDNLRRLEEVQRKRNESSKKKKETEGILEDGEKILNEANALSDDINRGTEEL 1828
Cdd:COG4372 176 lseaeaeQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1829 EEMKRDLGPLHDQLDYRvsRLAQVVEDDKLKDLVLRAENHAAQLNDSATILDRSSWPAKNLSFNATAAFNAYSNIKNYID 1908
Cdd:COG4372 256 ILKEIEELELAILVEKD--TEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALA 333
|
.
gi 2196706209 1909 E 1909
Cdd:COG4372 334 I 334
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1609-1881 |
1.47e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 49.91 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1609 SNLGSLVTEMDELLSRANKVSAdgEQTDSDAERSHKRAQdLEQFVK--NTLLA-AEALRDKARELNAtlgRRDDGVEKsV 1685
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELRE--EIEELKEKRDELNEE-LKELAEkrDELNAqVKELREEAQELRE---KRDELNEK-V 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1686 NEM---QDEIKAMMNELRsrqlthphthtvqEELRAAQDLLLKVQRGFAAPHRVSEELQ-----QEVSSKLRDHD----D 1753
Cdd:COG1340 74 KELkeeRDELNEKLNELR-------------EELDELRKELAELNKAGGSIDKLRKEIErlewrQQTEVLSPEEEkelvE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1754 KLQGAQELLEEAQNnignARTLNsdnlrrlEEVQRKRNESSKKKKETEGILEDGEKILNEANALSDDINRGTEELEEMKR 1833
Cdd:COG1340 141 KIKELEKELEKAKK----ALEKN-------EKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRK 209
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2196706209 1834 D--------------LGPLHDQLDYRVSRLAQVveDDKLKDlvLRAENHAAQLNDSATILDR 1881
Cdd:COG1340 210 EadelhkeiveaqekADELHEEIIELQKELREL--RKELKK--LRKKQRALKREKEKEELEE 267
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1602-1878 |
1.52e-05 |
|
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: 50.94 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1602 RLLQLADSNLGSLVTEMDELLSRANKVSADGEQTDSDAE----RSHKRAQDLEQFVKNtlLAAEA---------LRDKAR 1668
Cdd:pfam01576 155 KLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEerlkKEEKGRQELEKAKRK--LEGEStdlqeqiaeLQAQIA 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1669 ELNATLGRRDDGVEKSVNEMQDEIKAMMNELRSRQLTHPHTHTVQEELRAAqdlllKVQRGFAAPHR--VSEEL------ 1740
Cdd:pfam01576 233 ELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESE-----RAARNKAEKQRrdLGEELealkte 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1741 ----------QQEVSSK---------------LRDHDDKLQGA-----------QELLEEAQNNIGN----ARTLNSDNL 1780
Cdd:pfam01576 308 ledtldttaaQQELRSKreqevtelkkaleeeTRSHEAQLQEMrqkhtqaleelTEQLEQAKRNKANlekaKQALESENA 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1781 RRLEEV---QRKRNESSKKKKETEGILE-------DGEKILNEanaLSDDINRGTEELEEMKRDLGplhdQLDYRVSRLA 1850
Cdd:pfam01576 388 ELQAELrtlQQAKQDSEHKRKKLEGQLQelqarlsESERQRAE---LAEKLSKLQSELESVSSLLN----EAEGKNIKLS 460
|
330 340 350
....*....|....*....|....*....|.
gi 2196706209 1851 QVVE--DDKLKDLV-LRAENHAAQLNDSATI 1878
Cdd:pfam01576 461 KDVSslESQLQDTQeLLQEETRQKLNLSTRL 491
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1617-1833 |
4.69e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.61 E-value: 4.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1617 EMDELLSRANKVSADGEQTDSDAERSHKRAQDLEQFVKNTLLAAEALRDKARELN---ATLGRRDDGVEKSVNEMQDEIK 1693
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEaelAELEKEIAELRAELEAQKEELA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1694 AMMNEL-RSRQLTHPhthtvqeELRAAQDLLLKVQRGFAAPHRVSEELQQEVSsKLRDHDDKLQGAQELLEEAQNNIGNA 1772
Cdd:COG4942 108 ELLRALyRLGRQPPL-------ALLLSPEDFLDAVRRLQYLKYLAPARREQAE-ELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2196706209 1773 RTLNSDNLRRLEEVQRKRNESSKK-KKETEGILEDGEKILNEANALSDDINRGTEELEEMKR 1833
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARlEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1619-1859 |
7.28e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 7.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1619 DELLSRANKVSADgEQTDSDAERSHKRAQDLEQFVK-NTLLAAEALRdKARELNATLGRRDDGVEKSVNEMQDEIKAMMN 1697
Cdd:PTZ00121 1513 DEAKKAEEAKKAD-EAKKAEEAKKADEAKKAEEKKKaDELKKAEELK-KAEEKKKAEEAKKAEEDKNMALRKAEEAKKAE 1590
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1698 ELRSRQLTHPHTHTVQ---EELRAAQDLLLKvqrgfAAPHRVSEELQQEVSSKLRDHDDKLQGAQELLEEAQNNIGNART 1774
Cdd:PTZ00121 1591 EARIEEVMKLYEEEKKmkaEEAKKAEEAKIK-----AEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAE 1665
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1775 L---------NSDNLRRLEEVQRKRNESSKKKKETEGILEDGEKILNEANALSDDINRGTEE----LEEMKRDlgplhDQ 1841
Cdd:PTZ00121 1666 EakkaeedkkKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEEnkikAEEAKKE-----AE 1740
|
250
....*....|....*...
gi 2196706209 1842 LDYRVSRLAQVVEDDKLK 1859
Cdd:PTZ00121 1741 EDKKKAEEAKKDEEEKKK 1758
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1645-1881 |
8.92e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.39 E-value: 8.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1645 RAQDLEQFVKNTL--LAAEA--------LRDKARELNATL-GRRDDGVEKSVNEMQDEIKAMMNELRSRQLTHPHTHTVQ 1713
Cdd:COG1196 190 RLEDILGELERQLepLERQAekaeryreLKEELKELEAELlLLKLRELEAELEELEAELEELEAELEELEAELAELEAEL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1714 EELRAAQDLLLKVQRGFAAPHRVSEELQQEVSSKLRDHDDKLQGAQELLEEAQNNIGNARTLNSDNLRRLEEVQRKRNES 1793
Cdd:COG1196 270 EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1794 SKKKKETEGILEDGEKILNEANALSDDINRgtEELEEMKRDLGPLHDQLDYR--VSRLAQVVEDDKLKDLVLRAENHAAQ 1871
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEAEE--ELEELAEELLEALRAAAELAaqLEELEEAEEALLERLERLEEELEELE 427
|
250
....*....|
gi 2196706209 1872 LNDSATILDR 1881
Cdd:COG1196 428 EALAELEEEE 437
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1612-1874 |
1.13e-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: 48.13 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1612 GSLVTEMDELlsrankVSADGEQTDSDAERSHK---RAQDLEQFVKNTLLAAEALRDKARELNATLGRRDD------GVE 1682
Cdd:TIGR02168 645 YRIVTLDGDL------VRPGGVITGGSAKTNSSileRRREIEELEEKIEELEEKIAELEKALAELRKELEEleeeleQLR 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1683 KSVNEMQDEIKAMMNELRSRQLThphthtvQEELRAAQDLLLKVQRGFAAPHRVSEELQQEVSSKLRDHDDKLQGAQELL 1762
Cdd:TIGR02168 719 KELEELSRQISALRKDLARLEAE-------VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQI 791
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1763 EEAQNNIGNARTlNSDNLR--------RLEEVQRKRNESSKKKKETEGILEDGEKILNEanaLSDDINRGTEELEEMKRD 1834
Cdd:TIGR02168 792 EQLKEELKALRE-ALDELRaeltllneEAANLRERLESLERRIAATERRLEDLEEQIEE---LSEDIESLAAEIEELEEL 867
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2196706209 1835 LGPLHDQLDYRVSRLAQVVEDdkLKDLVLRAENHAAQLND 1874
Cdd:TIGR02168 868 IEELESELEALLNERASLEEA--LALLRSELEELSEELRE 905
|
|
| Seryl_tRNA_N |
pfam02403 |
Seryl-tRNA synthetase N-terminal domain; This domain is found associated with the Pfam tRNA ... |
1782-1835 |
1.39e-04 |
|
Seryl-tRNA synthetase N-terminal domain; This domain is found associated with the Pfam tRNA synthetase class II domain (pfam00587) and represents the N-terminal domain of seryl-tRNA synthetase.
