|
Name |
Accession |
Description |
Interval |
E-value |
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
38-289 |
1.48e-92 |
|
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: 300.43 E-value: 1.48e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 38 HQQRGLFPAVLNLASSALITTNATCGEKGPEMYCKLVEHVpgqpVRNPQCRIChqNSSNPHLRHPITNAIDGKN----TW 113
Cdd:smart00136 2 GRPRSCYPPFVNLAFGREVTATSTCGEPGPERYCKLVGHT----EQGKKCDYC--DARNPRRSHPAENLTDGNNpnnpTW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 114 WQSPSIKNGIeyHYVTITLDLQQVFQIAYVIVKAAnSPRPGNWILERSLDDVDYKPWQYHAvtdTECLTLYNIyPRTGPP 193
Cdd:smart00136 76 WQSEPLSNGP--QNVNLTLDLGKEFHVTYVILKFC-SPRPSLWILERSDFGKTWQPWQYFS---SDCRRTFGR-PPRGPI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 194 SYAKDDEVICTSFYSKIHPLENGEIHISLINGRPSADDL--SPELLEFTSARYIRLRFQRIRTLNADLMMfahkdpreID 271
Cdd:smart00136 149 TKGNEDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDFdnSPVLQEWVTATNIRVRLTRLRTLGDELMD--------DR 220
|
250
....*....|....*...
gi 1814459924 272 PIVTRRYYYSVKDISVGG 289
Cdd:smart00136 221 PEVTRRYYYAISDIAVGG 238
|
|
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
43-289 |
3.27e-87 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 284.86 E-value: 3.27e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 43 LFPAVLNLASSALITTNATCGEKGPEMYCKLVEHVPGQpvrnpQCRIChqNSSNPHLRHPITNAIDGKN----TWWQSPS 118
Cdd:pfam00055 1 CYPAFGNLAFGREVSATSTCGLNGPERYCILSGLEGGK-----KCFIC--DSRDPHNSHPPSNLTDSNNgtneTWWQSET 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 119 IKngIEYHYVTITLDLQQVFQIAYVIVKAAnSPRPGNWILERSLD-DVDYKPWQYHAvtdTECLTLYNIypRTGPPSYAK 197
Cdd:pfam00055 74 GV--IQYENVNLTLDLGKEFHFTYLILKFK-SPRPAAMVLERSTDfGKTWQPYQYFA---SDCRRTFGR--PSGPSRGIK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 198 DDEVICTSFYSKIHPLENGEIHISLINGRPSA--DDLSPELLEFTSARYIRLRFQRIRTLNadlmmfahkDPREIDPIVT 275
Cdd:pfam00055 146 DDEVICTSEYSDISPLTGGEVIFSTLEGRPSAniFDYSPELQDWLTATNIRIRLLRLHTLG---------DELLDDPSVL 216
|
250
....*....|....
gi 1814459924 276 RRYYYSVKDISVGG 289
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 ... |
1598-1856 |
4.85e-84 |
|
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: 276.99 E-value: 4.85e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1598 MSIN-LTGPLPAPYKILYGLENMTQELKHLLSPQRAPERLIQLAEGNLNTLVTEMNELLTRATKVTADGEQTGQDAERTN 1676
Cdd:pfam06008 2 LSLNsLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1677 TRANSLGEFIKDLAQHAEAVSEKAVKLNETlgiQDKAFERNLQELQNEVDKMMTELRRKNLDTQKEVAEDELVAAEALLK 1756
Cdd:pfam06008 82 GHAKELAEAIKNLIDNIKEINEKVATLGEN---DFALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQDLLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1757 KVKKLFGESRGKNEEMEKDLREKLADYKSKVHDAWDLLREATDKIKEANLLSAENQKNMTALEKKKEAIESGKRQTEDTL 1836
Cdd:pfam06008 159 RIQTWFQSPQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEETL 238
|
250 260
....*....|....*....|
gi 1814459924 1837 KEGTDILDEANRLADEINSV 1856
Cdd:pfam06008 239 KTARDSLDAANLLLQEIDDA 258
|
|
| Laminin_II |
pfam06009 |
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 ... |
2041-2177 |
3.42e-49 |
|
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: 172.29 E-value: 3.42e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2041 VKDKARQANDTAKDVLAQIKDLHQNLDGLKKNYNQLADSVAKTNAVVKDpsKNKIIADADATVKNLEQEADRLIDKLKPI 2120
Cdd:pfam06009 1 SKELAREANETAKEVLEQLAPLSQNLENTSEKLSGINRSLEETNELVND--ANKALDDAGRSVKKLEELAPDLLDKLKPL 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2121 KELEDN---LKKNISEIKELINQARKQANSIKVSVSSGGDCIRTYKPEIKKGSYNSIIVN 2177
Cdd:pfam06009 79 KQLEVNsssLSDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTSL 138
|
|
| LamB |
smart00281 |
Laminin B domain; |
1233-1368 |
1.48e-48 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 169.75 E-value: 1.48e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1233 HLEPFYWKLPEQFEGKKLMAYGGKLKYTIYFEAREEtGFSTYNPQVIIRGGtpsHVRIIIRHMAAPLIGQLTRHEIEMTE 1312
Cdd:smart00281 1 DNEPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRRG-GTHVSAPDVILEGN---GLRISHPAEGPPLPDELTTVEVRFRE 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1814459924 1313 KKWKYYGddpriSRTVTREDFLDVLYDIHYILIKATYGNIMRQSRISEISLEVAEQ 1368
Cdd:smart00281 77 ENWQYYG-----GRPVTREDLMMVLANLTAILIRATYSQQMAGSRLSDVSLEVAVP 127
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
1238-1382 |
6.54e-46 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 162.82 E-value: 6.54e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1238 YWKLPEQFEGKKLMAYGGKLKYTIYFEAREETGFSTYNPQVIIRGGtpsHVRIIIRHMA--APLIGQLTRHEIEMTEKKW 1315
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGGGSLNSEPDVILEGN---GLRLSYSSPDqpPPDPGQEQTYSVRLHEENW 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1814459924 1316 KYygddpRISRTVTREDFLDVLYDIHYILIKATYGNIMRQSRISEISLEVAEQGRItamTPPAHLIE 1382
Cdd:pfam00052 78 RD-----SDGAPVSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSAVPGGS---GPPASWVE 136
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2797-2925 |
1.11e-44 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 159.02 E-value: 1.11e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2797 VRTEAESGLLFYMARINHADFATVQLRNGLPYFSYDLGSGDTNTMIPTKINDGHWHKIKIIRIKQEGIIYVDG-ASNRTI 2875
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGeARPTGE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1814459924 2876 SPKKADI-LDVVGMLYIGGLPINYTTRRIGPVTYSIDGCIRNLQMAEAPAD 2925
Cdd:pfam00054 81 SPLGATTdLDVDGPLYVGGLPSLGVKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
587-726 |
2.26e-41 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 149.73 E-value: 2.26e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 587 YWSAPALYLGNKLTAVGGQLTFTVSYDLEEEEEDTehILQLMIILEGNDLRISTAQDE-VYLQPSEEHINVLSLKEDLFT 665
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGGGSL--NSEPDVILEGNGLRLSYSSPDqPPPDPGQEQTYSVRLHEENWR 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1814459924 666 iHGTNFPVSRKEFMTVLANLKRVLIQITYSLGMDAIfRLSSVGLESAVPYPTDRSiAAAVE 726
Cdd:pfam00052 79 -DSDGAPVSREDFMMVLANLTAILIRATYSTGSGQV-SLSNVSLDSAVPGGSGPP-ASWVE 136
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2372-2511 |
9.57e-41 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 147.85 E-value: 9.57e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2372 FRTFSSNALLMYLATRDLKDFMSVELTDGHIKVSYDLGSGMASVVSNQNHNDGKWKSFTLSRTQKQANISIVDidtnqEE 2451
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDG-----EA 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1814459924 2452 NIATSSP-GNNFglDLKADDKIYFGGLPtlrNLSMKARPEVNLKKYSGCLRDIEISRTPYN 2511
Cdd:pfam00054 76 RPTGESPlGATT--DLDVDGPLYVGGLP---SLGVKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| LamB |
smart00281 |
Laminin B domain; |
582-714 |
3.19e-39 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 143.17 E-value: 3.19e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 582 LPQSYYWSAPALYLGNKLTAVGGQLTFTVSYDLeeeEEDTEHILQLMIILEGNDLRISTAQdEVYLQPSEEHINVLSLKE 661
Cdd:smart00281 1 DNEPVYWVAPEQFLGDKVTSYGGKLRYTLSFDG---RRGGTHVSAPDVILEGNGLRISHPA-EGPPLPDELTTVEVRFRE 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1814459924 662 DLFTIHGtNFPVSRKEFMTVLANLKRVLIQITYSLGMDAIfRLSSVGLESAVP 714
Cdd:smart00281 77 ENWQYYG-GRPVTREDLMMVLANLTAILIRATYSQQMAGS-RLSDVSLEVAVP 127
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2770-2919 |
2.15e-37 |
|
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: 138.71 E-value: 2.15e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2770 FGLSRNSHIAIAFDDTKvKNRLTIEFEVRTEAESGLLFYMARINHADFATVQLRNGLPYFSYDLGSGDTNTMIPTKINDG 2849
Cdd:cd00110 2 VSFSGSSYVRLPTLPAP-RTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1814459924 2850 HWHKIKIIRIKQEGIIYVDG-ASNRTISPKKADILDVVGMLYIGGLPINYTTRRIgPVTYSIDGCIRNLQM 2919
Cdd:cd00110 81 QWHSVSVERNGRSVTLSVDGeRVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGL-PVSPGFVGCIRDLKV 150
|
|
| LamG |
smart00282 |
Laminin G domain; |
2792-2919 |
1.22e-35 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 133.23 E-value: 1.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2792 TIEFEVRTEAESGLLFYMARINHADFATVQLRNGLPYFSYDLGSGDTNTMI-PTKINDGHWHKIKIIRIKQEGIIYVDG- 2869
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSdPTPLNDGQWHRVAVERNGRSVTLSVDGg 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2870 ASNRTISPKKADILDVVGMLYIGGLPINYtTRRIGPVTYSIDGCIRNLQM 2919
Cdd:smart00282 81 NRVSGESPGGLTILNLDGPLYLGGLPEDL-KLPPLPVTPGFRGCIRNLKV 129
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2178-2318 |
1.73e-34 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 129.74 E-value: 1.73e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2178 VKTAVADNLLFYLGSAKFIDFLAIEMRKGKVSFLWDVGSGVGRVEYPDlTIDDSYWYRIEASRTGRNGTISVRALDGPka 2257
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGD-KLNDGKWHSVELERNGRSGTLSVDGEARP-- 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1814459924 2258 simpstyHSASPPGYTIlDVDANAMLFVGGLTG-KLKKADAVRVITFTGCMGEAYFDSKPIG 2318
Cdd:pfam00054 78 -------TGESPLGATT-DLDVDGPLYVGGLPSlGVKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2945-3097 |
4.65e-34 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 129.46 E-value: 4.65e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2945 GTYFDGTGFAKAVDGFKVGLDLLVEFEFRTTRTTGVLLGISSQ-KMDGMGIEMIAEKLMFHVDNGAGRftAVYDAgiPGH 3023
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQnGGDFLALELEDGRLVLRYDLGSGS--LVLSS--KTP 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1814459924 3024 LCDGQWHKVTANKVKHRIELTVDGNQVEAQSPNRASTSADTNDPVFVGGFPEGLNQLGLTTNIRFRGCIRSLRL 3097
Cdd:cd00110 77 LNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKV 150
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2344-2505 |
9.28e-33 |
|
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: 125.61 E-value: 9.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2344 TIQFDGEGYALVSRPIRWYPNiSTVMFKFRTFSSNALLMYLATRDLKDFMSVELTDGHIKVSYDLGSGMASVVSNQNHND 2423
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRTR-LSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLND 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2424 GKWKSFTLSRTQKQANISIvdidtNQEENIATSSPGNNFGLDLkaDDKIYFGGLPTlrnlSMKARPEVNLKKYSGCLRDI 2503
Cdd:cd00110 80 GQWHSVSVERNGRSVTLSV-----DGERVVESGSPGGSALLNL--DGPLYLGGLPE----DLKSPGLPVSPGFVGCIRDL 148
|
..
gi 1814459924 2504 EI 2505
Cdd:cd00110 149 KV 150
|
|
| LamG |
smart00282 |
Laminin G domain; |
2367-2507 |
6.63e-32 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 122.45 E-value: 6.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2367 TVMFKFRTFSSNALLMYLATRDLKDFMSVELTDGHIKVSYDLGSGMASVVSNQNH-NDGKWKSFTLSRTQKQANISIvdi 2445
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPlNDGQWHRVAVERNGRSVTLSV--- 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1814459924 2446 dtNQEENIATSSPGNNFGLDLkaDDKIYFGGLPTlrnlSMKARPEVNLKKYSGCLRDIEISR 2507
Cdd:smart00282 78 --DGGNRVSGESPGGLTILNL--DGPLYLGGLPE----DLKLPPLPVTPGFRGCIRNLKVNG 131
|
|
| LamG |
smart00282 |
Laminin G domain; |
2968-3097 |
8.49e-31 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 119.37 E-value: 8.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2968 VEFEFRTTRTTGVLLGISS-QKMDGMGIEMIAEKLMFHVDNGAGRFTAVYDagiPGHLCDGQWHKVTANKVKHRIELTVD 3046
Cdd:smart00282 2 ISFSFRTTSPNGLLLYAGSkGGGDYLALELRDGRLVLRYDLGSGPARLTSD---PTPLNDGQWHRVAVERNGRSVTLSVD 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1814459924 3047 G-NQVEAQSPnRASTSADTNDPVFVGGFPEGLNQLGLTTNIRFRGCIRSLRL 3097
Cdd:smart00282 79 GgNRVSGESP-GGLTILNLDGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKV 129
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2558-2699 |
1.60e-28 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 112.80 E-value: 1.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2558 FSTKNESGIILlgSGGTpapprrkrrQTGQAYYAIFLNKGRLEVHLSTGARTmrkiAVKPEPSLLHDGREHSVHVERTRG 2637
Cdd:pfam00054 1 FRTTEPSGLLL--YNGT---------QTERDFLALELRDGRLEVSYDLGSGA----AVVRSGDKLNDGKWHSVELERNGR 65
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1814459924 2638 IFTVQVDEDRRHV--QNLTVEQAIEV-KKLFVGGAPPE-FQPSPLRNIPPFEGCIWNLVINSVPMD 2699
Cdd:pfam00054 66 SGTLSVDGEARPTgeSPLGATTDLDVdGPLYVGGLPSLgVKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2532-2694 |
8.67e-28 |
|
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: 111.36 E-value: 8.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2532 TVSFPKPGFVELSPVPID-VGTEINLSFSTKNESGIILLGSGgtpapprrkrrQTGQAYYAIFLNKGRLEVHLSTGARTM 2610
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPrTRLSISFSFRTTSPNGLLLYAGS-----------QNGGDFLALELEDGRLVLRYDLGSGSL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2611 RkiaVKPePSLLHDGREHSVHVERTRGIFTVQVDEDR--RHVQNLTVEQAIEVKKLFVGGAPPEFQPSPLRNIPPFEGCI 2688
Cdd:cd00110 70 V---LSS-KTPLNDGQWHSVSVERNGRSVTLSVDGERvvESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCI 145
|
....*.
gi 1814459924 2689 WNLVIN 2694
Cdd:cd00110 146 RDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
2173-2315 |
4.62e-27 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 108.58 E-value: 4.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2173 SIIVNVKTAVADNLLFYLGSAKFIDFLAIEMRKGKVSFLWDVGSGVGRVEYPDLTIDDSYWYRIEASRTGRNGTISVral 2252
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLNDGQWHRVAVERNGRSVTLSV--- 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1814459924 2253 DGPKASIMPstyhsaSPPGYTILDVDANamLFVGGLTGKLKKADAVRVITFTGCMGEAYFDSK 2315
Cdd:smart00282 78 DGGNRVSGE------SPGGLTILNLDGP--LYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2154-2313 |
1.03e-25 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 105.58 E-value: 1.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2154 SGGDCIRtYKPEIKKGSYNSIIVNVKTAVADNLLFYLGSAKFIDFLAIEMRKGKVSFLWDVGSGVGRVEYPDlTIDDSYW 2233
Cdd:cd00110 5 SGSSYVR-LPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKT-PLNDGQW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2234 YRIEASRTGRNGTISVralDGPKasimpsTYHSASPPGYTILDVDANamLFVGGLTGKLKKADAVRVITFTGCMGEAYFD 2313
Cdd:cd00110 83 HSVSVERNGRSVTLSV---DGER------VVESGSPGGSALLNLDGP--LYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2972-3097 |
1.55e-25 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 104.04 E-value: 1.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2972 FRTTRTTGVLLGISSQKMDGMGIEMIAEKLMFHVDNGAGRFTAVYdagIPGHLCDGQWHKVTANKVKHRIELTVDGNQVE 3051
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDFLALELVNGRLVLRYDLGSGPESLLS---SGKNLNDGQWHSVRVERNGNTLTLSVDGQTVV 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1814459924 3052 AQSPNRASTSADTNDPVFVGGFPEGLNQLGLTTNIRFRGCIRSLRL 3097
Cdd:pfam02210 78 SSLPPGESLLLNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRV 123
|
|
| LamG |
smart00282 |
Laminin G domain; |
2553-2696 |
4.71e-23 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 97.02 E-value: 4.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2553 EINLSFSTKNESGIILLGSGGTpapprrkrrqtGQAYYAIFLNKGRLEVHLSTGARTmrkIAVKPEPSLLHDGREHSVHV 2632
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKG-----------GGDYLALELRDGRLVLRYDLGSGP---ARLTSDPTPLNDGQWHRVAV 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1814459924 2633 ERTRGIFTVQVD-EDRRHVQNLTVEQAIEVK-KLFVGGAPPEFQPSPLRNIPPFEGCIWNLVINSV 2696
Cdd:smart00282 67 ERNGRSVTLSVDgGNRVSGESPGGLTILNLDgPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1611-2174 |
9.92e-18 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 90.89 E-value: 9.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1611 KILYGLENMTQELKHLLSPQRAPERLIQLAEGNLNTLVTEMNELLTRATKVTADGEQTG---QDAERTNTRANSLGEFIK 1687
Cdd:PRK03918 169 EVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEkevKELEELKEEIEELEKELE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1688 DLAQHAEAVSEKAVKLNETLGIQDKAFE------RNLQELQNEVDKMMT--ELRRKNLDTQKEVaEDELVAAEALLKKVK 1759
Cdd:PRK03918 249 SLEGSKRKLEEKIRELEERIEELKKEIEeleekvKELKELKEKAEEYIKlsEFYEEYLDELREI-EKRLSRLEEEINGIE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1760 KLFGESRGKNEEME------KDLREKLADYKSKVhdawDLLREATDKIKEANLLSAENQ-KNMTALEKKKEAIESGKRQT 1832
Cdd:PRK03918 328 ERIKELEEKEERLEelkkklKELEKRLEELEERH----ELYEEAKAKKEELERLKKRLTgLTPEKLEKELEELEKAKEEI 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1833 EDTLKEgtdILDEANRLADEINSVIDYVEDIQT---KLP----PLSEDLKG--------KIEDLSQEIKdrKLAEKVSQA 1897
Cdd:PRK03918 404 EEEISK---ITARIGELKKEIKELKKAIEELKKakgKCPvcgrELTEEHRKelleeytaELKRIEKELK--EIEEKERKL 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1898 ESHAAQ----LNDSSAV--LDRILDEAKNISfnataafkaySNIKDY-IDKAEKIAKEAKVLAHEATELatgpqGSLQEG 1970
Cdd:PRK03918 479 RKELRElekvLKKESELikLKELAEQLKELE----------EKLKKYnLEELEKKAEEYEKLKEKLIKL-----KGEIKS 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1971 AKGSLQKSFGFLNEAKKLANDVKENDEHLNGLTSRL--------DNANVRNRDLLRALNDTLErLSAIPNDTAAKLQAVK 2042
Cdd:PRK03918 544 LKKELEKLEELKKKLAELEKKLDELEEELAELLKELeelgfesvEELEERLKELEPFYNEYLE-LKDAEKELEREEKELK 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2043 DKARQANDTAKD---VLAQIKDLHQNLDGLKKNYNQladsvaKTNAVVKDP--SKNKIIADADATVKNLEQEADRLIDKL 2117
Cdd:PRK03918 623 KLEEELDKAFEElaeTEKRLEELRKELEELEKKYSE------EEYEELREEylELSRELAGLRAELEELEKRREEIKKTL 696
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 1814459924 2118 KPIKELEDNLKKNISEIkELINQARKQANSIKvsvssggDCIRTYKPEIKKGSYNSI 2174
Cdd:PRK03918 697 EKLKEELEEREKAKKEL-EKLEKALERVEELR-------EKVKKYKALLKERALSKV 745
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1610-2168 |
2.28e-17 |
|
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: 89.31 E-value: 2.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1610 YKILYGLENMTQELKHLLSPQRAPERLIQLAEGNLNTLVTEMNELLTRATKV----TADgEQTGQDAERTNTRANSLGEF 1685
Cdd:TIGR04523 141 DKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIknklLKL-ELLLSNLKKKIQKNKSLESQ 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1686 IKDLAQH----AEAVSEKAVKLNETLGIQDKAfERNLQELQNEVDKMMTELRRKNLDTQKevAEDELVAAEALLKKVK-K 1760
Cdd:TIGR04523 220 ISELKKQnnqlKDNIEKKQQEINEKTTEISNT-QTQLNQLKDEQNKIKKQLSEKQKELEQ--NNKKIKELEKQLNQLKsE 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1761 LFGESRGKNEEMEKDLREKLADYKSKVHDAWDLLREATDKI-----------KEANLLSAENQKNMTALEKKKEAIESGK 1829
Cdd:TIGR04523 297 ISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIIsqlneqisqlkKELTNSESENSEKQRELEEKQNEIEKLK 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1830 RQTEDTLKEGTDILDEANRLADEINSVIDYVEDIQTKLpplsEDLKGKIEDLSQEIKDrkLAEKVSQAESHAAQLNDSSA 1909
Cdd:TIGR04523 377 KENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQI----KKLQQEKELLEKEIER--LKETIIKNNSEIKDLTNQDS 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1910 VLDRILDEAKNIsfnaTAAFKaySNIKDYIDKAEKIAKEAKVLAHEATelatgpqgslqegakgslQKSfgflNEAKKLA 1989
Cdd:TIGR04523 451 VKELIIKNLDNT----RESLE--TQLKVLSRSINKIKQNLEQKQKELK------------------SKE----KELKKLN 502
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1990 NDVKENDEHLNGLTSRLDNANVRNRDL----------LRALNDTLERLSAipNDTAAKLQAVKDKARQandtakdvlaQI 2059
Cdd:TIGR04523 503 EEKKELEEKVKDLTKKISSLKEKIEKLesekkekeskISDLEDELNKDDF--ELKKENLEKEIDEKNK----------EI 570
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2060 KDLHQNLDGLKKNYNQLADSVAKTNAVVKDpsKNKIIADADATVKNLEQEAD-------RLIDKLKPIKELEDNLKKNIS 2132
Cdd:TIGR04523 571 EELKQTQKSLKKKQEEKQELIDQKEKEKKD--LIKEIEEKEKKISSLEKELEkakkeneKLSSIIKNIKSKKNKLKQEVK 648
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1814459924 2133 EIKELINQAR-KQAN---SIKVSVSSGGDCIRT-----------YKPEIKK 2168
Cdd:TIGR04523 649 QIKETIKEIRnKWPEiikKIKESKTKIDDIIELmkdwlkelslhYKKYITR 699
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1739-2080 |
8.36e-14 |
|
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: 78.17 E-value: 8.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1739 TQKEVAEDELVAAEALLKKVKKLFGESRGKNEEMEK--DLREKLADYKSKvhdawdlLREAtdkikEANLLSAEnqknMT 1816
Cdd:TIGR02168 172 ERRKETERKLERTRENLDRLEDILNELERQLKSLERqaEKAERYKELKAE-------LREL-----ELALLVLR----LE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1817 ALEKKKEAIESGKRQTEDTLKEGTDILDEA----NRLADEINSVIDYVEDIQTKLpplsEDLKGKIEDLSQEIkdRKLAE 1892
Cdd:TIGR02168 236 ELREELEELQEELKEAEEELEELTAELQELeeklEELRLEVSELEEEIEELQKEL----YALANEISRLEQQK--QILRE 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1893 KVSQAESHAAQLNDSSAVLDRILDEAKnisFNATAAFKAYSNIKDYIDKAEKIAKEAKVLAHEATELATGPQGSLQEGAK 1972
Cdd:TIGR02168 310 RLANLERQLEELEAQLEELESKLDELA---EELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1973 GSLQKsfgfLNEAKKLANDVKENDEHLNGLTSRLDNANVRNRDLLR-------------------ALNDTLERLSAIpND 2033
Cdd:TIGR02168 387 KVAQL----ELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKkleeaelkelqaeleeleeELEELQEELERL-EE 461
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1814459924 2034 TAAKLQAVKDKARQANDTAKDVLAQ-------IKDLHQNLDG-------LKKNYNQLADSV 2080
Cdd:TIGR02168 462 ALEELREELEEAEQALDAAERELAQlqarldsLERLQENLEGfsegvkaLLKNQSGLSGIL 522
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
921-967 |
1.36e-13 |
|
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: 67.38 E-value: 1.36e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1814459924 921 PCLCNANGSFSEVCHAQTGQCECKPNVQGRQCDECKPETFGLQSARG 967
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGG 47
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1621-1950 |
2.61e-13 |
|
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: 76.63 E-value: 2.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1621 QELKHLLSPQRAPERLIQLAEGNLNTLVTEMNELLTRATKVTADGEQTGQD--------------AERTNTRANSLGEFI 1686
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQisalrkdlarleaeVEQLEERIAQLSKEL 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1687 KDLAQHAEAVSEKAVKLNETLgiqdKAFERNLQELQNEVDKMMTELR--RKNLDTQKEVAEDELVAAEALLKKVKKLFGE 1764
Cdd:TIGR02168 757 TELEAEIEELEERLEEAEEEL----AEAEAEIEELEAQIEQLKEELKalREALDELRAELTLLNEEAANLRERLESLERR 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1765 SRGKNEEME------KDLREKLADYKSKVHDAWDLLREATDKIKEANLLSAENQKNMTALEKKKEAIESGKRQTEDTLKE 1838
Cdd:TIGR02168 833 IAATERRLEdleeqiEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1839 GTDILDEANrladeinsviDYVEDIQTKLPPLSEDLKGKIEDLSQEIKD--RKLAEKVSQAESHAAQLNDSSAVLDRILD 1916
Cdd:TIGR02168 913 LRRELEELR----------EKLAQLELRLEGLEVRIDNLQERLSEEYSLtlEEAEALENKIEDDEEEARRRLKRLENKIK 982
|
330 340 350
....*....|....*....|....*....|....
gi 1814459924 1917 EAKNISFNATAAFKAYSNIKDYIDKAEKIAKEAK 1950
Cdd:TIGR02168 983 ELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAK 1016
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1689-2150 |
2.95e-13 |
|
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: 76.31 E-value: 2.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1689 LAQHAEAVSEKAVKLNETLGIQDKA----------FERNLQELQNEVDKmMTELRRKNLDTQKEVAED------ELVAAE 1752
Cdd:pfam15921 80 LEEYSHQVKDLQRRLNESNELHEKQkfylrqsvidLQTKLQEMQMERDA-MADIRRRESQSQEDLRNQlqntvhELEAAK 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1753 ALLKKVKKlfgesrGKNEEMEKdLREKLADYKSKVHDAWDLL---REAT-DKIKEANLLSAENQKNM-TALEKkkeaies 1827
Cdd:pfam15921 159 CLKEDMLE------DSNTQIEQ-LRKMMLSHEGVLQEIRSILvdfEEASgKKIYEHDSMSTMHFRSLgSAISK------- 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1828 gkrqtedTLKEgtdiLD-EANRLADEINSVIDYVEDI----QTKLPPLSEDLKGKIEDL--SQEIKDRKLAEKVSQAESH 1900
Cdd:pfam15921 225 -------ILRE----LDtEISYLKGRIFPVEDQLEALksesQNKIELLLQQHQDRIEQLisEHEVEITGLTEKASSARSQ 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1901 AaqlNDSSAVLDRILDEAKN--------ISFNATAAFKAYSNIKD----YIDKAEKIAKEAKVLAHEATELATGPQGSLQ 1968
Cdd:pfam15921 294 A---NSIQSQLEIIQEQARNqnsmymrqLSDLESTVSQLRSELREakrmYEDKIEELEKQLVLANSELTEARTERDQFSQ 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1969 EGAK--GSLQKSFGFLNEAKKLANDVKENDEHL------NGLT-----SRLDNANV---RNRDLLRAL------------ 2020
Cdd:pfam15921 371 ESGNldDQLQKLLADLHKREKELSLEKEQNKRLwdrdtgNSITidhlrRELDDRNMevqRLEALLKAMksecqgqmerqm 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2021 ------NDTLERLSAIpndtAAKLQAVKDKARQandtakdVLAQIKDLHQNLDGLKKNYNQLADSVAKtnavvkdpsKNK 2094
Cdd:pfam15921 451 aaiqgkNESLEKVSSL----TAQLESTKEMLRK-------VVEELTAKKMTLESSERTVSDLTASLQE---------KER 510
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1814459924 2095 IIADADATVKNLEQEADRLIDKLKPIKELEDNLKKNISEIKELINQARKQANSIKV 2150
Cdd:pfam15921 511 AIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEI 566
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1702-2100 |
3.53e-13 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 74.17 E-value: 3.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1702 KLNETLGIQDKAFERNLQELQNEVDKMMTELRRknldTQKEVAEdelvaaeallkkvkklfgesrgKNEEMEKdLREKLA 1781
Cdd:COG4372 17 GLRPKTGILIAALSEQLRKALFELDKLQEELEQ----LREELEQ----------------------AREELEQ-LEEELE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1782 DYKSKVHDAWDLLREATDKIKEANLLSAENQKNMTALEKKKEAIEsgkRQTEDTLKEGTDILDEANRLADEINSVIDYVE 1861
Cdd:COG4372 70 QARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQ---EELEELQKERQDLEQQRKQLEAQIAELQSEIA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1862 DIQTKLpplsEDLKGKIEDLSQEIKdrKLAEKVSQAESHAAQlndssAVLDRILDEAKNISFNATAAFKAysniKDYIDK 1941
Cdd:COG4372 147 EREEEL----KELEEQLESLQEELA--ALEQELQALSEAEAE-----QALDELLKEANRNAEKEEELAEA----EKLIES 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1942 AEKIAKEAKVLAHEATELATGPQGSLQEGAKGSLQKSFGFLNEAKKLANDVKEN--DEHLNGLTSRLDNANVRNRDLLRA 2019
Cdd:COG4372 212 LPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELaiLVEKDTEEEELEIAALELEALEEA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2020 LNDTLERLSAIPNDTAAKLQAVKDKARQANDTAKdvlAQIKDLHQNLDGLKKNYNQLADSVAKTNAVVKDPSKNKIIADA 2099
Cdd:COG4372 292 ALELKLLALLLNLAALSLIGALEDALLAALLELA---KKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVA 368
|
.
gi 1814459924 2100 D 2100
Cdd:COG4372 369 D 369
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
971-1015 |
5.40e-13 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 65.41 E-value: 5.40e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1814459924 971 CNCNSFGSKSFDCE-ESGQCWCQPGVTGKKCDRCAHGYFNFQEGGC 1015
Cdd:smart00180 1 CDCDPGGSASGTCDpDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
922-968 |
8.51e-13 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 65.07 E-value: 8.51e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1814459924 922 CLCNANGSFSEVCHAQTGQCECKPNVQGRQCDECKPETFGLQ--SARGC 968
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPsdPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
922-968 |
9.99e-13 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 64.64 E-value: 9.99e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1814459924 922 CLCNANGSFSEVCHAQTGQCECKPNVQGRQCDECKPETFGlQSARGC 968
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYG-DGPPGC 46
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1770-2149 |
1.43e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 73.94 E-value: 1.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1770 EEMEKDLRE--KLADYKSkvhdAWDLLREAtdkIKEanllsaenqknmtaLEKKKEAIESGKRQTEDtlkegtdILDEAN 1847
Cdd:PRK03918 145 ESREKVVRQilGLDDYEN----AYKNLGEV---IKE--------------IKRRIERLEKFIKRTEN-------IEELIK 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1848 RLADEINSVIDYVEDIQTKLPPLSEDL-------------KGKIEDLSQEIKD-----RKLAEKVSQAESHAAQLNDSSA 1909
Cdd:PRK03918 197 EKEKELEEVLREINEISSELPELREELeklekevkeleelKEEIEELEKELESlegskRKLEEKIRELEERIEELKKEIE 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1910 VLDRILDEAKNISFNAtaafKAYSNIKDYIDKAEKIAKEAKVLAHEATELATGPQGSLQEGAKGSlqksfgflNEAKKLA 1989
Cdd:PRK03918 277 ELEEKVKELKELKEKA----EEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKE--------ERLEELK 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1990 NDVKENDEHLNGLTSRldnanVRNRDLLRALNDTLERLSA-----IPNDTAAKLQAVKDKARQANDTAKDVLAQIKDLHQ 2064
Cdd:PRK03918 345 KKLKELEKRLEELEER-----HELYEEAKAKKEELERLKKrltglTPEKLEKELEELEKAKEEIEEEISKITARIGELKK 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2065 NLDGLKKNYNQLADSVAK---TNAVVKDPSKNKIIADADATVKNLEQEADRLIDKLKPIKELEDNLKKNISEIKELINQa 2141
Cdd:PRK03918 420 EIKELKKAIEELKKAKGKcpvCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKL- 498
|
....*...
gi 1814459924 2142 RKQANSIK 2149
Cdd:PRK03918 499 KELAEQLK 506
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1718-1906 |
6.71e-12 |
|
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: 68.03 E-value: 6.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1718 LQELQNEVDKMMTELRR-----KNLDTQKEVAEDELVAAEALLKKVKKlfgeSRGKNEEMEKDLREKLADYKSKvhdawd 1792
Cdd:COG1579 12 LQELDSELDRLEHRLKElpaelAELEDELAALEARLEAAKTELEDLEK----EIKRLELEIEEVEARIKKYEEQ------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1793 llreatdkikeanLLSAENQKNMTALEKKKEAIESGKRQTEDTLKEgtdILDEANRLADEINSVIDYVEDIQTKLpplsE 1872
Cdd:COG1579 82 -------------LGNVRNNKEYEALQKEIESLKRRISDLEDEILE---LMERIEELEEELAELEAELAELEAEL----E 141
|
170 180 190
....*....|....*....|....*....|....
gi 1814459924 1873 DLKGKIEDLSQEIkDRKLAEKVSQAESHAAQLND 1906
Cdd:COG1579 142 EKKAELDEELAEL-EAELEELEAEREELAAKIPP 174
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
970-1016 |
7.70e-12 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 62.37 E-value: 7.70e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1814459924 970 PCNCNSFGSKSFDCE-ESGQCWCQPGVTGKKCDRCAHGYFNF--QEGGCT 1016
Cdd:cd00055 1 PCDCNGHGSLSGQCDpGTGQCECKPNTTGRRCDRCAPGYYGLpsQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
868-920 |
5.38e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 60.06 E-value: 5.38e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1814459924 868 PCQCNDNldFSIPGSCDSLSGSCLiCKPGTTGRYCELCADGYFGDAVDAKNCQ 920
Cdd:cd00055 1 PCDCNGH--GSLSGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1064-1112 |
6.39e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 59.67 E-value: 6.39e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1814459924 1064 CNCSSVGSLDFQCNLN*GQCNCRPKFSG*KCTECNRGHWSYPHCNPCDC 1112
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
971-1018 |
7.84e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 59.29 E-value: 7.84e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1814459924 971 CNCNSFGSKSFDCE-ESGQCWCQPGVTGKKCDRCAHGYFNFQEGGCTAC 1018
Cdd:pfam00053 1 CDCNPHGSLSDTCDpETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1531-1568 |
9.49e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 59.29 E-value: 9.49e-11
10 20 30
....*....|....*....|....*....|....*...
gi 1814459924 1531 CECDPHGSLPVPCDPVTGICTCRPGATGQKCDGCKHWH 1568
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGY 39
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
760-809 |
3.59e-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: 3.59e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1814459924 760 PCQCFGHA---ESCDDITGECLnCKDHTGGLYCNKCLPGFYGDPTKGtsDDCQ 809
Cdd:cd00055 1 PCDCNGHGslsGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQG--GGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1531-1571 |
6.51e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.55 E-value: 6.51e-10
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1814459924 1531 CECDPHGSLPVPCDPVTGICTCRPGATGQKCDGCKHWHVRE 1571
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGD 41
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
418-475 |
9.50e-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: 56.21 E-value: 9.50e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1814459924 418 CHCDPIGSLSEVCVkdekraqrgLAPGSCHCKPGFRGVSCDRCARGYTGYPDCKPCNC 475
Cdd:pfam00053 1 CDCNPHGSLSDTCD---------PETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1531-1566 |
1.03e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 56.21 E-value: 1.03e-09
10 20 30
....*....|....*....|....*....|....*.