Pssm-ID: 426757 [Multi-domain] Cd Length: 108 Bit Score: 43.73 E-value: 1.39e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2196706209 1782 RLEEVQRKRNESSKKKKETEGILEDGEKILNEANALSDDINRGTEELEEMKRDL 1835
Cdd:pfam02403 44 ELEELQAERNELSKEIGQAKKKKEDADALIAEVKELKDELKALEAELKELEAEL 97
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1934-2117 |
1.64e-04 |
|
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: 47.07 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1934 ALKDEAKISLQKSQRLWNEAKNLENVVKDNGDNLGVLQQRLKSADAKNKELLKGLDENLAVLraipndtaAKLMATKQKA 2013
Cdd:COG4942 45 ALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL--------AELLRALYRL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2014 SKANdtAIEVLARLKDMNQNLMGLNRNFSTLKDDINKANNLIQDPEKNTiihaagAKVKDLEDEAERLLEKLKPIRELQD 2093
Cdd:COG4942 117 GRQP--PLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELA------ALRAELEAERAELEALLAELEEERA 188
|
170 180
....*....|....*....|....
gi 2196706209 2094 NLRKNISQIKELINQARKQANSIK 2117
Cdd:COG4942 189 ALEALKAERQKLLARLEKELAELA 212
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1620-1956 |
1.64e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 47.51 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1620 ELLSRANKVSADgeQTDSDAER--SHKRAQD---LEQFVKNTL-----LAAEALRDKAReLNATLGRRDDGVEKSVNEMQ 1689
Cdd:NF041483 75 EQLLRNAQIQAD--QLRADAERelRDARAQTqriLQEHAEHQArlqaeLHTEAVQRRQQ-LDQELAERRQTVESHVNENV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1690 deikAMMNELRSRqlTHPHTHTVQEELRAAQDLLLKVQRgfAAPHRVSEELQQEVSSK------------LRDHDDklqg 1757
Cdd:NF041483 152 ----AWAEQLRAR--TESQARRLLDESRAEAEQALAAAR--AEAERLAEEARQRLGSEaesaraeaeailRRARKD---- 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1758 AQELLE----EAQNNIGNARTLNSDNLRRLEEVQRKRNESSK----KKKETEGILE----DGEKILNEA---------NA 1816
Cdd:NF041483 220 AERLLNaastQAQEATDHAEQLRSSTAAESDQARRQAAELSRaaeqRMQEAEEALRearaEAEKVVAEAkeaaakqlaSA 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1817 LSDDINRGTEELEEMKRDLGPLHDQLDYRVSRLAQVVED-----DKL------KDLVLRAENHAAQLNDSA----TILDR 1881
Cdd:NF041483 300 ESANEQRTRTAKEEIARLVGEATKEAEALKAEAEQALADaraeaEKLvaeaaeKARTVAAEDTAAQLAKAArtaeEVLTK 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1882 SSWPAKNLSfnaTAAFNAYSNIKNYIDeadkaaKQAKATATEAVQLATGPRGALKDEAK------ISLQ-KSQRLWNEAK 1954
Cdd:NF041483 380 ASEDAKATT---RAAAEEAERIRREAE------AEADRLRGEAADQAEQLKGAAKDDTKeyraktVELQeEARRLRGEAE 450
|
..
gi 2196706209 1955 NL 1956
Cdd:NF041483 451 QL 452
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1689-1872 |
1.95e-04 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 46.57 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1689 QDEIKAMMNELRSRQLthphthtVQEELRAAQdLLLKVQRGfaaphRVSEELQQEVSSKLRDHDDKLQGAQELLEEAQNn 1768
Cdd:pfam15558 40 RDQKRQETLERERRLL-------LQQSQEQWQ-AEKEQRKA-----RLGREERRRADRREKQVIEKESRWREQAEDQEN- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1769 ignartlnsdnlRRLEEVQRKRNESSKKKKETEGILEDGEKILNEANALSDDINRGTEELEEMKRDLGPLHDQLDYRVSR 1848
Cdd:pfam15558 106 ------------QRQEKLERARQEAEQRKQCQEQRLKEKEEELQALREQNSLQLQERLEEACHKRQLKEREEQKKVQENN 173
|
170 180
....*....|....*....|....*..
gi 2196706209 1849 LAQVVEDDKLKDLV---LRAENHAAQL 1872
Cdd:pfam15558 174 LSELLNHQARKVLVdcqAKAEELLRRL 200
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1968-2117 |
2.16e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.43 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1968 GVLQQRLKSADAKNKELLKGLDENLAVLRAIPNDTAAKLMATKQKASKANDTAIEVLARLKDMNQNLMGLNRNFSTLKDD 2047
Cdd:COG4372 23 GILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEE 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2048 INKANNliqdpEKNTIIhaagAKVKDLEDEAERLLEKLKPIRELQDNLRKNISQIKELINQARKQANSIK 2117
Cdd:COG4372 103 LESLQE-----EAEELQ----EELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQ 163
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1795-2113 |
2.39e-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: 46.97 E-value: 2.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1795 KKKKETEgiledgeKILNEANalsDDINRGTEELEEMKRDLGPLHDQldyrvSRLAQvveddKLKDlvLRAENHAAQLND 1874
Cdd:TIGR02168 172 ERRKETE-------RKLERTR---ENLDRLEDILNELERQLKSLERQ-----AEKAE-----RYKE--LKAELRELELAL 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1875 SATILD--RSSWPAKNLSFNATAA-FNAYSNIKNYIDEADKAAKQAKATATEAVQLATGPRGALKDE-AKISLQKsQRLW 1950
Cdd:TIGR02168 230 LVLRLEelREELEELQEELKEAEEeLEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEiSRLEQQK-QILR 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1951 NEAKNLENvvkdngdNLGVLQQRLKSADAKNKELLkgldENLAVLRAIPNDTAAKLMATKQKASKANDTAIEVLARLKDM 2030
Cdd:TIGR02168 309 ERLANLER-------QLEELEAQLEELESKLDELA----EELAELEEKLEELKEELESLEAELEELEAELEELESRLEEL 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2031 NQNLMGLNRNFSTLKDDINKANNLIQdpekntiihAAGAKVKDLEDEAERLL-EKLKPIRELQDNLRKNISQIKELINQA 2109
Cdd:TIGR02168 378 EEQLETLRSKVAQLELQIASLNNEIE---------RLEARLERLEDRRERLQqEIEELLKKLEEAELKELQAELEELEEE 448
|
....
gi 2196706209 2110 RKQA 2113
Cdd:TIGR02168 449 LEEL 452
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1696-1874 |
2.49e-04 |
|
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: 45.30 E-value: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1696 MNELRSRQLTHPhthtvqEELRAAQDLLLKVQRGFAAPHRVSEELQQEvsskLRDHDDKLQGAQELLEEAQNNIGNARtl 1775
Cdd:COG1579 19 LDRLEHRLKELP------AELAELEDELAALEARLEAAKTELEDLEKE----IKRLELEIEEVEARIKKYEEQLGNVR-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1776 NSDNLRRLE---EVQRKRNESSKKKketegILEdgekILNEANALSDDINRGTEELEEMKRDLGPLHDQLDYRVSRLaqv 1852
Cdd:COG1579 87 NNKEYEALQkeiESLKRRISDLEDE-----ILE----LMERIEELEEELAELEAELAELEAELEEKKAELDEELAEL--- 154
|
170 180
....*....|....*....|..
gi 2196706209 1853 veDDKLKDLVLRAENHAAQLND 1874
Cdd:COG1579 155 --EAELEELEAEREELAAKIPP 174
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1615-1878 |
3.24e-04 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 46.44 E-value: 3.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1615 VTEMDELLSRAnkvsadgEQTDSDAERSHKRAQDLEQFVKNTLLAAEALRDKARElnatlGRRDDGVEKsvnEMQDEIKA 1694
Cdd:COG5278 85 RAEIDELLAEL-------RSLTADNPEQQARLDELEALIDQWLAELEQVIALRRA-----GGLEAALAL---VRSGEGKA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1695 MMNELRSRQLTHPHTHTVQEELRAAQDLLLKVQRGFAAPHRVSEELQQEVSSKLRDHDDKLQGAQELLEEAQNNIGNART 1774
Cdd:COG5278 150 LMDEIRARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAAL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1775 LNSDNLRRLEEVQRKRNESSKKKKETEGILEDGEKILNEANALSDDINRGTEELEEMKRDLGPLHDQLDYRVSRLAQVVE 1854
Cdd:COG5278 230 AALELLAALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLA 309
|
250 260
....*....|....*....|....
gi 2196706209 1855 DDKLKDLVLRAENHAAQLNDSATI 1878
Cdd:COG5278 310 AAAAAAAAAAAAAAALAALLALAL 333
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1598-2115 |
3.75e-04 |
|
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: 46.37 E-value: 3.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1598 RAPERLLQLADSNLGSLVTEMDELLSRANKVSAdgeqtdsdAERSHK----RAQDLEQ-FVKNTLLAAEALRDKARELNA 1672
Cdd:pfam12128 326 ALEDQHGAFLDADIETAAADQEQLPSWQSELEN--------LEERLKaltgKHQDVTAkYNRRRSKIKEQNNRDIAGIKD 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1673 TLGRRDDGVEKSVNEMQDEIKAMMNELRSrQLTHPHTHTVQEELRAAQDL-LLKVQrgFAAPHRVSEEL-QQEVSSKLRD 1750
Cdd:pfam12128 398 KLAKIREARDRQLAVAEDDLQALESELRE-QLEAGKLEFNEEEYRLKSRLgELKLR--LNQATATPELLlQLENFDERIE 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1751 H-DDKLQGAQELLEEAQNNIGNARTLNSDNLRRLEEVQRKRNESSKKKKETEGILEDGEKIL-----NEANALSDDINR- 1823
Cdd:pfam12128 475 RaREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLlhflrKEAPDWEQSIGKv 554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1824 -GTEELeeMKRDLGP-----------------LH-DQLDYRVS---------RLAQVVED-DKLKDLVLRAENHAAQLND 1874
Cdd:pfam12128 555 iSPELL--HRTDLDPevwdgsvggelnlygvkLDlKRIDVPEWaaseeelreRLDKAEEAlQSAREKQAAAEEQLVQANG 632
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1875 SatiLDRSSwpaKNLSFNATAAFNAYSNIKNYIDEADKAAKQAKATATEAVQLATGPRGALKDEAKIsLQKSQRLWNEAK 1954
Cdd:pfam12128 633 E---LEKAS---REETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQ-LDKKHQAWLEEQ 705
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1955 NlenvvkdnGDNLGVLQQRLksadAKNKELLKGLDENLAVLRAIpndtaaklMATKQKASKANDTAIEvlarlKDMNQNL 2034
Cdd:pfam12128 706 K--------EQKREARTEKQ----AYWQVVEGALDAQLALLKAA--------IAARRSGAKAELKALE-----TWYKRDL 760
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2035 MGLN---RNFSTLKDDINKANNLIQDPEKNtiihaaGAKVKDLED--------EAERLLEKLKPI----RELQDNLRKNI 2099
Cdd:pfam12128 761 ASLGvdpDVIAKLKREIRTLERKIERIAVR------RQEVLRYFDwyqetwlqRRPRLATQLSNIeraiSELQQQLARLI 834
|
570
....*....|....*.