gi 1814459924 1531 CECDPHGSLPVPCDPVTGICTCRPGATGQKCDGCKH 1566
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKP 36
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1424-1470 |
2.27e-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: 2.27e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1424 CQCHGHSSL---CDPETSICQnCQHHTAGDFCERCVLGYYGIVKGLPDDC 1470
Cdd:pfam00053 1 CDCNPHGSLsdtCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1652-2146 |
2.42e-09 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 63.69 E-value: 2.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1652 NELLTRATKVTADGEQTGQ----DAER--TNTRAnslgEFIKDLAQ-HAEAvSEKAVKLNETLGIQDKAFERNLQELQNE 1724
Cdd:NF041483 538 AEAEEQAEEVRAAAERAARelreETERaiAARQA----EAAEELTRlHTEA-EERLTAAEEALADARAEAERIRREAAEE 612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1725 VDKMMTEL--RRKNLDTQKEVAEDEL---VAAEAllkkvkklfGESRGKNEEMEKDLREKLAD----YKSKVHDAWDLLR 1795
Cdd:NF041483 613 TERLRTEAaeRIRTLQAQAEQEAERLrteAAADA---------SAARAEGENVAVRLRSEAAAeaerLKSEAQESADRVR 683
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1796 -EATdkiKEANLLSAENQKnmtALEKKKEAIESGKRQTEDTLKEGTDILDEANRLADE-----INSVIDYVEDIQTKLPP 1869
Cdd:NF041483 684 aEAA---AAAERVGTEAAE---ALAAAQEEAARRRREAEETLGSARAEADQERERAREqseelLASARKRVEEAQAEAQR 757
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1870 LSEDlkgkiedlsqeiKDRKLAEKVSQAESHAAQLNDSSAVLDrilDEAKN-ISFNATAAFKAYSNIK-DYIDKAEKIAK 1947
Cdd:NF041483 758 LVEE------------ADRRATELVSAAEQTAQQVRDSVAGLQ---EQAEEeIAGLRSAAEHAAERTRtEAQEEADRVRS 822
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1948 EAKVLAHEATELATGPQGSLQE---GAKGSLQKSFG-FLNEAKKLANDVKENDEHLNglTSRLDNANVRNRDLLRALNDT 2023
Cdd:NF041483 823 DAYAERERASEDANRLRREAQEeteAAKALAERTVSeAIAEAERLRSDASEYAQRVR--TEASDTLASAEQDAARTRADA 900
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2024 LERLSAIPNDTAAklQAVKDKARQANDTAKDVLAQIKDLHQNLDGLKKNYNQL-ADSVAKTNAVVKDPSKN--KIIADAD 2100
Cdd:NF041483 901 REDANRIRSDAAA--QADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVrADAAAQAEQLIAEATGEaeRLRAEAA 978
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1814459924 2101 ATVKNLEQEADRLIDKLKPIK-----ELEDNLKKNISEIKELINQARKQAN 2146
Cdd:NF041483 979 ETVGSAQQHAERIRTEAERVKaeaaaEAERLRTEAREEADRTLDEARKDAN 1029
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1017-1062 |
5.09e-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: 54.28 E-value: 5.09e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1017 ACDCSHLG---NNCDPKTGRCICPPNTIGEKCSKCVPNTWGH-SITTGCK 1062
Cdd:cd00055 1 PCDCNGHGslsGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLpSQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1423-1471 |
5.09e-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: 54.28 E-value: 5.09e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1814459924 1423 PCQCHGHSSL---CDPETSICQnCQHHTAGDFCERCVLGYYGIVKGlPDDCQ 1471
Cdd:cd00055 1 PCDCNGHGSLsgqCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQ-GGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
473-519 |
7.79e-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: 53.90 E-value: 7.79e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1814459924 473 CNCSGAGSTNE--DPCFGPCNCKENVEGGDCSRCKFGFFNLQEDNHRGC 519
Cdd:pfam00053 1 CDCNPHGSLSDtcDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
869-912 |
7.90e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 53.47 E-value: 7.90e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1814459924 869 CQCNdnLDFSIPGSCDSLSGSCLiCKPGTTGRYCELCADGYFGD 912
Cdd:smart00180 1 CDCD--PGGSASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD 41
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1018-1061 |
7.90e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 53.47 E-value: 7.90e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1814459924 1018 CDCS---HLGNNCDPKTGRCICPPNTIGEKCSKCVPNTWGHSiTTGC 1061
Cdd:smart00180 1 CDCDpggSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG-PPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1063-1105 |
8.30e-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: 8.30e-09
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1814459924 1063 PCNCSSVGSLDFQCNLN*GQCNCRPKFSG*KCTECNRGHWSYP 1105
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1110-1167 |
9.85e-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: 53.51 E-value: 9.85e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1814459924 1110 CDCFLPG*DDSTCDLETkkcsctdktGQCTCKVNVEGVRCDRCRLGKFGLEAKNPLGC 1167
Cdd:pfam00053 1 CDCNPHGSLSDTCDPET---------GQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
417-469 |
1.73e-08 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 52.74 E-value: 1.73e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1814459924 417 PCHCDPIGSLSEVCVKDEkraqrglapGSCHCKPGFRGVSCDRCARGYTGYPD 469
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGT---------GQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
869-915 |
2.78e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 52.36 E-value: 2.78e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1814459924 869 CQCNDNLdfSIPGSCDSLSGSCLiCKPGTTGRYCELCADGYFGDAVD 915
Cdd:pfam00053 1 CDCNPHG--SLSDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSD 44
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1018-1061 |
2.98e-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: 51.97 E-value: 2.98e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1814459924 1018 CDCSHLG---NNCDPKTGRCICPPNTIGEKCSKCVPNTWGHSITTGC 1061
Cdd:pfam00053 1 CDCNPHGslsDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQ 47
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1983-2150 |
3.38e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 58.76 E-value: 3.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1983 NEAKKLANDVKENDEHLNGLTSRLDNAN-----VRNRdlLRALNDTLERLSAIPNDTAAKLQAVKDKARQANDTAKDVLA 2057
Cdd:COG4372 45 EELEQLREELEQAREELEQLEEELEQARseleqLEEE--LEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQK 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2058 QIKDLHQNLDGLKKNYNQLadsvaktnavvkdpskNKIIADADATVKNLEQEADRLIDKLKPIKELEDNLKKN--ISEIK 2135
Cdd:COG4372 123 ERQDLEQQRKQLEAQIAEL----------------QSEIAEREEELKELEEQLESLQEELAALEQELQALSEAeaEQALD 186
|
170
....*....|....*
gi 1814459924 2136 ELINQARKQANSIKV 2150
Cdd:COG4372 187 ELLKEANRNAEKEEE 201
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
761-801 |
3.59e-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: 51.97 E-value: 3.59e-08
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1814459924 761 CQCFGHA---ESCDDITGECLnCKDHTGGLYCNKCLPGFYGDPT 801
Cdd:pfam00053 1 CDCNPHGslsDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPS 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1110-1167 |
4.56e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 51.54 E-value: 4.56e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1814459924 1110 CDCFLPG*DDSTCDLETkkcsctdktGQCTCKVNVEGVRCDRCRLGKFGleaKNPLGC 1167
Cdd:smart00180 1 CDCDPGGSASGTCDPDT---------GQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1109-1167 |
4.56e-08 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 51.59 E-value: 4.56e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1814459924 1109 PCDCFLPG*DDSTCDLETkkcsctdktGQCTCKVNVEGVRCDRCRLGKFGLeAKNPLGC 1167
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGT---------GQCECKPNTTGRRCDRCAPGYYGL-PSQGGGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1064-1107 |
5.71e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 51.16 E-value: 5.71e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1814459924 1064 CNCSSVGSLDFQCNLN*GQCNCRPKFSG*KCTECNRGHW--SYPHC 1107
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYgdGPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
418-470 |
6.55e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 51.16 E-value: 6.55e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1814459924 418 CHCDPIGSLSEVCVKDEkraqrglapGSCHCKPGFRGVSCDRCARGYTG--YPDC 470
Cdd:smart00180 1 CDCDPGGSASGTCDPDT---------GQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1672-1958 |
3.21e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.69 E-value: 3.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1672 AERTNTRANSL--GEFIKDLAQHAEAVSEKAVKLNETLgiqDKAFERNlqELQNEVDKMMTELRRKNLDTQKEVAEDELV 1749
Cdd:PTZ00121 1615 AEEAKIKAEELkkAEEEKKKVEQLKKKEAEEKKKAEEL---KKAEEEN--KIKAAEEAKKAEEDKKKAEEAKKAEEDEKK 1689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1750 AAEALLKK---------VKKLFGESRGKNEEMEKDLREKladyKSKVHDAWDllREATDKIKEANLLSAENQKNMTALEK 1820
Cdd:PTZ00121 1690 AAEALKKEaeeakkaeeLKKKEAEEKKKAEELKKAEEEN----KIKAEEAKK--EAEEDKKKAEEAKKDEEEKKKIAHLK 1763
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1821 KKE--AIESGKRQTEDTLKEGTDILDEANRLADE--INSVIDYVEDIQ---TKLPPLSEDLKGKIEDLSQEIKDRK--LA 1891
Cdd:PTZ00121 1764 KEEekKAEEIRKEKEAVIEEELDEEDEKRRMEVDkkIKDIFDNFANIIeggKEGNLVINDSKEMEDSAIKEVADSKnmQL 1843
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1814459924 1892 EKVSQAESHAAQLNDSSAVldrilDEAKNISFNataafKAYSNIKDYIDKAEKiAKEAKVLAHEATE 1958
Cdd:PTZ00121 1844 EEADAFEKHKFNKNNENGE-----DGNKEADFN-----KEKDLKEDDEEEIEE-ADEIEKIDKDDIE 1899
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
761-803 |
4.98e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 48.46 E-value: 4.98e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1814459924 761 CQC--FGHA-ESCDDITGECLnCKDHTGGLYCNKCLPGFYGDPTKG 803
Cdd:smart00180 1 CDCdpGGSAsGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
291-338 |
6.06e-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: 6.06e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1814459924 291 CICYGHA---RACplDPVTnkSRCECEHNTCGDSCDQCCPGFHQKPWRAGT 338
Cdd:cd00055 2 CDCNGHGslsGQC--DPGT--GQCECKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
811-866 |
1.74e-06 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 46.96 E-value: 1.74e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1814459924 811 CACPLNIPSnnfSPTCHLDrnlGLICDeCPVGYTGPHCERCAEGYFGQPSLPGGSC 866
Cdd:pfam00053 1 CDCNPHGSL---SDTCDPE---TGQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
810-867 |
1.93e-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: 46.96 E-value: 1.93e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1814459924 810 PCACPLNIpsnNFSPTCHLDrnlGLICdECPVGYTGPHCERCAEGYFGQPSLPGGsCQ 867
Cdd:cd00055 1 PCDCNGHG---SLSGQCDPG---TGQC-ECKPNTTGRRCDRCAPGYYGLPSQGGG-CQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
472-519 |
2.42e-06 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 46.58 E-value: 2.42e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1814459924 472 PCNCSGAGSTNE--DPCFGPCNCKENVEGGDCSRCKFGFFNLQEDNHrGC 519
Cdd:cd00055 1 PCDCNGHGSLSGqcDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGG-GC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1424-1470 |
7.76e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 44.99 E-value: 7.76e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1424 CQCH--GHSSL-CDPETSICQnCQHHTAGDFCERCVLGYYGIVkglPDDC 1470
Cdd:smart00180 1 CDCDpgGSASGtCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDG---PPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
811-859 |
1.04e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 44.99 E-value: 1.04e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1814459924 811 CACPlniPSNNFSPTCHLDrnlGLICdECPVGYTGPHCERCAEGYFGQP 859
Cdd:smart00180 1 CDCD---PGGSASGTCDPD---TGQC-ECKPNVTGRRCDRCAPGYYGDG 42
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1982-2168 |
1.13e-05 |
|
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: 51.17 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1982 LNEAKKLANDVKENDEHLNGLTSRL-DNANVRNrdllrALNDTLERLSAIPNDTAAKLQAVKDKARQANDTAKDVLAQIK 2060
Cdd:TIGR04523 39 EKKLKTIKNELKNKEKELKNLDKNLnKDEEKIN-----NSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2061 DLHQNLDGLKKNYNQLADSVAKTnavvkdpskNKIIADADATVKNLEQEADRLIDKL----KPIKELEDN---LKKNISE 2133
Cdd:TIGR04523 114 NDKEQKNKLEVELNKLEKQKKEN---------KKNIDKFLTEIKKKEKELEKLNNKYndlkKQKEELENElnlLEKEKLN 184
|
170 180 190
....*....|....*....|....*....|....*
gi 1814459924 2134 IKELINQARKQANSIKVSVSSggdcIRTYKPEIKK 2168
Cdd:TIGR04523 185 IQKNIDKIKNKLLKLELLLSN----LKKKIQKNKS 215
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1608-1814 |
1.56e-05 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 49.68 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1608 APYKILYGLENMTQELKHLLSPQRAP--ERLIQLAEGNLNTLVTEMNELLTRATKVtadgeqtgqdaertntrANSLGEF 1685
Cdd:cd22656 85 AGGTIDSYYAEILELIDDLADATDDEelEEAKKTIKALLDDLLKEAKKYQDKAAKV-----------------VDKLTDF 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1686 IKDLAQHAEAVSEKAVKLNETLGIQDKAFER-NLQELQNEVDKMMTELRRKNLDTQKEVaEDELVAAEALLKKVKKLFGE 1764
Cdd:cd22656 148 ENQTEKDQTALETLEKALKDLLTDEGGAIARkEIKDLQKELEKLNEEYAAKLKAKIDEL-KALIADDEAKLAAALRLIAD 226
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1814459924 1765 SRGKNEEMeKDLREKLADYKS---KVHDAWDLLREATDKIKeaNLLSAENQKN 1814
Cdd:cd22656 227 LTAADTDL-DNLLALIGPAIPaleKLQGAWQAIATDLDSLK--DLLEDDISKI 276
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1933-2150 |
2.29e-05 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 49.29 E-value: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1933 SNIKDYIDKAE-KIAKEAKVLAHEATELATGPQGSLQEGAKGSLQK-SFGFLNEAKKLANDVKENDEHLNGLTSRLDNAN 2010
Cdd:cd22656 76 GDIYNYAQNAGgTIDSYYAEILELIDDLADATDDEELEEAKKTIKAlLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQ 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2011 VRNRDLLRALNDTLER-LSAIPNDTAAKLQAVKDKARQAndtakdvlaQIKDLHQNLDGLKKNYNQLADSVAKTNAVVKD 2089
Cdd:cd22656 156 TALETLEKALKDLLTDeGGAIARKEIKDLQKELEKLNEE---------YAAKLKAKIDELKALIADDEAKLAAALRLIAD 226
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1814459924 2090 psknkiIADADATVKNLEQEADRLIDKLKPIKELEDNLKKNISEIKELINQARKQANSIKV 2150
Cdd:cd22656 227 ------LTAADTDLDNLLALIGPAIPALEKLQGAWQAIATDLDSLKDLLEDDISKIPAAIL 281
|
|
| alph_xenorhab_A |
NF033928 |
alpha-xenorhabdolysin family binary toxin subunit A; Alpha-xenorhabdolysin was the founding ... |
1908-2149 |
2.69e-05 |
|
alpha-xenorhabdolysin family binary toxin subunit A; Alpha-xenorhabdolysin was the founding member of a family of alpha-helical pore-forming binary toxins. YaxAB from Yersinia enterocolitica has been studied structurally. This HMM represents subunit A proteins such as XaxA and YaxA, capable of binding to the membrane even in the absence of the B subunit. This family is related to the Bacillus haemolytic enterotoxin family (see PF05791.9), although thresholds for this HMM are set to exclude that family.
Pssm-ID: 468250 [Multi-domain] Cd Length: 340 Bit Score: 49.22 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1908 SAVLDRILDEAKNISfNATAAFKAYSN-IKDYIDKAeKIAKEAKVLAHEATELATGPQGSLQEGAKGSLQKsfgFLneaK 1986
Cdd:NF033928 62 SNLEPKIKQLANDLA-NYARNIVVTGNpIIDLINEM-PIIKRGDLTEEELSELPPIPLSSDDKEIVKELKE---IL---E 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1987 KLANDVKENDEHLNGLTSRLDnanvrnrDLLRALNDTLerlsaipndtAAKLQAVKDKAR--QANDTAKDVLAQIKDLHQ 2064
Cdd:NF033928 134 DLKNDIKDYQQKADDVKKELD-------DFENDLREEL----------LPQLKLKKKLYDdnLGSDSIEELREKIDQLEK 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2065 NLDGLKKNYNQLADSVAKT----NAVVkdpsknkII---------ADADATVKNLEQEADRLIDKLK---PIKELEDNLK 2128
Cdd:NF033928 197 EIEQLNKEYDDYVKLSFTGlaggPIGL-------AItggifgskaEKIRKEKNALIQEIDELQEQLKkknALLGSLERLQ 269
|
250 260
....*....|....*....|.
gi 1814459924 2129 KNISEIKELINQARKQANSIK 2149
Cdd:NF033928 270 TSLDDILTRMEDALPALKKLK 290
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
473-519 |
4.12e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 43.07 E-value: 4.12e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1814459924 473 CNCSGAGSTNE--DPCFGPCNCKENVEGGDCSRCKFGFFNlqeDNHRGC 519
Cdd:smart00180 1 CDCDPGGSASGtcDPDTGQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1631-2040 |
5.39e-05 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 49.05 E-value: 5.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1631 RAPERLIQLAEGNLNTLVTEMNELLT----RATKVTADGEQTGQdaERTNTRANSLGEFIKDLAQHAEAVSEKAvklnet 1706
Cdd:NF041483 261 RAAEQRMQEAEEALREARAEAEKVVAeakeAAAKQLASAESANE--QRTRTAKEEIARLVGEATKEAEALKAEA------ 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1707 lgiqdkafERNLQELQNEVDKMMTELRRKNL-----DTQKEVAEDELVAAEALLKKVKKLFGESRGKNEEMEKDLREKLA 1781
Cdd:NF041483 333 --------EQALADARAEAEKLVAEAAEKARtvaaeDTAAQLAKAARTAEEVLTKASEDAKATTRAAAEEAERIRREAEA 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1782 D---YKSKVHDAWDLLR-EATDKIKEANLLSAENQKNMTAL-----EKKKEAIESGKRQTEDTLKEGTDILDEANRLADE 1852
Cdd:NF041483 405 EadrLRGEAADQAEQLKgAAKDDTKEYRAKTVELQEEARRLrgeaeQLRAEAVAEGERIRGEARREAVQQIEEAARTAEE 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1853 I-----------------------NSVIDYVEDIQTKLPPLSEDLKGKIEDLSQEIKDRklAEKV-SQAESHAAQLNDSS 1908
Cdd:NF041483 485 LltkakadadelrstataeservrTEAIERATTLRRQAEETLERTRAEAERLRAEAEEQ--AEEVrAAAERAARELREET 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1909 --AVLDRILDEAKNISFNATAAFK----AYSNIKDYIDKAEKI----AKEAKVLAHEATELATgpqgSLQEGAKgslqks 1978
Cdd:NF041483 563 erAIAARQAEAAEELTRLHTEAEErltaAEEALADARAEAERIrreaAEETERLRTEAAERIR----TLQAQAE------ 632
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1814459924 1979 fgflNEAKKLANDVKENDEHlngltSRLDNANVRNRDLLRALNDTlERLSAIPNDTAAKLQA 2040
Cdd:NF041483 633 ----QEAERLRTEAAADASA-----ARAEGENVAVRLRSEAAAEA-ERLKSEAQESADRVRA 684
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1473-1528 |
1.71e-04 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 41.57 E-value: 1.71e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1814459924 1473 CACPLISSSnnfSPSCVTEGlddYRCTaCPREYEGQYCERCAPGYTGSPSSPGGSC 1528
Cdd:pfam00053 1 CDCNPHGSL---SDTCDPET---GQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
310-334 |
3.31e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 40.76 E-value: 3.31e-04
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1383-1411 |
7.84e-04 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 39.64 E-value: 7.84e-04
10 20
....*....|....*....|....*....
gi 1814459924 1383 RCDCPPGYSGLSCEACMPGFYRLRSEPGG 1411
Cdd:pfam00053 19 QCLCKPGVTGRHCDRCKPGYYGLPSDPPQ 47
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1383-1411 |
1.19e-03 |
|
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: 39.26 E-value: 1.19e-03
10 20
....*....|....*....|....*....
gi 1814459924 1383 RCDCPPGYSGLSCEACMPGFYRLRSEPGG 1411
Cdd:cd00055 20 QCECKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| TNFRSF21 |
cd10583 |
Tumor necrosis factor receptor superfamily member 21 (TNFRSF21), also known as death receptor ... |
827-933 |
1.49e-03 |
|
Tumor necrosis factor receptor superfamily member 21 (TNFRSF21), also known as death receptor (DR6); TNFRSF21 (also known as death receptor 6 (DR6), CD358, BM-018) is highly expressed in differentiating neurons as well as in the adult brain, and is upregulated in injured neurons. DR6 negatively regulates neurondendrocyte, axondendrocyte, and oligodendrocyte survival, hinders axondendrocyte and oligodendrocyte regeneration and its inhibition has a neuro-protective effect in nerve injury. It activates nuclear factor kappa-B (NFkB) and mitogen-activated protein kinase 8 (MAPK8, also called c-Jun N-terminal kinase 1), and induces cell apoptosis by associating with TNFRSF1A-associated via death domain (TRADD), which is known to mediate signal transduction of tumor necrosis factor receptors. TNFRSF21 plays a role in T-helper cell activation, and may be involved in inflammation and immune regulation. Its possible ligand is alpha-amyloid precursor protein (APP), hence probably involved in the development of Alzheimer's disease; when released, APP binds in an autocrine/paracrine manner to activate a caspase-dependent self-destruction program that removes unnecessary or connectionless axons. Increasing beta-catenin levels in brain endothelium upregulates TNFRSF21 and TNFRSF19, indicating that these death receptors are downstream target genes of Wnt/beta-catenin signaling, which has been shown to be required for blood-brain barrier development. DR6 is up-regulated in numerous solid tumors as well as in tumor vascular cells, including ovarian cancer and may be a clinically useful diagnostic and predictive serum biomarker for some adult sarcoma subtypes.
Pssm-ID: 276909 [Multi-domain] Cd Length: 159 Bit Score: 42.05 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 827 HLDRNLG--LICDECPVG-YTGPH--------CERCAEGYFGQPSLPGGSCQPCQ--CNDNLDFSIPgsCDSLSGSCLIC 893
Cdd:cd10583 4 HVDPATGtqLTCDKCPAGtYVSKHctetslreCSPCPNGTFTRHENGIEQCHRCRkpCPAPMIEKTP--CTALTDRECTC 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1814459924 894 KPGT--TGRYC---ELCADGY----FGDAVDAKNCQPClcnANGSFSEV 933
Cdd:cd10583 82 PPGTflSNDTCvphSVCPVGWgvrkKGTETEDVRCKPC---PRGTFSDV 127
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1727-1899 |
2.06e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 43.08 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1727 KMMTELRRKNLDTQKEVAE---DELVAAEALLKKvkklfgesrgkNEEMEKDLREKLADYKSKVHDAWDLLREATDKIke 1803
Cdd:smart00787 132 KMWYEWRMKLLEGLKEGLDenlEGLKEDYKLLMK-----------ELELLNSIKPKLRDRKDALEEELRQLKQLEDEL-- 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1804 anllsaeNQKNMTALEKKKEAIESGKRQTEDTLKEGTDILDEANRLADEINSVIDYVEDIQTKLpplsEDLKGKIEDLSQ 1883
Cdd:smart00787 199 -------EDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEI----AEAEKKLEQCRG 267
|
170
....*....|....*...
gi 1814459924 1884 -EIKD-RKLAEKVSQAES 1899
Cdd:smart00787 268 fTFKEiEKLKEQLKLLQS 285
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1473-1529 |
3.92e-03 |
|
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: 37.72 E-value: 3.92e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1814459924 1473 CACPLISSSNnfsPSCVTEGLddyRCTaCPREYEGQYCERCAPGYTGSPSSPGGsCQ 1529
Cdd:cd00055 2 CDCNGHGSLS---GQCDPGTG---QCE-CKPNTTGRRCDRCAPGYYGLPSQGGG-CQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1473-1521 |
9.99e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 36.52 E-value: 9.99e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1814459924 1473 CACPLissSNNFSPSCVtegLDDYRCTaCPREYEGQYCERCAPGYTGSP 1521
Cdd:smart00180 1 CDCDP---GGSASGTCD---PDTGQCE-CKPNVTGRRCDRCAPGYYGDG 42
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
38-289 |
1.48e-92 |
|
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: 300.43 E-value: 1.48e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 38 HQQRGLFPAVLNLASSALITTNATCGEKGPEMYCKLVEHVpgqpVRNPQCRIChqNSSNPHLRHPITNAIDGKN----TW 113
Cdd:smart00136 2 GRPRSCYPPFVNLAFGREVTATSTCGEPGPERYCKLVGHT----EQGKKCDYC--DARNPRRSHPAENLTDGNNpnnpTW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 114 WQSPSIKNGIeyHYVTITLDLQQVFQIAYVIVKAAnSPRPGNWILERSLDDVDYKPWQYHAvtdTECLTLYNIyPRTGPP 193
Cdd:smart00136 76 WQSEPLSNGP--QNVNLTLDLGKEFHVTYVILKFC-SPRPSLWILERSDFGKTWQPWQYFS---SDCRRTFGR-PPRGPI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 194 SYAKDDEVICTSFYSKIHPLENGEIHISLINGRPSADDL--SPELLEFTSARYIRLRFQRIRTLNADLMMfahkdpreID 271
Cdd:smart00136 149 TKGNEDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDFdnSPVLQEWVTATNIRVRLTRLRTLGDELMD--------DR 220
|
250
....*....|....*...
gi 1814459924 272 PIVTRRYYYSVKDISVGG 289
Cdd:smart00136 221 PEVTRRYYYAISDIAVGG 238
|
|
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
43-289 |
3.27e-87 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 284.86 E-value: 3.27e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 43 LFPAVLNLASSALITTNATCGEKGPEMYCKLVEHVPGQpvrnpQCRIChqNSSNPHLRHPITNAIDGKN----TWWQSPS 118
Cdd:pfam00055 1 CYPAFGNLAFGREVSATSTCGLNGPERYCILSGLEGGK-----KCFIC--DSRDPHNSHPPSNLTDSNNgtneTWWQSET 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 119 IKngIEYHYVTITLDLQQVFQIAYVIVKAAnSPRPGNWILERSLD-DVDYKPWQYHAvtdTECLTLYNIypRTGPPSYAK 197
Cdd:pfam00055 74 GV--IQYENVNLTLDLGKEFHFTYLILKFK-SPRPAAMVLERSTDfGKTWQPYQYFA---SDCRRTFGR--PSGPSRGIK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 198 DDEVICTSFYSKIHPLENGEIHISLINGRPSA--DDLSPELLEFTSARYIRLRFQRIRTLNadlmmfahkDPREIDPIVT 275
Cdd:pfam00055 146 DDEVICTSEYSDISPLTGGEVIFSTLEGRPSAniFDYSPELQDWLTATNIRIRLLRLHTLG---------DELLDDPSVL 216
|
250
....*....|....
gi 1814459924 276 RRYYYSVKDISVGG 289
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 ... |
1598-1856 |
4.85e-84 |
|
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: 276.99 E-value: 4.85e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1598 MSIN-LTGPLPAPYKILYGLENMTQELKHLLSPQRAPERLIQLAEGNLNTLVTEMNELLTRATKVTADGEQTGQDAERTN 1676
Cdd:pfam06008 2 LSLNsLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1677 TRANSLGEFIKDLAQHAEAVSEKAVKLNETlgiQDKAFERNLQELQNEVDKMMTELRRKNLDTQKEVAEDELVAAEALLK 1756
Cdd:pfam06008 82 GHAKELAEAIKNLIDNIKEINEKVATLGEN---DFALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQDLLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1757 KVKKLFGESRGKNEEMEKDLREKLADYKSKVHDAWDLLREATDKIKEANLLSAENQKNMTALEKKKEAIESGKRQTEDTL 1836
Cdd:pfam06008 159 RIQTWFQSPQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEETL 238
|
250 260
....*....|....*....|
gi 1814459924 1837 KEGTDILDEANRLADEINSV 1856
Cdd:pfam06008 239 KTARDSLDAANLLLQEIDDA 258
|
|
| Laminin_II |
pfam06009 |
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 ... |
2041-2177 |
3.42e-49 |
|
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: 172.29 E-value: 3.42e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2041 VKDKARQANDTAKDVLAQIKDLHQNLDGLKKNYNQLADSVAKTNAVVKDpsKNKIIADADATVKNLEQEADRLIDKLKPI 2120
Cdd:pfam06009 1 SKELAREANETAKEVLEQLAPLSQNLENTSEKLSGINRSLEETNELVND--ANKALDDAGRSVKKLEELAPDLLDKLKPL 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2121 KELEDN---LKKNISEIKELINQARKQANSIKVSVSSGGDCIRTYKPEIKKGSYNSIIVN 2177
Cdd:pfam06009 79 KQLEVNsssLSDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTSL 138
|
|
| LamB |
smart00281 |
Laminin B domain; |
1233-1368 |
1.48e-48 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 169.75 E-value: 1.48e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1233 HLEPFYWKLPEQFEGKKLMAYGGKLKYTIYFEAREEtGFSTYNPQVIIRGGtpsHVRIIIRHMAAPLIGQLTRHEIEMTE 1312
Cdd:smart00281 1 DNEPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRRG-GTHVSAPDVILEGN---GLRISHPAEGPPLPDELTTVEVRFRE 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1814459924 1313 KKWKYYGddpriSRTVTREDFLDVLYDIHYILIKATYGNIMRQSRISEISLEVAEQ 1368
Cdd:smart00281 77 ENWQYYG-----GRPVTREDLMMVLANLTAILIRATYSQQMAGSRLSDVSLEVAVP 127
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
1238-1382 |
6.54e-46 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 162.82 E-value: 6.54e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1238 YWKLPEQFEGKKLMAYGGKLKYTIYFEAREETGFSTYNPQVIIRGGtpsHVRIIIRHMA--APLIGQLTRHEIEMTEKKW 1315
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGGGSLNSEPDVILEGN---GLRLSYSSPDqpPPDPGQEQTYSVRLHEENW 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1814459924 1316 KYygddpRISRTVTREDFLDVLYDIHYILIKATYGNIMRQSRISEISLEVAEQGRItamTPPAHLIE 1382
Cdd:pfam00052 78 RD-----SDGAPVSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSAVPGGS---GPPASWVE 136
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2797-2925 |
1.11e-44 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 159.02 E-value: 1.11e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2797 VRTEAESGLLFYMARINHADFATVQLRNGLPYFSYDLGSGDTNTMIPTKINDGHWHKIKIIRIKQEGIIYVDG-ASNRTI 2875
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGeARPTGE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1814459924 2876 SPKKADI-LDVVGMLYIGGLPINYTTRRIGPVTYSIDGCIRNLQMAEAPAD 2925
Cdd:pfam00054 81 SPLGATTdLDVDGPLYVGGLPSLGVKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
587-726 |
2.26e-41 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 149.73 E-value: 2.26e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 587 YWSAPALYLGNKLTAVGGQLTFTVSYDLEEEEEDTehILQLMIILEGNDLRISTAQDE-VYLQPSEEHINVLSLKEDLFT 665
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGGGSL--NSEPDVILEGNGLRLSYSSPDqPPPDPGQEQTYSVRLHEENWR 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1814459924 666 iHGTNFPVSRKEFMTVLANLKRVLIQITYSLGMDAIfRLSSVGLESAVPYPTDRSiAAAVE 726
Cdd:pfam00052 79 -DSDGAPVSREDFMMVLANLTAILIRATYSTGSGQV-SLSNVSLDSAVPGGSGPP-ASWVE 136
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2372-2511 |
9.57e-41 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 147.85 E-value: 9.57e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2372 FRTFSSNALLMYLATRDLKDFMSVELTDGHIKVSYDLGSGMASVVSNQNHNDGKWKSFTLSRTQKQANISIVDidtnqEE 2451
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDG-----EA 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1814459924 2452 NIATSSP-GNNFglDLKADDKIYFGGLPtlrNLSMKARPEVNLKKYSGCLRDIEISRTPYN 2511
Cdd:pfam00054 76 RPTGESPlGATT--DLDVDGPLYVGGLP---SLGVKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| LamB |
smart00281 |
Laminin B domain; |
582-714 |
3.19e-39 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 143.17 E-value: 3.19e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 582 LPQSYYWSAPALYLGNKLTAVGGQLTFTVSYDLeeeEEDTEHILQLMIILEGNDLRISTAQdEVYLQPSEEHINVLSLKE 661
Cdd:smart00281 1 DNEPVYWVAPEQFLGDKVTSYGGKLRYTLSFDG---RRGGTHVSAPDVILEGNGLRISHPA-EGPPLPDELTTVEVRFRE 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1814459924 662 DLFTIHGtNFPVSRKEFMTVLANLKRVLIQITYSLGMDAIfRLSSVGLESAVP 714
Cdd:smart00281 77 ENWQYYG-GRPVTREDLMMVLANLTAILIRATYSQQMAGS-RLSDVSLEVAVP 127
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2770-2919 |
2.15e-37 |
|
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: 138.71 E-value: 2.15e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2770 FGLSRNSHIAIAFDDTKvKNRLTIEFEVRTEAESGLLFYMARINHADFATVQLRNGLPYFSYDLGSGDTNTMIPTKINDG 2849
Cdd:cd00110 2 VSFSGSSYVRLPTLPAP-RTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1814459924 2850 HWHKIKIIRIKQEGIIYVDG-ASNRTISPKKADILDVVGMLYIGGLPINYTTRRIgPVTYSIDGCIRNLQM 2919
Cdd:cd00110 81 QWHSVSVERNGRSVTLSVDGeRVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGL-PVSPGFVGCIRDLKV 150
|
|
| LamG |
smart00282 |
Laminin G domain; |
2792-2919 |
1.22e-35 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 133.23 E-value: 1.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2792 TIEFEVRTEAESGLLFYMARINHADFATVQLRNGLPYFSYDLGSGDTNTMI-PTKINDGHWHKIKIIRIKQEGIIYVDG- 2869
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSdPTPLNDGQWHRVAVERNGRSVTLSVDGg 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2870 ASNRTISPKKADILDVVGMLYIGGLPINYtTRRIGPVTYSIDGCIRNLQM 2919
Cdd:smart00282 81 NRVSGESPGGLTILNLDGPLYLGGLPEDL-KLPPLPVTPGFRGCIRNLKV 129
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2178-2318 |
1.73e-34 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 129.74 E-value: 1.73e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2178 VKTAVADNLLFYLGSAKFIDFLAIEMRKGKVSFLWDVGSGVGRVEYPDlTIDDSYWYRIEASRTGRNGTISVRALDGPka 2257
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGD-KLNDGKWHSVELERNGRSGTLSVDGEARP-- 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1814459924 2258 simpstyHSASPPGYTIlDVDANAMLFVGGLTG-KLKKADAVRVITFTGCMGEAYFDSKPIG 2318
Cdd:pfam00054 78 -------TGESPLGATT-DLDVDGPLYVGGLPSlGVKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2945-3097 |
4.65e-34 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 129.46 E-value: 4.65e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2945 GTYFDGTGFAKAVDGFKVGLDLLVEFEFRTTRTTGVLLGISSQ-KMDGMGIEMIAEKLMFHVDNGAGRftAVYDAgiPGH 3023
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQnGGDFLALELEDGRLVLRYDLGSGS--LVLSS--KTP 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1814459924 3024 LCDGQWHKVTANKVKHRIELTVDGNQVEAQSPNRASTSADTNDPVFVGGFPEGLNQLGLTTNIRFRGCIRSLRL 3097
Cdd:cd00110 77 LNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKV 150
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2344-2505 |
9.28e-33 |
|
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: 125.61 E-value: 9.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2344 TIQFDGEGYALVSRPIRWYPNiSTVMFKFRTFSSNALLMYLATRDLKDFMSVELTDGHIKVSYDLGSGMASVVSNQNHND 2423
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRTR-LSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLND 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2424 GKWKSFTLSRTQKQANISIvdidtNQEENIATSSPGNNFGLDLkaDDKIYFGGLPTlrnlSMKARPEVNLKKYSGCLRDI 2503
Cdd:cd00110 80 GQWHSVSVERNGRSVTLSV-----DGERVVESGSPGGSALLNL--DGPLYLGGLPE----DLKSPGLPVSPGFVGCIRDL 148
|
..
gi 1814459924 2504 EI 2505
Cdd:cd00110 149 KV 150
|
|
| LamG |
smart00282 |
Laminin G domain; |
2367-2507 |
6.63e-32 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 122.45 E-value: 6.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2367 TVMFKFRTFSSNALLMYLATRDLKDFMSVELTDGHIKVSYDLGSGMASVVSNQNH-NDGKWKSFTLSRTQKQANISIvdi 2445
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPlNDGQWHRVAVERNGRSVTLSV--- 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1814459924 2446 dtNQEENIATSSPGNNFGLDLkaDDKIYFGGLPTlrnlSMKARPEVNLKKYSGCLRDIEISR 2507
Cdd:smart00282 78 --DGGNRVSGESPGGLTILNL--DGPLYLGGLPE----DLKLPPLPVTPGFRGCIRNLKVNG 131
|
|
| LamG |
smart00282 |
Laminin G domain; |
2968-3097 |
8.49e-31 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 119.37 E-value: 8.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2968 VEFEFRTTRTTGVLLGISS-QKMDGMGIEMIAEKLMFHVDNGAGRFTAVYDagiPGHLCDGQWHKVTANKVKHRIELTVD 3046
Cdd:smart00282 2 ISFSFRTTSPNGLLLYAGSkGGGDYLALELRDGRLVLRYDLGSGPARLTSD---PTPLNDGQWHRVAVERNGRSVTLSVD 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1814459924 3047 G-NQVEAQSPnRASTSADTNDPVFVGGFPEGLNQLGLTTNIRFRGCIRSLRL 3097
Cdd:smart00282 79 GgNRVSGESP-GGLTILNLDGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKV 129
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2558-2699 |
1.60e-28 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 112.80 E-value: 1.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2558 FSTKNESGIILlgSGGTpapprrkrrQTGQAYYAIFLNKGRLEVHLSTGARTmrkiAVKPEPSLLHDGREHSVHVERTRG 2637
Cdd:pfam00054 1 FRTTEPSGLLL--YNGT---------QTERDFLALELRDGRLEVSYDLGSGA----AVVRSGDKLNDGKWHSVELERNGR 65
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1814459924 2638 IFTVQVDEDRRHV--QNLTVEQAIEV-KKLFVGGAPPE-FQPSPLRNIPPFEGCIWNLVINSVPMD 2699
Cdd:pfam00054 66 SGTLSVDGEARPTgeSPLGATTDLDVdGPLYVGGLPSLgVKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2532-2694 |
8.67e-28 |
|
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: 111.36 E-value: 8.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2532 TVSFPKPGFVELSPVPID-VGTEINLSFSTKNESGIILLGSGgtpapprrkrrQTGQAYYAIFLNKGRLEVHLSTGARTM 2610
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPrTRLSISFSFRTTSPNGLLLYAGS-----------QNGGDFLALELEDGRLVLRYDLGSGSL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2611 RkiaVKPePSLLHDGREHSVHVERTRGIFTVQVDEDR--RHVQNLTVEQAIEVKKLFVGGAPPEFQPSPLRNIPPFEGCI 2688
Cdd:cd00110 70 V---LSS-KTPLNDGQWHSVSVERNGRSVTLSVDGERvvESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCI 145
|
....*.
gi 1814459924 2689 WNLVIN 2694
Cdd:cd00110 146 RDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
2173-2315 |
4.62e-27 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 108.58 E-value: 4.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2173 SIIVNVKTAVADNLLFYLGSAKFIDFLAIEMRKGKVSFLWDVGSGVGRVEYPDLTIDDSYWYRIEASRTGRNGTISVral 2252
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLNDGQWHRVAVERNGRSVTLSV--- 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1814459924 2253 DGPKASIMPstyhsaSPPGYTILDVDANamLFVGGLTGKLKKADAVRVITFTGCMGEAYFDSK 2315
Cdd:smart00282 78 DGGNRVSGE------SPGGLTILNLDGP--LYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2797-2919 |
8.85e-26 |
|
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: 104.81 E-value: 8.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2797 VRTEAESGLLFYMARINHaDFATVQLRNGLPYFSYDLGSGDTNTM-IPTKINDGHWHKIKIIRIKQEGIIYVDGASNRTI 2875
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGS-DFLALELVNGRLVLRYDLGSGPESLLsSGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSS 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1814459924 2876 S-PKKADILDVVGMLYIGGLPINYTTRRIgPVTYSIDGCIRNLQM 2919
Cdd:pfam02210 80 LpPGESLLLNLNGPLYLGGLPPLLLLPAL-PVRAGFVGCIRDVRV 123
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2154-2313 |
1.03e-25 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 105.58 E-value: 1.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2154 SGGDCIRtYKPEIKKGSYNSIIVNVKTAVADNLLFYLGSAKFIDFLAIEMRKGKVSFLWDVGSGVGRVEYPDlTIDDSYW 2233
Cdd:cd00110 5 SGSSYVR-LPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKT-PLNDGQW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2234 YRIEASRTGRNGTISVralDGPKasimpsTYHSASPPGYTILDVDANamLFVGGLTGKLKKADAVRVITFTGCMGEAYFD 2313
Cdd:cd00110 83 HSVSVERNGRSVTLSV---DGER------VVESGSPGGSALLNLDGP--LYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2972-3097 |
1.55e-25 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 104.04 E-value: 1.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2972 FRTTRTTGVLLGISSQKMDGMGIEMIAEKLMFHVDNGAGRFTAVYdagIPGHLCDGQWHKVTANKVKHRIELTVDGNQVE 3051
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDFLALELVNGRLVLRYDLGSGPESLLS---SGKNLNDGQWHSVRVERNGNTLTLSVDGQTVV 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1814459924 3052 AQSPNRASTSADTNDPVFVGGFPEGLNQLGLTTNIRFRGCIRSLRL 3097
Cdd:pfam02210 78 SSLPPGESLLLNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRV 123
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2372-2505 |
6.02e-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: 6.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2372 FRTFSSNALLMYlATRDLKDFMSVELTDGHIKVSYDLGSG-MASVVSNQNHNDGKWKSFTLSRTQKQANISIvdidtNQE 2450
Cdd:pfam02210 1 FRTRQPNGLLLY-AGGGGSDFLALELVNGRLVLRYDLGSGpESLLSSGKNLNDGQWHSVRVERNGNTLTLSV-----DGQ 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1814459924 2451 ENIATSSPGNNFGLDLKADdkIYFGGLPTLRNLSmkarPEVNLKKYSGCLRDIEI 2505
Cdd:pfam02210 75 TVVSSLPPGESLLLNLNGP--LYLGGLPPLLLLP----ALPVRAGFVGCIRDVRV 123
|
|
| LamG |
smart00282 |
Laminin G domain; |
2553-2696 |
4.71e-23 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 97.02 E-value: 4.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2553 EINLSFSTKNESGIILLGSGGTpapprrkrrqtGQAYYAIFLNKGRLEVHLSTGARTmrkIAVKPEPSLLHDGREHSVHV 2632
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKG-----------GGDYLALELRDGRLVLRYDLGSGP---ARLTSDPTPLNDGQWHRVAV 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1814459924 2633 ERTRGIFTVQVD-EDRRHVQNLTVEQAIEVK-KLFVGGAPPEFQPSPLRNIPPFEGCIWNLVINSV 2696
Cdd:smart00282 67 ERNGRSVTLSVDgGNRVSGESPGGLTILNLDgPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2972-3095 |
2.52e-21 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 91.99 E-value: 2.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2972 FRTTRTTGVLLGISSQ-KMDGMGIEMIAEKLMFHVDNGAGRFTAVYdagiPGHLCDGQWHKVTANKVKHRIELTVDGNQV 3050
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQtERDFLALELRDGRLEVSYDLGSGAAVVRS----GDKLNDGKWHSVELERNGRSGTLSVDGEAR 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1814459924 3051 E-AQSPNRASTSADTNDPVFVGGFPE-GLNQLGLTTNIRFRGCIRSL 3095
Cdd:pfam00054 77 PtGESPLGATTDLDVDGPLYVGGLPSlGVKKRRLAISPSFDGCIRDV 123
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1611-2174 |
9.92e-18 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 90.89 E-value: 9.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1611 KILYGLENMTQELKHLLSPQRAPERLIQLAEGNLNTLVTEMNELLTRATKVTADGEQTG---QDAERTNTRANSLGEFIK 1687
Cdd:PRK03918 169 EVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEkevKELEELKEEIEELEKELE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1688 DLAQHAEAVSEKAVKLNETLGIQDKAFE------RNLQELQNEVDKMMT--ELRRKNLDTQKEVaEDELVAAEALLKKVK 1759
Cdd:PRK03918 249 SLEGSKRKLEEKIRELEERIEELKKEIEeleekvKELKELKEKAEEYIKlsEFYEEYLDELREI-EKRLSRLEEEINGIE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1760 KLFGESRGKNEEME------KDLREKLADYKSKVhdawDLLREATDKIKEANLLSAENQ-KNMTALEKKKEAIESGKRQT 1832
Cdd:PRK03918 328 ERIKELEEKEERLEelkkklKELEKRLEELEERH----ELYEEAKAKKEELERLKKRLTgLTPEKLEKELEELEKAKEEI 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1833 EDTLKEgtdILDEANRLADEINSVIDYVEDIQT---KLP----PLSEDLKG--------KIEDLSQEIKdrKLAEKVSQA 1897
Cdd:PRK03918 404 EEEISK---ITARIGELKKEIKELKKAIEELKKakgKCPvcgrELTEEHRKelleeytaELKRIEKELK--EIEEKERKL 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1898 ESHAAQ----LNDSSAV--LDRILDEAKNISfnataafkaySNIKDY-IDKAEKIAKEAKVLAHEATELatgpqGSLQEG 1970
Cdd:PRK03918 479 RKELRElekvLKKESELikLKELAEQLKELE----------EKLKKYnLEELEKKAEEYEKLKEKLIKL-----KGEIKS 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1971 AKGSLQKSFGFLNEAKKLANDVKENDEHLNGLTSRL--------DNANVRNRDLLRALNDTLErLSAIPNDTAAKLQAVK 2042
Cdd:PRK03918 544 LKKELEKLEELKKKLAELEKKLDELEEELAELLKELeelgfesvEELEERLKELEPFYNEYLE-LKDAEKELEREEKELK 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2043 DKARQANDTAKD---VLAQIKDLHQNLDGLKKNYNQladsvaKTNAVVKDP--SKNKIIADADATVKNLEQEADRLIDKL 2117
Cdd:PRK03918 623 KLEEELDKAFEElaeTEKRLEELRKELEELEKKYSE------EEYEELREEylELSRELAGLRAELEELEKRREEIKKTL 696
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 1814459924 2118 KPIKELEDNLKKNISEIkELINQARKQANSIKvsvssggDCIRTYKPEIKKGSYNSI 2174
Cdd:PRK03918 697 EKLKEELEEREKAKKEL-EKLEKALERVEELR-------EKVKKYKALLKERALSKV 745
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2558-2696 |
1.29e-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: 81.31 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2558 FSTKNESGIILLGSGGtpapprrkrrqtGQAYYAIFLNKGRLEVHLSTGARTMRkiaVKPEPSLLHDGREHSVHVERTRG 2637
Cdd:pfam02210 1 FRTRQPNGLLLYAGGG------------GSDFLALELVNGRLVLRYDLGSGPES---LLSSGKNLNDGQWHSVRVERNGN 65
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1814459924 2638 IFTVQVDEDRRHVQNLTVEQAI--EVKKLFVGGAPPEFQPSPLRNIPPFEGCIWNLVINSV 2696
Cdd:pfam02210 66 TLTLSVDGQTVVSSLPPGESLLlnLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1610-2168 |
2.28e-17 |
|
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: 89.31 E-value: 2.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1610 YKILYGLENMTQELKHLLSPQRAPERLIQLAEGNLNTLVTEMNELLTRATKV----TADgEQTGQDAERTNTRANSLGEF 1685
Cdd:TIGR04523 141 DKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIknklLKL-ELLLSNLKKKIQKNKSLESQ 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1686 IKDLAQH----AEAVSEKAVKLNETLGIQDKAfERNLQELQNEVDKMMTELRRKNLDTQKevAEDELVAAEALLKKVK-K 1760
Cdd:TIGR04523 220 ISELKKQnnqlKDNIEKKQQEINEKTTEISNT-QTQLNQLKDEQNKIKKQLSEKQKELEQ--NNKKIKELEKQLNQLKsE 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1761 LFGESRGKNEEMEKDLREKLADYKSKVHDAWDLLREATDKI-----------KEANLLSAENQKNMTALEKKKEAIESGK 1829
Cdd:TIGR04523 297 ISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIIsqlneqisqlkKELTNSESENSEKQRELEEKQNEIEKLK 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1830 RQTEDTLKEGTDILDEANRLADEINSVIDYVEDIQTKLpplsEDLKGKIEDLSQEIKDrkLAEKVSQAESHAAQLNDSSA 1909
Cdd:TIGR04523 377 KENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQI----KKLQQEKELLEKEIER--LKETIIKNNSEIKDLTNQDS 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1910 VLDRILDEAKNIsfnaTAAFKaySNIKDYIDKAEKIAKEAKVLAHEATelatgpqgslqegakgslQKSfgflNEAKKLA 1989
Cdd:TIGR04523 451 VKELIIKNLDNT----RESLE--TQLKVLSRSINKIKQNLEQKQKELK------------------SKE----KELKKLN 502
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1990 NDVKENDEHLNGLTSRLDNANVRNRDL----------LRALNDTLERLSAipNDTAAKLQAVKDKARQandtakdvlaQI 2059
Cdd:TIGR04523 503 EEKKELEEKVKDLTKKISSLKEKIEKLesekkekeskISDLEDELNKDDF--ELKKENLEKEIDEKNK----------EI 570
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2060 KDLHQNLDGLKKNYNQLADSVAKTNAVVKDpsKNKIIADADATVKNLEQEAD-------RLIDKLKPIKELEDNLKKNIS 2132
Cdd:TIGR04523 571 EELKQTQKSLKKKQEEKQELIDQKEKEKKD--LIKEIEEKEKKISSLEKELEkakkeneKLSSIIKNIKSKKNKLKQEVK 648
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1814459924 2133 EIKELINQAR-KQAN---SIKVSVSSGGDCIRT-----------YKPEIKK 2168
Cdd:TIGR04523 649 QIKETIKEIRnKWPEiikKIKESKTKIDDIIELmkdwlkelslhYKKYITR 699
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2178-2315 |
6.10e-17 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 79.39 E-value: 6.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2178 VKTAVADNLLFYLGSAKfIDFLAIEMRKGKVSFLWDVGSGVGRVEYPDLTIDDSYWYRIEASRTGRNGTISVralDGpka 2257
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGG-SDFLALELVNGRLVLRYDLGSGPESLLSSGKNLNDGQWHSVRVERNGNTLTLSV---DG--- 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1814459924 2258 simpsTYHSASPPGYTILDVDANAMLFVGGLTGKLKKADAVRVITFTGCMGEAYFDSK 2315
Cdd:pfam02210 74 -----QTVVSSLPPGESLLLNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1686-2181 |
6.79e-17 |
|
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: 87.77 E-value: 6.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1686 IKDLAQHAEAVSEKAVKLN---ETLGIQDKAFERNLQELQNEVDKMMTELRRKNLdtqkevaedELVAAEALLKKVKKL- 1761
Cdd:TIGR04523 147 IKKKEKELEKLNNKYNDLKkqkEELENELNLLEKEKLNIQKNIDKIKNKLLKLEL---------LLSNLKKKIQKNKSLe 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1762 --FGESRGKNEEMEKDLREKladyKSKVHDAWDLLREATDKIKEanlLSAENQKNMTALEKKKEAIESGKR---QTEDTL 1836
Cdd:TIGR04523 218 sqISELKKQNNQLKDNIEKK----QQEINEKTTEISNTQTQLNQ---LKDEQNKIKKQLSEKQKELEQNNKkikELEKQL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1837 KE-GTDILD-----EAN---RLADEINSVIDYVEDIQTKLpplSE------DLKGKIEDLSQEI---------KDRKLAE 1892
Cdd:TIGR04523 291 NQlKSEISDlnnqkEQDwnkELKSELKNQEKKLEEIQNQI---SQnnkiisQLNEQISQLKKELtnsesenseKQRELEE 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1893 KVSQAESHAAQlNDSSavldriLDEAKNISfnataafkaySNIKDYIDKAEKIAKEAKVLAHEATELatgpqgslqEGAK 1972
Cdd:TIGR04523 368 KQNEIEKLKKE-NQSY------KQEIKNLE----------SQINDLESKIQNQEKLNQQKDEQIKKL---------QQEK 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1973 GSLQKsfgflnEAKKLANDVKENDEHLNGLTSRlDNA---NVRNRDLLR-ALNDTLERLSA----IPNDTAAKLQAVKDK 2044
Cdd:TIGR04523 422 ELLEK------EIERLKETIIKNNSEIKDLTNQ-DSVkelIIKNLDNTReSLETQLKVLSRsinkIKQNLEQKQKELKSK 494
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2045 ARQA---NDTAKDVLAQIKDLHQNLDGLKKNYNQLADSVAKTNAVVKDPSKNKIIADADATVKNLEQEADRLIDKLKPIK 2121
Cdd:TIGR04523 495 EKELkklNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELK 574
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1814459924 2122 ELEDNLKKNISEIKELINQARKQANSIK-------VSVSSGGDCIRTYKPEIKKgsYNSIIVNVKTA 2181
Cdd:TIGR04523 575 QTQKSLKKKQEEKQELIDQKEKEKKDLIkeieekeKKISSLEKELEKAKKENEK--LSSIIKNIKSK 639
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1721-2145 |
2.87e-15 |
|
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: 82.81 E-value: 2.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1721 LQNEVDKM--MTELRRKNL----------DTQKEVAEDELVAAEALLKKVKKLFGESRGKNEEMEKDlREKLADYKskvh 1788
Cdd:TIGR02169 140 LQGDVTDFisMSPVERRKIideiagvaefDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRE-REKAERYQ---- 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1789 dawDLLREatdKIK-EANLLSAENQknmtALEKKKEAIEsgkRQTEDTLKEGTDILDEANRLADEINSVIDYVEDIQTKL 1867
Cdd:TIGR02169 215 ---ALLKE---KREyEGYELLKEKE----ALERQKEAIE---RQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKI 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1868 PPLSED----LKGKIEDLSQEIK--DRKLAEKVSQAESHAAQLNDSSAVLDRILDEAKNISfnataafkaySNIKDYIDK 1941
Cdd:TIGR02169 282 KDLGEEeqlrVKEKIGELEAEIAslERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELE----------REIEEERKR 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1942 AEKIAKEAKVLAHEATELatgpQGSLQEGAKgslqksfgflnEAKKLANDVKENDEHLNGLTSRLDNANvRNRDllrALN 2021
Cdd:TIGR02169 352 RDKLTEEYAELKEELEDL----RAELEEVDK-----------EFAETRDELKDYREKLEKLKREINELK-RELD---RLQ 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2022 DTLERLSAIPNDTAAKLQAVKDKARQANDTAKDVLAQIKDLHQNLDGLKKnynqladsvaktnavvkdpsknkIIADADA 2101
Cdd:TIGR02169 413 EELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAA-----------------------DLSKYEQ 469
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1814459924 2102 TVKNLEQEADRLidklkpikelEDNLKKNISEIKELinQARKQA 2145
Cdd:TIGR02169 470 ELYDLKEEYDRV----------EKELSKLQRELAEA--EAQARA 501
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1708-2140 |
2.31e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 79.70 E-value: 2.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1708 GIQDKAFERNLQELQNEVDKMMTELRRKNldTQKEVAEDELVAAEALLKkvkklfgESRGKNEEME------KDLREKLA 1781
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAELDEEIERYE--EQREQARETRDEADEVLE-------EHEERREELEtleaeiEDLRETIA 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1782 -------DYKSKVHDAWD----LLREATDKIKEANLLSAENqknmTALEKKKEAIESGKRQTEDTLKE----GTDILDEA 1846
Cdd:PRK02224 269 eterereELAEEVRDLRErleeLEEERDDLLAEAGLDDADA----EAVEARREELEDRDEELRDRLEEcrvaAQAHNEEA 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1847 NRLADEINSVIDYVEDIQTKlpplSEDLKGKIEDLSQEIKDRK--LAEKVSQAESHAAQLNDSSAVLDRI------LDEA 1918
Cdd:PRK02224 345 ESLREDADDLEERAEELREE----AAELESELEEAREAVEDRReeIEELEEEIEELRERFGDAPVDLGNAedfleeLREE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1919 KNISFNATAAFKA-YSNIKDYIDKAEKI-----------------------AKEAKVLAHEAtELATgpqgslQEGAKGS 1974
Cdd:PRK02224 421 RDELREREAELEAtLRTARERVEEAEALleagkcpecgqpvegsphvetieEDRERVEELEA-ELED------LEEEVEE 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1975 LQKSFGFLNEAKKLANDVKENDEHLNGLTSRLDNAnvrnRDLLRALNDTLERLSAIPNDTAAKLQAVKDKARQANDTAKD 2054
Cdd:PRK02224 494 VEERLERAEDLVEAEDRIERLEERREDLEELIAER----RETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEE 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2055 VLAQIKDLHQNLDGLKKNYNQLADsvaktnavvkdpsknkiIADADATVKNLEQEADRLIDKLKPIKELEDNLKKNISEI 2134
Cdd:PRK02224 570 AREEVAELNSKLAELKERIESLER-----------------IRTLLAAIADAEDEIERLREKREALAELNDERRERLAEK 632
|
....*.
gi 1814459924 2135 KELINQ 2140
Cdd:PRK02224 633 RERKRE 638
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1609-2137 |
5.48e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 78.54 E-value: 5.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1609 PYKILYGLE----NMTQELKHLLSPQ-RAPERLiqlaeGNLNTLVTEMNELLTRATKVTADGEQTGQDAERTNTRANSLG 1683
Cdd:PRK02224 204 LHERLNGLEselaELDEEIERYEEQReQARETR-----DEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELA 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1684 EFIKDLAQHAEAVSEKAVKLNETLGIQDKAFERnLQELQNEVDKMMTELRRKnLDTQKEVAEDELVAAEALLKKVKKLfg 1763
Cdd:PRK02224 279 EEVRDLRERLEELEEERDDLLAEAGLDDADAEA-VEARREELEDRDEELRDR-LEECRVAAQAHNEEAESLREDADDL-- 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1764 esrgknEEMEKDLREKLADYKSKVHDAWDLLREATDKIKEanlLSAENQKNMTA-----------------LEKKKEAIE 1826
Cdd:PRK02224 355 ------EERAEELREEAAELESELEEAREAVEDRREEIEE---LEEEIEELRERfgdapvdlgnaedfleeLREERDELR 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1827 SGKRQTEDTLKEGTDILDEANRLADE--------------INSVIDYVEDIQTKLPPLSEDLKGKIEDLSQEIkDRklAE 1892
Cdd:PRK02224 426 EREAELEATLRTARERVEEAEALLEAgkcpecgqpvegspHVETIEEDRERVEELEAELEDLEEEVEEVEERL-ER--AE 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1893 KVSQAESHAAQLNDSSAVLDRILDEAKNIsfnataafkaysnIKDYIDKAEKIAKEAKVLAHEAtelatgpqgslqEGAK 1972
Cdd:PRK02224 503 DLVEAEDRIERLEERREDLEELIAERRET-------------IEEKRERAEELRERAAELEAEA------------EEKR 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1973 GSLQKSFGflnEAKKLANDVKENDEHLNGLTSRLDNANvRNRDLLRALNDTLERLSAIpndtAAKLQAVKDKarqaNDTA 2052
Cdd:PRK02224 558 EAAAEAEE---EAEEAREEVAELNSKLAELKERIESLE-RIRTLLAAIADAEDEIERL----REKREALAEL----NDER 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2053 KDVLAQIKDLHQnldglkknynQLADSVaktnavvkDPSKnkiIADADATVKNLEQEADRLIDKLKPIKELEDNLKKNI- 2131
Cdd:PRK02224 626 RERLAEKRERKR----------ELEAEF--------DEAR---IEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIg 684
|
....*....
gi 1814459924 2132 ---SEIKEL 2137
Cdd:PRK02224 685 aveNELEEL 693
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1722-2145 |
6.94e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 78.16 E-value: 6.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1722 QNEVDKM----------MTE--LRRKNLDTQKEVAEDELVAAEALLKKVKKLFGESRGKNEEME-KDLREKLADYKSKvh 1788
Cdd:PRK02224 137 QGEVNKLinatpsdrqdMIDdlLQLGKLEEYRERASDARLGVERVLSDQRGSLDQLKAQIEEKEeKDLHERLNGLESE-- 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1789 dawdlLREATDKIKEanllsaenqknmtaLEKKKEAIESGKRQTEDTLKEGTDILDEANRLADEINSVIDYVEDIQTKlp 1868
Cdd:PRK02224 215 -----LAELDEEIER--------------YEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETERE-- 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1869 plSEDLKGKIEDLSQ---EIKDRkLAEKVSQAESHAAqlnDSSAVLDRI--LDEAKN-----ISFNATAAFKAYSNIKDY 1938
Cdd:PRK02224 274 --REELAEEVRDLRErleELEEE-RDDLLAEAGLDDA---DAEAVEARReeLEDRDEelrdrLEECRVAAQAHNEEAESL 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1939 IDKAEKIAKEAKVLAHEATELATGPQGSLQEGAKGSlqksfgflNEAKKLANDVKENDEHLNGLTSRLDNANVRNRDLLR 2018
Cdd:PRK02224 348 REDADDLEERAEELREEAAELESELEEAREAVEDRR--------EEIEELEEEIEELRERFGDAPVDLGNAEDFLEELRE 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2019 ALNDTLERLsaipNDTAAKLQAVKDKARQAN---------------------DTAKDVLAQIKDLHQNLDGLKKNYNQLA 2077
Cdd:PRK02224 420 ERDELRERE----AELEATLRTARERVEEAEalleagkcpecgqpvegsphvETIEEDRERVEELEAELEDLEEEVEEVE 495
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1814459924 2078 DSVAKTNAVVKdpsknkiiadadatvknLEQEADRLIDKLKPIKELEDNLKKNISEIKELINQARKQA 2145
Cdd:PRK02224 496 ERLERAEDLVE-----------------AEDRIERLEERREDLEELIAERRETIEEKRERAEELRERA 546
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1739-2080 |
8.36e-14 |
|
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: 78.17 E-value: 8.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1739 TQKEVAEDELVAAEALLKKVKKLFGESRGKNEEMEK--DLREKLADYKSKvhdawdlLREAtdkikEANLLSAEnqknMT 1816
Cdd:TIGR02168 172 ERRKETERKLERTRENLDRLEDILNELERQLKSLERqaEKAERYKELKAE-------LREL-----ELALLVLR----LE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1817 ALEKKKEAIESGKRQTEDTLKEGTDILDEA----NRLADEINSVIDYVEDIQTKLpplsEDLKGKIEDLSQEIkdRKLAE 1892
Cdd:TIGR02168 236 ELREELEELQEELKEAEEELEELTAELQELeeklEELRLEVSELEEEIEELQKEL----YALANEISRLEQQK--QILRE 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1893 KVSQAESHAAQLNDSSAVLDRILDEAKnisFNATAAFKAYSNIKDYIDKAEKIAKEAKVLAHEATELATGPQGSLQEGAK 1972
Cdd:TIGR02168 310 RLANLERQLEELEAQLEELESKLDELA---EELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1973 GSLQKsfgfLNEAKKLANDVKENDEHLNGLTSRLDNANVRNRDLLR-------------------ALNDTLERLSAIpND 2033
Cdd:TIGR02168 387 KVAQL----ELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKkleeaelkelqaeleeleeELEELQEELERL-EE 461
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1814459924 2034 TAAKLQAVKDKARQANDTAKDVLAQ-------IKDLHQNLDG-------LKKNYNQLADSV 2080
Cdd:TIGR02168 462 ALEELREELEEAEQALDAAERELAQlqarldsLERLQENLEGfsegvkaLLKNQSGLSGIL 522
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
921-967 |
1.36e-13 |
|
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: 67.38 E-value: 1.36e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1814459924 921 PCLCNANGSFSEVCHAQTGQCECKPNVQGRQCDECKPETFGLQSARG 967
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGG 47
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1621-1950 |
2.61e-13 |
|
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: 76.63 E-value: 2.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1621 QELKHLLSPQRAPERLIQLAEGNLNTLVTEMNELLTRATKVTADGEQTGQD--------------AERTNTRANSLGEFI 1686
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQisalrkdlarleaeVEQLEERIAQLSKEL 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1687 KDLAQHAEAVSEKAVKLNETLgiqdKAFERNLQELQNEVDKMMTELR--RKNLDTQKEVAEDELVAAEALLKKVKKLFGE 1764
Cdd:TIGR02168 757 TELEAEIEELEERLEEAEEEL----AEAEAEIEELEAQIEQLKEELKalREALDELRAELTLLNEEAANLRERLESLERR 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1765 SRGKNEEME------KDLREKLADYKSKVHDAWDLLREATDKIKEANLLSAENQKNMTALEKKKEAIESGKRQTEDTLKE 1838
Cdd:TIGR02168 833 IAATERRLEdleeqiEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1839 GTDILDEANrladeinsviDYVEDIQTKLPPLSEDLKGKIEDLSQEIKD--RKLAEKVSQAESHAAQLNDSSAVLDRILD 1916
Cdd:TIGR02168 913 LRRELEELR----------EKLAQLELRLEGLEVRIDNLQERLSEEYSLtlEEAEALENKIEDDEEEARRRLKRLENKIK 982
|
330 340 350
....*....|....*....|....*....|....
gi 1814459924 1917 EAKNISFNATAAFKAYSNIKDYIDKAEKIAKEAK 1950
Cdd:TIGR02168 983 ELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAK 1016
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1689-2150 |
2.95e-13 |
|
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: 76.31 E-value: 2.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1689 LAQHAEAVSEKAVKLNETLGIQDKA----------FERNLQELQNEVDKmMTELRRKNLDTQKEVAED------ELVAAE 1752
Cdd:pfam15921 80 LEEYSHQVKDLQRRLNESNELHEKQkfylrqsvidLQTKLQEMQMERDA-MADIRRRESQSQEDLRNQlqntvhELEAAK 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1753 ALLKKVKKlfgesrGKNEEMEKdLREKLADYKSKVHDAWDLL---REAT-DKIKEANLLSAENQKNM-TALEKkkeaies 1827
Cdd:pfam15921 159 CLKEDMLE------DSNTQIEQ-LRKMMLSHEGVLQEIRSILvdfEEASgKKIYEHDSMSTMHFRSLgSAISK------- 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1828 gkrqtedTLKEgtdiLD-EANRLADEINSVIDYVEDI----QTKLPPLSEDLKGKIEDL--SQEIKDRKLAEKVSQAESH 1900
Cdd:pfam15921 225 -------ILRE----LDtEISYLKGRIFPVEDQLEALksesQNKIELLLQQHQDRIEQLisEHEVEITGLTEKASSARSQ 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1901 AaqlNDSSAVLDRILDEAKN--------ISFNATAAFKAYSNIKD----YIDKAEKIAKEAKVLAHEATELATGPQGSLQ 1968
Cdd:pfam15921 294 A---NSIQSQLEIIQEQARNqnsmymrqLSDLESTVSQLRSELREakrmYEDKIEELEKQLVLANSELTEARTERDQFSQ 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1969 EGAK--GSLQKSFGFLNEAKKLANDVKENDEHL------NGLT-----SRLDNANV---RNRDLLRAL------------ 2020
Cdd:pfam15921 371 ESGNldDQLQKLLADLHKREKELSLEKEQNKRLwdrdtgNSITidhlrRELDDRNMevqRLEALLKAMksecqgqmerqm 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2021 ------NDTLERLSAIpndtAAKLQAVKDKARQandtakdVLAQIKDLHQNLDGLKKNYNQLADSVAKtnavvkdpsKNK 2094
Cdd:pfam15921 451 aaiqgkNESLEKVSSL----TAQLESTKEMLRK-------VVEELTAKKMTLESSERTVSDLTASLQE---------KER 510
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1814459924 2095 IIADADATVKNLEQEADRLIDKLKPIKELEDNLKKNISEIKELINQARKQANSIKV 2150
Cdd:pfam15921 511 AIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEI 566
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1702-2100 |
3.53e-13 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 74.17 E-value: 3.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1702 KLNETLGIQDKAFERNLQELQNEVDKMMTELRRknldTQKEVAEdelvaaeallkkvkklfgesrgKNEEMEKdLREKLA 1781
Cdd:COG4372 17 GLRPKTGILIAALSEQLRKALFELDKLQEELEQ----LREELEQ----------------------AREELEQ-LEEELE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1782 DYKSKVHDAWDLLREATDKIKEANLLSAENQKNMTALEKKKEAIEsgkRQTEDTLKEGTDILDEANRLADEINSVIDYVE 1861
Cdd:COG4372 70 QARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQ---EELEELQKERQDLEQQRKQLEAQIAELQSEIA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1862 DIQTKLpplsEDLKGKIEDLSQEIKdrKLAEKVSQAESHAAQlndssAVLDRILDEAKNISFNATAAFKAysniKDYIDK 1941
Cdd:COG4372 147 EREEEL----KELEEQLESLQEELA--ALEQELQALSEAEAE-----QALDELLKEANRNAEKEEELAEA----EKLIES 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1942 AEKIAKEAKVLAHEATELATGPQGSLQEGAKGSLQKSFGFLNEAKKLANDVKEN--DEHLNGLTSRLDNANVRNRDLLRA 2019
Cdd:COG4372 212 LPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELaiLVEKDTEEEELEIAALELEALEEA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2020 LNDTLERLSAIPNDTAAKLQAVKDKARQANDTAKdvlAQIKDLHQNLDGLKKNYNQLADSVAKTNAVVKDPSKNKIIADA 2099
Cdd:COG4372 292 ALELKLLALLLNLAALSLIGALEDALLAALLELA---KKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVA 368
|
.
gi 1814459924 2100 D 2100
Cdd:COG4372 369 D 369
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1621-2142 |
4.23e-13 |
|
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: 75.98 E-value: 4.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1621 QELKHLlspQRAPERLIQLAEGNL-------NTLVTEMNELLTRATKVTADGEQTGQDAERTNtraNSLGEFIKDLAQHA 1693
Cdd:pfam01576 327 QEVTEL---KKALEEETRSHEAQLqemrqkhTQALEELTEQLEQAKRNKANLEKAKQALESEN---AELQAELRTLQQAK 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1694 EAVSEKAVKLnetlgiqdkafERNLQELQnevdkmmteLRRKNLDTQKEVAEDELVAAEALLKKVKKLFGESRGKNEEME 1773
Cdd:pfam01576 401 QDSEHKRKKL-----------EGQLQELQ---------ARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLS 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1774 KDlrekLADYKSKVHDAWDLLREAT-DKIKEANLLSA-ENQKNmtALEKKKEAIESGKRQTEDTLKEGTDILDEANRLAD 1851
Cdd:pfam01576 461 KD----VSSLESQLQDTQELLQEETrQKLNLSTRLRQlEDERN--SLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLE 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1852 EINSVIDYVEDIQTKlpplsedLKGKIEDLSQEIKDRKLA-EKVSQAESHAAQ-LNDSSAVLDR---------------- 1913
Cdd:pfam01576 535 EDAGTLEALEEGKKR-------LQRELEALTQQLEEKAAAyDKLEKTKNRLQQeLDDLLVDLDHqrqlvsnlekkqkkfd 607
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1914 -ILDEAKNISfnataafkaySNIKDYIDKAEKIA--KEAKVLA-HEATELATGPQGSLQEGAKgSLQKSFGFLNEAKkla 1989
Cdd:pfam01576 608 qMLAEEKAIS----------ARYAEERDRAEAEAreKETRALSlARALEEALEAKEELERTNK-QLRAEMEDLVSSK--- 673
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1990 NDVKENDEHLN----GLTSRLDNANVRNRDL---LRALNDTLERLSAipNDTAAKLQAVKD-KAR--QANDTAKDVLAQI 2059
Cdd:pfam01576 674 DDVGKNVHELErskrALEQQVEEMKTQLEELedeLQATEDAKLRLEV--NMQALKAQFERDlQARdeQGEEKRRQLVKQV 751
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2060 KDLHQNLDGLKKNYNQLADSVAKTNAVVKDpsknkIIADADATVKNLEqEADRLIDKLKP-IKELEDNLKKNISEIKELI 2138
Cdd:pfam01576 752 RELEAELEDERKQRAQAVAAKKKLELDLKE-----LEAQIDAANKGRE-EAVKQLKKLQAqMKDLQRELEEARASRDEIL 825
|
....
gi 1814459924 2139 NQAR 2142
Cdd:pfam01576 826 AQSK 829
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
971-1015 |
5.40e-13 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 65.41 E-value: 5.40e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1814459924 971 CNCNSFGSKSFDCE-ESGQCWCQPGVTGKKCDRCAHGYFNFQEGGC 1015
Cdd:smart00180 1 CDCDPGGSASGTCDpDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
922-968 |
8.51e-13 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 65.07 E-value: 8.51e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1814459924 922 CLCNANGSFSEVCHAQTGQCECKPNVQGRQCDECKPETFGLQ--SARGC 968
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPsdPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
922-968 |
9.99e-13 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 64.64 E-value: 9.99e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1814459924 922 CLCNANGSFSEVCHAQTGQCECKPNVQGRQCDECKPETFGlQSARGC 968
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYG-DGPPGC 46
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1770-2149 |
1.43e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 73.94 E-value: 1.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1770 EEMEKDLRE--KLADYKSkvhdAWDLLREAtdkIKEanllsaenqknmtaLEKKKEAIESGKRQTEDtlkegtdILDEAN 1847
Cdd:PRK03918 145 ESREKVVRQilGLDDYEN----AYKNLGEV---IKE--------------IKRRIERLEKFIKRTEN-------IEELIK 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1848 RLADEINSVIDYVEDIQTKLPPLSEDL-------------KGKIEDLSQEIKD-----RKLAEKVSQAESHAAQLNDSSA 1909
Cdd:PRK03918 197 EKEKELEEVLREINEISSELPELREELeklekevkeleelKEEIEELEKELESlegskRKLEEKIRELEERIEELKKEIE 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1910 VLDRILDEAKNISFNAtaafKAYSNIKDYIDKAEKIAKEAKVLAHEATELATGPQGSLQEGAKGSlqksfgflNEAKKLA 1989
Cdd:PRK03918 277 ELEEKVKELKELKEKA----EEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKE--------ERLEELK 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1990 NDVKENDEHLNGLTSRldnanVRNRDLLRALNDTLERLSA-----IPNDTAAKLQAVKDKARQANDTAKDVLAQIKDLHQ 2064
Cdd:PRK03918 345 KKLKELEKRLEELEER-----HELYEEAKAKKEELERLKKrltglTPEKLEKELEELEKAKEEIEEEISKITARIGELKK 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2065 NLDGLKKNYNQLADSVAK---TNAVVKDPSKNKIIADADATVKNLEQEADRLIDKLKPIKELEDNLKKNISEIKELINQa 2141
Cdd:PRK03918 420 EIKELKKAIEELKKAKGKcpvCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKL- 498
|
....*...
gi 1814459924 2142 RKQANSIK 2149
Cdd:PRK03918 499 KELAEQLK 506
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1685-2144 |
6.23e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 71.34 E-value: 6.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1685 FIKDLAQHAEAVSEKAVKLNETLGIQDKAFERNLQELQNEVDKMMTELRRKN-LDTQKEVAEDELVAAEALLKKVKKLfg 1763
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEeLEEELEELEAELEELREELEKLEKL-- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1764 ESRGKNEEMEKDLREKLADYKSKvhdaWDLLREATDKIKEA--NLLSAENQknmtaLEKKKEAIESGKRQT-EDTLKEGT 1840
Cdd:COG4717 125 LQLLPLYQELEALEAELAELPER----LEELEERLEELRELeeELEELEAE-----LAELQEELEELLEQLsLATEEELQ 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1841 DILDEANRLADEINSVIDYVEDIQTKLpplsEDLKGKIEDLSQEIKDRKLAEKVSQAESHAAQLNdSSAVLDRILDEAKN 1920
Cdd:COG4717 196 DLAEELEELQQRLAELEEELEEAQEEL----EELEEELEQLENELEAAALEERLKEARLLLLIAA-ALLALLGLGGSLLS 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1921 ISFNATAAFKAYSNIkdYIDKAEKIAKEAKVLAHEATELATGP-QGSLQEGAKGSLQKSFGFLNEAkklandvkeNDEHL 1999
Cdd:COG4717 271 LILTIAGVLFLVLGL--LALLFLLLAREKASLGKEAEELQALPaLEELEEEELEELLAALGLPPDL---------SPEEL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2000 NGLTSRLDNAnvrnRDLLRALNDTLERLsaipndtaaKLQAVKDKARQ----ANDTAKDVLAQIKDLHQNLDGLKKNYNQ 2075
Cdd:COG4717 340 LELLDRIEEL----QELLREAEELEEEL---------QLEELEQEIAAllaeAGVEDEEELRAALEQAEEYQELKEELEE 406
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1814459924 2076 LADSVAKTNAVVKDPSknkiiadADATVKNLEQEADRLIDKLKPIKELEDNLKKNISEIKELINQARKQ 2144
Cdd:COG4717 407 LEEQLEELLGELEELL-------EALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEED 468
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1718-1906 |
6.71e-12 |
|
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: 68.03 E-value: 6.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1718 LQELQNEVDKMMTELRR-----KNLDTQKEVAEDELVAAEALLKKVKKlfgeSRGKNEEMEKDLREKLADYKSKvhdawd 1792
Cdd:COG1579 12 LQELDSELDRLEHRLKElpaelAELEDELAALEARLEAAKTELEDLEK----EIKRLELEIEEVEARIKKYEEQ------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1793 llreatdkikeanLLSAENQKNMTALEKKKEAIESGKRQTEDTLKEgtdILDEANRLADEINSVIDYVEDIQTKLpplsE 1872
Cdd:COG1579 82 -------------LGNVRNNKEYEALQKEIESLKRRISDLEDEILE---LMERIEELEEELAELEAELAELEAEL----E 141
|
170 180 190
....*....|....*....|....*....|....
gi 1814459924 1873 DLKGKIEDLSQEIkDRKLAEKVSQAESHAAQLND 1906
Cdd:COG1579 142 EKKAELDEELAEL-EAELEELEAEREELAAKIPP 174
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
970-1016 |
7.70e-12 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 62.37 E-value: 7.70e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1814459924 970 PCNCNSFGSKSFDCE-ESGQCWCQPGVTGKKCDRCAHGYFNF--QEGGCT 1016
Cdd:cd00055 1 PCDCNGHGSLSGQCDpGTGQCECKPNTTGRRCDRCAPGYYGLpsQGGGCQ 50
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1689-2237 |
1.46e-11 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 70.70 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1689 LAQHAEAVSeKAVKLNeTLGIQDKAFERNLQELQNEVDKMM--TELRRKNLdtqkevaEDELVAAEALLKKVKKLfgesr 1766
Cdd:PRK01156 106 IAEGFDDTT-KYIEKN-ILGISKDVFLNSIFVGQGEMDSLIsgDPAQRKKI-------LDEILEINSLERNYDKL----- 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1767 gknEEMEKDLREKLADYkskvHDAWDLLREATDKIKEANLLSAENQKNMTALEKKKEAIESGKRQTEDTLKEGTDILDEA 1846
Cdd:PRK01156 172 ---KDVIDMLRAEISNI----DYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNEL 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1847 NRLADEINSvidYVEDIQTklpplSEDLKGKIEDLSQEIKDrkLAEKVSQAESHAAQLNdSSAVLDRILDEAKNISFNat 1926
Cdd:PRK01156 245 SSLEDMKNR---YESEIKT-----AESDLSMELEKNNYYKE--LEERHMKIINDPVYKN-RNYINDYFKYKNDIENKK-- 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1927 aafKAYSNIKDYIDKAEKIAKEAKVLAHEATELAtgpqgslqegakgSLQKSFgflNEAKKLANDVKENDEHLNGLTSRL 2006
Cdd:PRK01156 312 ---QILSNIDAEINKYHAIIKKLSVLQKDYNDYI-------------KKKSRY---DDLNNQILELEGYEMDYNSYLKSI 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2007 DNANVRNR-------DLLRALNDTLERLSAIPNDTAAKLQAVKDKARQANDTAKDVLAQIKDLHQNLDGLKKNYNQL-AD 2078
Cdd:PRK01156 373 ESLKKKIEeysknieRMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLnGQ 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2079 SVA----------KTNAVVKDPSKNKIIADADatVKNLEQEADRLIDKLKPIKELEDNLKKniSEIKELINQ------AR 2142
Cdd:PRK01156 453 SVCpvcgttlgeeKSNHIINHYNEKKSRLEEK--IREIEIEVKDIDEKIVDLKKRKEYLES--EEINKSINEynkiesAR 528
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2143 KQANSIKVSVSSGGDciRTYKPEIKKGSYNSIIVNVKTAVADNLLFYLGSAKFIDFLAIEMRKGKVSF-LWDVGSGVGRV 2221
Cdd:PRK01156 529 ADLEDIKIKINELKD--KHDKYEEIKNRYKSLKLEDLDSKRTSWLNALAVISLIDIETNRSRSNEIKKqLNDLESRLQEI 606
|
570
....*....|....*....