gi 2196706209 2100 SQIKELINQARKQANS 2115
Cdd:pfam12128 835 ADTKLRRAKLEMERKA 850
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1439-1493 |
4.37e-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: 40.42 E-value: 4.37e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2196706209 1439 PCACplsNPENNFSPSCVTEgfsDYRCTaCPEGYIGKYCERCATGYHGDPRRAGG 1493
Cdd:cd00055 1 PCDC---NGHGSLSGQCDPG---TGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1738-2147 |
4.39e-04 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 46.36 E-value: 4.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1738 EELQQEVSSKLRDHDDKLQGAQELLEEAQNNIGNArtlnSDNLRRLEEVQRKRNESSKKKKETEGI-----LEDGEKILN 1812
Cdd:PTZ00440 1362 EQIKEEISNKRKEINKYLSNIKSNKEKCDLHVRNA----SRGKDKIDFLNKHEAIEPSNSKEVNIIkitdnINKCKQYSN 1437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1813 EANALSDDINRGTEELEEMKRDLGPLHDQldyrVSRLAQVVEDDKLKDlvlRAENHAAQLNDSATILDRSSwpaKNLSFN 1892
Cdd:PTZ00440 1438 EAMETENKADENNDSIIKYEKEITNILNN----SSILGKKTKLEKKKK---EATNIMDDINGEHSIIKTKL---TKSSEK 1507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1893 ataaFNAYSNIKNYIDEADKAAKQAKATATEAVQLATGP-RGALKDEAKISlQKSQRLWNEAKNLENVVKDNGDNLGVLQ 1971
Cdd:PTZ00440 1508 ----LNQLNEQPNIKREGDVLNNDKSTIAYETIQYNLGRvKHNLLNILNIK-DEIETILNKAQDLMRDISKISKIVENKN 1582
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1972 -QRLKSADAKNKELLkgldENLAVLRAIPNDTAAKLMATKQ---------KASKANdTAIEVLARLKDMNQN-------- 2033
Cdd:PTZ00440 1583 lENLNDKEADYVKYL----DNILKEKQLMEAEYKKLNEIYSdvdniekelKKHKKN-YEIGLLEKVIEINKNiklymdst 1657
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2034 ---LMGLNRNFSTLKD--DINKANnliqdPEKNTIIHAAgaKVKDLEDEAERLLEKL--KPIRELQDNLrkNISQIKELi 2106
Cdd:PTZ00440 1658 kesLNSLVNNFSSLFNnfYLNKYN-----INENLEKYKK--KLNEIYNEFMESYNIIqeKMKEVSNDDV--DYNEAKTL- 1727
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2196706209 2107 nqaRKQANSIKVSVSSGGDCIRTYRPDIKKGRYNTIVLNVK 2147
Cdd:PTZ00440 1728 ---REEAQKEEVNLNNKEEEAKKYLNDIKKQESFRFILYMK 1765
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1659-1835 |
4.41e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 4.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1659 AAEALRDKARELNATLGRRDDgVEKSVNEMQDEIKAMMNELRSrqlthphthtVQEELRAAQDLLLKVQRGFAAPHRVSE 1738
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEA-AQAELDALQAELEELNEEYNE----------LQAELEALQAEIDKLQAEIAEAEAEIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1739 ELQQEVSSKLRD--HDDKLQGAQELLEEAQN------NIGNARTLNSDNLRRLEEVQRKRNESSKKKKETEGILEDGEKI 1810
Cdd:COG3883 83 ERREELGERARAlyRSGGSVSYLDVLLGSESfsdfldRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEAL 162
|
170 180
....*....|....*....|....*
gi 2196706209 1811 LNEANALSDDINRGTEELEEMKRDL 1835
Cdd:COG3883 163 KAELEAAKAELEAQQAEQEALLAQL 187
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1633-1881 |
6.61e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 6.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1633 EQTDSDAERSHKRAQDLEQfvkntllAAEALRDKARELNATLGRRDDgvEKSVNEMQDEIKAMMNELRSRQLTHPhthtv 1712
Cdd:COG4913 620 AELEEELAEAEERLEALEA-------ELDALQERREALQRLAEYSWD--EIDVASAEREIAELEAELERLDASSD----- 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1713 qeELRAAQDLLLKVQRGFAAphrvSEELQQEVSSKLRDHDDKLQGAQELLEEAQNNIGNARTLNSDNLR-----RLEEVQ 1787
Cdd:COG4913 686 --DLAALEEQLEELEAELEE----LEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRalleeRFAAAL 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1788 RKRNESSKKKKETEGILEDGEKILNEANALSDDINRGTEELEEMKRDLGP-LHDQLDYRvSRLAQVVEDD------KLKD 1860
Cdd:COG4913 760 GDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDAdLESLPEYL-ALLDRLEEDGlpeyeeRFKE 838
|
250 260
....*....|....*....|....*..
gi 2196706209 1861 LVLRAENH-----AAQLNDSA-TILDR 1881
Cdd:COG4913 839 LLNENSIEfvadlLSKLRRAIrEIKER 865
|
|
| COG4192 |
COG4192 |
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ... |
1575-1769 |
7.30e-04 |
|
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal transduction mechanisms];
Pssm-ID: 443346 [Multi-domain] Cd Length: 640 Bit Score: 45.06 E-value: 7.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1575 PPYGALYRVENMTDELKHMLsPH----RAPERLLQLADsNLGSLVTEMDELLSranKVSADGEQTDSDAERSHKRAQDLE 1650
Cdd:COG4192 52 PKLQASLKLEENSNELVAAL-PEfaaaTNTTERSQLRN-QLNTQLADIEELLA---ELEQLTQDAGDLRAAVADLRNLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1651 QF---VKNTLLAAEALRDKARELNATlgrRDDgveksvneMQDEIKAMMNELRSRQLTHPHTHTVQEELRAAQDLLLKVQ 1727
Cdd:COG4192 127 QLdslLTQRIALRRRLQELLEQINWL---HQD--------FNSELTPLLQEASWQQTRLLDSVETTESLRNLQNELQLLL 195
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2196706209 1728 RGFAAPHRVSEELqQEVSSkLRDHDDKLQGA---QELLEEAQNNI 1769
Cdd:COG4192 196 RLLAIENQIVSLL-REVAA-ARDQADVDNLFdrlQYLKDELDRNL 238
|
|
| TNFRSF16 |
cd13416 |
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 ... |
1364-1440 |
7.64e-04 |
|
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 neurotrophin receptor (p75NTR) or CD271; TNFRSF16 (also known as nerve growth factor receptor (NGFR) or p75 neurotrophin receptor (p75NTR or p75(NTR)), CD271, Gp80-LNGFR) is a common receptor for both neurotrophins and proneurotrophins, and plays a diverse role in many tissues, including the nervous system. It has been shown to be expressed in various types of stem cells and has been used to prospectively isolate stem cells with different degrees of potency. p75NTR owes its signaling to the recruitment of intracellular binding proteins, leading to the activation of different signaling pathways. It binds nerve growth factor (NGF) and the complex can initiate a signaling cascade which has been associated with both neuronal apoptosis and neuronal survival of discrete populations of neurons, depending on the presence or absence of intracellular signaling molecules downstream of p75NTR (e.g. NF-kB, JNK, or p75NTR intracellular death domain). p75NTR can also bind NGF in concert with the neurotrophic tyrosine kinase receptor type 1 (TrkA) protein where it is thought to modulate the formation of the high-affinity neurotrophin binding complex. On melanoma cell, p75NTR is an immunosuppressive factor, induced by interferon (IFN)-gamma, and mediates down-regulation of melanoma antigens. It can interact with the aggregated form of amyloid beta (Abeta) peptides, and plays an important role in etiopathogenesis of Alzheimer's disease by influencing protein tau hyper-phosphorylation. p75(NTR) is involved in the formation and progression of retina diseases; its expression is induced in retinal pigment epithelium (RPE) cells and its knockdown rescues RPE cell proliferation activity and inhibits RPE apoptosis induced by hypoxia. It can therefore be a potential therapeutic target for RPE hypoxia or oxidative stress diseases.