gi 1814459924 2222 E--YPDL-TIDDSYWYRIE 2237
Cdd:PRK01156 607 EigFPDDkSYIDKSIREIE 625
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1698-2116 |
3.64e-11 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 68.73 E-value: 3.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1698 EKAVKLNETLGIQDKaFERNLQELQNEVDKMMTELrrknldtqkevaEDELVAAEALLKKVKklFGESRGKNEEMEKDLR 1777
Cdd:pfam06160 32 SKVKKLNLTGETQEK-FEEWRKKWDDIVTKSLPDI------------EELLFEAEELNDKYR--FKKAKKALDEIEELLD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1778 EKLADYKsKVHDAWDLLREATDK----IKEANLLSAENQKNMTA-----------LEKKKEAIESgKRQTEDTLKEGTDI 1842
Cdd:pfam06160 97 DIEEDIK-QILEELDELLESEEKnreeVEELKDKYRELRKTLLAnrfsygpaideLEKQLAEIEE-EFSQFEELTESGDY 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1843 LdEANRLADEINSVIDYVEDIQTKLPPLSEDLKGKIEDLSQEIKD---------------------RKLAEKVSQAESHA 1901
Cdd:pfam06160 175 L-EAREVLEKLEEETDALEELMEDIPPLYEELKTELPDQLEELKEgyremeeegyalehlnvdkeiQQLEEQLEENLALL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1902 AQLN--DSSAVLDRILDEAKNI--SFNATAAFKAY-----SNIKDYIDKAEKIAKEAKvlaheaTELAtgpqgslqegak 1972
Cdd:pfam06160 254 ENLEldEAEEALEEIEERIDQLydLLEKEVDAKKYveknlPEIEDYLEHAEEQNKELK------EELE------------ 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1973 gSLQKSFGF----LNEAKKLANDVKENDEHLNGLTSRLDNANVRNRDLLRALNDTLERLSAIpNDTAAKLQAVKDKARQA 2048
Cdd:pfam06160 316 -RVQQSYTLneneLERVRGLEKQLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQLEEI-EEEQEEFKESLQSLRKD 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2049 NDTAKDVLAQIK-DLH--------QNLDGLKKNY-NQLADSVAKTNAVVKDPSK--------NKIIADADATVKNLEQEA 2110
Cdd:pfam06160 394 ELEAREKLDEFKlELReikrlvekSNLPGLPESYlDYFFDVSDEIEDLADELNEvplnmdevNRLLDEAQDDVDTLYEKT 473
|
....*.
gi 1814459924 2111 DRLIDK 2116
Cdd:pfam06160 474 EELIDN 479
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1616-1998 |
4.67e-11 |
|
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: 68.98 E-value: 4.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1616 LENMTQELKHLLSPQRAPERLIQLAEGNLNTLVTEMNELLTRATKVTADGEQTGQDAERTNTranSLGEFIKDLAQHAEA 1695
Cdd:pfam05483 298 LEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTC---SLEELLRTEQQRLEK 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1696 vSEKAVKLnETLGIQDKAFErnLQELQNEVDKMMTELRrknlDTQKEVAEDELVAAEAllKKVKKLFGESRGKNEEM--- 1772
Cdd:pfam05483 375 -NEDQLKI-ITMELQKKSSE--LEEMTKFKNNKEVELE----ELKKILAEDEKLLDEK--KQFEKIAEELKGKEQELifl 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1773 ----EK---DLREKLA-------DYKSKVHD-AWDLLREATDKIK---EANLLSAENQK------NMT-ALEKKKEAIES 1827
Cdd:pfam05483 445 lqarEKeihDLEIQLTaiktseeHYLKEVEDlKTELEKEKLKNIEltaHCDKLLLENKEltqeasDMTlELKKHQEDIIN 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1828 GKRQTEDTLKEGTDILDEANRLADEINSV----IDYVEDIQTKLPPLSEDLKGKIEDLSQEIKDRKLAEkvSQAESHAAQ 1903
Cdd:pfam05483 525 CKKQEERMLKQIENLEEKEMNLRDELESVreefIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILE--NKCNNLKKQ 602
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1904 LNDSSAVLDRILDEAKNISFNATAAFKaysNIKDYIDKAEKIAKEAKVLAHEATELATGPQGSL------QEGAKGSLQK 1977
Cdd:pfam05483 603 IENKNKNIEELHQENKALKKKGSAENK---QLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIedkkisEEKLLEEVEK 679
|
410 420
....*....|....*....|.
gi 1814459924 1978 SFGFLNEAKKLANDVKENDEH 1998
Cdd:pfam05483 680 AKAIADEAVKLQKEIDKRCQH 700
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
868-920 |
5.38e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 60.06 E-value: 5.38e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1814459924 868 PCQCNDNldFSIPGSCDSLSGSCLiCKPGTTGRYCELCADGYFGDAVDAKNCQ 920
Cdd:cd00055 1 PCDCNGH--GSLSGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1064-1112 |
6.39e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 59.67 E-value: 6.39e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1814459924 1064 CNCSSVGSLDFQCNLN*GQCNCRPKFSG*KCTECNRGHWSYPHCNPCDC 1112
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
971-1018 |
7.84e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 59.29 E-value: 7.84e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1814459924 971 CNCNSFGSKSFDCE-ESGQCWCQPGVTGKKCDRCAHGYFNFQEGGCTAC 1018
Cdd:pfam00053 1 CDCNPHGSLSDTCDpETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1701-2174 |
8.63e-11 |
|
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: 68.54 E-value: 8.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1701 VKLNETLGIQDKAferNLQELQNEVDK-------MMTELRRKNLdTQKEVAEDELVAAEALLKKvkKLFGE-SRGKNEEM 1772
Cdd:TIGR01612 684 VKENAIDNTEDKA---KLDDLKSKIDKeydkiqnMETATVELHL-SNIENKKNELLDIIVEIKK--HIHGEiNKDLNKIL 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1773 E------KDLREKLADYkSKVHDAWDLLREATDKIKEA--NLLSAENQKNMTA---LEKKKEAIESGKRQTEDTLKegtd 1841
Cdd:TIGR01612 758 EdfknkeKELSNKINDY-AKEKDELNKYKSKISEIKNHynDQINIDNIKDEDAkqnYDKSKEYIKTISIKEDEIFK---- 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1842 ILDEANRLADEINSVID-YV-------EDIQTKLPPLSEdLKGKIEDlsqEIKDRKLA---EKVSQAESHAAQLNDS--- 1907
Cdd:TIGR01612 833 IINEMKFMKDDFLNKVDkFInfennckEKIDSEHEQFAE-LTNKIKA---EISDDKLNdyeKKFNDSKSLINEINKSiee 908
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1908 -------------------------------SAVLDRILDEAKNISFNATAAFKAYSN-----IKDYIDKAEKIAKEAKV 1951
Cdd:TIGR01612 909 eyqnintlkkvdeyikicentkesiekfhnkQNILKEILNKNIDTIKESNLIEKSYKDkfdntLIDKINELDKAFKDASL 988
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1952 LAHEA--TELA---TGPQGSLQEGAKGSLQKSFgflNEAKKLANDVKENDEHLNGLTSRLD------------------- 2007
Cdd:TIGR01612 989 NDYEAknNELIkyfNDLKANLGKNKENMLYHQF---DEKEKATNDIEQKIEDANKNIPNIEiaihtsiyniideiekeig 1065
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2008 -NANVRNRDLLRALNDTLERLSAIPNDTaaKLQAVKDKARQANDTAKDVLAQIKDLHQNLD-GLKKNYNQLADSVAKTNA 2085
Cdd:TIGR01612 1066 kNIELLNKEILEEAEINITNFNEIKEKL--KHYNFDDFGKEENIKYADEINKIKDDIKNLDqKIDHHIKALEEIKKKSEN 1143
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2086 VVKDPSK--NKIIADADATVKN-----LEQEADRLIDKLKPIKELEDNLKKNISEIKElINQARKQANSIK-VSVSSGGD 2157
Cdd:TIGR01612 1144 YIDEIKAqiNDLEDVADKAISNddpeeIEKKIENIVTKIDKKKNIYDEIKKLLNEIAE-IEKDKTSLEEVKgINLSYGKN 1222
|
570 580
....*....|....*....|
gi 1814459924 2158 CIRTYKPEI---KKGSYNSI 2174
Cdd:TIGR01612 1223 LGKLFLEKIdeeKKKSEHMI 1242
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1531-1568 |
9.49e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 59.29 E-value: 9.49e-11
10 20 30
....*....|....*....|....*....|....*...
gi 1814459924 1531 CECDPHGSLPVPCDPVTGICTCRPGATGQKCDGCKHWH 1568
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGY 39
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1616-2139 |
1.49e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.39 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1616 LENMTQELKHLLSPQRAPERLIQLAEGNLNTLVTEMNEL-----LTRATKVTADGEQTGQDAERTNTRANSLGEFIKDLA 1690
Cdd:TIGR02168 353 LESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLelqiaSLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1691 QHAEAVSEKAVKLNETLGIQDKAFER---NLQELQNEVDKMMTELRRknldtqkevAEDELVAAEALLKKVKKLF----G 1763
Cdd:TIGR02168 433 AELKELQAELEELEEELEELQEELERleeALEELREELEEAEQALDA---------AERELAQLQARLDSLERLQenleG 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1764 ESRGKNEEMEKdlREKLADYKSKVhdaWDLL--REATDKIKEANLLSAENQKNMTALEKKKEAIES------GKR----- 1830
Cdd:TIGR02168 504 FSEGVKALLKN--QSGLSGILGVL---SELIsvDEGYEAAIEAALGGRLQAVVVENLNAAKKAIAFlkqnelGRVtflpl 578
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1831 ----------QTEDTLKEGTDILDEANRL---ADEINSVIDY-------VEDIQT------KLPP------LSEDL---- 1874
Cdd:TIGR02168 579 dsikgteiqgNDREILKNIEGFLGVAKDLvkfDPKLRKALSYllggvlvVDDLDNalelakKLRPgyrivtLDGDLvrpg 658
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1875 -----------------KGKIEDLSQEIKD-----RKLAEKVSQAESHAAQLNDSSAVLDRILDEaKNISFNAtaafkAY 1932
Cdd:TIGR02168 659 gvitggsaktnssilerRREIEELEEKIEEleekiAELEKALAELRKELEELEEELEQLRKELEE-LSRQISA-----LR 732
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1933 SNIKDYIDKAEKIAKEAKVLAHEATELATGPQGSLQEgakgsLQKSFGFLNEAK----KLANDVKENDEHLNGLTSRLDN 2008
Cdd:TIGR02168 733 KDLARLEAEVEQLEERIAQLSKELTELEAEIEELEER-----LEEAEEELAEAEaeieELEAQIEQLKEELKALREALDE 807
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2009 ANVRNRDLLRALNDTLERLSAIPNDTAAKLQAVKDKARQANDTAKDVL---AQIKDLHQNLDGLKKNYNQLADSVAKTNA 2085
Cdd:TIGR02168 808 LRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIEslaAEIEELEELIEELESELEALLNERASLEE 887
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 1814459924 2086 VVKDPSKNKI-----IADADATVKNLEQEADRLIDKLKPIKELEDNLKKNISEIKELIN 2139
Cdd:TIGR02168 888 ALALLRSELEelseeLRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLS 946
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1616-1956 |
2.02e-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: 2.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1616 LENMTQELKHLLSPQRAPERLiqlaegnLNTLVTEMNELLTRATKVTADGEQTGQDAERTNTRANSLGEFIKDLAQHAEA 1695
Cdd:TIGR02169 683 LEGLKRELSSLQSELRRIENR-------LDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIEN 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1696 V--------------SEKAVKLNETLG-IQDKAFERNLQELQNEVDKMMTELRR------------KNLDTQKEVAEDE- 1747
Cdd:TIGR02169 756 VkselkelearieelEEDLHKLEEALNdLEARLSHSRIPEIQAELSKLEEEVSRiearlreieqklNRLTLEKEYLEKEi 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1748 --LVAAEALLKKVKKLFG----ESRGKNEEME----------KDLREKLADYKSKVHDAWDLLREATDKIKEANLLSAEN 1811
Cdd:TIGR02169 836 qeLQEQRIDLKEQIKSIEkeieNLNGKKEELEeeleeleaalRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKK 915
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1812 QKNMTALEKKKEAIESGKRQTEDTLKEGtdildeanrladeinsvidyvEDIQTKLPPLsEDLKGKIEDLSQEIkdRKLA 1891
Cdd:TIGR02169 916 RKRLSELKAKLEALEEELSEIEDPKGED---------------------EEIPEEELSL-EDVQAELQRVEEEI--RALE 971
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1814459924 1892 E----KVSQAESHAAQLNDSSAVLDRILDEAKnisfnataafkaysNIKDYIDKAEKIAKEAKVLAHEA 1956
Cdd:TIGR02169 972 PvnmlAIQEYEEVLKRLDELKEKRAKLEEERK--------------AILERIEEYEKKKREVFMEAFEA 1026
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1663-2116 |
2.84e-10 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 66.01 E-value: 2.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1663 ADGEQTGQDAERTNTRANslgeFIKdlAQHAEAVSEKavKLNETlgiqdkafERNLQELQNEVDkmmtELRRKNLDTQKE 1742
Cdd:PRK04778 82 PDIEEQLFEAEELNDKFR----FRK--AKHEINEIES--LLDLI--------EEDIEQILEELQ----ELLESEEKNREE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1743 VAEdelvaAEALLKKVKK-------LFGESrgkNEEMEKDLREKLADYKSkvhdaWDLLREATDKIKEAN-LLSAENQkn 1814
Cdd:PRK04778 142 VEQ-----LKDLYRELRKsllanrfSFGPA---LDELEKQLENLEEEFSQ-----FVELTESGDYVEAREiLDQLEEE-- 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1815 MTALEKKKEAIESGKRQTEDTLKEG-TDILDEANRLADEiNSVIDYVeDIQTKLpplsEDLKGKIEDLSQEIKDRKLAEk 1893
Cdd:PRK04778 207 LAALEQIMEEIPELLKELQTELPDQlQELKAGYRELVEE-GYHLDHL-DIEKEI----QDLKEQIDENLALLEELDLDE- 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1894 vsqAESHAAQLNDSsavLDRILD------EAKNisfnatAAFKAYSNIKDYIDKAEKIAKEakvLAHEATELatgpqgsl 1967
Cdd:PRK04778 280 ---AEEKNEEIQER---IDQLYDilerevKARK------YVEKNSDTLPDFLEHAKEQNKE---LKEEIDRV-------- 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1968 qegakgslQKSFgFLNE-----AKKLANDVKENDEHLNGLTSRLDNANVRNRDLLRALNDTLERLSAIPN---DTAAKLQ 2039
Cdd:PRK04778 337 --------KQSY-TLNEselesVRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKeqeKLSEMLQ 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2040 AVKDKARQANDTAKDVLAQIKDLH-----QNLDGLKKNY-NQLADSVAKTNAVVKDPSKNKI--------IADADATVKN 2105
Cdd:PRK04778 408 GLRKDELEAREKLERYRNKLHEIKrylekSNLPGLPEDYlEMFFEVSDEIEALAEELEEKPInmeavnrlLEEATEDVET 487
|
490
....*....|.
gi 1814459924 2106 LEQEADRLIDK 2116
Cdd:PRK04778 488 LEEETEELVEN 498
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
760-809 |
3.59e-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: 3.59e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1814459924 760 PCQCFGHA---ESCDDITGECLnCKDHTGGLYCNKCLPGFYGDPTKGtsDDCQ 809
Cdd:cd00055 1 PCDCNGHGslsGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQG--GGCQ 50
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1660-2188 |
5.79e-10 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 65.62 E-value: 5.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1660 KVTADGEQTGQdAERTNTRANSLG---EFIKDLAQHAEAVSEKAVKLNETLGIQDKaFERNL-----QELQNEVDKMMT- 1730
Cdd:PTZ00440 1111 VVNADKEKNKQ-TEHYNKKKKSLEkiyKQMEKTLKELENMNLEDITLNEVNEIEIE-YERILidhivEQINNEAKKSKTi 1188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1731 ----ELRRKNLDTQKEVAEDELVA-------------AEALLKKVKKLFGESRGKNEEMEKDLR-EKLADYKSKVHDAWD 1792
Cdd:PTZ00440 1189 meeiESYKKDIDQVKKNMSKERNDhlttfeynayydkATASYENIEELTTEAKGLKGEANRSTNvDELKEIKLQVFSYLQ 1268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1793 LLREATDKIKEAnLLSAENQKNM---TALEKKKEAIESGKRQTEDTLKEGTDILDEANRLadeINSVIDYVEDIQTKLPP 1869
Cdd:PTZ00440 1269 QVIKENNKMENA-LHEIKNMYEFlisIDSEKILKEILNSTKKAEEFSNDAKKELEKTDNL---IKQVEAKIEQAKEHKNK 1344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1870 LSEDLK--------GKIEDLSQEIKDRKLA---------EKVSQAESHAAQLNDSSAVLDrILDEAKNISFNATAAFKAy 1932
Cdd:PTZ00440 1345 IYGSLEdkqiddeiKKIEQIKEEISNKRKEinkylsnikSNKEKCDLHVRNASRGKDKID-FLNKHEAIEPSNSKEVNI- 1422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1933 SNIKDYIDKAEKIAKEAKVLAHEATElatgPQGSLQEGAKG--SLQKSFGFLNEAKKLANDVKENDEHLNGLtsRLDNAN 2010
Cdd:PTZ00440 1423 IKITDNINKCKQYSNEAMETENKADE----NNDSIIKYEKEitNILNNSSILGKKTKLEKKKKEATNIMDDI--NGEHSI 1496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2011 VRNRdlLRALNDTLERLSAIPNDTAAKLQAVKDKARQANDT-------AKDVLAQIKDLHQNLDGLKKNYNQLADSVAKT 2083
Cdd:PTZ00440 1497 IKTK--LTKSSEKLNQLNEQPNIKREGDVLNNDKSTIAYETiqynlgrVKHNLLNILNIKDEIETILNKAQDLMRDISKI 1574
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2084 NAVVKDPSKNKIIADADATVKNLEQ----------EADRLIDKLKPIKELEDNLKK--------NISEIKELINQARKQA 2145
Cdd:PTZ00440 1575 SKIVENKNLENLNDKEADYVKYLDNilkekqlmeaEYKKLNEIYSDVDNIEKELKKhkknyeigLLEKVIEINKNIKLYM 1654
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1814459924 2146 NSIKVSVSSGGDCIRT---------YKPE------IKK---------GSYNSIIVNVKTAVADNLLF 2188
Cdd:PTZ00440 1655 DSTKESLNSLVNNFSSlfnnfylnkYNINenlekyKKKlneiynefmESYNIIQEKMKEVSNDDVDY 1721
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1531-1571 |
6.51e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.55 E-value: 6.51e-10
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1814459924 1531 CECDPHGSLPVPCDPVTGICTCRPGATGQKCDGCKHWHVRE 1571
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGD 41
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1865-2149 |
7.71e-10 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 63.01 E-value: 7.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1865 TKLPPLSEDLKGKIEDLSQEIKD--RKLAEKVSQAESHAAQLNDSSAVLDRILDEAKNI-----SFNAtaafkaysNIKD 1937
Cdd:COG1340 4 DELSSSLEELEEKIEELREEIEElkEKRDELNEELKELAEKRDELNAQVKELREEAQELrekrdELNE--------KVKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1938 YIDKAEKIAKEAKVLAHEATElatgpqgslqegakgsLQKSFGFLNEAKKlanDVKENDEHLNGLTSRLDNANVrNRDLL 2017
Cdd:COG1340 76 LKEERDELNEKLNELREELDE----------------LRKELAELNKAGG---SIDKLRKEIERLEWRQQTEVL-SPEEE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2018 RALNDTLERLsaipndtAAKLQAVKdKARQANDTAKDVLAQIKDLHQNLDGLKKNYNQLADSVAKTnavvkdpsKNKIIA 2097
Cdd:COG1340 136 KELVEKIKEL-------EKELEKAK-KALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQEL--------HEEMIE 199
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1814459924 2098 ---DADATVKNLE---QEADRLIDKLKPIKELEDNLKKNISEIKELINQARKQANSIK 2149
Cdd:COG1340 200 lykEADELRKEADelhKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALK 257
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1643-2166 |
9.19e-10 |
|
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: 65.07 E-value: 9.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1643 NLNTLvTEMNELLtratKVTadgEQTGQDAERTNTRANSLGEFIK---DLAQHAEAVsEKAVKlnetlgiqDKaFERNLQ 1719
Cdd:TIGR01612 912 NINTL-KKVDEYI----KIC---ENTKESIEKFHNKQNILKEILNkniDTIKESNLI-EKSYK--------DK-FDNTLI 973
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1720 ELQNEVDKMMTELRRKNLdtqkEVAEDELVAaeaLLKKVKKLFGESRG--------KNEEMEKDLREKLADYKSKVHDA- 1790
Cdd:TIGR01612 974 DKINELDKAFKDASLNDY----EAKNNELIK---YFNDLKANLGKNKEnmlyhqfdEKEKATNDIEQKIEDANKNIPNIe 1046
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1791 -------WDLLREATDKI-KEANLLSAENQK----NMTALEKKKEAIEsgKRQTEDTLKEGT-DILDEANRLADEINSVI 1857
Cdd:TIGR01612 1047 iaihtsiYNIIDEIEKEIgKNIELLNKEILEeaeiNITNFNEIKEKLK--HYNFDDFGKEENiKYADEINKIKDDIKNLD 1124
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1858 DYVEDIQTKLpplsEDLKGKIEDLSQEIKdrklaekvsqaeshaAQLNDSSAVLDRIL--DEAKNISfnataafKAYSNI 1935
Cdd:TIGR01612 1125 QKIDHHIKAL----EEIKKKSENYIDEIK---------------AQINDLEDVADKAIsnDDPEEIE-------KKIENI 1178
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1936 KDYIDKAEKIAKEAKVLAHEATELATGpQGSLQE--GAKGSLQKSFGFL------NEAKKLANDVKENDEHLNGLtsrld 2007
Cdd:TIGR01612 1179 VTKIDKKKNIYDEIKKLLNEIAEIEKD-KTSLEEvkGINLSYGKNLGKLflekidEEKKKSEHMIKAMEAYIEDL----- 1252
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2008 nanvrnrDLLRALNDTLERLSAIPNDTAAKLQAVK---DKARQANDTAKDVLAQIKDL-HQNLDGLKKNYNQladsvAKT 2083
Cdd:TIGR01612 1253 -------DEIKEKSPEIENEMGIEMDIKAEMETFNishDDDKDHHIISKKHDENISDIrEKSLKIIEDFSEE-----SDI 1320
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2084 NAVVKDPSKNkiIADADATVKNLEQEADRlIDKLKPIKELeDNLKKNISEIKELINQARKQANSIKVSVSSGGDCIRTYK 2163
Cdd:TIGR01612 1321 NDIKKELQKN--LLDAQKHNSDINLYLNE-IANIYNILKL-NKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIK 1396
|
...
gi 1814459924 2164 PEI 2166
Cdd:TIGR01612 1397 DDI 1399
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
418-475 |
9.50e-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: 56.21 E-value: 9.50e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1814459924 418 CHCDPIGSLSEVCVkdekraqrgLAPGSCHCKPGFRGVSCDRCARGYTGYPDCKPCNC 475
Cdd:pfam00053 1 CDCNPHGSLSDTCD---------PETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1729-2122 |
9.69e-10 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 64.21 E-value: 9.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1729 MTELRRKNLDTQKEVAEDELVAA--EALLKKVKKLFGESRGKNEEMEKDLREKLADYKSKVHDAWDLLREATDKIK-EAN 1805
Cdd:COG5185 231 IEEALKGFQDPESELEDLAQTSDklEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDiKKA 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1806 LLSAENQKNMTA----LEKKKEAIESG-KRQTEDTLKEGTDILDEANRLADEINSVIDYVEdiqtklpplSEDLKGKIED 1880
Cdd:COG5185 311 TESLEEQLAAAEaeqeLEESKRETETGiQNLTAEIEQGQESLTENLEAIKEEIENIVGEVE---------LSKSSEELDS 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1881 LSQEI--KDRKLAEKVSQAESH----AAQLNDSSAVLDRildEAKNISFNataafkaysnikdyIDKAEKIAKEAKVLAH 1954
Cdd:COG5185 382 FKDTIesTKESLDEIPQNQRGYaqeiLATLEDTLKAADR---QIEELQRQ--------------IEQATSSNEEVSKLLN 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1955 EATELATGPQGSLQEGAKGSLQksfgflNEAKKLANDVKENDEHLNGLTSRLDNAnvrnrdlLRALNDTLERLSAipnDT 2034
Cdd:COG5185 445 ELISELNKVMREADEESQSRLE------EAYDEINRSVRSKKEDLNEELTQIESR-------VSTLKATLEKLRA---KL 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2035 AAKLQAVKDKARQANDTAKDVLAQIKDLHqnldgLKKNYNQLADSVAKTNavvkDPSKNKIIADADATVKNLEQEADRLI 2114
Cdd:COG5185 509 ERQLEGVRSKLDQVAESLKDFMRARGYAH-----ILALENLIPASELIQA----SNAKTDGQAANLRTAVIDELTQYLST 579
|
....*...
gi 1814459924 2115 DKLKPIKE 2122
Cdd:COG5185 580 IESQQARE 587
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1531-1566 |
1.03e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 56.21 E-value: 1.03e-09
10 20 30
....*....|....*....|....*....|....*.
gi 1814459924 1531 CECDPHGSLPVPCDPVTGICTCRPGATGQKCDGCKH 1566
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKP 36
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1647-2186 |
1.43e-09 |
|
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: 64.30 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1647 LVTEMNELLTRATKVtaDGEQTgqdaeRTNTRANSLGEFIKDLAQHAEAVsEKAVKLNetlgiqdKAFERN---LQELQN 1723
Cdd:TIGR01612 577 LEKEIKDLFDKYLEI--DDEII-----YINKLKLELKEKIKNISDKNEYI-KKAIDLK-------KIIENNnayIDELAK 641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1724 EVDKMMTElRRKNLDTQKEVAEDELvaAEALLKKVKKLFGESRGKNEEMEKDLRE---KLADYKSKVHDAWDLLREATDK 1800
Cdd:TIGR01612 642 ISPYQVPE-HLKNKDKIYSTIKSEL--SKIYEDDIDALYNELSSIVKENAIDNTEdkaKLDDLKSKIDKEYDKIQNMETA 718
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1801 IKEANLLSAENQKNM---TALEKKKEaiesgkrqtedtlkegtdILDEANRladEINSVidyVEDIQTKlpplSEDLKGK 1877
Cdd:TIGR01612 719 TVELHLSNIENKKNElldIIVEIKKH------------------IHGEINK---DLNKI---LEDFKNK----EKELSNK 770
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1878 IEDLSQEiKDR--KLAEKVSQAESHaaqLNDSSAVlDRILDEAKNISFNATAAFKAYSNIKDyiDKAEKIAKEAKVLAHE 1955
Cdd:TIGR01612 771 INDYAKE-KDElnKYKSKISEIKNH---YNDQINI-DNIKDEDAKQNYDKSKEYIKTISIKE--DEIFKIINEMKFMKDD 843
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1956 AtelatgpqgslqegakgsLQKSFGFLNeakkLANDVKEN----DEHLNGLTSRLDN--ANVRNRDLLRALNDTLERLSA 2029
Cdd:TIGR01612 844 F------------------LNKVDKFIN----FENNCKEKidseHEQFAELTNKIKAeiSDDKLNDYEKKFNDSKSLINE 901
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2030 IPNDTAAKLQAVK--DKARQANDTAKDVLAQIKDLHQNLDGLKKNYNQLADSVAKTNAVVK---DPSKNKII-------- 2096
Cdd:TIGR01612 902 INKSIEEEYQNINtlKKVDEYIKICENTKESIEKFHNKQNILKEILNKNIDTIKESNLIEKsykDKFDNTLIdkineldk 981
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2097 ADADATVKNLEQEADRLIdklKPIKELEDNLKKNISE-IKELINQARKQANSIKVSVSSGGDCIRTYKPEIKKGSYNsII 2175
Cdd:TIGR01612 982 AFKDASLNDYEAKNNELI---KYFNDLKANLGKNKENmLYHQFDEKEKATNDIEQKIEDANKNIPNIEIAIHTSIYN-II 1057
|
570
....*....|.
gi 1814459924 2176 VNVKTAVADNL 2186
Cdd:TIGR01612 1058 DEIEKEIGKNI 1068
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1665-2028 |
1.44e-09 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 63.00 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1665 GEQTGQDAERTNTRANSLGEFIKDLAQHAEAVSEKAVKLNETLgiqdKAFERNLQELQNEVDKMMTELRRKN-----LDT 1739
Cdd:COG4372 5 GEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEEL----EQLREELEQAREELEQLEEELEQARseleqLEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1740 QKEVAEDELVAAEALLKKVKKLFGESRGKNEEMEKDL------REKLADYKSKVHDAWDLLrEATDKIKEANLLSAENQk 1813
Cdd:COG4372 81 ELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELeelqkeRQDLEQQRKQLEAQIAEL-QSEIAEREEELKELEEQ- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1814 nMTALEKKKEAIESGKRQ--TEDTLKEGTDILDEANRLAdeinsvidYVEDIQTKLPPLSEDLKGKIEDLSQEIKDRKLA 1891
Cdd:COG4372 159 -LESLQEELAALEQELQAlsEAEAEQALDELLKEANRNA--------EKEEELAEAEKLIESLPRELAEELLEAKDSLEA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1892 EKVSQAESHAAQLNDSSAVLDRILDEAKNISFNATAAFKAYSNIKDYIDKAEKIAKEAKVLAHEATELATGPQGSLQEGA 1971
Cdd:COG4372 230 KLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSL 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1814459924 1972 KGSLQksfgflNEAKKLANDVKENDEHLNGLTSRLDNANVRNRDLLRALNDTLERLS 2028
Cdd:COG4372 310 IGALE------DALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLS 360
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1690-2144 |
1.80e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 64.01 E-value: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1690 AQHAEAV--SEKAVKLNETLGIQDKafERNLQELQNEVDKMMTELRRKNLDTQKEVAE--DELVAAEAL-----LKKV-- 1758
Cdd:PTZ00121 1223 AKKAEAVkkAEEAKKDAEEAKKAEE--ERNNEEIRKFEEARMAHFARRQAAIKAEEARkaDELKKAEEKkkadeAKKAee 1300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1759 KKLFGESRGKNEEMEK--DLREKLADYKSKvhdAWDLLREATDKIKEANLLSAENQKNMTALEKKKEAIESGKRQTEdtl 1836
Cdd:PTZ00121 1301 KKKADEAKKKAEEAKKadEAKKKAEEAKKK---ADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKE--- 1374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1837 kegtdildEANRLADEINSVIDYVEDiqtklpplSEDLKGKIEDlsqeikDRKLAEKVSQAESHAAQLNDS--SAVLDRI 1914
Cdd:PTZ00121 1375 --------EAKKKADAAKKKAEEKKK--------ADEAKKKAEE------DKKKADELKKAAAAKKKADEAkkKAEEKKK 1432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1915 LDEAKNisfNATAAFKAysnikdyiDKAEKIAKEAKVlAHEATELAtgpqgslQEGAKGslqksfgflNEAKKLANDVKE 1994
Cdd:PTZ00121 1433 ADEAKK---KAEEAKKA--------DEAKKKAEEAKK-AEEAKKKA-------EEAKKA---------DEAKKKAEEAKK 1484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1995 NDEhlngLTSRLDNANVRNRDLLRALNdtlERLSAipnDTAAKLQAVK--DKARQANDTAKDVLAQIKDLHQNLDGLKKn 2072
Cdd:PTZ00121 1485 ADE----AKKKAEEAKKKADEAKKAAE---AKKKA---DEAKKAEEAKkaDEAKKAEEAKKADEAKKAEEKKKADELKK- 1553
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1814459924 2073 ynqlADSVAKTNAVVKDPSKNKiiADADATVKNLEQEADRLIDKlkpiKELEDNLKKNISEIKELINQARKQ 2144
Cdd:PTZ00121 1554 ----AEELKKAEEKKKAEEAKK--AEEDKNMALRKAEEAKKAEE----ARIEEVMKLYEEEKKMKAEEAKKA 1615
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1424-1470 |
2.27e-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: 2.27e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1424 CQCHGHSSL---CDPETSICQnCQHHTAGDFCERCVLGYYGIVKGLPDDC 1470
Cdd:pfam00053 1 CDCNPHGSLsdtCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1652-2146 |
2.42e-09 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 63.69 E-value: 2.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1652 NELLTRATKVTADGEQTGQ----DAER--TNTRAnslgEFIKDLAQ-HAEAvSEKAVKLNETLGIQDKAFERNLQELQNE 1724
Cdd:NF041483 538 AEAEEQAEEVRAAAERAARelreETERaiAARQA----EAAEELTRlHTEA-EERLTAAEEALADARAEAERIRREAAEE 612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1725 VDKMMTEL--RRKNLDTQKEVAEDEL---VAAEAllkkvkklfGESRGKNEEMEKDLREKLAD----YKSKVHDAWDLLR 1795
Cdd:NF041483 613 TERLRTEAaeRIRTLQAQAEQEAERLrteAAADA---------SAARAEGENVAVRLRSEAAAeaerLKSEAQESADRVR 683
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1796 -EATdkiKEANLLSAENQKnmtALEKKKEAIESGKRQTEDTLKEGTDILDEANRLADE-----INSVIDYVEDIQTKLPP 1869
Cdd:NF041483 684 aEAA---AAAERVGTEAAE---ALAAAQEEAARRRREAEETLGSARAEADQERERAREqseelLASARKRVEEAQAEAQR 757
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1870 LSEDlkgkiedlsqeiKDRKLAEKVSQAESHAAQLNDSSAVLDrilDEAKN-ISFNATAAFKAYSNIK-DYIDKAEKIAK 1947
Cdd:NF041483 758 LVEE------------ADRRATELVSAAEQTAQQVRDSVAGLQ---EQAEEeIAGLRSAAEHAAERTRtEAQEEADRVRS 822
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1948 EAKVLAHEATELATGPQGSLQE---GAKGSLQKSFG-FLNEAKKLANDVKENDEHLNglTSRLDNANVRNRDLLRALNDT 2023
Cdd:NF041483 823 DAYAERERASEDANRLRREAQEeteAAKALAERTVSeAIAEAERLRSDASEYAQRVR--TEASDTLASAEQDAARTRADA 900
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2024 LERLSAIPNDTAAklQAVKDKARQANDTAKDVLAQIKDLHQNLDGLKKNYNQL-ADSVAKTNAVVKDPSKN--KIIADAD 2100
Cdd:NF041483 901 REDANRIRSDAAA--QADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVrADAAAQAEQLIAEATGEaeRLRAEAA 978
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1814459924 2101 ATVKNLEQEADRLIDKLKPIK-----ELEDNLKKNISEIKELINQARKQAN 2146
Cdd:NF041483 979 ETVGSAQQHAERIRTEAERVKaeaaaEAERLRTEAREEADRTLDEARKDAN 1029
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1616-2144 |
3.04e-09 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 63.14 E-value: 3.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1616 LENMTQElKHLLSpQRAPERLIQLAEGNLNTLVTEMN------ELLTRATKVTADGEQTGQDAER--------------- 1674
Cdd:TIGR00606 328 LEKLNKE-RRLLN-QEKTELLVEQGRLQLQADRHQEHirardsLIQSLATRLELDGFERGPFSERqiknfhtlvierqed 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1675 -TNTRANSLGEFIKDLAQHAEAVSEKAVK---LNETLGIQDKAFERNLQELQNEVDKM------MTELRRKNLDTQKEVA 1744
Cdd:TIGR00606 406 eAKTAAQLCADLQSKERLKQEQADEIRDEkkgLGRTIELKKEILEKKQEELKFVIKELqqlegsSDRILELDQELRKAER 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1745 E----DELVAAEALLKKVKKLFGES-------RGKNEEMEKDLREKLADYKSKVhdawdLLREATDKIKEANLLSAENQK 1813
Cdd:TIGR00606 486 ElskaEKNSLTETLKKEVKSLQNEKadldrklRKLDQEMEQLNHHTTTRTQMEM-----LTKDKMDKDEQIRKIKSRHSD 560
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1814 NMTA----------LEKKKEAIESGKRQTEDTLKEGTDILDEANRLADEINSVIDYVEDIQTKLPPL------SEDLKGK 1877
Cdd:TIGR00606 561 ELTSllgyfpnkkqLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKlfdvcgSQDEESD 640
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1878 IEDLSQEI-KDRK----LAEKVSQAESHAAQLNDSSA----VLDRILDEAKNISfnaTAAFKAYSNIKDYIDKAEKIAKE 1948
Cdd:TIGR00606 641 LERLKEEIeKSSKqramLAGATAVYSQFITQLTDENQsccpVCQRVFQTEAELQ---EFISDLQSKLRLAPDKLKSTESE 717
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1949 AKVLAHEATE---LATGPQGSLQEGAK--GSLQKSFGFLN-EAKKLANDVKENDEHLNGLTSRLDNANVRNRD--LLRAL 2020
Cdd:TIGR00606 718 LKKKEKRRDEmlgLAPGRQSIIDLKEKeiPELRNKLQKVNrDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDvtIMERF 797
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2021 NDTLERLSAIPNDTAAKLQAVkdkarqandtakDVLAQIKDLHQNLDGLKKNYNQLADSVAKTNAVVKDpsKNKIIADAD 2100
Cdd:TIGR00606 798 QMELKDVERKIAQQAAKLQGS------------DLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQD--QQEQIQHLK 863
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 1814459924 2101 ATVKNLEQEADRLIDKLKPIKELEDNLKKNISEIKEL---INQARKQ 2144
Cdd:TIGR00606 864 SKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLireIKDAKEQ 910
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1770-2152 |
3.05e-09 |
|
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: 63.16 E-value: 3.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1770 EEMEKD---LREKLADYKSKVHDAWDLLREATDKI----KEANLLSAENQKNMTALEKKKEAIESgkrqtedtlkegtdi 1842
Cdd:TIGR02169 684 EGLKRElssLQSELRRIENRLDELSQELSDASRKIgeieKEIEQLEQEEEKLKERLEELEEDLSS--------------- 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1843 ldeanrLADEINSVIDYVEDIQTKLPPLSEDLkGKIEDLSQEIKDRKLAEKVSQAESHAAQLNDSSAVLDRILDEAKnis 1922
Cdd:TIGR02169 749 ------LEQEIENVKSELKELEARIEELEEDL-HKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIE--- 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1923 fnatAAFKAYSNIKDYIDKaEKIAKEAKVLAHEATELATGPQGSLQEGAKGSLQKsfgflnEAKKLANDVKENDEHLNGL 2002
Cdd:TIGR02169 819 ----QKLNRLTLEKEYLEK-EIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEE------ELEELEAALRDLESRLGDL 887
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2003 TSRLDNAnvrnRDLLRALNDTLERLSAipndtaaklqavkdKARQANDTAKDVLAQIKDLHQNLDGLKKNYNQLadsvak 2082
Cdd:TIGR02169 888 KKERDEL----EAQLRELERKIEELEA--------------QIEKKRKRLSELKAKLEALEEELSEIEDPKGED------ 943
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2083 tnavVKDPSKNKIIADADATVKNLE--------------QEADRLIDKLKPIKELEDNLKKNISEIKELINQARKQANSI 2148
Cdd:TIGR02169 944 ----EEIPEEELSLEDVQAELQRVEeeiralepvnmlaiQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREV 1019
|
....
gi 1814459924 2149 KVSV 2152
Cdd:TIGR02169 1020 FMEA 1023
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1680-2153 |
3.10e-09 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 63.00 E-value: 3.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1680 NSLGEFIKDLAQHAEAVSEKAVKLNETLGiQDKAFERNLQELQNEVDKMMTELRRKN--LDTQKEVaEDELVAAEALLKK 1757
Cdd:PRK01156 190 EKLKSSNLELENIKKQIADDEKSHSITLK-EIERLSIEYNNAMDDYNNLKSALNELSslEDMKNRY-ESEIKTAESDLSM 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1758 VKKLFGESRGKNEEMEKDLREKLADYKSKVHDAWDLLREATDKIKEANLLSAENQKnMTALEKKKEAIESGKRQTEDTLK 1837
Cdd:PRK01156 268 ELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINK-YHAIIKKLSVLQKDYNDYIKKKS 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1838 EGTDI---LDEANRLADEINSVIDYVEDIQTKLpplsEDLKGKIEDLSQEIKdRKLAEKVSQAESHAAQLNDSSAVLDRI 1914
Cdd:PRK01156 347 RYDDLnnqILELEGYEMDYNSYLKSIESLKKKI----EEYSKNIERMSAFIS-EILKIQEIDPDAIKKELNEINVKLQDI 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1915 ldEAKNISFNATaafkaysnIKDYIDKAEKIAKEAKVLAHEA------TELATGPQGSLQEGAKgslQKSFGFLNEAKKL 1988
Cdd:PRK01156 422 --SSKVSSLNQR--------IRALRENLDELSRNMEMLNGQSvcpvcgTTLGEEKSNHIINHYN---EKKSRLEEKIREI 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1989 ANDVKENDEHLNGLTSRLDNANVRNRDLLRALNDTLERLSAIPNDTAAKLQAVKDKarqaNDTAKDVLAQIKDLH-QNLD 2067
Cdd:PRK01156 489 EIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDK----HDKYEEIKNRYKSLKlEDLD 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2068 GLKKNYNQLA---DSVAKTNAVVKDPSKNKIIADA------------------DATVKNLEQEADRLIDKLKPIKELE-- 2124
Cdd:PRK01156 565 SKRTSWLNALaviSLIDIETNRSRSNEIKKQLNDLesrlqeieigfpddksyiDKSIREIENEANNLNNKYNEIQENKil 644
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1814459924 2125 --------DNLKKNISEIKELI-----------------NQARKQANSIKVSVS 2153
Cdd:PRK01156 645 ieklrgkiDNYKKQIAEIDSIIpdlkeitsrindiednlKKSRKALDDAKANRA 698
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1818-2149 |
4.05e-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: 62.35 E-value: 4.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1818 LEKKKEAIESGKRQTEDTLKegtDILDEANRLADEINSvidyvediqtklpplsedLKGKIEDLSQEIKDRKLAEKVSQa 1897
Cdd:TIGR04523 38 LEKKLKTIKNELKNKEKELK---NLDKNLNKDEEKINN------------------SNNKIKILEQQIKDLNDKLKKNK- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1898 eshaAQLNDSSAVLDRILDEAKNisfnataafkaysnikdyiDKAEKIAKEakvlaheaTELAtgpqgSLQEGAKGSLQK 1977
Cdd:TIGR04523 96 ----DKINKLNSDLSKINSEIKN-------------------DKEQKNKLE--------VELN-----KLEKQKKENKKN 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1978 SFGFLNEAKKLANDVKEndehlngLTSRLDNANVRNRDLLRALNDTLERLSAIPND-TAAKLQAVKDKARQANDTAKDvl 2056
Cdd:TIGR04523 140 IDKFLTEIKKKEKELEK-------LNNKYNDLKKQKEELENELNLLEKEKLNIQKNiDKIKNKLLKLELLLSNLKKKI-- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2057 AQIKDLHQNLDGLKKNYNQLADSVAKTNAVVKDpsKNKIIADADATVKNLEQEADRLIDKL-----------KPIKELED 2125
Cdd:TIGR04523 211 QKNKSLESQISELKKQNNQLKDNIEKKQQEINE--KTTEISNTQTQLNQLKDEQNKIKKQLsekqkeleqnnKKIKELEK 288
|
330 340
....*....|....*....|....
gi 1814459924 2126 NLKKNISEIKELINQarKQANSIK 2149
Cdd:TIGR04523 289 QLNQLKSEISDLNNQ--KEQDWNK 310
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1634-2185 |
4.09e-09 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 62.93 E-value: 4.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1634 ERLIQLAEGNLNTLVTEMNELLTR-ATKVTADGEQTGQDAErtntraNSLGEFIKD---LAQHAEAVSEKAVKLNETLGI 1709
Cdd:PTZ00440 601 EELINEALFNKEKFINEKNDLQEKvKYILNKFYKGDLQELL------DELSHFLDDhkyLYHEAKSKEDLQTLLNTSKNE 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1710 QDKAFERNLQELQNEVDKMMTELrrKNLDTQKEVAEDELvaaealLKKVKKLFGESRGKNEEMEKDLREKLADYKSKVHD 1789
Cdd:PTZ00440 675 YEKLEFMKSDNIDNIIKNLKKEL--QNLLSLKENIIKKQ------LNNIEQDISNSLNQYTIKYNDLKSSIEEYKEEEEK 746
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1790 AWDLlREATDKIKEAnLLSAENQKNMTALEkkkeaiesGKRQTEDTLKEGTDILDEANRLADEINSVIDYVEDIQTKLPP 1869
Cdd:PTZ00440 747 LEVY-KHQIINRKNE-FILHLYENDKDLPD--------GKNTYEEFLQYKDTILNKENKISNDINILKENKKNNQDLLNS 816
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1870 ---LSEDLKG-------KIEDLSQEIKDRKLAEKVSQAEShaaQLNDSSAVLDRILDEAKNISFNaTAAFKAYSNIKDYI 1939
Cdd:PTZ00440 817 yniLIQKLEAhtekndeELKQLLQKFPTEDENLNLKELEK---EFNENNQIVDNIIKDIENMNKN-INIIKTLNIAINRS 892
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1940 DKAEKIAKEakvLAHEATELatgpqgslqegaKGSLQKSFGFLNEAKKLANDVKENdeHLNGLTSRLDNANvrnrdllRA 2019
Cdd:PTZ00440 893 NSNKQLVEH---LLNNKIDL------------KNKLEQHMKIINTDNIIQKNEKLN--LLNNLNKEKEKIE-------KQ 948
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2020 LNDT-LERLSAIPNDTAAKLQAVKDKARQANDTAKDVLAQIKD----LHQNLDGLKKNYNQLAdsvAKTNAVVKDPsKNK 2094
Cdd:PTZ00440 949 LSDTkINNLKMQIEKTLEYYDKSKENINGNDGTHLEKLDKEKDewehFKSEIDKLNVNYNILN---KKIDDLIKKQ-HDD 1024
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2095 IIADADATVKNLEQEADRLIDKLkpIKELEDnLKKNISEIKELINQARKQANSIKVSVSSGGDCIRTYKPEIKKGsyNSI 2174
Cdd:PTZ00440 1025 IIELIDKLIKEKGKEIEEKVDQY--ISLLEK-MKTKLSSFHFNIDIKKYKNPKIKEEIKLLEEKVEALLKKIDEN--KNK 1099
|
570
....*....|.
gi 1814459924 2175 IVNVKTAVADN 2185
Cdd:PTZ00440 1100 LIEIKNKSHEH 1110
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1017-1062 |
5.09e-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: 54.28 E-value: 5.09e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1017 ACDCSHLG---NNCDPKTGRCICPPNTIGEKCSKCVPNTWGH-SITTGCK 1062
Cdd:cd00055 1 PCDCNGHGslsGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLpSQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1423-1471 |
5.09e-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: 54.28 E-value: 5.09e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1814459924 1423 PCQCHGHSSL---CDPETSICQnCQHHTAGDFCERCVLGYYGIVKGlPDDCQ 1471
Cdd:cd00055 1 PCDCNGHGSLsgqCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQ-GGGCQ 50
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1684-2068 |
6.03e-09 |
|
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: 62.01 E-value: 6.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1684 EFIKDLAQHAEAVSEKAVKLNEtLGIQDKAFERN---LQELQNEVDKMMTE----------------------LRRKN-L 1737
Cdd:TIGR02169 157 KIIDEIAGVAEFDRKKEKALEE-LEEVEENIERLdliIDEKRQQLERLRRErekaeryqallkekreyegyelLKEKEaL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1738 DTQKEVAEDELVAAEALLKKVKKLFgesrgknEEMEKDLREKLadykskvhdawDLLREATDKIKeanllsAENQKNMTA 1817
Cdd:TIGR02169 236 ERQKEAIERQLASLEEELEKLTEEI-------SELEKRLEEIE-----------QLLEELNKKIK------DLGEEEQLR 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1818 LEKKKEAIESGKRQTEDTLKEGTDILDEA-NRLAD---EINSVIDYVEDIQTKLpplsEDLKGKIEDLSQEIKDRK--LA 1891
Cdd:TIGR02169 292 VKEKIGELEAEIASLERSIAEKERELEDAeERLAKleaEIDKLLAEIEELEREI----EEERKRRDKLTEEYAELKeeLE 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1892 EKVSQAEShaaqlndssavldriLDEAKNISFNATAAFKaySNIKDYIDKAEKIAKEAKVLAHEATELaTGPQGSLQEGA 1971
Cdd:TIGR02169 368 DLRAELEE---------------VDKEFAETRDELKDYR--EKLEKLKREINELKRELDRLQEELQRL-SEELADLNAAI 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1972 KGSLQKSFGFLNEAKKLANDVKENDEHLNGLTSRLDNAnvrnRDLLRALNDTLERLSAIPNDTAAKLQAVKDKARQANDT 2051
Cdd:TIGR02169 430 AGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKY----EQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEER 505
|
410
....*....|....*..
gi 1814459924 2052 AKDVLAQIKDLHQNLDG 2068
Cdd:TIGR02169 506 VRGGRAVEEVLKASIQG 522
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
473-519 |
7.79e-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: 53.90 E-value: 7.79e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1814459924 473 CNCSGAGSTNE--DPCFGPCNCKENVEGGDCSRCKFGFFNLQEDNHRGC 519
Cdd:pfam00053 1 CDCNPHGSLSDtcDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
869-912 |
7.90e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 53.47 E-value: 7.90e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1814459924 869 CQCNdnLDFSIPGSCDSLSGSCLiCKPGTTGRYCELCADGYFGD 912
Cdd:smart00180 1 CDCD--PGGSASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD 41
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1018-1061 |
7.90e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 53.47 E-value: 7.90e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1814459924 1018 CDCS---HLGNNCDPKTGRCICPPNTIGEKCSKCVPNTWGHSiTTGC 1061
Cdd:smart00180 1 CDCDpggSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG-PPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1063-1105 |
8.30e-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: 8.30e-09
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1814459924 1063 PCNCSSVGSLDFQCNLN*GQCNCRPKFSG*KCTECNRGHWSYP 1105
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
1693-1838 |
9.83e-09 |
|
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.
Pssm-ID: 403808 [Multi-domain] Cd Length: 142 Bit Score: 56.54 E-value: 9.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1693 AEAVSEKAVKLNEtlgiQDKAFERNLQELQNEVdkmmTELRRKNldtqkEVAEDELVAAEALLKKVKKLFGES---RGKN 1769
Cdd:pfam12718 9 AENAQERAEELEE----KVKELEQENLEKEQEI----KSLTHKN-----QQLEEEVEKLEEQLKEAKEKAEESeklKTNN 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1814459924 1770 EEMEK---DLREKLADYKSKvhdawdlLREATDKIKEANLLSAENQKNMTALEKKKEAIESGKRQTEDTLKE 1838
Cdd:pfam12718 76 ENLTRkiqLLEEELEESDKR-------LKETTEKLRETDVKAEHLERKVQALEQERDEWEKKYEELEEKYKE 140
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1110-1167 |
9.85e-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: 53.51 E-value: 9.85e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1814459924 1110 CDCFLPG*DDSTCDLETkkcsctdktGQCTCKVNVEGVRCDRCRLGKFGLEAKNPLGC 1167
Cdd:pfam00053 1 CDCNPHGSLSDTCDPET---------GQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1634-2149 |
1.56e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.72 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1634 ERLIQLAEGNLNTLVTEMNELLTRATKVTADGEQTGQDAERTNTRANSLGEFIKDLAQHAEAVSEKAVKLNETLgiqdKA 1713
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR----RE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1714 FERNLQELQNEVDkmmtELRRKNLDTQKEVAE--DELVAAEALLKKVKKLFGESRGKNEEMEKDLREKLADYKSKVHDAW 1791
Cdd:COG1196 314 LEERLEELEEELA----ELEEELEELEEELEEleEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1792 DLLREATDKIKEANLLSAENQKNMTALEKKKEAIES-------GKRQTEDTLKEGTDILDEANRLADEINSVIDYVEDIQ 1864
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEEleealaeLEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1865 TKLP---PLSEDLKGKIEDLSQEIKDRKLAEKVSQAESH---AAQLNDSSAVLDRILDEAKNISFNATAAFKAY--SNIK 1936
Cdd:COG1196 470 EEAAlleAALAELLEELAEAAARLLLLLEAEADYEGFLEgvkAALLLAGLRGLAGAVAVLIGVEAAYEAALEAAlaAALQ 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1937 DYIDKAEKIAKEA-----KVLAHEATELA--TGPQGSLQEGAKGSLQKSFGFL---NEAKKLANDVKENDEHLNGLTS-- 2004
Cdd:COG1196 550 NIVVEDDEVAAAAieylkAAKAGRATFLPldKIRARAALAAALARGAIGAAVDlvaSDLREADARYYVLGDTLLGRTLva 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2005 -RLDNANVRNRDLLRALNDTLERLSAIPNDTAAKLQAVKDKARQANDTAKDVLAQIKDLHQNLDGLKKNYNQLADSVAKT 2083
Cdd:COG1196 630 aRLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEEREL 709
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1814459924 2084 NAVVKDPSKNKIIADADAtvKNLEQEADRLIDKLKPIKELEDNLKKNISEIKELINQARKQANSIK 2149
Cdd:COG1196 710 AEAEEERLEEELEEEALE--EQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLE 773
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
417-469 |
1.73e-08 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 52.74 E-value: 1.73e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1814459924 417 PCHCDPIGSLSEVCVKDEkraqrglapGSCHCKPGFRGVSCDRCARGYTGYPD 469
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGT---------GQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1643-2157 |
2.66e-08 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 60.23 E-value: 2.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1643 NLNTLVT--EMNELLTRATKVTADGEQTGQDAERTNTRANSL-GEFIKDLAQHAEAVSEKAVKLN-ETLGIQDKAFERNL 1718
Cdd:PTZ00440 1286 NMYEFLIsiDSEKILKEILNSTKKAEEFSNDAKKELEKTDNLiKQVEAKIEQAKEHKNKIYGSLEdKQIDDEIKKIEQIK 1365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1719 QELQNEVDKMMTELrrKNLDTQKEVAEDELVAAE------ALLKKvKKLFGESRGKNEEMEKdLREKLADYKSKVHDAWD 1792
Cdd:PTZ00440 1366 EEISNKRKEINKYL--SNIKSNKEKCDLHVRNASrgkdkiDFLNK-HEAIEPSNSKEVNIIK-ITDNINKCKQYSNEAME 1441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1793 LlreaTDKIKEANLLSAENQKNMTALEKKKEAIESGKRqTEDTLKEGTDILDEANrladEINSVIdyvediQTKLPPLSE 1872
Cdd:PTZ00440 1442 T----ENKADENNDSIIKYEKEITNILNNSSILGKKTK-LEKKKKEATNIMDDIN----GEHSII------KTKLTKSSE 1506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1873 DLK--GKIEDLSQEIKDrkLAEKVSQAESHAAQLNDSSAV-----LDRILDEAKNISFNATAAFKAYSNIK--------- 1936
Cdd:PTZ00440 1507 KLNqlNEQPNIKREGDV--LNNDKSTIAYETIQYNLGRVKhnllnILNIKDEIETILNKAQDLMRDISKISkivenknle 1584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1937 -------DYIDKAEKIAKEAKVLAHEATELatGPQGSLQEGAKGSLQKS-----FGFLNEAKKLANDVK----ENDEHLN 2000
Cdd:PTZ00440 1585 nlndkeaDYVKYLDNILKEKQLMEAEYKKL--NEIYSDVDNIEKELKKHkknyeIGLLEKVIEINKNIKlymdSTKESLN 1662
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2001 GL----TSRLDNANVRNRDLLRALNDTLERLSAIPNDTAAKLQAVKDKARQANDTAKDvLAQIKDLHQNLdglKKNYNQL 2076
Cdd:PTZ00440 1663 SLvnnfSSLFNNFYLNKYNINENLEKYKKKLNEIYNEFMESYNIIQEKMKEVSNDDVD-YNEAKTLREEA---QKEEVNL 1738
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2077 ADSVAKTNAVVKDpsknkiiadadatVKNleQEADRLIDKlkpIKELEDNLKKNISEIKELINQARKQANSIKVSVSSGG 2156
Cdd:PTZ00440 1739 NNKEEEAKKYLND-------------IKK--QESFRFILY---MKEKLDELSKMCKQQYNIVDEGYNYIKKKIEYIKTLN 1800
|
.
gi 1814459924 2157 D 2157
Cdd:PTZ00440 1801 D 1801
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
869-915 |
2.78e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 52.36 E-value: 2.78e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1814459924 869 CQCNDNLdfSIPGSCDSLSGSCLiCKPGTTGRYCELCADGYFGDAVD 915
Cdd:pfam00053 1 CDCNPHG--SLSDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSD 44
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1018-1061 |
2.98e-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: 51.97 E-value: 2.98e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1814459924 1018 CDCSHLG---NNCDPKTGRCICPPNTIGEKCSKCVPNTWGHSITTGC 1061
Cdd:pfam00053 1 CDCNPHGslsDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQ 47
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1983-2150 |
3.38e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 58.76 E-value: 3.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1983 NEAKKLANDVKENDEHLNGLTSRLDNAN-----VRNRdlLRALNDTLERLSAIPNDTAAKLQAVKDKARQANDTAKDVLA 2057
Cdd:COG4372 45 EELEQLREELEQAREELEQLEEELEQARseleqLEEE--LEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQK 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2058 QIKDLHQNLDGLKKNYNQLadsvaktnavvkdpskNKIIADADATVKNLEQEADRLIDKLKPIKELEDNLKKN--ISEIK 2135
Cdd:COG4372 123 ERQDLEQQRKQLEAQIAEL----------------QSEIAEREEELKELEEQLESLQEELAALEQELQALSEAeaEQALD 186
|
170
....*....|....*
gi 1814459924 2136 ELINQARKQANSIKV 2150
Cdd:COG4372 187 ELLKEANRNAEKEEE 201
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
761-801 |
3.59e-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: 51.97 E-value: 3.59e-08
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1814459924 761 CQCFGHA---ESCDDITGECLnCKDHTGGLYCNKCLPGFYGDPT 801
Cdd:pfam00053 1 CDCNPHGslsDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPS 43
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1651-1905 |
3.88e-08 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 58.75 E-value: 3.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1651 MNELLTraTKVTADGEQTGQDAERTNTRA----NSLGEFIK---DLAQHAEAVSEKAVKLNETLGIQDKAFERNLQELQN 1723
Cdd:pfam07888 3 LDELVT--LEEESHGEEGGTDMLLVVPRAellqNRLEECLQeraELLQAQEAANRQREKEKERYKRDREQWERQRRELES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1724 EVDKMMTELRRKNLDTQK-EVAEDELVAAEALLKKVKKLFGESRGKNEEMEKDLREKLADYKSKVHDAWDLLREATDKIK 1802
Cdd:pfam07888 81 RVAELKEELRQSREKHEElEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1803 EANLLSAENQKNMTALEKKKEAIESGKRQTEDTLKEGTDILDE----ANRLADEINSVIDYVEDIQTK---LPPLSEDLK 1875
Cdd:pfam07888 161 KAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQrdtqVLQLQDTITTLTQKLTTAHRKeaeNEALLEELR 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1814459924 1876 G----------KIEDLSQE------IKDRKLAEkVSQAESHAAQLN 1905
Cdd:pfam07888 241 SlqerlnaserKVEGLGEElssmaaQRDRTQAE-LHQARLQAAQLT 285
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1763-2158 |
4.28e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 58.38 E-value: 4.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1763 GESRGKNEEMEKDLREKLADYKSKVHDAwdlLREATDKIKEAnllsaenQKNMTALEKKKEAIESGKRQTEDTLKEGTDI 1842
Cdd:COG4372 5 GEKVGKARLSLFGLRPKTGILIAALSEQ---LRKALFELDKL-------QEELEQLREELEQAREELEQLEEELEQARSE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1843 LDEANRLADEINsvidyvEDIQTKLPPLsEDLKGKIEDLSQEIKdrKLAEKVSQAESHAAQLNDSSAVLDRILDEAKnis 1922
Cdd:COG4372 75 LEQLEEELEELN------EQLQAAQAEL-AQAQEELESLQEEAE--ELQEELEELQKERQDLEQQRKQLEAQIAELQ--- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1923 fnataafkaySNIKDYIDKAEKIAKEAKVLAHEATELATGPQGSLQEGAKGSLQKsfgFLNEAKKLANDVKENDEHLNGL 2002
Cdd:COG4372 143 ----------SEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDE---LLKEANRNAEKEEELAEAEKLI 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2003 TSRLDNANVRNRDLLRALNDTLERLSAIPNDTAAKLQAVKDKARQANDtaKDVLAQIKDLHQNLDGLKKNYNQLADSVAK 2082
Cdd:COG4372 210 ESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVIL--KEIEELELAILVEKDTEEEELEIAALELEA 287
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1814459924 2083 TNAVVKDPSKNKIIADADATVKNLEQEADRLIDKLKPIKELEDNLKKNISEIKELINQARKQANSIKVSVSSGGDC 2158
Cdd:COG4372 288 LEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGA 363
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1110-1167 |
4.56e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 51.54 E-value: 4.56e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1814459924 1110 CDCFLPG*DDSTCDLETkkcsctdktGQCTCKVNVEGVRCDRCRLGKFGleaKNPLGC 1167
Cdd:smart00180 1 CDCDPGGSASGTCDPDT---------GQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1109-1167 |
4.56e-08 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 51.59 E-value: 4.56e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1814459924 1109 PCDCFLPG*DDSTCDLETkkcsctdktGQCTCKVNVEGVRCDRCRLGKFGLeAKNPLGC 1167
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGT---------GQCECKPNTTGRRCDRCAPGYYGL-PSQGGGC 49
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1734-2149 |
5.12e-08 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 58.69 E-value: 5.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1734 RKNLDTQKEVAEDELVAAEAL-----LKKVKKL--FGESRGKNEEMEKDLRE----KLADYKSKVHDAwdllREATDKIk 1802
Cdd:PRK04778 24 RKRNYKRIDELEERKQELENLpvndeLEKVKKLnlTGQSEEKFEEWRQKWDEivtnSLPDIEEQLFEA----EELNDKF- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1803 eaNLLSAenQKNMTALEKKKEAIESgkrQTEDTLKEGTDIL--DEANRlaDEINSVIDYVEDIQTKL-----------PP 1869
Cdd:PRK04778 99 --RFRKA--KHEINEIESLLDLIEE---DIEQILEELQELLesEEKNR--EEVEQLKDLYRELRKSLlanrfsfgpalDE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1870 LSEDLKgKIEDLSQEIKDRKLAEKVSQAESHAAQLNDSSAVLDRILDEaknisfnataafkaysnIKDYIDKAEKiakea 1949
Cdd:PRK04778 170 LEKQLE-NLEEEFSQFVELTESGDYVEAREILDQLEEELAALEQIMEE-----------------IPELLKELQT----- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1950 kVLAHEATELATGPQGSLQEGAKgslQKSFGFLNEAKKLANDVKENDEHLNGLtsRLDNANVRNRDL---LRALNDTLER 2026
Cdd:PRK04778 227 -ELPDQLQELKAGYRELVEEGYH---LDHLDIEKEIQDLKEQIDENLALLEEL--DLDEAEEKNEEIqerIDQLYDILER 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2027 lsaipnDTAAKLQAVKDKARQANDTAKdVLAQIKDLHQNLDGLKKNYnQLADS-VAKTNAVVKDpsKNKIIADADATVKN 2105
Cdd:PRK04778 301 ------EVKARKYVEKNSDTLPDFLEH-AKEQNKELKEEIDRVKQSY-TLNESeLESVRQLEKQ--LESLEKQYDEITER 370
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1814459924 2106 LEQEA----------DRLIDKLKPIKELEDNLKKNISEIKELINQARKQANSIK 2149
Cdd:PRK04778 371 IAEQEiayselqeelEEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYR 424
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1982-2154 |
5.25e-08 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 57.23 E-value: 5.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1982 LNEAKKLANDVKENDEHLNGLTSRLDNANVRNRDLLRALNDTLERLSAIPNDTAAKLQAVKDKARQAndtaKDVLAQIKD 2061
Cdd:COG1340 31 RDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDEL----RKELAELNK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2062 LHQNLDGLKKNYNQLADsvAKTNAVVkDPSK-NKIIAdadaTVKNLEQEADRL---IDKLKPIKELE---DNLKKNISEI 2134
Cdd:COG1340 107 AGGSIDKLRKEIERLEW--RQQTEVL-SPEEeKELVE----KIKELEKELEKAkkaLEKNEKLKELRaelKELRKEAEEI 179
|
170 180
....*....|....*....|
gi 1814459924 2135 KELINQARKQANSIKVSVSS 2154
Cdd:COG1340 180 HKKIKELAEEAQELHEEMIE 199
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1064-1107 |
5.71e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 51.16 E-value: 5.71e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1814459924 1064 CNCSSVGSLDFQCNLN*GQCNCRPKFSG*KCTECNRGHW--SYPHC 1107
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYgdGPPGC 46
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1630-2129 |
5.96e-08 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 59.03 E-value: 5.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1630 QRAPERLIQLAE-----GNLNTL-------VTEMNELLTRATKVTADGEQTGQDAERTntrANSLGEFIKDL-AQHAEAV 1696
Cdd:pfam01576 159 ERISEFTSNLAEeeekaKSLSKLknkheamISDLEERLKKEEKGRQELEKAKRKLEGE---STDLQEQIAELqAQIAELR 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1697 SEKAVKLNETLGIQDKAFERNLQelQNEVDKMMTELRRKNLDTQKEVaEDELVAaeallkkvkklfgesRGKNEEMEKDL 1776
Cdd:pfam01576 236 AQLAKKEEELQAALARLEEETAQ--KNNALKKIRELEAQISELQEDL-ESERAA---------------RNKAEKQRRDL 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1777 REKLADYKSKVHDAWD-----------------LLREATD---KIKEANLLSAEnQKNMTALEKKKEAIESGKRQTEDTL 1836
Cdd:pfam01576 298 GEELEALKTELEDTLDttaaqqelrskreqevtELKKALEeetRSHEAQLQEMR-QKHTQALEELTEQLEQAKRNKANLE 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1837 KEGTDILDEANRLADEINSVIDYVEDIQTKlpplsedlKGKIEDLSQEikdrkLAEKVSQAESHAAQLNDSsavLDRILD 1916
Cdd:pfam01576 377 KAKQALESENAELQAELRTLQQAKQDSEHK--------RKKLEGQLQE-----LQARLSESERQRAELAEK---LSKLQS 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1917 EAKNISfnataafkaySNIKDYIDKAEKIAKEAKVLA---HEATELatgpqgsLQEGAKGSLqksfgflneakKLANDVK 1993
Cdd:pfam01576 441 ELESVS----------SLLNEAEGKNIKLSKDVSSLEsqlQDTQEL-------LQEETRQKL-----------NLSTRLR 492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1994 ENDEHLNGLTSRLDNANVRNRDLLRALNDTLERLSaipnDTAAKLQAVKDKARQANDTAKDVLAQIKDLHQNLDGLKKNY 2073
Cdd:pfam01576 493 QLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLS----DMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAY 568
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1814459924 2074 NQLadsvaktnavvkdpsknkiiadaDATVKNLEQEADRLIDKLKPIKELEDNLKK 2129
Cdd:pfam01576 569 DKL-----------------------EKTKNRLQQELDDLLVDLDHQRQLVSNLEK 601
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1732-2149 |
6.29e-08 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 58.33 E-value: 6.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1732 LRRKN------LDTQKEVAEDELVAAEalLKKVKKL--FGESRGKNEEMEKDLRE----KLADYKSKVHDAwdllREATD 1799
Cdd:pfam06160 4 LRKKIykeideLEERKNELMNLPVQEE--LSKVKKLnlTGETQEKFEEWRKKWDDivtkSLPDIEELLFEA----EELND 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1800 KIKeanLLSAenQKNMTALEKKKEAIESgkrQTEDTLKEGTDILDEANRLADEINSVIDYVEDIQTKLppLSEDLK-GKI 1878
Cdd:pfam06160 78 KYR---FKKA--KKALDEIEELLDDIEE---DIKQILEELDELLESEEKNREEVEELKDKYRELRKTL--LANRFSyGPA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1879 EDlsqeikdrKLAEKVSQAE---SHAAQLNDSSAVLD--RILDEAKNisfnATAAFKAY-SNIKDYIDKAEKiakeakVL 1952
Cdd:pfam06160 148 ID--------ELEKQLAEIEeefSQFEELTESGDYLEarEVLEKLEE----ETDALEELmEDIPPLYEELKT------EL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1953 AHEATELATGPQgSLQEgaKGSLQKSFGFLNEAKKLANDVKENDEHLNGLtsRLDNANVRNRDL---LRALNDTLERlsa 2029
Cdd:pfam06160 210 PDQLEELKEGYR-EMEE--EGYALEHLNVDKEIQQLEEQLEENLALLENL--ELDEAEEALEEIeerIDQLYDLLEK--- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2030 ipnDTAAKLQAVKDKarqanDTAKDVLAQIKDLHQNL----DGLKKNYnQLADSVAktnAVVKDPSK--NKIIADADATV 2103
Cdd:pfam06160 282 ---EVDAKKYVEKNL-----PEIEDYLEHAEEQNKELkeelERVQQSY-TLNENEL---ERVRGLEKqlEELEKRYDEIV 349
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1814459924 2104 KNLEQEA----------DRLIDKLKPIKELEDNLKKNISEIKELINQARKQANSIK 2149
Cdd:pfam06160 350 ERLEEKEvayselqeelEEILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFK 405
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
418-470 |
6.55e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 51.16 E-value: 6.55e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1814459924 418 CHCDPIGSLSEVCVKDEkraqrglapGSCHCKPGFRGVSCDRCARGYTG--YPDC 470
Cdd:smart00180 1 CDCDPGGSASGTCDPDT---------GQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1648-2138 |
2.19e-07 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 57.01 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1648 VTEMNELLTRATkVTADGEQTGQDAER-------TNTRANSLGE-FIKDLAQHAEAVSEKAVKLNETLGIQ---DKAFER 1716
Cdd:COG5022 857 AKKRFSLLKKET-IYLQSAQRVELAERqlqelkiDVKSISSLKLvNLELESEIIELKKSLSSDLIENLEFKtelIARLKK 935
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1717 NLQ--ELQNEVDKMMTELRRKN-LDTQKEVAEDELVAAEALLKKVKKLFGESRGKNEEME---KDLREKLADYKSkvhda 1790
Cdd:COG5022 936 LLNniDLEEGPSIEYVKLPELNkLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKnfkKELAELSKQYGA----- 1010
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1791 wdlLREATDKIKEANLLSAENQKNMTalEKKKEAIESGKRQTEDTLKEGTDIldEANRLADEINSVIDYVEDIQTKLPPL 1870
Cdd:COG5022 1011 ---LQESTKQLKELPVEVAELQSASK--IISSESTELSILKPLQKLKGLLLL--ENNQLQARYKALKLRRENSLLDDKQL 1083
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1871 SEDLKGKIEDLSQEIKDRKLAEKVSQAESHAAQLNDSSAV-LDRILDEAKNISfnataafKAYSNIKDYIDKAEKIAKEA 1949
Cdd:COG5022 1084 YQLESTENLLKTINVKDLEVTNRNLVKPANVLQFIVAQMIkLNLLQEISKFLS-------QLVNTLEPVFQKLSVLQLEL 1156
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1950 KVLAHEATELATGPQGSLqegaKGSLQKSFgFLNEAKKLANdvKENDEHLNGLTSRLDN--ANVRNRDLLRALNDTLERL 2027
Cdd:COG5022 1157 DGLFWEANLEALPSPPPF----AALSEKRL-YQSALYDEKS--KLSSSEVNDLKNELIAlfSKIFSGWPRGDKLKKLISE 1229
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2028 SAIPNDTAAKLQAVKD----KARQANDTAKDVLAQIKDLHQNLDGLKKNYNQLADSVAKTNAVVKDPSKNKIIADADA-- 2101
Cdd:COG5022 1230 GWVPTEYSTSLKGFNNlnkkFDTPASMSNEKLLSLLNSIDNLLSSYKLEEEVLPATINSLLQYINVGLFNALRTKASSlr 1309
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1814459924 2102 --TVKNLEQEADRLIDKLKPIK------ELEDN---------LKKNISEIKELI 2138
Cdd:COG5022 1310 wkSATEVNYNSEELDDWCREFEisdvdeELEELiqavkvlqlLKDDLNKLDELL 1363
|
|
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
1776-2187 |
2.23e-07 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 56.57 E-value: 2.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1776 LREKLADYKSKVHDAWDLLREATDKIKEANLLSAENQKNMTALEKKKEAIESGKRQTEDTLKEGTDILDEANRLADEINS 1855
Cdd:COG0840 4 LLLLLALLLALLLLALSLLALLAAALLILLALLLAALTALALLLLLSLLALLLLLLLLALALLLVLLALLLLLALVVLLA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1856 VIDYVEDIQTKLPPLSEDLKGKIEDLSQEIKDRKLAEKVSQAESHAAQLNDSSAVLDRILDEAKNISFNATAAFKAYSNI 1935
Cdd:COG0840 84 LLLALLLLLLALLALALAALALLAALAALLALLELLLAALLAALAIALLALAALLALAALALALLALALLAAAAAAAAAL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1936 KDYIDKAEKIAKEAKVLAHEATELATGPQGSLQEGAKGSLQKSFGFLNEAKKLANDVKENDehlngLTSRLDnanVRNRD 2015
Cdd:COG0840 164 AALLEAAALALAAAALALALLAAALLALVALAIILALLLSRSITRPLRELLEVLERIAEGD-----LTVRID---VDSKD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2016 ----LLRALNDTLERLSAIpndtaakLQAVKDKARQANDTAKDVLAQIKDLHQNLDGLKKNYNQLADSVAKTNAVVKDps 2091
Cdd:COG0840 236 eigqLADAFNRMIENLREL-------VGQVRESAEQVASASEELAASAEELAAGAEEQAASLEETAAAMEELSATVQE-- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2092 knkiIADADATVKNLEQEADRLIDKlkpIKELEDNLKKNISEIKELINQARKQANSIKVSVSsggdcirtykpEIKKgsy 2171
Cdd:COG0840 307 ----VAENAQQAAELAEEASELAEE---GGEVVEEAVEGIEEIRESVEETAETIEELGESSQ-----------EIGE--- 365
|
410
....*....|....*...
gi 1814459924 2172 nsiIVNVKTAVAD--NLL 2187
Cdd:COG0840 366 ---IVDVIDDIAEqtNLL 380
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1656-2149 |
2.33e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.07 E-value: 2.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1656 TRATKVTADGEQTGQDAERTNT-RANSLGEfikdlAQHAEAVSEKAVKLNETLGIQDKafeRNLQELQNEVDKMMTELRR 1734
Cdd:PTZ00121 1087 NRADEATEEAFGKAEEAKKTETgKAEEARK-----AEEAKKKAEDARKAEEARKAEDA---RKAEEARKAEDAKRVEIAR 1158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1735 KNLDTQKevAEDELVAAEAllKKVkklfgESRGKNEEMEKDLREKLADYKSKVHDAwdllREATDKIKEANLLSAENQKN 1814
Cdd:PTZ00121 1159 KAEDARK--AEEARKAEDA--KKA-----EAARKAEEVRKAEELRKAEDARKAEAA----RKAEEERKAEEARKAEDAKK 1225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1815 MTALEKKKEAiesgKRQTEDTLKEgtdildEANRLADEINSvidYVEDIQTKLPPLSEDLKGKIEDLSQEIKDrklAEKV 1894
Cdd:PTZ00121 1226 AEAVKKAEEA----KKDAEEAKKA------EEERNNEEIRK---FEEARMAHFARRQAAIKAEEARKADELKK---AEEK 1289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1895 SQAEshaaQLNDSSAVldRILDEAKNisfNATAAFKAySNIKDYIDKAEKIAKEAKVLAHEATELATGPQGSlQEGAKGS 1974
Cdd:PTZ00121 1290 KKAD----EAKKAEEK--KKADEAKK---KAEEAKKA-DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAE-AEAAADE 1358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1975 LQKSfgflnEAKKLANDVKENDEHLNGLTSRLDNANVRNRDLLRALNDTLERLSaipnDTAAKLQAVKDKARQANDTAKD 2054
Cdd:PTZ00121 1359 AEAA-----EEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKA----DELKKAAAAKKKADEAKKKAEE 1429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2055 VlaqikdlhQNLDGLKKNynqlADSVAKTNAVVKDPSKNKiiaDADATVKNLEQ--EADRLIDKLKPIKELEDnLKKNIS 2132
Cdd:PTZ00121 1430 K--------KKADEAKKK----AEEAKKADEAKKKAEEAK---KAEEAKKKAEEakKADEAKKKAEEAKKADE-AKKKAE 1493
|
490
....*....|....*..