Pssm-ID: 276921 [Multi-domain] Cd Length: 159 Bit Score: 42.67 E-value: 7.64e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2196706209 1364 ECAAGFYRLSSrvsvsrfrsgMGSCVRCEcnghsvSCDPDTGVCQNCQHNTEGEkCERCSAGFYGVVRGSPDDCKPC 1440
Cdd:cd13416 79 ECAYGYYLDED----------SGTCEPCT------VCPPGQGVVQSCGPNQDTV-CEACPEGTYSDEDSSTDPCLPC 138
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
292-315 |
8.44e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 39.60 E-value: 8.44e-04
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1761-2153 |
9.42e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 45.43 E-value: 9.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1761 LLEEAQNNIG-NARTLNSDNLRRLEEVQRKRNESSKKKKE---TEGILEDGEKILNEANALSDDI-------NRGTEELE 1829
Cdd:TIGR01612 1056 IIDEIEKEIGkNIELLNKEILEEAEINITNFNEIKEKLKHynfDDFGKEENIKYADEINKIKDDIknldqkiDHHIKALE 1135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1830 EMKRDLGPLHDQLDYRVSRLAQV----VEDDKLKDLVLRAENhaaqlndSATILDRSSwpaknlsfnataafNAYSNIKN 1905
Cdd:TIGR01612 1136 EIKKKSENYIDEIKAQINDLEDVadkaISNDDPEEIEKKIEN-------IVTKIDKKK--------------NIYDEIKK 1194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1906 YIDE-ADKAAKQAKATATEAVQLATGPR-GAL----KDEAKislQKSQrlwNEAKNLENVVKD---------NGDNLGVL 1970
Cdd:TIGR01612 1195 LLNEiAEIEKDKTSLEEVKGINLSYGKNlGKLflekIDEEK---KKSE---HMIKAMEAYIEDldeikekspEIENEMGI 1268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1971 QQRLK----------SADAKNKELLKGLDENLAVLRaipnDTAAKLMATKQKASKANDTAIEVLARL-------KDMNQN 2033
Cdd:TIGR01612 1269 EMDIKaemetfnishDDDKDHHIISKKHDENISDIR----EKSLKIIEDFSEESDINDIKKELQKNLldaqkhnSDINLY 1344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2034 LMGLNRNFSTLKddINKANNLIQDPEKNT-IIHAAGAKVKDLEDEAERLLEKLKPirelQDNLRKNISQIKEL-----IN 2107
Cdd:TIGR01612 1345 LNEIANIYNILK--LNKIKKIIDEVKEYTkEIEENNKNIKDELDKSEKLIKKIKD----DINLEECKSKIESTlddkdID 1418
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2196706209 2108 QARKQANSIKVSVSSGGDCIRTYRPDIKKGRYNtIVLNVKTLA-ADN 2153
Cdd:TIGR01612 1419 ECIKKIKELKNHILSEESNIDTYFKNADENNEN-VLLLFKNIEmADN 1464
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1713-1843 |
1.08e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 44.68 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1713 QEELRAAQDLLLKVQRGFAA----PHRVSEELQQEVS--SKLRDHDDKLQGAQELLEEAQNNIGNA-RTLNS--DNL--- 1780
Cdd:COG0497 215 RRRLSNAEKLREALQEALEAlsggEGGALDLLGQALRalERLAEYDPSLAELAERLESALIELEEAaSELRRylDSLefd 294
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2196706209 1781 -RRLEEVQRKRNE--SSKKK--KETEGILEDGEKILNEANALSDdinrGTEELEEMKRDLGPLHDQLD 1843
Cdd:COG0497 295 pERLEEVEERLALlrRLARKygVTVEELLAYAEELRAELAELEN----SDERLEELEAELAEAEAELL 358
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1970-2117 |
1.11e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1970 LQQRLKSADAKnkelLKGLDENLAVLRAIPNDTAAKLMATKQKASKAN----------DTAIEVLA-RLKDMNQNLMGLN 2038
Cdd:COG3883 28 LQAELEAAQAE----LDALQAELEELNEEYNELQAELEALQAEIDKLQaeiaeaeaeiEERREELGeRARALYRSGGSVS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2039 --------RNFSTLkddINKANNL--IQDPEKNtIIHAAGAKVKDLEDEAERLLEKLKPIRELQDNLRKNISQIKELINQ 2108
Cdd:COG3883 104 yldvllgsESFSDF---LDRLSALskIADADAD-LLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAE 179
|
....*....
gi 2196706209 2109 ARKQANSIK 2117
Cdd:COG3883 180 QEALLAQLS 188
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1952-2117 |
1.13e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.44 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1952 EAKNLENVVKDNGDNLGVLqqRLKSADAKNKELLKGLDENLAVLRaipndtaaKLMATKQKASKANDTAIEVLARLKDMN 2031
Cdd:PRK04778 257 EIQDLKEQIDENLALLEEL--DLDEAEEKNEEIQERIDQLYDILE--------REVKARKYVEKNSDTLPDFLEHAKEQN 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2032 QNLMG----LNRNFS----------TLKDDINKANNLIQDPEKNTiihAAGAKV-KDLEDEAERLLEKLKPIRELQDNLR 2096
Cdd:PRK04778 327 KELKEeidrVKQSYTlneselesvrQLEKQLESLEKQYDEITERI---AEQEIAySELQEELEEILKQLEEIEKEQEKLS 403
|
170 180
....*....|....*....|.
gi 2196706209 2097 KNISQIKELINQARKQANSIK 2117
Cdd:PRK04778 404 EMLQGLRKDELEAREKLERYR 424
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2018-2125 |
1.27e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.75 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2018 DTAIEVLARLKDMNQNLMGLNRNFSTLKDDINKANNLIQDP--EKNTIIhaagAKVKDLEDEAERLLEK----LKPIREL 2091
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELaeKRDELN----AQVKELREEAQELREKrdelNEKVKEL 76
|
90 100 110
....*....|....*....|....*....|....
gi 2196706209 2092 QDNLRKNISQIKELINQARKQANSIKVSVSSGGD 2125
Cdd:COG1340 77 KEERDELNEKLNELREELDELRKELAELNKAGGS 110
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1781-2179 |
1.42e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.74 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1781 RRLEEVQRKRNESSKKKKETEGI-----------LEDGEKILNEANALSDDINRGTEELEEMKRDLGPLHDQLDYRVSRL 1849
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILiaalseqlrkaLFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1850 AQVveDDKLKDLVLRAENHAAQLNdsatildrsswpaknlsfnataafnaysniknyideadkaakqakatateavqlat 1929
Cdd:COG4372 83 EEL--NEQLQAAQAELAQAQEELE-------------------------------------------------------- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1930 gprgALKDEAKISLQKSQRLWNEAKNLENVVKDNGDNLGVLQQRLKSADAKNKELLKGLDENLAVLraipndtaAKLMAT 2009
Cdd:COG4372 105 ----SLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEEL--------AALEQE 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2010 KQKASKANdtAIEVLARL-KDMNQNLMGLNRNFSTLKDDINKANNLIQDPE--KNTIIHAAGAKVKDLEDEAERLLEKLK 2086
Cdd:COG4372 173 LQALSEAE--AEQALDELlKEANRNAEKEEELAEAEKLIESLPRELAEELLeaKDSLEAKLGLALSALLDALELEEDKEE 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2087 PIRELQDNLRKN----ISQIKELINQARKQANSIKVSVSSGGDCIRTYRPDIKKGRYNTIVLNVKTLAADNLLFYLGSAK 2162
Cdd:COG4372 251 LLEEVILKEIEElelaILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLEL 330
|
410
....*....|....*..
gi 2196706209 2163 FVDFLAIEMRKGK*NFL 2179
Cdd:COG4372 331 ALAILLAELADLLQLLL 347
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1710-1861 |
1.47e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.99 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1710 HTVQEELRAAQDLLLKVQRgfaaphrvSEELQQEVSSKLRDHDDKLQGAQELLEEAQNNIGNARTLNSDNLRRLEEVQRK 1789
Cdd:COG1579 3 PEDLRALLDLQELDSELDR--------LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1790 RNESSKKK------KETEGILEDGEKILNEANALSDDINRGTEELEEMKRDLGPLHDQLDYRVSRLAQVVE--DDKLKDL 1861
Cdd:COG1579 75 IKKYEEQLgnvrnnKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAelDEELAEL 154
|
|
| DUF445 |
pfam04286 |
Protein of unknown function (DUF445); Predicted to be a membrane protein. |
1641-1872 |
1.86e-03 |
|
Protein of unknown function (DUF445); Predicted to be a membrane protein.