gi 1814459924 2133 EIKELINQARKQANSIK 2149
Cdd:PTZ00121 1494 EAKKKADEAKKAAEAKK 1510
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1621-1926 |
2.77e-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: 2.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1621 QELKHLLSPQRAPERLIQLAEGNLNTLVTEMNELLTRATKVTADGEQTGQDAERTNTRA----NSLGEFIKDLAQHAEAV 1696
Cdd:TIGR02168 701 AELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELeaeiEELEERLEEAEEELAEA 780
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1697 SEKAVKLNETLG---IQDKAFERNLQELQNEVD------------------------KMMTELRRK-------------- 1735
Cdd:TIGR02168 781 EAEIEELEAQIEqlkEELKALREALDELRAELTllneeaanlrerleslerriaateRRLEDLEEQieelsedieslaae 860
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1736 --NLDTQKEVAEDELvaaEALLKKVKKLFGESRGKNEEMEkDLREKLADYKSKVHDAWDLLREATDKIKEANLlsAENQK 1813
Cdd:TIGR02168 861 ieELEELIEELESEL---EALLNERASLEEALALLRSELE-ELSEELRELESKRSELRRELEELREKLAQLEL--RLEGL 934
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1814 NMTALEKKKEAIESGKRQTEDTLKEGTDILDEANRLADEInsvidyvEDIQTKLPPLS----------EDLKGKIEDLSQ 1883
Cdd:TIGR02168 935 EVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRL-------KRLENKIKELGpvnlaaieeyEELKERYDFLTA 1007
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1814459924 1884 EIKDrkLAEKVSQAEShaaqlndssaVLDRILDEAKNiSFNAT 1926
Cdd:TIGR02168 1008 QKED--LTEAKETLEE----------AIEEIDREARE-RFKDT 1037
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1616-1914 |
3.17e-07 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 56.59 E-value: 3.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1616 LENMT-------QELKHLLSP-QRAPERLIQLAEGNLNTL---VTEMNELLTRATKVTADGEQTGQDAERTNTRansLGE 1684
Cdd:TIGR00606 700 LQSKLrlapdklKSTESELKKkEKRRDEMLGLAPGRQSIIdlkEKEIPELRNKLQKVNRDIQRLKNDIEEQETL---LGT 776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1685 FIKDLAQHAEAVSEKAV--KLNETLGIQDKAFERNLQELQN-EVDKMMTELRRKNLDTQKEVaeDELVAAEALLKKVkkl 1761
Cdd:TIGR00606 777 IMPEEESAKVCLTDVTImeRFQMELKDVERKIAQQAAKLQGsDLDRTVQQVNQEKQEKQHEL--DTVVSKIELNRKL--- 851
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1762 fgeSRGKNEEMEKdLREKLADYKSKVHDAWDLLREATDKIKEANLLSAENQKNMTALEKKKEAIESGKRQTEDTLKEGTD 1841
Cdd:TIGR00606 852 ---IQDQQEQIQH-LKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEE 927
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1814459924 1842 IL---DEANRLADeinsviDYVEDIQTKLPPLSEDLKgKIEDLSQEIKDRKLAEKVSQAESHAAQLNDSSAVLDRI 1914
Cdd:TIGR00606 928 LIsskETSNKKAQ------DKVNDIKEKVKNIHGYMK-DIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKI 996
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1672-1958 |
3.21e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.69 E-value: 3.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1672 AERTNTRANSL--GEFIKDLAQHAEAVSEKAVKLNETLgiqDKAFERNlqELQNEVDKMMTELRRKNLDTQKEVAEDELV 1749
Cdd:PTZ00121 1615 AEEAKIKAEELkkAEEEKKKVEQLKKKEAEEKKKAEEL---KKAEEEN--KIKAAEEAKKAEEDKKKAEEAKKAEEDEKK 1689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1750 AAEALLKK---------VKKLFGESRGKNEEMEKDLREKladyKSKVHDAWDllREATDKIKEANLLSAENQKNMTALEK 1820
Cdd:PTZ00121 1690 AAEALKKEaeeakkaeeLKKKEAEEKKKAEELKKAEEEN----KIKAEEAKK--EAEEDKKKAEEAKKDEEEKKKIAHLK 1763
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1821 KKE--AIESGKRQTEDTLKEGTDILDEANRLADE--INSVIDYVEDIQ---TKLPPLSEDLKGKIEDLSQEIKDRK--LA 1891
Cdd:PTZ00121 1764 KEEekKAEEIRKEKEAVIEEELDEEDEKRRMEVDkkIKDIFDNFANIIeggKEGNLVINDSKEMEDSAIKEVADSKnmQL 1843
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1814459924 1892 EKVSQAESHAAQLNDSSAVldrilDEAKNISFNataafKAYSNIKDYIDKAEKiAKEAKVLAHEATE 1958
Cdd:PTZ00121 1844 EEADAFEKHKFNKNNENGE-----DGNKEADFN-----KEKDLKEDDEEEIEE-ADEIEKIDKDDIE 1899
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1645-2118 |
3.28e-07 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 56.37 E-value: 3.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1645 NTLVTEMNELLTR-ATKVTADGEQTGQDAERTNTRANSLGEfIKDLAQHAEavsekaVKLNETLGIQDKAfeRNLQELQN 1723
Cdd:pfam10174 341 AILQTEVDALRLRlEEKESFLNKKTKQLQDLTEEKSTLAGE-IRDLKDMLD------VKERKINVLQKKI--ENLQEQLR 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1724 EVDKMMTELRRK---------NLDTQKEVAEDELVAAEALLKKVKKLFG-ESRGKNEEMEkDLREKLADYKSKVhDAwdL 1793
Cdd:pfam10174 412 DKDKQLAGLKERvkslqtdssNTDTALTTLEEALSEKERIIERLKEQRErEDRERLEELE-SLKKENKDLKEKV-SA--L 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1794 LREATDkiKEANLLSAENQKnmTALEKKKEAIESGKRQTEDTLKEGTdilDEANRLADEINSVIDYVEDIQTKlpplsED 1873
Cdd:pfam10174 488 QPELTE--KESSLIDLKEHA--SSLASSGLKKDSKLKSLEIAVEQKK---EECSKLENQLKKAHNAEEAVRTN-----PE 555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1874 LKGKIEDLSQEIKDRKLAEKVSQAEshaaqlndssavLDRILDeaknisfnataAFKAYSNIKDyiDKAEKIAKEAKVLA 1953
Cdd:pfam10174 556 INDRIRLLEQEVARYKEESGKAQAE------------VERLLG-----------ILREVENEKN--DKDKKIAELESLTL 610
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1954 HEATELATgPQGSLQEGAKGSLQKSFGFLNEAKKLANDVKENDEHLngLTSRLDNANVRNRDLLRAlndTLERLSAIPND 2033
Cdd:pfam10174 611 RQMKEQNK-KVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQL--QLEELMGALEKTRQELDA---TKARLSSTQQS 684
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2034 TAAK--------------LQAVKDKARQAndtakdVLAQIKDLHQNLDGLkknynQLADSVAKTNAvvkdpsknkiiada 2099
Cdd:pfam10174 685 LAEKdghltnlraerrkqLEEILEMKQEA------LLAAISEKDANIALL-----ELSSSKKKKTQ-------------- 739
|
490
....*....|....*....
gi 1814459924 2100 dATVKNLEQEADRLIDKLK 2118
Cdd:pfam10174 740 -EEVMALKREKDRLVHQLK 757
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1794-2188 |
4.41e-07 |
|
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: 56.21 E-value: 4.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1794 LREATDKIKEANLLSAENQKNMTALEKKKEAIESGKRQTEDTLKE--GTDILDEANRLADEINSVIDYVEDIQTKLPPLS 1871
Cdd:TIGR01612 1485 INELKEHIDKSKGCKDEADKNAKAIEKNKELFEQYKKDVTELLNKysALAIKNKFAKTKKDSEIIIKEIKDAHKKFILEA 1564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1872 EDLKGKIedlsQEIKDRKLaekvsQAESHAAQLNDSSAVLDRILDEAKNISfnatAAFKAYSNIK----DYIDKAEKIAK 1947
Cdd:TIGR01612 1565 EKSEQKI----KEIKKEKF-----RIEDDAAKNDKSNKAAIDIQLSLENFE----NKFLKISDIKkkinDCLKETESIEK 1631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1948 EAKVLA--HEATELATGPQ--GSLQE------GAKGSLQ---KSFGFLN-EAKKLANDVKENDEHLN-GLTSRLDNANVR 2012
Cdd:TIGR01612 1632 KISSFSidSQDTELKENGDnlNSLQEfleslkDQKKNIEdkkKELDELDsEIEKIEIDVDQHKKNYEiGIIEKIKEIAIA 1711
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2013 NRDLLRALNDTLErlSAIPNDTAA----KLQAVkdkarQANDTAKDVLAQIKDLHQNldgLKKNYNQLA---DSVAKtNA 2085
Cdd:TIGR01612 1712 NKEEIESIKELIE--PTIENLISSfntnDLEGI-----DPNEKLEEYNTEIGDIYEE---FIELYNIIAgclETVSK-EP 1780
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2086 VVKDPSKNKIIADADATVKNLEQEadrlidklKPIKELEDNLKknISEIKELINQARKQANSIKVSVSsggdciRTYKpE 2165
Cdd:TIGR01612 1781 ITYDEIKNTRINAQNEFLKIIEIE--------KKSKSYLDDIE--AKEFDRIINHFKKKLDHVNDKFT------KEYS-K 1843
|
410 420
....*....|....*....|....*.
gi 1814459924 2166 IKKGsYNSI---IVNVKTAVADNLLF 2188
Cdd:TIGR01612 1844 INEG-FDDIsksIENVKNSTDENLLF 1868
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
761-803 |
4.98e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 48.46 E-value: 4.98e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1814459924 761 CQC--FGHA-ESCDDITGECLnCKDHTGGLYCNKCLPGFYGDPTKG 803
Cdd:smart00180 1 CDCdpGGSAsGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1690-2084 |
5.01e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.92 E-value: 5.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1690 AQHAEAVSEKAVKLNETLGIQDKAFERNLQELQNEVDKMMTELRRKnldtqkevAEDELVAAEALLK--KVKKLFGESRG 1767
Cdd:PTZ00121 1569 AKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKK--------AEEAKIKAEELKKaeEEKKKVEQLKK 1640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1768 KNEEMEKDLRE-KLADYKSKVHDAWDLLREATDKIKEANLLSAENQKNMTALEKKKEAIESGK------------RQTED 1834
Cdd:PTZ00121 1641 KEAEEKKKAEElKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKaeelkkkeaeekKKAEE 1720
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1835 TLKEgtdilDEANRLAdeinsvidyVEDIQTKlpplSEDLKGKIEDLSQEIKDRKLAEKVSQAESHAAQ--LNDSSAVLD 1912
Cdd:PTZ00121 1721 LKKA-----EEENKIK---------AEEAKKE----AEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEeiRKEKEAVIE 1782
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1913 RIL---DEAKNISFNATA--AFKAYSNIKDYIDKAEKIAKEAKVLAHEATELATGPQGSLQEGAKGSLQKSFGFLNEAKK 1987
Cdd:PTZ00121 1783 EELdeeDEKRRMEVDKKIkdIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGE 1862
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1988 LANdvKENDEHLNGLTSRLDNANVRNRDLLRALN-DTLERlsAIPNDTAA---------KLQAVKDKARQANDTAKDVLA 2057
Cdd:PTZ00121 1863 DGN--KEADFNKEKDLKEDDEEEIEEADEIEKIDkDDIER--EIPNNNMAgknndiiddKLDKDEYIKRDAEETREEIIK 1938
|
410 420
....*....|....*....|....*..
gi 1814459924 2058 QIKDLHQNLDGLKKNYNQLADSVAKTN 2084
Cdd:PTZ00121 1939 ISKKDMCINDFSSKFCDYMKDNISSGN 1965
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1673-2180 |
5.63e-07 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 55.99 E-value: 5.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1673 ERTNTRANSlgEFIKDLAQHAEAVSEKAVKLNETLGIQDK-------AFERNLQELQNEVDKMMTE---LRRKNLDTQKE 1742
Cdd:PTZ00440 943 EKIEKQLSD--TKINNLKMQIEKTLEYYDKSKENINGNDGthlekldKEKDEWEHFKSEIDKLNVNyniLNKKIDDLIKK 1020
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1743 VAEDELVAAEALLKkvkklfgesrgkneEMEKDLREKLADYKSKVHDAWDLLREATDKIKEANLLSAENQKNMTALEKKK 1822
Cdd:PTZ00440 1021 QHDDIIELIDKLIK--------------EKGKEIEEKVDQYISLLEKMKTKLSSFHFNIDIKKYKNPKIKEEIKLLEEKV 1086
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1823 EAIESgkrqtedTLKEGTDILDEANRLADEINSVIDYVEDIQTKlppLSEDLKGKIEDLSQEIKDR-KLAEKVSQAESHA 1901
Cdd:PTZ00440 1087 EALLK-------KIDENKNKLIEIKNKSHEHVVNADKEKNKQTE---HYNKKKKSLEKIYKQMEKTlKELENMNLEDITL 1156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1902 AQLNDSSAVLDRIL--DEAKNISFNATAAFKAYSNIKDYIDKAE----KIAKEAKvlAHEATELATGPQGSL---QEGAK 1972
Cdd:PTZ00440 1157 NEVNEIEIEYERILidHIVEQINNEAKKSKTIMEEIESYKKDIDqvkkNMSKERN--DHLTTFEYNAYYDKAtasYENIE 1234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1973 GSLQKSFGFLNEA--KKLANDVKENDEHLNgltSRLDNANVRNRDL---LRALNDTLERLSAIPNDTAAK---------- 2037
Cdd:PTZ00440 1235 ELTTEAKGLKGEAnrSTNVDELKEIKLQVF---SYLQQVIKENNKMenaLHEIKNMYEFLISIDSEKILKeilnstkkae 1311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2038 ---LQAVKDkARQANDTAKDVLAQIKDL--HQNLDGLKKNYNQLADSVAKTNAVVKDPSK-----NKIIADADATVKNLE 2107
Cdd:PTZ00440 1312 efsNDAKKE-LEKTDNLIKQVEAKIEQAkeHKNKIYGSLEDKQIDDEIKKIEQIKEEISNkrkeiNKYLSNIKSNKEKCD 1390
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2108 QE---ADR---LIDKLKPIKELEDNLKK--NISEIKELINQARK---QANSIKVSVSSGGDCIRTYKPEIKKGSYNSIIV 2176
Cdd:PTZ00440 1391 LHvrnASRgkdKIDFLNKHEAIEPSNSKevNIIKITDNINKCKQysnEAMETENKADENNDSIIKYEKEITNILNNSSIL 1470
|
....
gi 1814459924 2177 NVKT 2180
Cdd:PTZ00440 1471 GKKT 1474
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1698-2152 |
5.92e-07 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 55.82 E-value: 5.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1698 EKAVKLNETLGIQDKAFERNLQELQNEVDKMMTElrRKNLDTQKEVAEDEL----VAAEALLKKVKKLFGESRGKNEEME 1773
Cdd:TIGR00606 301 EQLNDLYHNHQRTVREKERELVDCQRELEKLNKE--RRLLNQEKTELLVEQgrlqLQADRHQEHIRARDSLIQSLATRLE 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1774 KDLREKLADYKSKVHDAWDLLREA-TDKIKEANLLSAENQKNMTALEKKKEAIESGKRQTEDTLKEGTDILDEAnrlADE 1852
Cdd:TIGR00606 379 LDGFERGPFSERQIKNFHTLVIERqEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKK---QEE 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1853 INSVIDYVEDIQTKlpplSEDLKGKIEDLSQEIKDRKLAEKVSQAESHAAQ---LNDSSAVLDRIL----DEAKNISFNA 1925
Cdd:TIGR00606 456 LKFVIKELQQLEGS----SDRILELDQELRKAERELSKAEKNSLTETLKKEvksLQNEKADLDRKLrkldQEMEQLNHHT 531
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1926 TAAFKAYSNIKDYIDKAEKIAKEAKVLAHEATELATG-PQgslqegaKGSLQKSFgflneaKKLANDVKENdehlnglts 2004
Cdd:TIGR00606 532 TTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYfPN-------KKQLEDWL------HSKSKEINQT--------- 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2005 rldnanvrnRDLLRALNDTLERLSAIPNDTAAKLQAVKDKARQANDTAKDVLAQiKDLHQNLDGLK----KNYNQLADSV 2080
Cdd:TIGR00606 590 ---------RDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGS-QDEESDLERLKeeieKSSKQRAMLA 659
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2081 AKTNA----VVKDPSKNKIIADADATVKNLEQEADRLIDKLK--------PIKELEDNLKKNISEIKELINQARKQANSI 2148
Cdd:TIGR00606 660 GATAVysqfITQLTDENQSCCPVCQRVFQTEAELQEFISDLQsklrlapdKLKSTESELKKKEKRRDEMLGLAPGRQSII 739
|
....
gi 1814459924 2149 KVSV 2152
Cdd:TIGR00606 740 DLKE 743
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
291-338 |
6.06e-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: 6.06e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1814459924 291 CICYGHA---RACplDPVTnkSRCECEHNTCGDSCDQCCPGFHQKPWRAGT 338
Cdd:cd00055 2 CDCNGHGslsGQC--DPGT--GQCECKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1621-2149 |
6.14e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.69 E-value: 6.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1621 QELKHLLSPQRApERLIQLAEGNLNTLVTEMNELLTRATKVTAdgEQTGQDAERTNTRA----------NSLGEFIKDLA 1690
Cdd:COG4913 275 EYLRAALRLWFA-QRRLELLEAELEELRAELARLEAELERLEA--RLDALREELDELEAqirgnggdrlEQLEREIERLE 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1691 QHAEAVSEKAVKLNE---TLGIQDKAFERNLQELQNEVDKmmtelRRKNLDTQKEVAEDELVAAEALLKKVKKlfgESRG 1767
Cdd:COG4913 352 RELEERERRRARLEAllaALGLPLPASAEEFAALRAEAAA-----LLEALEEELEALEEALAEAEAALRDLRR---ELRE 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1768 KNEEMEkDLREKLADYKSKVHDAWDLLREATdKIKEANL--------LSAENqknmtalEKKKEAIES---GKRqtedtl 1836
Cdd:COG4913 424 LEAEIA-SLERRKSNIPARLLALRDALAEAL-GLDEAELpfvgelieVRPEE-------ERWRGAIERvlgGFA------ 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1837 kegTDILDEANRLADeinsVIDYVEDIQTKL----------------PPLSED-LKGKI--------------------- 1878
Cdd:COG4913 489 ---LTLLVPPEHYAA----ALRWVNRLHLRGrlvyervrtglpdperPRLDPDsLAGKLdfkphpfrawleaelgrrfdy 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1879 ------EDLSQ------------------EIKDRKL-----------AEKVSQAESHAAQLNDSSAVLDRILDEAKNISF 1923
Cdd:COG4913 562 vcvdspEELRRhpraitragqvkgngtrhEKDDRRRirsryvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELD 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1924 NATAAFKAYSNIKDY----IDKAEkIAKEAKVLAHEATELATGPqGSLQEgakgsLQKSfgfLNEAKKLANDVKENDEHL 1999
Cdd:COG4913 642 ALQERREALQRLAEYswdeIDVAS-AEREIAELEAELERLDASS-DDLAA-----LEEQ---LEELEAELEELEEELDEL 711
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2000 NGLTSRLDNANVRNRDLLRALNDTLERLSAIPN-DTAAKLQAVKDKARQANDTAKdvlaQIKDLHQNLDGLKKNYNQLAD 2078
Cdd:COG4913 712 KGEIGRLEKELEQAEEELDELQDRLEAAEDLARlELRALLEERFAAALGDAVERE----LRENLEERIDALRARLNRAEE 787
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2079 SVAKT----NAVVKDPSknkiiADADATVKNLEQ--------EADRLIDKLKPIKELednLKKN-ISEIKELINQARKQA 2145
Cdd:COG4913 788 ELERAmrafNREWPAET-----ADLDADLESLPEylalldrlEEDGLPEYEERFKEL---LNENsIEFVADLLSKLRRAI 859
|
....
gi 1814459924 2146 NSIK 2149
Cdd:COG4913 860 REIK 863
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1616-2014 |
7.41e-07 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 54.96 E-value: 7.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1616 LENMTQELKHL-LSPQRAPERLIQLAEGNLNTLVTEMNELLTR--ATKVTADGEQTGQDAERTNTRANSLGEFIKDLAQH 1692
Cdd:COG5185 189 LKGISELKKAEpSGTVNSIKESETGNLGSESTLLEKAKEIINIeeALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1693 AEAVS-EKAVKLNETLGIQDKAFErNLQELQNEVDK---MMTELRRKNLDTQKEVAEDELVAA-EALLKKVKKLFGESRG 1767
Cdd:COG5185 269 KLGENaESSKRLNENANNLIKQFE-NTKEKIAEYTKsidIKKATESLEEQLAAAEAEQELEESkRETETGIQNLTAEIEQ 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1768 KNEEMEKDLREKLADYKSKVHdawdlLREATDKIKEANLLSAE--------NQKNMTALEKKKEaiesGKRQTEDTLKEg 1839
Cdd:COG5185 348 GQESLTENLEAIKEEIENIVG-----EVELSKSSEELDSFKDTiestkeslDEIPQNQRGYAQE----ILATLEDTLKA- 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1840 tdILDEANRLADEINSVIDYVEDIQTKLPPLSEDLKgKIEDLSQEIKDRKLAEKVSQAESHAAQ-LNDSSAVLDRILDEA 1918
Cdd:COG5185 418 --ADRQIEELQRQIEQATSSNEEVSKLLNELISELN-KVMREADEESQSRLEEAYDEINRSVRSkKEDLNEELTQIESRV 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1919 ----KNISFNATAAFKAYSNIKDYIDKAEKIAKEAKVLAHEATELATGPQGSlqegAKGSLQKSFGFLNEakKLAND-VK 1993
Cdd:COG5185 495 stlkATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALENLIP----ASELIQASNAKTDG--QAANLrTA 568
|
410 420
....*....|....*....|.
gi 1814459924 1994 ENDEhLNGLTSRLDNANVRNR 2014
Cdd:COG5185 569 VIDE-LTQYLSTIESQQARED 588
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1770-2048 |
7.79e-07 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 53.76 E-value: 7.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1770 EEMEKDLREKLADYKSKVHDAWDLLREATDKIKE-ANLLSAENQKnmtaLEKKKEAIESGKRQTEDTLKEGTDILDEANR 1848
Cdd:COG1340 7 SSSLEELEEKIEELREEIEELKEKRDELNEELKElAEKRDELNAQ----VKELREEAQELREKRDELNEKVKELKEERDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1849 LADEINSVIDYVEDIQTKLPPLSEDlKGKIEDLSQEI---------------KDRKLAEKVSQaeshaaqlndssavLDR 1913
Cdd:COG1340 83 LNEKLNELREELDELRKELAELNKA-GGSIDKLRKEIerlewrqqtevlspeEEKELVEKIKE--------------LEK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1914 ILDEAKnisfnatAAFKAYSNIKDYIDKAEKIAKEAKVLAHEATELAtgpqGSLQEgAKGSLQKSFGFLNEAKKLANDVK 1993
Cdd:COG1340 148 ELEKAK-------KALEKNEKLKELRAELKELRKEAEEIHKKIKELA----EEAQE-LHEEMIELYKEADELRKEADELH 215
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1814459924 1994 ENDEHLNGLTSRLDNANVRNRDLLRALNDTLERLSAIPNDTA--AKLQAVKDKARQA 2048
Cdd:COG1340 216 KEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKreKEKEELEEKAEEI 272
|
|
| PLU-1 |
pfam08429 |
PLU-1-like protein; Sequences in this family bear similarity to the central region of PLU-1. ... |
1774-2082 |
1.46e-06 |
|
PLU-1-like protein; Sequences in this family bear similarity to the central region of PLU-1. This is a nuclear protein that may have a role in DNA-binding and transcription, and is closely associated with the malignant phenotype of breast cancer. This region is found in various other Jumonji/ARID domain-containing proteins (see pfam02373, pfam01388).
Pssm-ID: 462475 [Multi-domain] Cd Length: 336 Bit Score: 52.98 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1774 KDLREKLADYKSKVHDAWDLLREATDKIKEANLLSAENQ-----KNMTalEKKKEAIESGKRQTEDTLKEGTDILDEANR 1848
Cdd:pfam08429 19 KELRALLNEAEKIKFPLPELLQDLRAFVQRANKWVEEAQqllsrKQQT--RRKNEAEEDEREREKRTVEELRKLLEEADN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1849 LADEINSVidyvediqtklpplsedlkGKIEDLSQEIKD-RKLAEKVSQAESHaaqlNDSSAVLDRILDEAKNISFNATA 1927
Cdd:pfam08429 97 LPFDCPEI-------------------EQLKELLEEIEEfQKRAREALSEEPP----SLSIEELEELLEEGKSFNVDLPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1928 afkaysnikdyIDKAEKIAKEAKVLAhEATELATGPQGSLQEgakgsLQKsfgFLNEAKKLANdVKENDEHLNGLTSRLD 2007
Cdd:pfam08429 154 -----------LEELEKVLEQLKWLE-EVRETSRKKSLTLED-----VRE---LIEEGVELGI-PPPYEDLMAELQELLT 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2008 NANVRN---RDLLRALNDTLERLSAIPN---------DTAAKLQAVKDKARqandtakDVLAQIKDLHQNLDGLKKN-YN 2074
Cdd:pfam08429 213 AGERWEekaKELLSRERVSLAQLEALSKeaqeipvslPNLAALDEILKKAR-------EWQRQIEALYQRSDFGKRPtLD 285
|
....*...
gi 1814459924 2075 QLADSVAK 2082
Cdd:pfam08429 286 ELEELLAK 293
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1690-2149 |
1.65e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.38 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1690 AQHAEAVSEKAVKLNETLGIQDKAFERNLQElqnEVDKMMTELRRKnlDTQKEVAEDELVAAEALLKKV--KKLFGESRg 1767
Cdd:PTZ00121 1443 AKKADEAKKKAEEAKKAEEAKKKAEEAKKAD---EAKKKAEEAKKA--DEAKKKAEEAKKKADEAKKAAeaKKKADEAK- 1516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1768 KNEEMEKDLREKLADYKSKVhdawDLLREATDKIKEANLLSAENQKNmtALEKKKeaIESGKRQTEDTlkegtdilDEAN 1847
Cdd:PTZ00121 1517 KAEEAKKADEAKKAEEAKKA----DEAKKAEEKKKADELKKAEELKK--AEEKKK--AEEAKKAEEDK--------NMAL 1580
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1848 RLADEINSVIDyvEDIQTKLPPLSEDLKGKIEDLSQEIKDRKLAEKVSQAES---HAAQLNDSSAVLDRILDEAKnisfn 1924
Cdd:PTZ00121 1581 RKAEEAKKAEE--ARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEekkKVEQLKKKEAEEKKKAEELK----- 1653
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1925 ataafKAYSNIKDYIDKAEKIAKEAKVLAHEATElatgpqgslQEGAKGSLQKSFGFLNEAKKLANDVKENDEHlnglts 2004
Cdd:PTZ00121 1654 -----KAEEENKIKAAEEAKKAEEDKKKAEEAKK---------AEEDEKKAAEALKKEAEEAKKAEELKKKEAE------ 1713
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2005 rldnaNVRNRDLLRALNDtlERLSAIPNdtaAKLQAVKDKaRQANDTAKDVLAQIKDLHqnldgLKKNYNQLADSVAK-T 2083
Cdd:PTZ00121 1714 -----EKKKAEELKKAEE--ENKIKAEE---AKKEAEEDK-KKAEEAKKDEEEKKKIAH-----LKKEEEKKAEEIRKeK 1777
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1814459924 2084 NAVVK---DPSKNKIIADADATVKNLEQEADRLIDK-------LKPIKELEDnlkkniSEIKELINQARKQANSIK 2149
Cdd:PTZ00121 1778 EAVIEeelDEEDEKRRMEVDKKIKDIFDNFANIIEGgkegnlvINDSKEMED------SAIKEVADSKNMQLEEAD 1847
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
811-866 |
1.74e-06 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 46.96 E-value: 1.74e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1814459924 811 CACPLNIPSnnfSPTCHLDrnlGLICDeCPVGYTGPHCERCAEGYFGQPSLPGGSC 866
Cdd:pfam00053 1 CDCNPHGSL---SDTCDPE---TGQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
810-867 |
1.93e-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: 46.96 E-value: 1.93e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1814459924 810 PCACPLNIpsnNFSPTCHLDrnlGLICdECPVGYTGPHCERCAEGYFGQPSLPGGsCQ 867
Cdd:cd00055 1 PCDCNGHG---SLSGQCDPG---TGQC-ECKPNTTGRRCDRCAPGYYGLPSQGGG-CQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
472-519 |
2.42e-06 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 46.58 E-value: 2.42e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1814459924 472 PCNCSGAGSTNE--DPCFGPCNCKENVEGGDCSRCKFGFFNLQEDNHrGC 519
Cdd:cd00055 1 PCDCNGHGSLSGqcDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGG-GC 49
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1612-2145 |
2.93e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 53.51 E-value: 2.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1612 ILYGLENMTQELKHLLSPQRA---PERLIQLAEGNLNTLVTEM------NELLTRATKVTADGEQTGQDAERTNTRANSL 1682
Cdd:TIGR00606 459 VIKELQQLEGSSDRILELDQElrkAERELSKAEKNSLTETLKKevkslqNEKADLDRKLRKLDQEMEQLNHHTTTRTQME 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1683 gEFIKDLAQHAEAV----SEKAVKLNETLGI--QDKAFERNLQELQNEVDKMMTELRRKNLDTQK------EVAEDELVA 1750
Cdd:TIGR00606 539 -MLTKDKMDKDEQIrkikSRHSDELTSLLGYfpNKKQLEDWLHSKSKEINQTRDRLAKLNKELASleqnknHINNELESK 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1751 AEALLKKVKKLFGESRGKNEEMEKD-LREKLADY---------KSKVHDAWdlLREATDKI--------------KEANL 1806
Cdd:TIGR00606 618 EEQLSSYEDKLFDVCGSQDEESDLErLKEEIEKSskqramlagATAVYSQF--ITQLTDENqsccpvcqrvfqteAELQE 695
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1807 LSAENQKNMTALEKKKEAIESGKRQTEdtlKEGTDILDEANRLADEINSVIDYVEDIQTKLPPLSEDLKGKIEDLSqeiK 1886
Cdd:TIGR00606 696 FISDLQSKLRLAPDKLKSTESELKKKE---KRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIE---E 769
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1887 DRKLAEKVSQAESHAAQLNDSSAVLDRILDEAKNIS---------FNATAAFKAYSNI-KDYIDKAEKIAK------EAK 1950
Cdd:TIGR00606 770 QETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVErkiaqqaakLQGSDLDRTVQQVnQEKQEKQHELDTvvskieLNR 849
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1951 VLAHEATELATGPQGSLQEGAKGSLQKSFGfLNEAKKLANDVKENDEHLNGLTSRLDNANVRNRDLLRALNDTLERLSAI 2030
Cdd:TIGR00606 850 KLIQDQQEQIQHLKSKTNELKSEKLQIGTN-LQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEEL 928
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2031 PNDTAAKLQAVKDKARQANDTAKDVLAQIKDLHQNL-DGLKKNYNQLADSVAKTNAVVKDPSKN--KIIADADATVKNLE 2107
Cdd:TIGR00606 929 ISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIqDGKDDYLKQKETELNTVNAQLEECEKHqeKINEDMRLMRQDID 1008
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 1814459924 2108 QEADR---LIDKL------KPIKELEDNLKKNISEIKELINQARKQA 2145
Cdd:TIGR00606 1009 TQKIQerwLQDNLtlrkreNELKEVEEELKQHLKEMGQMQVLQMKQE 1055
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1620-1789 |
4.60e-06 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 49.57 E-value: 4.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1620 TQELKHLLSP--QRAPERLIQLAEGNLNTLVTEMNELLTRATKVTADGEQTgqdaertntransLGEFIKDLAQHAEAVS 1697
Cdd:pfam01442 13 AEELQEQLGPvaQELVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAK-------------LGQNVEELRQRLEPYT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1698 EKAVKlnetlgiqdkAFERNLQELQNEVDKMMTELR---RKNLDTQKEVAE---DELVA-----AEALLKKVKKLFGESR 1766
Cdd:pfam01442 80 EELRK----------RLNADAEELQEKLAPYGEELRerlEQNVDALRARLApyaEELRQklaerLEELKESLAPYAEEVQ 149
|
170 180
....*....|....*....|...
gi 1814459924 1767 GKNEEMEKDLREKLADYKSKVHD 1789
Cdd:pfam01442 150 AQLSQRLQELREKLEPQAEDLRE 172
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1789-2152 |
6.73e-06 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 51.88 E-value: 6.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1789 DAWDLLREATDKIKEANLLSAENQkNMTALEKKKEAIESGKRQTEDTLKEGTDILDEANRLADEINSVIDyVE-----DI 1863
Cdd:COG5185 87 KFLKEKKLDTKILQEYVNSLIKLP-NYEWSADILISLLYLYKSEIVALKDELIKVEKLDEIADIEASYGE-VEtgiikDI 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1864 QTKLPPLSEDLKGKIEDLSQEIKDRK--LAEKVSQAESHAAQLNDSSA---VLDRILDEAKNISFNATAAFKAYSNIKDY 1938
Cdd:COG5185 165 FGKLTQELNQNLKKLEIFGLTLGLLKgiSELKKAEPSGTVNSIKESETgnlGSESTLLEKAKEIINIEEALKGFQDPESE 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1939 IDKAEKIAKEAKVLAHEATELATGPQGSLQEGAKGslqksfgfLNEAK-KLANDVKENDEHLNgltsrldnANVRNRDLL 2017
Cdd:COG5185 245 LEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKR--------LNENAnNLIKQFENTKEKIA--------EYTKSIDIK 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2018 RALNDTlerlsaipNDTAAKLQAVKDKARQANDTAKDVLAQIKDLHQNLDGLKKNYNqladsvaKTNAVVKDPSKNKIIA 2097
Cdd:COG5185 309 KATESL--------EEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLE-------AIKEEIENIVGEVELS 373
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1814459924 2098 DADATVKNLEQEADRLIDKL--------KPIKE----LEDNLKKNISEIKELINQARKQANSIKVSV 2152
Cdd:COG5185 374 KSSEELDSFKDTIESTKESLdeipqnqrGYAQEilatLEDTLKAADRQIEELQRQIEQATSSNEEVS 440
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1616-1852 |
6.99e-06 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 50.97 E-value: 6.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1616 LENMTQElKHLLSPQRAPERLiqlaEGNLNTLVTEMNEL-------------LTRA-----TKVTADGeqtgqdaerTNT 1677
Cdd:pfam15905 87 QERGEQD-KRLQALEEELEKV----EAKLNAAVREKTSLsasvaslekqlleLTRVnellkAKFSEDG---------TQK 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1678 RANSLGEFIKDLAQHAEAVSEKAVKLNETLGIQDKAFERNLQELQNEVdkmmTELRRKNLDTQKEVAEdELVAAEALLKK 1757
Cdd:pfam15905 153 KMSSLSMELMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKV----AQLEEKLVSTEKEKIE-EKSETEKLLEY 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1758 VKKLFGESrgknEEMEKdlrekladYKSKVHDAWDLLREATD-------KIKEANLLSAENQKNMTA----LEKKKEAIE 1826
Cdd:pfam15905 228 ITELSCVS----EQVEK--------YKLDIAQLEELLKEKNDeieslkqSLEEKEQELSKQIKDLNEkcklLESEKEELL 295
|
250 260
....*....|....*....|....*.
gi 1814459924 1827 SGKRQTEDTLKEGTDILDEANRLADE 1852
Cdd:pfam15905 296 REYEEKEQTLNAELEELKEKLTLEEQ 321
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1637-1952 |
7.47e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.06 E-value: 7.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1637 IQLAEGNLNTLVTEMNELLTRATKVTADGEQTGQDAERTNTRANSLGEFIKDLAQHAEAVSEKAVKLNETlgiqdkafer 1716
Cdd:COG4372 47 LEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEE---------- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1717 nLQELQNEVDKMmtELRRKNLDTQKEVAEDELVAAEALLKKVKklfgesrgknEEMEKdLREKLADYKSKVhdAWDLLRE 1796
Cdd:COG4372 117 -LEELQKERQDL--EQQRKQLEAQIAELQSEIAEREEELKELE----------EQLES-LQEELAALEQEL--QALSEAE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1797 ATDKIKEANLLSAENQKNMTALEKKKEAIESGKRQTEDTLKEGTDILDEANRLADEINSVIDYVEDIQTKLPPLSED--- 1873
Cdd:COG4372 181 AEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILkei 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1874 ------LKGKIEDLSQEIKDRKLAEKVSQAESHAAQLNDSSAVLDRILDEAKNISFNATAAFKAYSNIKDYIDKAEKIAK 1947
Cdd:COG4372 261 eelelaILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELA 340
|
....*
gi 1814459924 1948 EAKVL 1952
Cdd:COG4372 341 DLLQL 345
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1694-2181 |
7.66e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 51.90 E-value: 7.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1694 EAVSEKAVK-LNETLGIQDKAFerNLQELQNEVDK--MMTELRRKNLDTqkevaedelVAAEALLKKVKklfgesrgknE 1770
Cdd:pfam02463 114 KNVTKKEVAeLLESQGISPEAY--NFLVQGGKIEIiaMMKPERRLEIEE---------EAAGSRLKRKK----------K 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1771 EMEKDLREKLADykskvhdawdllreatDKIKEANLLSAENQKNMTALEKKKEAIESGKRQTEDTLKEGTDILDEANRLA 1850
Cdd:pfam02463 173 EALKKLIEETEN----------------LAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNE 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1851 DEINSVIDYVEDIQTKLPPLSEDLKGKIEDLSQEIKDRKLAEKVSQ-AESHAAQLNDSSAVLDRILDEAKNisfnataaf 1929
Cdd:pfam02463 237 ERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKlQEEELKLLAKEEEELKSELLKLER--------- 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1930 kaysNIKDYIDKAEKIakEAKVLAHEATELATGPQGSLQEGAKGSLQKSFGFLNEAKKlanDVKENDEHLNGLTSRLDNA 2009
Cdd:pfam02463 308 ----RKVDDEEKLKES--EKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEE---ELEKLQEKLEQLEEELLAK 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2010 NVRNRDLLRALNDTLERLSAIPNDTAAKLQAVKDKARQANDTAKDvLAQIKDLHQNLDGLKKNYNQLADSVAKTNAVVKD 2089
Cdd:pfam02463 379 KKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKE-EKKEELEILEEEEESIELKQGKLTEEKEELEKQE 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2090 PSKNKiiadadatvknLEQEADRLIDKLKPIKELEDNLKKN--ISEIK-ELINQARKQANS---IKVSVSSGGDCIRTYK 2163
Cdd:pfam02463 458 LKLLK-----------DELELKKSEDLLKETQLVKLQEQLEllLSRQKlEERSQKESKARSglkVLLALIKDGVGGRIIS 526
|
490
....*....|....*...