Pssm-ID: 427840 [Multi-domain] Cd Length: 368 Bit Score: 43.38 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1641 RSHKR-AQDLEQFVKNTLLAAEALRDKARELN--ATLGR--RDDGVEKSVNEMQDEI-KAMMNELRSRQlthphthtVQE 1714
Cdd:pfam04286 36 RNKDRiAENLGNFVEEHLLTPEVLARKLREADpaERLGRwlADPTNAERLAREVAKLlAEILEDLDDER--------VQR 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1715 ELRAA-------QDLLLKVQRGFAAP------HRVSEELQQEVSSKLRDHDDKLQgAQELLEEAQNNIGNaRTLNSDNLR 1781
Cdd:pfam04286 108 LLKKAlrrrleeIDLAPLLGKLLELLlaegrhQALLDDLLDRLRDWLRSEEGKQR-IAEMIDEFLEEWGP-LVALLGGIA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1782 R---------LEEVQR-----KRNESSKKKKETEGILEDGEKILNEANAL------SDDINRGTEEL-----EEMKRDLG 1836
Cdd:pfam04286 186 EmilralsslLDEVQAdpdhpLRLAFDRAVRELITDLLNDPELRAEVEELkqkllaDPAVQDYVKALweslrSLLLDDLS 265
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2196706209 1837 PLHDQLDYRVSRLAQ-----VVEDDKLKDLVLR-AENHAAQL 1872
Cdd:pfam04286 266 DPDSALRRRISELLAefgerLAEDPELRDKLNEhLEDAAVGL 307
|
|
| TSPN |
smart00210 |
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ... |
2957-3105 |
2.01e-03 |
|
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of thrombospondin
Pssm-ID: 214560 Cd Length: 184 Bit Score: 41.96 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2957 GTGYAKAVSTYRVGN------------------EVTVALEFR-TSTATGVLLGV-SGQTMDGLGIELING--KLLFHADN 3014
Cdd:smart00210 20 VVGPEPGSPAYRLGDpalvpqptrdlfpsglpeDFSLLTTFRqTPKSRGVLFAIyDAQNVRQFGLEVDGRanTLLLRYQG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 3015 GVGRV-TATSQGAGLCDGQWHSVTAHKLKHRLELIVDGQKSEAASPDASSASADTNDPVFVGGypeglkqFGLTTSAPFK 3093
Cdd:smart00210 100 VDGKQhTVSFRNLPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGQPPIDTDGIEVRG-------AQAADRKPFQ 172
|
170
....*....|..
gi 2196706209 3094 GCMRNIKLIKAG 3105
Cdd:smart00210 173 GDLQQLKIVCDP 184
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1720-2148 |
2.24e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 44.05 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1720 QDLLLKVQRGFAAphrvSEELQQEVSSKL------RDHDDKLQGAQELLEE-----------AQNNIGNARTLNSDNLRR 1782
Cdd:PTZ00440 1038 KEIEEKVDQYISL----LEKMKTKLSSFHfnidikKYKNPKIKEEIKLLEEkveallkkideNKNKLIEIKNKSHEHVVN 1113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1783 LEEVQRKRNES-SKKKKETEGILEDGEKILNEANALSDDINRGTEELE-EMKRDLGPLHD---QLDYRVSRLAQVVEDDK 1857
Cdd:PTZ00440 1114 ADKEKNKQTEHyNKKKKSLEKIYKQMEKTLKELENMNLEDITLNEVNEiEIEYERILIDHiveQINNEAKKSKTIMEEIE 1193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1858 L--KDLVLRAENHAAQLNDSATildrsswpaknlSFNATAAFNAYSNIKNYIDEAdkaakqakatateaVQLATGPRG-- 1933
Cdd:PTZ00440 1194 SykKDIDQVKKNMSKERNDHLT------------TFEYNAYYDKATASYENIEEL--------------TTEAKGLKGea 1247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1934 -ALKDEAKISLQKSQRLwneaKNLENVVKDNGDnlgvLQQRLKsaDAKN-KELLKGLDENlAVLRAIPNDTAAKLMATKQ 2011
Cdd:PTZ00440 1248 nRSTNVDELKEIKLQVF----SYLQQVIKENNK----MENALH--EIKNmYEFLISIDSE-KILKEILNSTKKAEEFSND 1316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2012 -----------------KASKANDTAIEVLARLKDMN-----QNLMGLNRNFSTLKDDINKANNLIQDPEKNTIIHAAGA 2069
Cdd:PTZ00440 1317 akkelektdnlikqveaKIEQAKEHKNKIYGSLEDKQiddeiKKIEQIKEEISNKRKEINKYLSNIKSNKEKCDLHVRNA 1396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2070 KV-KDLEDeaerLLEKLKPIrelQDNLRK--NISQIKELINQARK---QANSIKVSVSSGGDCIRTYRPDIKKGRYNTIV 2143
Cdd:PTZ00440 1397 SRgKDKID----FLNKHEAI---EPSNSKevNIIKITDNINKCKQysnEAMETENKADENNDSIIKYEKEITNILNNSSI 1469
|
....*
gi 2196706209 2144 LNVKT 2148
Cdd:PTZ00440 1470 LGKKT 1474
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
786-841 |
2.46e-03 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 38.10 E-value: 2.46e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2196706209 786 CACPLQEPSnnfSPTCHLGEdgeVVCDrCPDGYSGSLCDRCDNGYFGSPRDVGGLC 841
Cdd:pfam00053 1 CDCNPHGSL---SDTCDPET---GQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1738-2113 |
3.58e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 3.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1738 EELQQEVSSKLRDHDDKLQGAQEL-LEEAQNNIGNARTLNSDNLRRLEEvqrKRNESSKKKKETEGILEDGEKILNEANA 1816
Cdd:PRK02224 179 ERVLSDQRGSLDQLKAQIEEKEEKdLHERLNGLESELAELDEEIERYEE---QREQARETRDEADEVLEEHEERREELET 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1817 LSDDINRGTEELEEMKRDlgplHDQLDYRVSRLAQVVED--DKLKDLVLRAENHAAqlnDSATILDRSSwpakNLSfnat 1894
Cdd:PRK02224 256 LEAEIEDLRETIAETERE----REELAEEVRDLRERLEEleEERDDLLAEAGLDDA---DAEAVEARRE----ELE---- 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1895 aafNAYSNIKNYIDEADKaakqakatateAVQLATGPRGALKDEAKISLQKSQRLWNEAKNLENVVKDNgdnlgvlqqrl 1974
Cdd:PRK02224 321 ---DRDEELRDRLEECRV-----------AAQAHNEEAESLREDADDLEERAEELREEAAELESELEEA----------- 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1975 KSADAKNKELLKGLDENLAVLRAIPNDTAAKLmatkqkaSKANDTAIEVLARLKDMNQNLMGLNRNFSTLKDDINKANNL 2054
Cdd:PRK02224 376 REAVEDRREEIEELEEEIEELRERFGDAPVDL-------GNAEDFLEELREERDELREREAELEATLRTARERVEEAEAL 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2055 I---------QDPEKNTII------------------------------HAAGAKVKDLEDEAERLLEKLKPIRELQDNL 2095
Cdd:PRK02224 449 LeagkcpecgQPVEGSPHVetieedrerveeleaeledleeeveeveerLERAEDLVEAEDRIERLEERREDLEELIAER 528
|
410
....*....|....*...