gi 1814459924 2164 PEIKKGSYNSIIVNVKTA 2181
Cdd:pfam02463 527 AHGRLGDLGVAVENYKVA 544
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1424-1470 |
7.76e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 44.99 E-value: 7.76e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1424 CQCH--GHSSL-CDPETSICQnCQHHTAGDFCERCVLGYYGIVkglPDDC 1470
Cdd:smart00180 1 CDCDpgGSASGtCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDG---PPGC 46
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1617-1837 |
9.60e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 51.59 E-value: 9.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1617 ENMTQELKHLLSPQRAPERLIQLAEGNLNTLVTEMNELLTRATKVTADGEQTGQDAERTNTRANSLGEFIKDLAQHAEAV 1696
Cdd:TIGR00606 832 QEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQD 911
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1697 S------EKAVKLNETL----GIQDKAFERNLQELQNEVDKMMteLRRKNLDTQ-KEVAEDELVAAEALLKKVKKLFGES 1765
Cdd:TIGR00606 912 SpletflEKDQQEKEELisskETSNKKAQDKVNDIKEKVKNIH--GYMKDIENKiQDGKDDYLKQKETELNTVNAQLEEC 989
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1814459924 1766 RGKNEEMEKDLREKLADYKS-KVHDAW---DL-LREATDKIKEANLLSAENQKNMTALEKKKEAIESGKRQTE-DTLK 1837
Cdd:TIGR00606 990 EKHQEKINEDMRLMRQDIDTqKIQERWlqdNLtLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENiDLIK 1067
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
811-859 |
1.04e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 44.99 E-value: 1.04e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1814459924 811 CACPlniPSNNFSPTCHLDrnlGLICdECPVGYTGPHCERCAEGYFGQP 859
Cdd:smart00180 1 CDCD---PGGSASGTCDPD---TGQC-ECKPNVTGRRCDRCAPGYYGDG 42
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1684-2189 |
1.11e-05 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 51.76 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1684 EFIKDLAQHAEAVSEKAVKLNETLGIQDKAFERNLQEL---QNEVDKMMTELRR-KNLDTQKEVAEDElvaaeallkkvk 1759
Cdd:PTZ00440 125 EMIHYATSYYDDLKKYSDKINEDVEPLNEEIIKNIEQClgnKNDLDNLIIVLENpEKYNVRKTLYDEK------------ 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1760 klFGESRGKNEEMEKDLREKLADYKSKVHDAWDLLREATDKIKEANLLSAENQKNM------------------TALEKK 1821
Cdd:PTZ00440 193 --FNEYKNKKEAFYNCLKNKKEDYDKKIKKINNEIRKLLKNIKCTGNMCKTDTYVDmvelyllrvnevpsnnydNYLNRA 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1822 KEAIESG-------KRQTEDTL---------KEGTDILDEANRLADEINSVIDYVEDIQT--KLPPLSED-LKGKIEDLS 1882
Cdd:PTZ00440 271 KELLESGsdlinkiKKELGDNKtiysinfiqEEIGDIIKRYNFHLKKIEKGKEYIKRIQNnnIPPQVKKDeLKKKYFESA 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1883 QEIKDRKL----AEKVSQAESHAAQL---------NDSSAVLDRILDEAKNISfnataafkAYSNIkdyIDKAEKIAKEA 1949
Cdd:PTZ00440 351 KHYASFKFslemLSMLDSLLIKKEKIlnnlfnklfGDLKEKIETLLDSEYFIS--------KYTNI---ISLSEHTLKAA 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1950 KVLAHEATEL----ATGPQGSLQEGAKGSLQKSF---GFLNEAKKLANDVKEndehlnglTSRLDNANVRNRDLLR---- 2018
Cdd:PTZ00440 420 EDVLKENSQKiadyALYSNLEIIEIKKKYDEKINelkKSINQLKTLISIMKS--------FYDLIISEKDSMDSKEkkes 491
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2019 ALNDTLERLSAIPNdtaaKLQAVKDKARQANDTAK---DVLAQIKDLHQNLDGLKKNYNQLADSVakTNAVVKDPSKNKI 2095
Cdd:PTZ00440 492 SDSNYQEKVDELLQ----IINSIKEKNNIVNNNFKnieDYYITIEGLKNEIEGLIELIKYYLQSI--ETLIKDEKLKRSM 565
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2096 IADADATVKNLEQEadrlIDKLKPIKELEDNLKKNISEIKELINQARKQANSIKVSVSSGGDCIRTYKPEIKKGSYNSII 2175
Cdd:PTZ00440 566 KNDIKNKIKYIEEN----VDHIKDIISLNDEIDNIIQQIEELINEALFNKEKFINEKNDLQEKVKYILNKFYKGDLQELL 641
|
570
....*....|....
gi 1814459924 2176 VNVKTAVADNLLFY 2189
Cdd:PTZ00440 642 DELSHFLDDHKYLY 655
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1982-2168 |
1.13e-05 |
|
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: 51.17 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1982 LNEAKKLANDVKENDEHLNGLTSRL-DNANVRNrdllrALNDTLERLSAIPNDTAAKLQAVKDKARQANDTAKDVLAQIK 2060
Cdd:TIGR04523 39 EKKLKTIKNELKNKEKELKNLDKNLnKDEEKIN-----NSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2061 DLHQNLDGLKKNYNQLADSVAKTnavvkdpskNKIIADADATVKNLEQEADRLIDKL----KPIKELEDN---LKKNISE 2133
Cdd:TIGR04523 114 NDKEQKNKLEVELNKLEKQKKEN---------KKNIDKFLTEIKKKEKELEKLNNKYndlkKQKEELENElnlLEKEKLN 184
|
170 180 190
....*....|....*....|....*....|....*
gi 1814459924 2134 IKELINQARKQANSIKVSVSSggdcIRTYKPEIKK 2168
Cdd:TIGR04523 185 IQKNIDKIKNKLLKLELLLSN----LKKKIQKNKS 215
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1692-1974 |
1.14e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.60 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1692 HAEA-VSEKAVKLNETLGIQDKAfERNLQELQNEVDKMMTELRRknLDTQKEVAEDELVAAEALLKKVKKlfgESRGKNE 1770
Cdd:COG3883 13 FADPqIQAKQKELSELQAELEAA-QAELDALQAELEELNEEYNE--LQAELEALQAEIDKLQAEIAEAEA---EIEERRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1771 EMEKDLReklADYKS-KVHDAWDLLREATDKikeANLLSaenqkNMTALEKkkeaiesgkrqtedtlkegtdILDEANRL 1849
Cdd:COG3883 87 ELGERAR---ALYRSgGSVSYLDVLLGSESF---SDFLD-----RLSALSK---------------------IADADADL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1850 ADEINSVIDYVEDIQTKLpplsEDLKGKIEDLSQEIKDRK--LAEKVSQAESHAAQLNDSSAVLDRILDEAKNISFNATA 1927
Cdd:COG3883 135 LEELKADKAELEAKKAEL----EAKLAELEALKAELEAAKaeLEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1814459924 1928 AFKAYSNIKDYIDKAEKIAKEAKVLAHEATELATGPQGSLQEGAKGS 1974
Cdd:COG3883 211 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGA 257
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1608-1814 |
1.56e-05 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 49.68 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1608 APYKILYGLENMTQELKHLLSPQRAP--ERLIQLAEGNLNTLVTEMNELLTRATKVtadgeqtgqdaertntrANSLGEF 1685
Cdd:cd22656 85 AGGTIDSYYAEILELIDDLADATDDEelEEAKKTIKALLDDLLKEAKKYQDKAAKV-----------------VDKLTDF 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1686 IKDLAQHAEAVSEKAVKLNETLGIQDKAFER-NLQELQNEVDKMMTELRRKNLDTQKEVaEDELVAAEALLKKVKKLFGE 1764
Cdd:cd22656 148 ENQTEKDQTALETLEKALKDLLTDEGGAIARkEIKDLQKELEKLNEEYAAKLKAKIDEL-KALIADDEAKLAAALRLIAD 226
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1814459924 1765 SRGKNEEMeKDLREKLADYKS---KVHDAWDLLREATDKIKeaNLLSAENQKN 1814
Cdd:cd22656 227 LTAADTDL-DNLLALIGPAIPaleKLQGAWQAIATDLDSLK--DLLEDDISKI 276
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1712-1892 |
1.94e-05 |
|
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: 48.77 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1712 KAFERNLQELQNEVDKMMTELRRKnldtqkevaEDELVAAEALLKKVKKLFGESRgKNEEMEkDLREKLADYKSKvhdaw 1791
Cdd:COG1579 41 AALEARLEAAKTELEDLEKEIKRL---------ELEIEEVEARIKKYEEQLGNVR-NNKEYE-ALQKEIESLKRR----- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1792 dlLREATDKIKEAnllsaenqknMTALEKKKEAIEsgkrQTEDTLKEGTDILDEANRLADEInsvidyVEDIQTKLppls 1871
Cdd:COG1579 105 --ISDLEDEILEL----------MERIEELEEELA----ELEAELAELEAELEEKKAELDEE------LAELEAEL---- 158
|
170 180
....*....|....*....|.
gi 1814459924 1872 EDLKGKIEDLSQEIKDRKLAE 1892
Cdd:COG1579 159 EELEAEREELAAKIPPELLAL 179
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1933-2150 |
2.29e-05 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 49.29 E-value: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1933 SNIKDYIDKAE-KIAKEAKVLAHEATELATGPQGSLQEGAKGSLQK-SFGFLNEAKKLANDVKENDEHLNGLTSRLDNAN 2010
Cdd:cd22656 76 GDIYNYAQNAGgTIDSYYAEILELIDDLADATDDEELEEAKKTIKAlLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQ 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2011 VRNRDLLRALNDTLER-LSAIPNDTAAKLQAVKDKARQAndtakdvlaQIKDLHQNLDGLKKNYNQLADSVAKTNAVVKD 2089
Cdd:cd22656 156 TALETLEKALKDLLTDeGGAIARKEIKDLQKELEKLNEE---------YAAKLKAKIDELKALIADDEAKLAAALRLIAD 226
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1814459924 2090 psknkiIADADATVKNLEQEADRLIDKLKPIKELEDNLKKNISEIKELINQARKQANSIKV 2150
Cdd:cd22656 227 ------LTAADTDLDNLLALIGPAIPALEKLQGAWQAIATDLDSLKDLLEDDISKIPAAIL 281
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1984-2149 |
2.59e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.44 E-value: 2.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1984 EAKKLANDVKENDEHLNGLTSRLDNANVRNRDLLRALNDTLERLSAIpNDTAAKLQAVKDKARQANDTAKDVLAQ-IKDL 2062
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEAL-QAEIDKLQAEIAEAEAEIEERREELGErARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2063 HQNLDGLK--------KNYNQLADSVAKTNAVVKdpSKNKIIADADATVKNLEQEADRLIDKLKPIKELEDNLKKNISEI 2134
Cdd:COG3883 96 YRSGGSVSyldvllgsESFSDFLDRLSALSKIAD--ADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170
....*....|....*
gi 1814459924 2135 KELINQARKQANSIK 2149
Cdd:COG3883 174 EAQQAEQEALLAQLS 188
|
|
| alph_xenorhab_A |
NF033928 |
alpha-xenorhabdolysin family binary toxin subunit A; Alpha-xenorhabdolysin was the founding ... |
1908-2149 |
2.69e-05 |
|
alpha-xenorhabdolysin family binary toxin subunit A; Alpha-xenorhabdolysin was the founding member of a family of alpha-helical pore-forming binary toxins. YaxAB from Yersinia enterocolitica has been studied structurally. This HMM represents subunit A proteins such as XaxA and YaxA, capable of binding to the membrane even in the absence of the B subunit. This family is related to the Bacillus haemolytic enterotoxin family (see PF05791.9), although thresholds for this HMM are set to exclude that family.
Pssm-ID: 468250 [Multi-domain] Cd Length: 340 Bit Score: 49.22 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1908 SAVLDRILDEAKNISfNATAAFKAYSN-IKDYIDKAeKIAKEAKVLAHEATELATGPQGSLQEGAKGSLQKsfgFLneaK 1986
Cdd:NF033928 62 SNLEPKIKQLANDLA-NYARNIVVTGNpIIDLINEM-PIIKRGDLTEEELSELPPIPLSSDDKEIVKELKE---IL---E 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1987 KLANDVKENDEHLNGLTSRLDnanvrnrDLLRALNDTLerlsaipndtAAKLQAVKDKAR--QANDTAKDVLAQIKDLHQ 2064
Cdd:NF033928 134 DLKNDIKDYQQKADDVKKELD-------DFENDLREEL----------LPQLKLKKKLYDdnLGSDSIEELREKIDQLEK 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2065 NLDGLKKNYNQLADSVAKT----NAVVkdpsknkII---------ADADATVKNLEQEADRLIDKLK---PIKELEDNLK 2128
Cdd:NF033928 197 EIEQLNKEYDDYVKLSFTGlaggPIGL-------AItggifgskaEKIRKEKNALIQEIDELQEQLKkknALLGSLERLQ 269
|
250 260
....*....|....*....|.
gi 1814459924 2129 KNISEIKELINQARKQANSIK 2149
Cdd:NF033928 270 TSLDDILTRMEDALPALKKLK 290
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
1642-2145 |
2.73e-05 |
|
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];
Pssm-ID: 444083 [Multi-domain] Cd Length: 1028 Bit Score: 50.01 E-value: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1642 GNLNTLVTEMNELLTRATKVTADGEQTGQDAERTNTRANSLGEFIKDLAQHAEAVSEKAVKLNETLGIQDKAFER----- 1716
Cdd:COG5271 276 DDADGLEAAEDDALDAELTAAQAADPESDDDADDSTLAALEGAAEDTEIATADELAAADDEDDDDSAAEDAAEEAataed 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1717 -NLQELQNEVDKMMTELRRKNLDTQKEVAEDELVAAEALLKKVKKLFGESRGK------NEEMEKDLREKLADYKSkvhd 1789
Cdd:COG5271 356 sAAEDTQDAEDEAAGEAADESEGADTDAAADEADAAADDSADDEEASADGGTSptsdtdEEEEEADEDASAGETED---- 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1790 awdllrEATDKIKEANLLSAENQKNMTALEKKKEAIESGKRQTEDTLKEGTDildeanrlADEINSVIDYVEDIQTKLPP 1869
Cdd:COG5271 432 ------ESTDVTSAEDDIATDEEADSLADEEEEAEAELDTEEDTESAEEDAD--------GDEATDEDDASDDGDEEEAE 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1870 LSEDLKGKIEDLSQEIKDRKLAEKVSQAESHAAQLNDSSAvlDRILDEAKNISFNATAafkaySNIKDYIDKAEKIAKEA 1949
Cdd:COG5271 498 EDAEAEADSDELTAEETSADDGADTDAAADPEDSDEDALE--DETEGEENAPGSDQDA-----DETDEPEATAEEDEPDE 570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1950 KVLahEATELATGPQGSLQEGAKGSLQKSFGFLNEAKKLANDVKE-NDEHLNGLTSRLDNANVRNRDLLRALNDTLERLS 2028
Cdd:COG5271 571 AEA--ETEDATENADADETEESADESEEAEASEDEAAEEEEADDDeADADADGAADEEETEEEAAEDEAAEPETDASEAA 648
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2029 AIPNDTAAKLQAVKDKARQANDTAKDVLAQIKDlhQNLDGLKKNYN------QLADSVAKTNAVVKDPSKNKIIAD---- 2098
Cdd:COG5271 649 DEDADAETEAEASADESEEEAEDESETSSEDAE--EDADAAAAEASddeeetEEADEDAETASEEADAEEADTEADgtae 726
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1814459924 2099 -----------ADATVKNLEQEADRLIDKLKPIKELEDNLKKNISEIKELINQARKQA 2145
Cdd:COG5271 727 eaeeaaeeaesADEEAASLPDEADAEEEAEEAEEAEEDDADGLEEALEEEKADAEEAA 784
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
1690-1780 |
3.02e-05 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 45.68 E-value: 3.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1690 AQHA-EAVSEKAVKLNETLGIQDKAFERnLQELQNEVDKMMTELRRKNLDTQKEVA--EDELVAAEAllkKVKKLFGESR 1766
Cdd:pfam20492 25 AQEElEESEETAEELEEERRQAEEEAER-LEQKRQEAEEEKERLEESAEMEAEEKEqlEAELAEAQE---EIARLEEEVE 100
|
90
....*....|....
gi 1814459924 1767 GKNEEMEKdLREKL 1780
Cdd:pfam20492 101 RKEEEARR-LQEEL 113
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1616-1907 |
3.67e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.13 E-value: 3.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1616 LENMTQELKHLLSPQRAPERLIQLAEGNLNTLVTEMNELLtratkvtadgeqtgqdAERtntranslgefiKDLAQHAEA 1695
Cdd:COG4372 82 LEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQ----------------KER------------QDLEQQRKQ 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1696 VSEKAVKLNETLGIQD---KAFERNLQELQNEVDKMMTELRRKNLD-TQKEVAEDELVAAEALLKKVKKLFGESRGKNEE 1771
Cdd:COG4372 134 LEAQIAELQSEIAEREeelKELEEQLESLQEELAALEQELQALSEAeAEQALDELLKEANRNAEKEEELAEAEKLIESLP 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1772 MEKDLREKLADYKSKVHDAWDLLREATDKIKEANLLSAENQKNMTALEKKKEAIESGKRQTEDTLKEGTDILDEANRLAD 1851
Cdd:COG4372 214 RELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAAL 293
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1814459924 1852 EINSVIDYVEDIQTKLPPLSEDLKGKIEDLSQEIKDRKLAEKVSQAESHAAQLNDS 1907
Cdd:COG4372 294 ELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVG 349
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1630-1919 |
3.85e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 49.84 E-value: 3.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1630 QRAPERLIQLAEGNLNTLVTEMNELLTRATKVTAdgEQTGQDAERTNTRANSLGEFIKDLAQHAEAVSEKAVKLNETLGI 1709
Cdd:pfam12128 670 NKALAERKDSANERLNSLEAQLKQLDKKHQAWLE--EQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKA 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1710 QDKAFErnlQELQNEVDKM-MTELRRKNLDTQKEVAEDELVAAEALLKKVKKLFGESRGKNEEMEKDLREKLADYKSKVH 1788
Cdd:pfam12128 748 ELKALE---TWYKRDLASLgVDPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAIS 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1789 DawdLLREATDKIKEANLLSAENQKNMTALEKKKEAIESGKRQTED------TLKEGTDildeANRLADEINSVIDYVED 1862
Cdd:pfam12128 825 E---LQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCemsklaTLKEDAN----SEQAQGSIGERLAQLED 897
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1814459924 1863 IQTKLPPLSEDLKGKIEDLSQEIKDRKLAEKVSQAESHAAQLNDSSAVLDRILDEAK 1919
Cdd:pfam12128 898 LKLKRDYLSESVKKYVEHFKNVIADHSGSGLAETWESLREEDHYQNDKGIRLLDYRK 954
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1735-1917 |
4.03e-05 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 47.72 E-value: 4.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1735 KNLDTQKEVAEDELVAAEALLKKVKKLFGESrgkneEME-KDLREKLADYKSKVHDAWDLLREATDKIKEANLLSAENQK 1813
Cdd:pfam00261 4 QQIKEELDEAEERLKEAMKKLEEAEKRAEKA-----EAEvAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESER 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1814 NMTALEKKKEAIESGKRQTEDTLKEGTDILDEANR-----------LADEINSVIDYVEDIQTKLPPLSEDLKGKIEDL- 1881
Cdd:pfam00261 79 GRKVLENRALKDEEKMEILEAQLKEAKEIAEEADRkyeevarklvvVEGDLERAEERAELAESKIVELEEELKVVGNNLk 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1882 SQEIKDRK--------------LAEKVSQAESHAAQLNDSSAVLDRILDE 1917
Cdd:pfam00261 159 SLEASEEKaseredkyeeqirfLTEKLKEAETRAEFAERSVQKLEKEVDR 208
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
473-519 |
4.12e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 43.07 E-value: 4.12e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1814459924 473 CNCSGAGSTNE--DPCFGPCNCKENVEGGDCSRCKFGFFNlqeDNHRGC 519
Cdd:smart00180 1 CDCDPGGSASGtcDPDTGQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
1948-2149 |
4.67e-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: 48.54 E-value: 4.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1948 EAKVLAHEATELATGPQGSLQEGAK-----GSLQKSfgfLNEAKKLANDVKEN-DEHLNGLTSRLDNANVRNRDLLRALN 2021
Cdd:pfam04108 4 SAQDLCRWANELLTDARSLLEELVVllakiAFLRRG---LSVQLANLEKVREGlEKVLNELKKDFKQLLKDLDAALERLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2022 DTLERLSAIPNDTAAKLQAVK----------DKARQANDTAKDVLAQIKDLHQNLDG-LKKNYNQLADSVAKTNAVVKDP 2090
Cdd:pfam04108 81 ETLDKLRNTPVEPALPPGEEKqktlldfideDSVEILRDALKELIDELQAAQESLDSdLKRFDDDLRDLQKELESLSSPS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2091 SKNKIIADADATVKNLEQEADRLIDKL--------------------------KPIKELED---NLKKNISEIKELINQA 2141
Cdd:pfam04108 161 ESISLIPTLLKELESLEEEMASLLESLtnhydqcvtavklteggraemlevleNDARELDDvvpELQDRLDEMENNYERL 240
|
....*...
gi 1814459924 2142 RKQANSIK 2149
Cdd:pfam04108 241 QKLLEQKN 248
|
|
| GvpP |
COG4980 |
Gas vesicle protein YhaH [General function prediction only]; |
1826-1908 |
4.90e-05 |
|
Gas vesicle protein YhaH [General function prediction only];
Pssm-ID: 444004 [Multi-domain] Cd Length: 106 Bit Score: 44.96 E-value: 4.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1826 ESGKRQTEDTLKEGTDILDEANRLADEI-NSVIDYVEDIQTKLPPLSEDLKGKIEDLSQEIKdrklaEKVSQAESHAAQL 1904
Cdd:COG4980 27 KSGKETRKKLKDKADDLKDKAEDLKDELkEKASELSEEAKEKLDELIEEIKEKIEELKEEVE-----PKIEELKEEAEKL 101
|
....
gi 1814459924 1905 NDSS 1908
Cdd:COG4980 102 QKEV 105
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1631-2040 |
5.39e-05 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 49.05 E-value: 5.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1631 RAPERLIQLAEGNLNTLVTEMNELLT----RATKVTADGEQTGQdaERTNTRANSLGEFIKDLAQHAEAVSEKAvklnet 1706
Cdd:NF041483 261 RAAEQRMQEAEEALREARAEAEKVVAeakeAAAKQLASAESANE--QRTRTAKEEIARLVGEATKEAEALKAEA------ 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1707 lgiqdkafERNLQELQNEVDKMMTELRRKNL-----DTQKEVAEDELVAAEALLKKVKKLFGESRGKNEEMEKDLREKLA 1781
Cdd:NF041483 333 --------EQALADARAEAEKLVAEAAEKARtvaaeDTAAQLAKAARTAEEVLTKASEDAKATTRAAAEEAERIRREAEA 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1782 D---YKSKVHDAWDLLR-EATDKIKEANLLSAENQKNMTAL-----EKKKEAIESGKRQTEDTLKEGTDILDEANRLADE 1852
Cdd:NF041483 405 EadrLRGEAADQAEQLKgAAKDDTKEYRAKTVELQEEARRLrgeaeQLRAEAVAEGERIRGEARREAVQQIEEAARTAEE 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1853 I-----------------------NSVIDYVEDIQTKLPPLSEDLKGKIEDLSQEIKDRklAEKV-SQAESHAAQLNDSS 1908
Cdd:NF041483 485 LltkakadadelrstataeservrTEAIERATTLRRQAEETLERTRAEAERLRAEAEEQ--AEEVrAAAERAARELREET 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1909 --AVLDRILDEAKNISFNATAAFK----AYSNIKDYIDKAEKI----AKEAKVLAHEATELATgpqgSLQEGAKgslqks 1978
Cdd:NF041483 563 erAIAARQAEAAEELTRLHTEAEErltaAEEALADARAEAERIrreaAEETERLRTEAAERIR----TLQAQAE------ 632
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1814459924 1979 fgflNEAKKLANDVKENDEHlngltSRLDNANVRNRDLLRALNDTlERLSAIPNDTAAKLQA 2040
Cdd:NF041483 633 ----QEAERLRTEAAADASA-----ARAEGENVAVRLRSEAAAEA-ERLKSEAQESADRVRA 684
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1718-1889 |
6.15e-05 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 47.06 E-value: 6.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1718 LQELQNEVDKMMTELRRKNLDTQKEVAEDELVAAEALLKKVKKLFGESRGKNEEME------------------------ 1773
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEalnelgeqlieeghpdaeeiqerl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1774 -------KDLREKLADYKSKVHDAWDLLREATD--------KIKEANLLSAENQKNMTALEKKKEAIEsgkrQTEDTLKE 1838
Cdd:cd00176 82 eelnqrwEELRELAEERRQRLEEALDLQQFFRDaddleqwlEEKEAALASEDLGKDLESVEELLKKHK----ELEEELEA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1814459924 1839 GTDILDEANRLADE-INSVIDYVED-IQTKLpplsEDLKGKIEDLSQEIKDRK 1889
Cdd:cd00176 158 HEPRLKSLNELAEElLEEGHPDADEeIEEKL----EELNERWEELLELAEERQ 206
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1740-1918 |
8.26e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 47.97 E-value: 8.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1740 QKEVAEdELVAAEALLKKVKKLFGESRGKNEEME---KDLREKLADYKSKVHDAWDLLREATDKIKEANLLSAENQKNMT 1816
Cdd:pfam07888 40 LQERAE-LLQAQEAANRQREKEKERYKRDREQWErqrRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1817 ALEKKKEAIESGKRQTEDTLK----EGTDILDEANRLADEINSVIDYVEDIQTKlpplSEDLKGKIEDLSQEIKD----- 1887
Cdd:pfam07888 119 ALLAQRAAHEARIRELEEDIKtltqRVLERETELERMKERAKKAGAQRKEEEAE----RKQLQAKLQQTEEELRSlskef 194
|
170 180 190
....*....|....*....|....*....|.
gi 1814459924 1888 RKLAEKVSQAESHAAQLNDSSAVLDRILDEA 1918
Cdd:pfam07888 195 QELRNSLAQRDTQVLQLQDTITTLTQKLTTA 225
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1693-2148 |
9.19e-05 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 48.11 E-value: 9.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1693 AEAVSEKAVKLNEtlgiQDKAFERNLQELQNEVDKMMTELRRKNLDTQKEVAEdELVAAEALLKKVKKlfgESRGKNEEM 1772
Cdd:COG3064 29 AEAEQKAKEEAEE----ERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAK-KLAEAEKAAAEAEK---KAAAEKAKA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1773 EKDLrEKLADYKSKVHDAWdllREATDKIKEAnllsAENQKNMTALEKKKEAIESGKRQTEDTLKEGTDILDEANRLADE 1852
Cdd:COG3064 101 AKEA-EAAAAAEKAAAAAE---KEKAEEAKRK----AEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1853 INSVIDYVEDIQTKLP-PLSEDLKGKIEDLSQEIKDRKLAEKVSQAESHAAQLNDSSAVLDRILDEAKNISFNATAAFKA 1931
Cdd:COG3064 173 RAAAGAAAALVAAAAAaVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1932 YSNIKDYIDKAEKIAKEAKVLAHEATELATGPQGSLQEGAKGSLQKSFGFLNEAKKLANDVKENDEHLNGLTSRLDNANV 2011
Cdd:COG3064 253 DLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2012 RNRDLLRALNDTLERLSAIPNDTAAKLQAVKDKARQANDTAKDVLAQIKDLHQNLDGLKKNYNQLADSVAkTNAVVKDPS 2091
Cdd:COG3064 333 GAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLG-LRLDLGAAL 411
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1814459924 2092 KNKIIADADATVKNLEQEADRLIDKLKPIKELEDNLKKNISEIKELINQARKQANSI 2148
Cdd:COG3064 412 LEAASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALTGDADALLGILKA 468
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1616-1919 |
9.46e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 9.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1616 LENMTQELKHLLSPQRAPERLIQLaEGNLNTLVTEMNELLTRATKVT---ADGEQTGQDAERTNTRANSLGEF------- 1685
Cdd:COG4717 114 LREELEKLEKLLQLLPLYQELEAL-EAELAELPERLEELEERLEELReleEELEELEAELAELQEELEELLEQlslatee 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1686 -IKDLAQHAEAVSEKAVKLNETLgiqdKAFERNLQELQNEVDKMMTELRRKNLDTQKEVAEDELVAAEALL--------- 1755
Cdd:COG4717 193 eLQDLAEELEELQQRLAELEEEL----EEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLallglggsl 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1756 ------------------------------------KKVKKLFGESRGKNEEMEKDLR----------EKLADYKSKVHD 1789
Cdd:COG4717 269 lsliltiagvlflvlgllallflllarekaslgkeaEELQALPALEELEEEELEELLAalglppdlspEELLELLDRIEE 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1790 AWDLLREATDKIKEANLLSAENQKN--------------------MTALEKKKEAIESGKRQTEDTLKEGTDILDEAN-- 1847
Cdd:COG4717 349 LQELLREAEELEEELQLEELEQEIAallaeagvedeeelraaleqAEEYQELKEELEELEEQLEELLGELEELLEALDee 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1848 RLADEINSVIDYVEDIQTKLpplsEDLKGKIEDLSQEIK----DRKLAEKVSQAESHAAQLND------SSAVLDRILDE 1917
Cdd:COG4717 429 ELEEELEELEEELEELEEEL----EELREELAELEAELEqleeDGELAELLQELEELKAELRElaeewaALKLALELLEE 504
|
..
gi 1814459924 1918 AK 1919
Cdd:COG4717 505 AR 506
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1693-1918 |
1.05e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 48.25 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1693 AEAVSEKAVKLNETLGIQDK--AFERNLQELQNEVDKMMTELRRKNLdtQKEVAEDELVAAEALLKKVKKlfgeSRGKNE 1770
Cdd:pfam01576 871 ASGASGKSALQDEKRRLEARiaQLEEELEEEQSNTELLNDRLRKSTL--QVEQLTTELAAERSTSQKSES----ARQQLE 944
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1771 EMEKDLREKLADYKSKVHDAWDLLREATdkikEANLLSAENQKNMTAlekkKEAIESGK--RQTEDTLKEGTDILDEANR 1848
Cdd:pfam01576 945 RQNKELKAKLQEMEGTVKSKFKSSIAAL----EAKIAQLEEQLEQES----RERQAANKlvRRTEKKLKEVLLQVEDERR 1016
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1849 LADEINsviDYVEDIQTKLpplsedlkgkiedlsqeikdRKLAEKVSQAESHAAQLNDSSAVLDRILDEA 1918
Cdd:pfam01576 1017 HADQYK---DQAEKGNSRM--------------------KQLKRQLEEAEEEASRANAARRKLQRELDDA 1063
|
|
| YkaA |
COG1392 |
Phosphate transport regulator YkaA, distantly related to PhoU, UPF0111/DUF47 family [Inorganic ... |
1773-1956 |
1.35e-04 |
|
Phosphate transport regulator YkaA, distantly related to PhoU, UPF0111/DUF47 family [Inorganic ion transport and metabolism];
Pssm-ID: 441002 [Multi-domain] Cd Length: 205 Bit Score: 45.63 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1773 EKDLREKLADYKSKVHDAWDLLREATDKIKEAnllsAENQKNMTALEKKKEAIesgKRQTEDTLKEG-------TDILde 1845
Cdd:COG1392 5 EKSFFDLLEEHAEKVVEAAELLVELLEDYEDV----EELAEEIKELEHEADEI---KREIREELNKTfitpfdrEDIL-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1846 anRLADEINSVIDYVEDIQTKLpplseDLKgKIEDLSQEIkdRKLAEKVSQAeshAAQLNDSSAVLDRILDEAKnisfna 1925
Cdd:COG1392 76 --ELASALDDIADYIEDIAGRL-----VLY-KIEELDEEL--LELAELLVEA---AEELVEAVKELRELLKKAE------ 136
|
170 180 190
....*....|....*....|....*....|.
gi 1814459924 1926 taafkaysNIKDYIDKAEKIAKEAKVLAHEA 1956
Cdd:COG1392 137 --------EVLELIIEINRLENEADDLYREA 159
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1684-1829 |
1.39e-04 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 47.30 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1684 EFIKDLAQHAEAVSEKAVKLNETLgiqdkafERNLQELQNEVDKMMTELRRK--NLDTQKEVAEDELVAAEALLK----- 1756
Cdd:pfam05262 195 NFRRDMTDLKERESQEDAKRAQQL-------KEELDKKQIDADKAQQKADFAqdNADKQRDEVRQKQQEAKNLPKpadts 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1757 --KVKKLFGESRGKNEEMEKDLREKLAD--YKSKVHDAWDLLREATDKIKEANLLSAENQKNM----TALEKKKEAIESG 1828
Cdd:pfam05262 268 spKEDKQVAENQKREIEKAQIEIKKNDEeaLKAKDHKAFDLKQESKASEKEAEDKELEAQKKRepvaEDLQKTKPQVEAQ 347
|
.
gi 1814459924 1829 K 1829
Cdd:pfam05262 348 P 348
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1848-2067 |
1.40e-04 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 45.33 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1848 RLADEINSVIDYVEDIQTKLPPLSEDLKGKIEDLSQEIKDR---KLAEKVSQAESHAAQLNdssAVLDRILDEAKNIsfn 1924
Cdd:pfam01442 1 LLEDSLDELSTYAEELQEQLGPVAQELVDRLEKETEALRERlqkDLEEVRAKLEPYLEELQ---AKLGQNVEELRQR--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1925 ataafkaysnIKDYIDKAEKIAKEAkvlAHEATELATGPQGSLQEGAKGSLQksfgflneakklanDVKendEHLNGLTS 2004
Cdd:pfam01442 75 ----------LEPYTEELRKRLNAD---AEELQEKLAPYGEELRERLEQNVD--------------ALR---ARLAPYAE 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1814459924 2005 RLdNANVRNRdlLRALNDTLerlsaipndtAAKLQAVKDKARQANDTAKDVLA-QIKDLHQNLD 2067
Cdd:pfam01442 125 EL-RQKLAER--LEELKESL----------APYAEEVQAQLSQRLQELREKLEpQAEDLREKLD 175
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1686-1849 |
1.44e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.83 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1686 IKDLAQHAEAVsEKAVKLNE----------TLGIQDKAFERNLQELQNEVDKM---MTELRRKnldtqkevaedelvaAE 1752
Cdd:COG1340 142 IKELEKELEKA-KKALEKNEklkelraelkELRKEAEEIHKKIKELAEEAQELheeMIELYKE---------------AD 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1753 ALLKKVKKLFGESRGKNEEMEKdLREKLADYKSKVHDawdlLREATDKIKEANLLSAENQKNMTALEKKKEAIE---SGK 1829
Cdd:COG1340 206 ELRKEADELHKEIVEAQEKADE-LHEEIIELQKELRE----LRKELKKLRKKQRALKREKEKEELEEKAEEIFEklkKGE 280
|
170 180
....*....|....*....|
gi 1814459924 1830 RQTEDTLKegtdILDEANRL 1849
Cdd:COG1340 281 KLTTEELK----LLQKSGLL 296
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
1616-1906 |
1.54e-04 |
|
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: 47.00 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1616 LENMTQELKHLLSpqrAPERLIQLAEGNLNTLVTEMNELLTRATKVTADGEQTGQDAERTNtransLGEFIkdlaqhaea 1695
Cdd:pfam04108 47 LEKVREGLEKVLN---ELKKDFKQLLKDLDAALERLEETLDKLRNTPVEPALPPGEEKQKT-----LLDFI--------- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1696 vSEKAV-KLNETLGIQDKAFERNLQELQNEVDKMMTELRrknlDTQKEVaeDELVAAEALLKKVKKLFGEsrgkNEEMEK 1774
Cdd:pfam04108 110 -DEDSVeILRDALKELIDELQAAQESLDSDLKRFDDDLR----DLQKEL--ESLSSPSESISLIPTLLKE----LESLEE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1775 DLREKLadyKSKVHDawdllreaTDKIKEANLLSAENQKNMTALEKKKEaiesgkRQTEDTLKEGTDILDE-------AN 1847
Cdd:pfam04108 179 EMASLL---ESLTNH--------YDQCVTAVKLTEGGRAEMLEVLENDA------RELDDVVPELQDRLDEmennyerLQ 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1814459924 1848 RLADEINSVIDYV-------EDIQTKLPPLSEDLKgkieDLSQEIKDRKLAekvsqAESHAAQLND 1906
Cdd:pfam04108 242 KLLEQKNSLIDELlsalqliAEIQSRLPEYLAALK----EFEERWEEEKET-----IEDYLSELED 298
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1473-1528 |
1.71e-04 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 41.57 E-value: 1.71e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1814459924 1473 CACPLISSSnnfSPSCVTEGlddYRCTaCPREYEGQYCERCAPGYTGSPSSPGGSC 1528
Cdd:pfam00053 1 CDCNPHGSL---SDTCDPET---GQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1735-1918 |
1.75e-04 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 44.95 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1735 KNLDTQKEVAEDELV-----AAEALLKKVKKLFGESRgknEEMEkDLREKLADYKSKVHDAWDllrEATDKIKEAnlLSA 1809
Cdd:pfam01442 7 DELSTYAEELQEQLGpvaqeLVDRLEKETEALRERLQ---KDLE-EVRAKLEPYLEELQAKLG---QNVEELRQR--LEP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1810 ENQKNMTALEKKKEAIEsgkrqteDTLKEgtdildeanrLADEINS-VIDYVEDIQTKLPPLSEDLKGKIEDLSQEIKDR 1888
Cdd:pfam01442 78 YTEELRKRLNADAEELQ-------EKLAP----------YGEELRErLEQNVDALRARLAPYAEELRQKLAERLEELKES 140
|
170 180 190
....*....|....*....|....*....|
gi 1814459924 1889 kLAEkvsQAESHAAQLNDSSAVLDRILDEA 1918
Cdd:pfam01442 141 -LAP---YAEEVQAQLSQRLQELREKLEPQ 166
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1593-2137 |
2.26e-04 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 47.13 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1593 LEQMAMSINLTGplpapYKILYGLENMtqELKHLLSPQRAPErLIQLAEGN----LNTLVTEMNEL-----LTRATKVTA 1663
Cdd:PTZ00440 1835 LGHVVKSANFIG-----IKIMTGLQPT--ELTPDASLETAPE-LTFESENNsdleLDHLSSNKNELdvyknIQDAYKSSL 1906
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1664 DGEQTGQDAERTNTRANSLGEFIKDLAQHAEAVSEKAVKLNETLGIQDkafernlqELQNEVDKMMTelrrknldtqkev 1743
Cdd:PTZ00440 1907 QILKYSDDIDKKQRDCNKLVEDGNEIYLKSTAINELKNMINSVKNKES--------AISNKIDNVSN------------- 1965
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1744 aedelvaaeaLLKKVKKLFGESRGKNEEMEKDLREKLADYKSkvhdawDLLREATDKIKEANLlsAENQKNMTALEKKKE 1823
Cdd:PTZ00440 1966 ----------KLSELNKITCNDESYDEILEKEEYEELKDLRN------SFNQEKAETLNNLKL--NKIKEDFNSYKNLLD 2027
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1824 AIESgkrqTEDTLKEG---TDILDEANRLADEINSVIDYVE-DIQTKLPPLSEDLK--GKIEDLSQEIKDRKLAEKVSqa 1897
Cdd:PTZ00440 2028 ELEK----SVKTLKASeniKKIVENKKTSIDAINTNIEDIEkEIESINPSLDELLKkgHKIEISRYTSIIDNVQTKIS-- 2101
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1898 eshaaqlNDSSavldRILDEAKNISFNATAAFKAYSNIKDYIDKAEKIAKEAKVLAHEATELATGPQGSLQEGAKGSlqK 1977
Cdd:PTZ00440 2102 -------NDSK----NINDIEKKAQIYLAYIKNNYNSIKKDISTLNEYFDEKQVSNYILTNIDKANKLSSELSEAVT--N 2168
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1978 SFGFLNEAKKLANDVKENDEhLNGLTSRLDNanvrnrdlLRALNDTLERLSAIPNDT-----AAKLQAVKDKARQANDTA 2052
Cdd:PTZ00440 2169 SEEIIENIKKEIIEINENTE-MNTLENTADK--------LKELYENLKKKKNIINNIykkinFIKLQEIENSSEKYNDIS 2239
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2053 KDVLAQIKDLHQNLDGLKKNYNQLADSVAktnavvkdpSKNKIIADADATVKnleqeadrlIDKLKPIKELEDNLKKNIS 2132
Cdd:PTZ00440 2240 KLFNNVVETQKKKLLDNKNKINNIKDKIN---------DKEKELINVDSSFT---------LESIKTFNEIYDDIKSNIG 2301
|
....*
gi 1814459924 2133 EIKEL 2137
Cdd:PTZ00440 2302 DLYKL 2306
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1806-2061 |
2.43e-04 |
|
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: 45.48 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1806 LLSAENQKNmtALEKKKEAIESGKRQTEDTLKEGTDILDEANRLADEINSVIDYVEDIQTKlpplSEDLKGKIEDLSQEI 1885
Cdd:pfam06008 18 NYNLENLTK--QLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAE----SERTLGHAKELAEAI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1886 KDrkLAEKVSQAESHAAQLND-----SSAVLDRILDEAKNISFNATAafkaySNIKDYIDKAEKIAKEAKVLAHEATELA 1960
Cdd:pfam06008 92 KN--LIDNIKEINEKVATLGEndfalPSSDLSRMLAEAQRMLGEIRS-----RDFGTQLQNAEAELKAAQDLLSRIQTWF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1961 TGPQGSLQegakgSLqksfgflneAKKLANDVKENDEHLNGLTSRLDNA----------NVRNRDLLRALNDTLERLSAI 2030
Cdd:pfam06008 165 QSPQEENK-----AL---------ANALRDSLAEYEAKLSDLRELLREAaaktrdanrlNLANQANLREFQRKKEEVSEQ 230
|
250 260 270
....*....|....*....|....*....|.
gi 1814459924 2031 PNDTAAKLQavkdKARQANDTAKDVLAQIKD 2061
Cdd:pfam06008 231 KNQLEETLK----TARDSLDAANLLLQEIDD 257
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
1717-1979 |
2.49e-04 |
|
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial virulence determinant and critical for gastric carcinogenesis. X-ray crystallographic analysis of the N-terminal CagA fragment (residues 1-876) revealed that the region has a structure comprised of three discrete domains. Domain I constitutes a mobile CagA N terminus, while Domain II tethers CagA to the plasma membrane by interacting with membrane phosphatidylserine. Domain III interacts intramolecularly with the intrinsically disordered C-terminal region, and this interaction potentiates the pathogenic scaffold/hub function of CagA.
Pssm-ID: 408741 [Multi-domain] Cd Length: 876 Bit Score: 47.07 E-value: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1717 NLQELQNEVDKMMT---ELRRKNLDTQKEVAEDELVAAEALLKKVKKLFGESRGKNEEMEKDLREKLaDYKSKVHDAWDL 1793
Cdd:pfam18971 571 SLQEANKLIKDFLSsnkELAGKALNFNKAVAEAKSTGNYDEVKKAQKDLEKSLRKREHLEKEVEKKL-ESKSGNKNKMEA 649
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1794 LREATDKIKEA-NLLSAENQKNMTALEKKKEaIESGKRQTEDTLKEGTDILDEANRLADEI----NSVIDYVEDIQTKLP 1868
Cdd:pfam18971 650 KAQANSQKDEIfALINKEANRDARAIAYTQN-LKGIKRELSDKLEKISKDLKDFSKSFDEFkngkNKDFSKAEETLKALK 728
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1869 PLSEDLK------GKIEDLSQEIKDRKLAE-----KVSQAESHAAQLNDSSAVLDRILDEAKNI--SFNATAAFKAYSNI 1935
Cdd:pfam18971 729 GSVKDLGinpewiSKVENLNAALNEFKNGKnkdfsKVTQAKSDLENSVKDVIINQKVTDKVDNLnqAVSVAKAMGDFSRV 808
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1814459924 1936 KDYIDKAEKIAKEAkvLAHEAT---ELATGPQGSLQEGAKGSLQKSF 1979
Cdd:pfam18971 809 EQVLADLKNFSKEQ--LAQQAQkneDFNTGKNSELYQSVKNSVNKTL 853
|
|
| OspD |
pfam03207 |
Borrelia outer surface protein D (OspD); |
1975-2148 |
3.00e-04 |
|
Borrelia outer surface protein D (OspD);
Pssm-ID: 367392 [Multi-domain] Cd Length: 254 Bit Score: 45.22 E-value: 3.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1975 LQKSFGFLNEAKKLANDVKENDEHLNGLTSRLDNANV--RNRDLLRALNDTLERLSAIPNDTAAKLQAVKDKARQANDTA 2052
Cdd:pfam03207 64 LKQTTNSLKEAKNTTDNLNASNEANKVVEAVINAVNLisSAADQVKSATKNMHDLAQMAEIDLEKIKNSSDKAIFASNLA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2053 KDVLAQIKDLHQNLDGLKKNYNQLADSVAKTnavvkDPSKNKIIADADATV----KNLEQEADRLIDKLKPIKELEDNLK 2128
Cdd:pfam03207 144 KEAYSLTKAAEQNMQKLYKEQQKISESESES-----DYSDSAEIKQAKEAVeiawKATVEAKDKLIDVENTVKETLDKIK 218
|
170 180
....*....|....*....|....*....
gi 1814459924 2129 K---------NISEIKELINQARKQANSI 2148
Cdd:pfam03207 219 TettnntklaDIKEAAELVLQIAKNAKEI 247
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1912-2141 |
3.04e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 3.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1912 DRILDEaKNISFNATAA---FKAYSNIKDYIDKAEK-------IAKEAKVLAHEATELATgpqgslQEGAKGSLQKSFGF 1981
Cdd:COG4913 215 EYMLEE-PDTFEAADALvehFDDLERAHEALEDAREqiellepIRELAERYAAARERLAE------LEYLRAALRLWFAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1982 L------NEAKKLANDVKENDEHLNGLTSRLDNANVRNRDLLRALN----DTLERLsaipndtAAKLQAVKDKARQANDT 2051
Cdd:COG4913 288 RrlelleAELEELRAELARLEAELERLEARLDALREELDELEAQIRgnggDRLEQL-------EREIERLERELEERERR 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2052 AKDVLAQIKDLH----QNLDGLKKNYNQLADSVAKTNAVVKDPSKNkiIADADATVKNLEQEADRLIDKlkpIKELEDNl 2127
Cdd:COG4913 361 RARLEALLAALGlplpASAEEFAALRAEAAALLEALEEELEALEEA--LAEAEAALRDLRRELRELEAE---IASLERR- 434
|
250
....*....|....*...
gi 1814459924 2128 KKNIS----EIKELINQA 2141
Cdd:COG4913 435 KSNIParllALRDALAEA 452
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
310-334 |
3.31e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 40.76 E-value: 3.31e-04
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1744-1975 |
3.66e-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: 45.91 E-value: 3.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1744 AEDELVAAEALLKKVKKlfgesrgkneEMEKdLREKLADYKSKVHDAWDLLREATDKIKEANLLSAENQKNMTALEKKKE 1823
Cdd:COG4942 18 QADAAAEAEAELEQLQQ----------EIAE-LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1824 AIESGKRQTEDTLKEGTDILDEANRLA------------------DEINSVIDYVEDIQTKLPPLSEDLKGKIEDLSQei 1885
Cdd:COG4942 87 ELEKEIAELRAELEAQKEELAELLRALyrlgrqpplalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAA-- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1886 KDRKLAEKVSQAESHAAQLNDSSAVLDRILDEAKNISFNATAAFKAYSN-IKDYIDKAEKIAKEAKVLAHEATELATGPQ 1964
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAeLAELQQEAEELEALIARLEAEAAAAAERTP 244
|
250
....*....|.
gi 1814459924 1965 GSLQEGAKGSL 1975
Cdd:COG4942 245 AAGFAALKGKL 255
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1589-1806 |
4.11e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 4.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1589 DLARLEQMAMSINLTGPLPAPYKILYGLENMTQELKHLLSPQRAPERLIQLAEgnlntLVTEMNELLTRAtKVTADGE-- 1666
Cdd:COG4717 315 ELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEE-----LEQEIAALLAEA-GVEDEEElr 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1667 QTGQDAERTNTRANSLGEFIKDLAQHAEAVSEKAVKLN-ETLGIQDKAFERNLQELQNEVDKMMTELRRknLDTQKEVAE 1745
Cdd:COG4717 389 AALEQAEEYQELKEELEELEEQLEELLGELEELLEALDeEELEEELEELEEELEELEEELEELREELAE--LEAELEQLE 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1814459924 1746 DELVAAEALLKKvkklfgesrgknEEMEKDLREKLADYKS-KVhdAWDLLREATDKIKEANL 1806
Cdd:COG4717 467 EDGELAELLQEL------------EELKAELRELAEEWAAlKL--ALELLEEAREEYREERL 514
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1617-1918 |
4.46e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.16 E-value: 4.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1617 ENMTQELKHLLSP---QRAPERLiQLAEGNLNTLVTE--MNELLTRATKVTADGEQ-------TGQDAERTNTRANSLGE 1684
Cdd:COG3206 81 SPLETQIEILKSRpvlERVVDKL-NLDEDPLGEEASReaAIERLRKNLTVEPVKGSnvieisyTSPDPELAAAVANALAE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1685 -FIKDLAQHAEAVSEKAVK-LNETLgiqdKAFERNLQELQNEVdkmmTELRRKN------------------LDTQKEVA 1744
Cdd:COG3206 160 aYLEQNLELRREEARKALEfLEEQL----PELRKELEEAEAAL----EEFRQKNglvdlseeaklllqqlseLESQLAEA 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1745 EDELVAAEALLKKVKKLFGESRGKNEEMEKDlrEKLADYKSKvhdawdlLREATDKIKEANLLSAENQKNMTALEKKKEA 1824
Cdd:COG3206 232 RAELAEAEARLAALRAQLGSGPDALPELLQS--PVIQQLRAQ-------LAELEAELAELSARYTPNHPDVIALRAQIAA 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1825 IESGKRQTEDTLKEGTDI-LDEANRLADEINSVIDYVEDIQTKLPPLSEDLkgkiEDLSQEIK-DRKLAEKVSQAeSHAA 1902
Cdd:COG3206 303 LRAQLQQEAQRILASLEAeLEALQAREASLQAQLAQLEARLAELPELEAEL----RRLEREVEvARELYESLLQR-LEEA 377
|
330
....*....|....*..
gi 1814459924 1903 QLNDSSAVLD-RILDEA 1918
Cdd:COG3206 378 RLAEALTVGNvRVIDPA 394
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2004-2153 |
5.05e-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: 44.53 E-value: 5.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2004 SRLDNANVRNRDL---LRALNDTLERLSAIPNDTAAKLQAVKDKARQANDTAKDVLAQIKDLHQNLDGLKKN--YNQLAD 2078
Cdd:COG1579 17 SELDRLEHRLKELpaeLAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNkeYEALQK 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1814459924 2079 SVAKTNAVVKDpsKNKIIADADATVKNLEQEADRLIDKLKPIK----ELEDNLKKNISEIKELINQARKQANSIKVSVS 2153
Cdd:COG1579 97 EIESLKRRISD--LEDEILELMERIEELEEELAELEAELAELEaeleEKKAELDEELAELEAELEELEAEREELAAKIP 173
|
|
| NtpE |
COG1390 |
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal ... |
1815-1956 |
5.35e-04 |
|
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 is part of the Pathway/BioSystem: A/V-type ATP synthase
Pssm-ID: 441000 [Multi-domain] Cd Length: 196 Bit Score: 43.78 E-value: 5.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1815 MTALEKKKEAIEsgkrqtEDTLKEGTDILDEANRLADEInsvidyVEDIQTKLpplsEDLKGKIEDLSQEIKDRKLAEKV 1894
Cdd:COG1390 1 MMSLEKIIEEIL------EEAEAEAEEILEEAEEEAEKI------LEEAEEEA----EEIKEEILEKAEREAEREKRRII 64
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1814459924 1895 SQA--ESHAAQLNDSSAVLDRILDEAKN--ISFNATAAFKAYsnIKDYIDKAEKIA--KEAKVLAHEA 1956
Cdd:COG1390 65 SSAelEARKELLEAKEELIEEVFEEALEklKNLPKDPEYKEL--LKKLLKEAAEELgsGDLVVYVNEK 130
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1686-1853 |
6.73e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 45.21 E-value: 6.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1686 IKDLAQHAEAVSEKAVK----------LNETLGIQDKAFERNLQELQNEVDKMmtelrRKNLDTQKEV---AEDELVAAE 1752
Cdd:PRK04778 315 LPDFLEHAKEQNKELKEeidrvkqsytLNESELESVRQLEKQLESLEKQYDEI-----TERIAEQEIAyseLQEELEEIL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1753 ALLKKVKKL---FGESRGKNEEMEKDLREKLADYKSKVH----------------DAWDLLREATDKIKEanlLSAE-NQ 1812
Cdd:PRK04778 390 KQLEEIEKEqekLSEMLQGLRKDELEAREKLERYRNKLHeikryleksnlpglpeDYLEMFFEVSDEIEA---LAEElEE 466
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1814459924 1813 K--NMTALEKKKEAIESgkrqTEDTLKEGTDILDEANRLADEI 1853
Cdd:PRK04778 467 KpiNMEAVNRLLEEATE----DVETLEEETEELVENATLTEQL 505
|
|
| V_Alix_like |
cd08915 |
Protein-interacting V-domain of mammalian Alix and related domains; This superfamily contains ... |
1955-2142 |
7.10e-04 |
|
Protein-interacting V-domain of mammalian Alix and related domains; This superfamily contains the V-shaped (V) domain of mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, and related domains. Alix, HD-PTP, Bro1, and Rim20 all interact with the ESCRT (Endosomal Sorting Complexes Required for Transport) system. Alix, also known as apoptosis-linked gene-2 interacting protein 1 (AIP1), participates in membrane remodeling processes during the budding of enveloped viruses, vesicle budding inside late endosomal multivesicular bodies (MVBs), and the abscission reactions of mammalian cell division. It also functions in apoptosis. HD-PTP functions in cell migration and endosomal trafficking, Bro1 in endosomal trafficking, and Rim20 in the response to the external pH via the Rim101 pathway. The Alix V-domain contains a binding site, partially conserved in this superfamily, for the retroviral late assembly (L) domain YPXnL motif. The Alix V-domain is also a dimerization domain. Members of this superfamily have an N-terminal Bro1-like domain, which binds components of the ESCRT-III complex. The Bro1-like domains of Alix and HD-PTP can also bind human immunodeficiency virus type 1 (HIV-1) nucleocapsid. Many members, including Alix, HD-PTP, and Bro1, also have a proline-rich region (PRR), which binds multiple partners in Alix, including Tsg101 (tumor susceptibility gene 101, a component of ESCRT-1) and the apoptotic protein ALG-2. The C-terminal portion (V-domain and PRR) of Bro1 interacts with Doa4, a ubiquitin thiolesterase needed to remove ubiquitin from MVB cargoes; it interacts with a YPxL motif in Doa4s catalytic domain to stimulate its deubiquitination activity. Rim20 may bind the ESCRT-III subunit Snf7, bringing the protease Rim13 (a YPxL-containing transcription factor) into proximity with Rim101, and promoting the proteolytic activation of Rim101. HD-PTP is encoded by the PTPN23 gene, a tumor suppressor gene candidate often absent in human kidney, breast, lung, and cervical tumors. HD-PTP has a C-terminal catalytically inactive tyrosine phosphatase domain.
Pssm-ID: 185746 [Multi-domain] Cd Length: 342 Bit Score: 44.64 E-value: 7.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1955 EATELATGPQGSLQEGAKGSLQKSFGFLNEAKKLANDVKENDEH-LNGLTSRLDnANVRNRDLLRA----LNDTLERLSA 2029
Cdd:cd08915 48 DDLQKPENLPDSIQHSQEIIEEGGLDNIEQSFKELSKLRQNVEElLQECEELLE-EEAAEDDQLRAkfgtLRWRRPSSDE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2030 IPNDTAAKLQAVKDKARQANDTAKDVLAQIKDLHQNLDGLKKNYNQLADSVAKTNaVVKDPSKNKIIADADATVKNLEqe 2109
Cdd:cd08915 127 AAKELYEKVTKLRGYLEQASNSDNEVLQCYESIDPNLVLLCGGYKELKAFIPSPY-PALDPEVSEVVSSLRPLLNEVS-- 203
|
170 180 190
....*....|....*....|....*....|...
gi 1814459924 2110 adrlidklkpikELEDNLKKNISEIKELINQAR 2142
Cdd:cd08915 204 ------------ELEKERERFISELEIKSRNND 224
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1383-1411 |
7.84e-04 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 39.64 E-value: 7.84e-04
10 20
....*....|....*....|....*....
gi 1814459924 1383 RCDCPPGYSGLSCEACMPGFYRLRSEPGG 1411
Cdd:pfam00053 19 QCLCKPGVTGRHCDRCKPGYYGLPSDPPQ 47
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1686-1888 |
8.82e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.01 E-value: 8.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1686 IKDLAQHAEAVSEKAVKLNETLGIQDKAFER-------NLQELQNEVDKMMTELrrKNLDTQKEVAEDELVAAE------ 1752
Cdd:PHA02562 176 IRELNQQIQTLDMKIDHIQQQIKTYNKNIEEqrkkngeNIARKQNKYDELVEEA--KTIKAEIEELTDELLNLVmdiedp 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1753 -ALLKKVKKLFGESRGKNEEMEKDLR-------------------EKLADYKSKVHDAWDLLREATDKIKEANLLSAENQ 1812
Cdd:PHA02562 254 sAALNKLNTAAAKIKSKIEQFQKVIKmyekggvcptctqqisegpDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFN 333
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1814459924 1813 KNMTALEKKKEAIESGKRQTEDTLKEGTDILDEANRLADEinsVIDYVEDIQTklppLSEDLKGKIEDLSQEIKDR 1888
Cdd:PHA02562 334 EQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAE---FVDNAEELAK----LQDELDKIVKTKSELVKEK 402
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1642-2185 |
9.73e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 9.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1642 GNLNTLVTEM----NELLTRATKVTA---DGEQTGQDAERTNTRANSLGEfIKDLAQHAEAVSEKAVKLNETLGIQDKAF 1714
Cdd:COG4913 207 GDLDDFVREYmleePDTFEAADALVEhfdDLERAHEALEDAREQIELLEP-IRELAERYAAARERLAELEYLRAALRLWF 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1715 -ERNLQELQNEVDKmmtelrrknldtqkevAEDELVAAEALLKKVKKLFGESRGKNEEMEKDLRE----KLADYKSKVHD 1789
Cdd:COG4913 286 aQRRLELLEAELEE----------------LRAELARLEAELERLEARLDALREELDELEAQIRGnggdRLEQLEREIER 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1790 A----------WDLLREATDKIKEANLLSAE----NQKNMTALEKKKEAIESGKRQTEDTLKEG-TDILDEANRLADEIN 1854
Cdd:COG4913 350 LereleererrRARLEALLAALGLPLPASAEefaaLRAEAAALLEALEEELEALEEALAEAEAAlRDLRRELRELEAEIA 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1855 SV------ID-YVEDI-----------QTKLPPLSE--DLKGK-------IE------------------DLSQEIKDRK 1889
Cdd:COG4913 430 SLerrksnIPaRLLALrdalaealgldEAELPFVGEliEVRPEeerwrgaIErvlggfaltllvppehyaAALRWVNRLH 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1890 LAEKV--SQAESHAAQLNDSSAVLDRILDEaknISFNATAAfkaysniKDYIDkaEKIAKEAKVL-AHEATELATGPQGS 1966
Cdd:COG4913 510 LRGRLvyERVRTGLPDPERPRLDPDSLAGK---LDFKPHPF-------RAWLE--AELGRRFDYVcVDSPEELRRHPRAI 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1967 LQEG----AKGSLQKS----------FGFLNEAKK--LANDVKENDEHLNGLTSRLDNANVRnRDLLRALNDTLERLSAI 2030
Cdd:COG4913 578 TRAGqvkgNGTRHEKDdrrrirsryvLGFDNRAKLaaLEAELAELEEELAEAEERLEALEAE-LDALQERREALQRLAEY 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2031 PND---------TAAKLQAVKDKARQANDT-------AKDVLAQIKDLHQNLDGLKKNYNQLADSVAKTNAVVKDpSKNK 2094
Cdd:COG4913 657 SWDeidvasaerEIAELEAELERLDASSDDlaaleeqLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDE-LQDR 735
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2095 IIADADATVKNLEQEADRLIDKL---KPIKELEDNLKKNISEIKELINQARKQANsikvsvssggDCIRTYKPEikkgsY 2171
Cdd:COG4913 736 LEAAEDLARLELRALLEERFAAAlgdAVERELRENLEERIDALRARLNRAEEELE----------RAMRAFNRE-----W 800
|
650
....*....|....
gi 1814459924 2172 NSIIVNVKTAVADN 2185
Cdd:COG4913 801 PAETADLDADLESL 814
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1819-2149 |
1.07e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.93 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1819 EKKKEAIEsgK-RQTEDTLKEGTDILDEanrladeinsvidyvedIQTKLPPLSED----LKGKieDLSQEIKDRKLAEK 1893
Cdd:COG1196 172 ERKEEAER--KlEATEENLERLEDILGE-----------------LERQLEPLERQaekaERYR--ELKEELKELEAELL 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1894 VSQAESHAAQLNDSSAVLDRILDEAKNISFNATAAFKAYSNIKDYIDKAEKIAKEAKVLAHEATELATGPQG---SLQEG 1970
Cdd:COG1196 231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQdiaRLEER 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1971 AKGSLQKSFGFLNEAKKLANDVKENDEHLNGLTSRLDNANVRNRDLLRALNDTLERLSAIPNDTAAKLQAVKDKARQAND 2050
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2051 TAKDVL----------AQIKDLHQNLDGLKKNYNQLADSVAKTNAVVKDpsKNKIIADADATVKNLEQEADRLIDKLKPI 2120
Cdd:COG1196 391 ALRAAAelaaqleeleEAEEALLERLERLEEELEELEEALAELEEEEEE--EEEALEEAAEEEAELEEEEEALLELLAEL 468
|
330 340
....*....|....*....|....*....
gi 1814459924 2121 KELEDNLKKNISEIKELINQARKQANSIK 2149
Cdd:COG1196 469 LEEAALLEAALAELLEELAEAAARLLLLL 497
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1383-1411 |
1.19e-03 |
|
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: 39.26 E-value: 1.19e-03
10 20
....*....|....*....|....*....
gi 1814459924 1383 RCDCPPGYSGLSCEACMPGFYRLRSEPGG 1411
Cdd:cd00055 20 QCECKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1718-1950 |
1.22e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 43.90 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1718 LQELQNEVDKMMTELRRKNLDTQKEVAEDELvaaEALLKKVKKLFGESrgkneemeKDLREKLADYKSKVHDAWDLLREA 1797
Cdd:cd22656 93 YAEILELIDDLADATDDEELEEAKKTIKALL---DDLLKEAKKYQDKA--------AKVVDKLTDFENQTEKDQTALETL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1798 TDKIKEanLLSAENQKN-MTALEKKKEAIESgkrQTEDTLKEGTDILDEANRLADEINSVIDYVEDIQTKLpplsEDLKG 1876
Cdd:cd22656 162 EKALKD--LLTDEGGAIaRKEIKDLQKELEK---LNEEYAAKLKAKIDELKALIADDEAKLAAALRLIADL----TAADT 232
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1814459924 1877 KIEDLSQEIKD-RKLAEKVsqaESHAAQLNDSsavLDRILDEAKNISFNATAAFKAYSNIKDYIDKAEKIAKEAK 1950
Cdd:cd22656 233 DLDNLLALIGPaIPALEKL---QGAWQAIATD---LDSLKDLLEDDISKIPAAILAKLELEKAIEKWNELAEKAD 301
|
|
| Phage_GP20 |
pfam06810 |
Phage minor structural protein GP20; This family consists of several phage minor structural ... |
1698-1845 |
1.45e-03 |
|
Phage minor structural protein GP20; This family consists of several phage minor structural protein GP20 sequences of around 180 residues in length. The function of this family is unknown.
Pssm-ID: 429131 [Multi-domain] Cd Length: 149 Bit Score: 41.57 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1698 EKAVKLNETLGIQDKAFERnLQELQNEVDKMMTEL--RRKNLDTQKEVAEDelvaAEALLKKVKKLfgesRGKNEEMEKD 1775
Cdd:pfam06810 1 EQADKVMEAENGKDIPKAK-FDEVNTERDTLKEQLatRDKQLKDLKKVAKD----NEELQKQIDEL----QAKNKDAEAD 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1814459924 1776 LREKLADykSKVHDAwdlLREAtdkIKEANllsAENQK------NMTALEKKKEA-IESGKRQTEdTLKEGTDILDE 1845
Cdd:pfam06810 72 YEAKIAD--LKFDNA---IKLA---LKGAK---AKNEKavkallDKDKLKLKDDGtLIGLDEQIE-GLKESDKYLFE 136
|
|
| TNFRSF21 |
cd10583 |
Tumor necrosis factor receptor superfamily member 21 (TNFRSF21), also known as death receptor ... |
827-933 |
1.49e-03 |
|
Tumor necrosis factor receptor superfamily member 21 (TNFRSF21), also known as death receptor (DR6); TNFRSF21 (also known as death receptor 6 (DR6), CD358, BM-018) is highly expressed in differentiating neurons as well as in the adult brain, and is upregulated in injured neurons. DR6 negatively regulates neurondendrocyte, axondendrocyte, and oligodendrocyte survival, hinders axondendrocyte and oligodendrocyte regeneration and its inhibition has a neuro-protective effect in nerve injury. It activates nuclear factor kappa-B (NFkB) and mitogen-activated protein kinase 8 (MAPK8, also called c-Jun N-terminal kinase 1), and induces cell apoptosis by associating with TNFRSF1A-associated via death domain (TRADD), which is known to mediate signal transduction of tumor necrosis factor receptors. TNFRSF21 plays a role in T-helper cell activation, and may be involved in inflammation and immune regulation. Its possible ligand is alpha-amyloid precursor protein (APP), hence probably involved in the development of Alzheimer's disease; when released, APP binds in an autocrine/paracrine manner to activate a caspase-dependent self-destruction program that removes unnecessary or connectionless axons. Increasing beta-catenin levels in brain endothelium upregulates TNFRSF21 and TNFRSF19, indicating that these death receptors are downstream target genes of Wnt/beta-catenin signaling, which has been shown to be required for blood-brain barrier development. DR6 is up-regulated in numerous solid tumors as well as in tumor vascular cells, including ovarian cancer and may be a clinically useful diagnostic and predictive serum biomarker for some adult sarcoma subtypes.
Pssm-ID: 276909 [Multi-domain] Cd Length: 159 Bit Score: 42.05 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 827 HLDRNLG--LICDECPVG-YTGPH--------CERCAEGYFGQPSLPGGSCQPCQ--CNDNLDFSIPgsCDSLSGSCLIC 893
Cdd:cd10583 4 HVDPATGtqLTCDKCPAGtYVSKHctetslreCSPCPNGTFTRHENGIEQCHRCRkpCPAPMIEKTP--CTALTDRECTC 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1814459924 894 KPGT--TGRYC---ELCADGY----FGDAVDAKNCQPClcnANGSFSEV 933
Cdd:cd10583 82 PPGTflSNDTCvphSVCPVGWgvrkKGTETEDVRCKPC---PRGTFSDV 127
|
|
| dnaK |
PRK00290 |
molecular chaperone DnaK; Provisional |
1801-1916 |
1.64e-03 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 234715 [Multi-domain] Cd Length: 627 Bit Score: 43.94 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1801 IKEAnllsaenQKNMTALEKKKEAIEsgKR--------QTEDTLKEGTDILDEANRlaDEINSVIDYV------EDIqtk 1866
Cdd:PRK00290 509 VKDA-------EANAEEDKKRKELVE--ARnqadsliyQTEKTLKELGDKVPADEK--EKIEAAIKELkealkgEDK--- 574
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1867 lpplsEDLKGKIEDLSQEIKdrKLAEKVSQAESHAAQLNDSSAVLDRILD 1916
Cdd:PRK00290 575 -----EAIKAKTEELTQASQ--KLGEAMYQQAQAAQGAAGAAAKDDDVVD 617
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1727-1899 |
2.06e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 43.08 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1727 KMMTELRRKNLDTQKEVAE---DELVAAEALLKKvkklfgesrgkNEEMEKDLREKLADYKSKVHDAWDLLREATDKIke 1803
Cdd:smart00787 132 KMWYEWRMKLLEGLKEGLDenlEGLKEDYKLLMK-----------ELELLNSIKPKLRDRKDALEEELRQLKQLEDEL-- 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1804 anllsaeNQKNMTALEKKKEAIESGKRQTEDTLKEGTDILDEANRLADEINSVIDYVEDIQTKLpplsEDLKGKIEDLSQ 1883
Cdd:smart00787 199 -------EDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEI----AEAEKKLEQCRG 267
|
170
....*....|....*...
gi 1814459924 1884 -EIKD-RKLAEKVSQAES 1899
Cdd:smart00787 268 fTFKEiEKLKEQLKLLQS 285
|
|
| BAR_SNX |
cd07596 |
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ... |
1644-1817 |
2.15e-03 |
|
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.
Pssm-ID: 153280 [Multi-domain] Cd Length: 218 Bit Score: 42.34 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1644 LNTLVTEMNELLTRATKVTADGEQTGQD-----------AERTNTRANSLGEFIKDLAQHAEAVS----EKAVKLNETLG 1708
Cdd:cd07596 13 ILKLEEQLKKLSKQAQRLVKRRRELGSAlgefgkaliklAKCEEEVGGELGEALSKLGKAAEELSslseAQANQELVKLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1709 IQDKAFERNLQELQNEVDkmmtelRRKNLDTQKEVAEDELVAAEALLKKVKKLFGESRGKNEEMEKDLREkladYKSKVH 1788
Cdd:cd07596 93 EPLKEYLRYCQAVKETLD------DRADALLTLQSLKKDLASKKAQLEKLKAAPGIKPAKVEELEEELEE----AESALE 162
|
170 180 190
....*....|....*....|....*....|
gi 1814459924 1789 DAWDLLREATDKIK-EANLLSAENQKNMTA 1817
Cdd:cd07596 163 EARKRYEEISERLKeELKRFHEERARDLKA 192
|
|
| ClyA-like |
cd21116 |
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ... |
2032-2151 |
3.53e-03 |
|
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including Bacillus cereus HblB, Aeromonas hydrophila AhlB, Bacillus thuringiensis Cry6Aa and similar proteins; This family belongs to the ClyA family of alpha-PFT bacterial toxins. PFTs form the major group of virulence factors in many pathogenic bacteria and in general are critical components of the molecular offensive and defensive machinery of cells in all kingdoms of life. Bacterial PFTs facilitate the takeover of host resources by puncturing holes in the membrane. PFTs can be classified as alpha-PFTs and beta-PFTs depending on the secondary structures of their membrane component. Alpha-PFTs use a ring of amphipathic helices while beta-PFTs use a beta-barrel to construct the pore. Members of this family include the toxins: Bacillus cereus hemolysin binding component B (HblB or HBL-B) of the diarrheal enterotoxin hemolysin BL, Aeromonas hydrophila hemolytic (Ahl) component B (AhlB) of the tripartite AhlABC toxin, Vibrio cholerae cytotoxin motility associated killing factor A (MakA) cytotoxin, Xenorhabdus nematophila alpha-xenorhabdolysin (XaxA), Bacillus thuringiensis crystal 6Aa (Cry6Aa) parasporal crystal (Cry) toxin, and Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA) of the non-hemolytic enterotoxin Nhe, which, despite its name, is hemolytic, among others. In solution, ClyA proteins have an elongated, almost entirely alpha-helical structure, except for a short hydrophobic beta-hairpin known as the beta-tongue. Pore formation by ClyA requires circular oligomerization of the toxin by a sequential mechanism. This, in turn, concentrates the amphipathic helices in the center of the ring-like structure, forming a helical barrel that inserts into the membrane by a wedge-like mechanism. Compared with ClyA, NheA is almost entirely alpha-helical with an enlarged "head" domain, and an enlarged beta-tongue; it has been proposed that NheA could even form beta-barrel pores. Alpha-PFTs with similar structures are increasingly being found in eukaryotes, in particular as components of the immune systems of animals. This family may be distantly related to Escherichia coli alpha-PFT hemolysin E (HlyE, also known as ClyA or SheA).
Pssm-ID: 439149 [Multi-domain] Cd Length: 224 Bit Score: 41.63 E-value: 3.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2032 NDTAAKLQAVKDKARQANDTAKDVLAQIKDLHQNLDGLKKNYNQLADSVAKTNAVVKDPSKNkiiadadatVKNLEQEAD 2111
Cdd:cd21116 94 QQLLQGLEALQSQVTKKQTSVTSFINELTTFKNDLDDDSRNLQTDATKAQAQVAVLNALKNQ---------LNSLAEQID 164
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1814459924 2112 RLIDKLKPIKELEDNLKKNISEIKELINQARKQANSIKVS 2151
Cdd:cd21116 165 AAIDALEKLSNDWQTLDSDIKELITDLEDAESSIDAAFLQ 204
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1672-1878 |
3.85e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.84 E-value: 3.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1672 AERTNTRANSLGEFIKDLAQH-AEAVSEKAVklnetLGIQDKAfernlQELQNEVDKmmtELRRKNLDTQKevAEDELVA 1750
Cdd:PRK12704 29 AEAKIKEAEEEAKRILEEAKKeAEAIKKEAL-----LEAKEEI-----HKLRNEFEK---ELRERRNELQK--LEKRLLQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1751 AEALLKKVKKLFGESRGKNEEMEKDLREKLADYKSKVHDAWDLLREATDKIKEANLLSAENQKNMtALEK-KKEA-IESG 1828
Cdd:PRK12704 94 KEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAKEI-LLEKvEEEArHEAA 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1814459924 1829 K--RQTEDTLKEgtdildEANRLADEInsVI--------DYVEDIQT---KLPplSEDLKGKI 1878
Cdd:PRK12704 173 VliKEIEEEAKE------EADKKAKEI--LAqaiqrcaaDHVAETTVsvvNLP--NDEMKGRI 225
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1473-1529 |
3.92e-03 |
|
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: 37.72 E-value: 3.92e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1814459924 1473 CACPLISSSNnfsPSCVTEGLddyRCTaCPREYEGQYCERCAPGYTGSPSSPGGsCQ 1529
Cdd:cd00055 2 CDCNGHGSLS---GQCDPGTG---QCE-CKPNTTGRRCDRCAPGYYGLPSQGGG-CQ 50
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1716-1914 |
5.29e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 5.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1716 RNLQELQNEVDKMMTELRRKNLDTQKEV------AEDElvaaEALLKKVKKLfgesrgkneEMEKDLREKLADYKSKVHD 1789
Cdd:COG4717 347 EELQELLREAEELEEELQLEELEQEIAAllaeagVEDE----EELRAALEQA---------EEYQELKEELEELEEQLEE 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 1790 AWDLLREATDKIKEANLlsaenqknMTALEKKKEAIESGKRQTEDTLKEGTDILDEANRLADEinsviDYVEDIQTKLpp 1869
Cdd:COG4717 414 LLGELEELLEALDEEEL--------EEELEELEEELEELEEELEELREELAELEAELEQLEED-----GELAELLQEL-- 478
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1814459924 1870 lsEDLKGKIEDLSQEIKDRKLAEKVSQAESHAAQLNDSSAVLDRI 1914
Cdd:COG4717 479 --EELKAELRELAEEWAALKLALELLEEAREEYREERLPPVLERA 521
|
|
| F5_F8_type_C |
pfam00754 |
F5/8 type C domain; This domain is also known as the discoidin (DS) domain family. |
94-178 |
6.38e-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: 39.35 E-value: 6.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 94 SSNPHLRHPITNAIDGK-NTWWQSPSIKNGieyhyVTITLDLQQVFQIAYVIVKAANSPRPGN---WILERSLDDVDYKP 169
Cdd:pfam00754 5 SSSYSGEGPAAAALDGDpNTAWSAWSGDDP-----QWIQVDLGKPKKITGVVTQGRQDGSNGYvtsYKIEYSLDGENWTT 79
|
....*....
gi 1814459924 170 WQYHAVTDT 178
Cdd:pfam00754 80 VKDEKIPGN 88
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
2038-2154 |
6.74e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 41.59 E-value: 6.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2038 LQAVKDKARQANDTAKDVLAQIKDLHQNLDGLKKNYNQLADSVAKtnavvKDPSKNKIIADADatvknleqeadrlIDKL 2117
Cdd:cd22656 123 LDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKD-----LLTDEGGAIARKE-------------IKDL 184
|
90 100 110
....*....|....*....|....*....|....*..
gi 1814459924 2118 KpiKELEDNLKKNISEIKELINQARKQANSIKVSVSS 2154
Cdd:cd22656 185 Q--KELEKLNEEYAAKLKAKIDELKALIADDEAKLAA 219
|
|
| CBD_MYO6-like |
cd21759 |
calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, ... |
2056-2144 |
7.43e-03 |
|
calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, which are actin-based motor molecules with ATPase activity, include unconventional myosins that serve in intracellular movements. Myosin-VI, also called unconventional myosin-6 (MYO6), is a reverse-direction motor protein that moves towards the minus-end of actin filaments. It is required for the structural integrity of the Golgi apparatus via the p53-dependent pro-survival pathway. Myosin-VI appears to be involved in a very early step of clathrin-mediated endocytosis in polarized epithelial cells. It modulates RNA polymerase II-dependent transcription. As part of the DISP (DOCK7-Induced Septin disPlacement) complex, Myosin-VI may regulate the association of septins with actin and thereby regulate the actin cytoskeleton. Myosin-VI is encoded by gene MYO6, the human homolog of the gene responsible for deafness in Snell's waltzer mice. It is mutated in autosomal dominant non-syndromic hearing loss. This family also includes Drosophila melanogaster unconventional myosin VI Jaguar (Jar; also called myosin heavy chain 95F (Mhc95F), or 95F MHC), which is a motor protein necessary for the morphogenesis of epithelial tissues during Drosophila development. Jar is required for basal protein targeting and correct spindle orientation in mitotic neuroblasts. It contributes to synaptic transmission and development at the Drosophila neuromuscular junction. Together with CLIP-190 (CAP-Gly domain-containing/cytoplasmic linker protein 190), Jar may coordinate the interaction between the actin and microtubule cytoskeleton. Jar may link endocytic vesicles to microtubules and possibly be involved in transport in the early embryo and in the dynamic process of dorsal closure; its function is believed to change during the life cycle. This model corresponds to the calmodulin (CaM) binding domain (CBD), which consists of three subdomains: a unique insert (Insert 2 or Ins2), an IQ motif, and a proximal tail domain (PTD, also known as lever arm extension or LAE).
Pssm-ID: 409646 [Multi-domain] Cd Length: 149 Bit Score: 39.41 E-value: 7.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814459924 2056 LAQIKDLHQNLDGLKKNYNQLadsvaktnavvkDPSKNKIIADadatVKNLEQEADRLIDKLK-----PIKELEDNLKKN 2130
Cdd:cd21759 71 LRKIRALEKQLKEMEEIASQL------------KKDKDKWTKQ----VKELKKEIDALIKKIKtndmiTRKEIDKLYNAL 134
|
90
....*....|....
gi 1814459924 2131 ISEIKELINQARKQ 2144
Cdd:cd21759 135 VKKVDKQLAELQKK 148
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1473-1521 |
9.99e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 36.52 E-value: 9.99e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1814459924 1473 CACPLissSNNFSPSCVtegLDDYRCTaCPREYEGQYCERCAPGYTGSP 1521
Cdd:smart00180 1 CDCDP---GGSASGTCD---PDTGQCE-CKPNVTGRRCDRCAPGYYGDG 42
|
|
| |