gi 2196706209 2096 RKNISQIKELINQARKQA 2113
Cdd:PRK02224 529 RETIEEKRERAEELRERA 546
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1626-2114 |
3.70e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 43.28 E-value: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1626 NKVSADGEQTDSDAE-----------RSHKRAQDLEQFVKNTLLA-----AEALRDKARELNATLgrrdDGVEKSVNEMQ 1689
Cdd:PTZ00440 2054 DAINTNIEDIEKEIEsinpsldellkKGHKIEISRYTSIIDNVQTkisndSKNINDIEKKAQIYL----AYIKNNYNSIK 2129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1690 DEIKAMMNELRSRQLTHPHTHTVQEELRAAQDLLLKVQrgfaAPHRVSEELQQEVSSkLRDHD--DKLQGAQELLEEAQN 1767
Cdd:PTZ00440 2130 KDISTLNEYFDEKQVSNYILTNIDKANKLSSELSEAVT----NSEEIIENIKKEIIE-INENTemNTLENTADKLKELYE 2204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1768 NIGNARTL-----NSDNLRRLEEVQR-------------KRNESSKKKKET--------EGILEDGEKILNEA------- 1814
Cdd:PTZ00440 2205 NLKKKKNIinniyKKINFIKLQEIENssekyndisklfnNVVETQKKKLLDnknkinniKDKINDKEKELINVdssftle 2284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1815 -----NALSDDIN---RGTEELEEMKRDLG---PLHD----QLDYRVSRLAQVV----EDDKLKDLVLRAEN----HAAQ 1871
Cdd:PTZ00440 2285 siktfNEIYDDIKsniGDLYKLEDTNNDELkkvKLYIenitHLLNRINTLINDLdnyqDENYGKDKNIELNNennsYIIK 2364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1872 LNDSATILDRS-SWPAKNLSFNATAAFNaySNIKNYIDEADKAAKQAKATATEAVQLatgprgalkdeaKISLQKSQRLW 1950
Cdd:PTZ00440 2365 TKEKINNLKEEfSKLLKNIKRNNTLCNN--NNIKDFISNIGKSVETIKQRFSSNLPE------------KEKLHQIEENL 2430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1951 NEAKNLENVVKDNGDNLGVLQQRLKSADAkNKELLKGLDENLAVLRAIPNDTAAKlMATKQKASKANDTAIEVLARLKDM 2030
Cdd:PTZ00440 2431 NEIKNIMNETKRISNVDAFTNKILQDIDN-EKNKENNNMNAEKIDDLIENVTSHN-EKIKSELLIINDALRRVKEKKDEM 2508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 2031 NQNLMGLNRNFSTL----KDDINKANNLIQDPEK-----NTIIHAAGAKVKDLEDEAERLLEKLKpiRELQDNLRKNISQ 2101
Cdd:PTZ00440 2509 NKLFNSLTENNNNNnnsaKNIVDNSTYIINELEShvsklNELLSYIDNEIKELENEKLKLLEKAK--IEESRKERERIES 2586
|
570
....*....|...
gi 2196706209 2102 IKELINQARKQAN 2114
Cdd:PTZ00440 2587 ETQEDNTDEEQIN 2599
|
|
| F5_F8_type_C |
pfam00754 |
F5/8 type C domain; This domain is also known as the discoidin (DS) domain family. |
75-159 |
3.76e-03 |
|
F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.
Pssm-ID: 459925 [Multi-domain] Cd Length: 127 Bit Score: 40.12 E-value: 3.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 75 SERPYERHPIEFAIDG--TNRWwqspSIKNGMDYHYvtITLDLQQVFQIAYVILKAANSPRPGN---WVLERSLDGETFT 149
Cdd:pfam00754 5 SSSYSGEGPAAAALDGdpNTAW----SAWSGDDPQW--IQVDLGKPKKITGVVTQGRQDGSNGYvtsYKIEYSLDGENWT 78
|
90
....*....|
gi 2196706209 150 PWQYFAITDT 159
Cdd:pfam00754 79 TVKDEKIPGN 88
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1601-1815 |
3.76e-03 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 41.66 E-value: 3.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1601 ERLLQLADsNLGSLVTEMDELLSrankvSADGEQTDSDAERSHKRAQDLEQFVKNTLLAAEALRDKARELNATLGRRDDG 1680
Cdd:cd00176 3 QQFLRDAD-ELEAWLSEKEELLS-----STDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1681 VEKSVNEMQ---DEIKAMMNElRSRQLThpHTHTVQEELRAAQDLL--LKVQRGFAAPHRVSEELqQEVSSKLRDHDD-- 1753
Cdd:cd00176 77 IQERLEELNqrwEELRELAEE-RRQRLE--EALDLQQFFRDADDLEqwLEEKEAALASEDLGKDL-ESVEELLKKHKEle 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2196706209 1754 -KLQGAQELLEEAqNNIGNArTLNSDNLRRLEEVQRKRNESSKKKKETEGILEDGEKILNEAN 1815
Cdd:cd00176 153 eELEAHEPRLKSL-NELAEE-LLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| VSP |
pfam03302 |
Giardia variant-specific surface protein; |
764-1087 |
4.64e-03 |
|
Giardia variant-specific surface protein;
Pssm-ID: 146106 [Multi-domain] Cd Length: 397 Bit Score: 42.26 E-value: 4.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 764 CDLCSPGYYGDATRGTSHDCRPCACPLQEPSNNfsptchlgeDGEVVCDRC-------PDGYSGSLCDRCDNGYFGSPRD 836
Cdd:pfam03302 1 CDECKPGYELSADKTKCTSSAPCKTENCKACSN---------DKREVCEECnsnnyltPTSQCIDDCAKIGNYYYTTNAN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 837 VGGLCRPCSCSGNLdlsvarSCDPlTGACLHCRRGY---------AGPNCETCADGYYGDAVgakncqlcECNSNGSVSE 907
Cdd:pfam03302 72 NKKICKECTVANCK------TCED-QGQCQACNDGFyksgdacspCHESCKTCSGGTASDCT--------ECLTGKALRY 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 908 VCNKESGQC--QCLQRVLGRACDQCspGTHMQAGSGCVPCHCNSFGSKSFDCSESGQ-----CRCQPGVTGqKCDRCSHG 980
Cdd:pfam03302 137 GNDGTKGTCgeGCTTGTGAGACKTC--GLTIDGTSYCSECATETEYPQNGVCTSTAAratatCKASSVANG-MCSSCANG 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 981 HFNfQEGGC---------TPCECSHVGNNCD---PGTGRCLCPLNTVGDRCEKCAPNhwghdiaTGCKACGCHVTGAVTQ 1048
Cdd:pfam03302 214 YFR-MNGGCyettkfpgkSVCEEANSGGTCQkeaPGYKLNNGDLVTCSPGCKTCTSN-------TVCTTCMDGYVKTSDS 285
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2196706209 1049 QCNVNTGCCFCRDEfkGEKCNECKLG-YRNFPHCVSCDCS 1087
Cdd:pfam03302 286 CTKCDSSCETCTGA--TTTCKTCATGyYKSGTGCVSCTSS 323
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1970-2116 |
6.02e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 6.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1970 LQQ---RLKSADAKNKEL---LKGLDENLAVLRAIPNDTAAKLMATKQKASKANDTAIEVLARLKDMNQNLMGL--NRNF 2041
Cdd:COG1579 12 LQEldsELDRLEHRLKELpaeLAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnNKEY 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2196706209 2042 STLKDDINKANNLIQDpekntiihaagakvkdLEDEAERLLEKLKPIRELQDNLRKNISQIKELINQARKQANSI 2116
Cdd:COG1579 92 EALQKEIESLKRRISD----------------LEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEE 150
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1646-1821 |
6.07e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 6.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1646 AQDLEQFVK--NTLLAAEALRDKARELNATLGRRDD---GVEKSVNEMQDEIKAMMNELRsrqlthphthTVQEELRAAQ 1720
Cdd:COG1579 3 PEDLRALLDlqELDSELDRLEHRLKELPAELAELEDelaALEARLEAAKTELEDLEKEIK----------RLELEIEEVE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1721 DLLLKVQR--GFAAPHRVSEELQQEVSS---KLRDHDDKLQGAQELLEEAQNNIGNARTLNSDNLRRLEEVQRKRNEssk 1795
Cdd:COG1579 73 ARIKKYEEqlGNVRNNKEYEALQKEIESlkrRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDE--- 149
|
170 180
....*....|....*....|....*.
gi 2196706209 1796 kkkETEGILEDGEKILNEANALSDDI 1821
Cdd:COG1579 150 ---ELAELEAELEELEAEREELAAKI 172
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
1778-1856 |
6.23e-03 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 41.98 E-value: 6.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1778 DNLRR-----LEEVQRKRNESSK-----KKKEtegilEDGEKILNEANALSDDINRGTEELEEmkrdlgpLHDQLDYRVS 1847
Cdd:PRK05431 34 DEERRelqteLEELQAERNALSKeigqaKRKG-----EDAEALIAEVKELKEEIKALEAELDE-------LEAELEELLL 101
|
....*....
gi 2196706209 1848 RLAQVVEDD 1856
Cdd:PRK05431 102 RIPNLPHDS 110
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1661-1835 |
7.06e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 42.13 E-value: 7.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1661 EALRDKARELNATLGRRD-DGVEKSVNEMQDEIKAMM----NELRSRQLTHPHTHTVQEELRAAQD----LLLKVQRgfa 1731
Cdd:PRK04778 259 QDLKEQIDENLALLEELDlDEAEEKNEEIQERIDQLYdileREVKARKYVEKNSDTLPDFLEHAKEqnkeLKEEIDR--- 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1732 aphrVSE--ELQQEVSSKLRDHDDKLQGAQELLEEAQNNIGNARTLNSDNLRRLEEVQrkrnesskkkKETEGILEDGEK 1809
Cdd:PRK04778 336 ----VKQsyTLNESELESVRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEIL----------KQLEEIEKEQEK 401
|
170 180
....*....|....*....|....*.
gi 2196706209 1810 ILNEANALSDDINRGTEELEEMKRDL 1835
Cdd:PRK04778 402 LSEMLQGLRKDELEAREKLERYRNKL 427
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1755-2017 |
7.35e-03 |
|
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: 41.67 E-value: 7.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1755 LQGAQELLEEAQNNIGNARtlnsdnlRRLEEVQRKRNESSKKKKETEGILEDGEKILNEAN----ALSDDINRGTEELEE 1830
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQ-------QEIAELEKELAALKKEEKALLKQLAALERRIAALArrirALEQELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1831 MKRDLGPLHDQLDYRVSRLAQVVEddklkdlvlraenhAAQLNdsatildrSSWPAKNLSFNATAAFNAYSNIKnYIDEA 1910
Cdd:COG4942 88 LEKEIAELRAELEAQKEELAELLR--------------ALYRL--------GRQPPLALLLSPEDFLDAVRRLQ-YLKYL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 1911 DKAAKQAKATATEAVQLATGPRGALKDEAKISLQKSQRLWNEAKNLENVVKDNGDNLGVLQQRLKSADAKNKELLKGLDE 1990
Cdd:COG4942 145 APARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
250 260
....*....|....*....|....*..
gi 2196706209 1991 NLAVLRAIPNDTAAKLMATKQKASKAN 2017
Cdd:COG4942 225 LEALIARLEAEAAAAAERTPAAGFAAL 251
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
786-834 |
7.89e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 36.52 E-value: 7.89e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2196706209 786 CACPlqePSNNFSPTCHLgEDGevVCdRCPDGYSGSLCDRCDNGYFGSP 834
Cdd:smart00180 1 CDCD---PGGSASGTCDP-DTG--QC-ECKPNVTGRRCDRCAPGYYGDG 42
|
|
| TNFRSF |
cd00185 |
Tumor necrosis factor receptor superfamily (TNFRSF); Members of TNFR superfamily (TNFRSF) ... |
764-845 |
8.02e-03 |
|
Tumor necrosis factor receptor superfamily (TNFRSF); Members of TNFR superfamily (TNFRSF) interactions with TNF superfamily (TNFSF) ligands (TNFL) control key cellular processes such as differentiation, proliferation, apoptosis, and cell growth. Dysregulation of these pathways has been shown to result in a wide range of pathological conditions, including autoimmune diseases, inflammation, cancer, and viral infection. There are 29 very diverse family members of TNFRSF reported in humans: 22 are type I transmembrane receptors (single pass with the N terminus on extracellular side of the cell membrane) and have a clear signal peptide; the remaining 7 members are either type III transmembrane receptors (single pass with the N terminus on extracellular side of the membrane but no signal sequence; TNFR13B, TNFR13C, TNFR17, and XEDAR), or attached to the membrane via a glycosylphosphatidylinositol (GPI) linker (TNFR10C), or secreted as soluble receptors (TNFR11B and TNFR6B). All TNFRs contain relatively short cysteine-rich domains (CRDs) in the ectodomain, and are involved in interaction with the TNF homology domain (THD) of their ligands. TNFRs often have multiple CRDs (between one and six), with the most frequent configurations of three or four copies; most CRDs possess three disulfide bridges, but could have between one and four. Localized or genome-wide duplication and evolution of the TNFRSF members appear to have paralleled the emergence of the adaptive immune system; teleosts (i.e. ray-finned, bony fish), which possess an immune system with B and T cells, possess primary and secondary lymphoid organs, and are capable of adaptive responses to pathogens also display several characteristics that are different from the mammalian immune system, making teleost TNFSF orthologs and paralogs of interest to better understand immune system evolution and the immunological pathways elicited to pathogens.
Pssm-ID: 276900 [Multi-domain] Cd Length: 87 Bit Score: 37.96 E-value: 8.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196706209 764 CDLCSPGYY--GDATRGTSHDCRPCACPLQEPSNNFSPTCHLgedgevvCDRCPDGYSG---------SLCDRCDNGYFG 832
Cdd:cd00185 2 CQRCPPGEYlsSDCTATTDTVCSPCPPGTYSESWNSLSKCLP-------CTTCGGGNQVektpctatdNRCCTCKPGFYC 74
|
90
....*....|...
gi 2196706209 833 SPRDVGGLCRPCS 845
Cdd:cd00185 75 DEGTNVEECKPCT 87
|
|
| |
