|
Name |
Accession |
Description |
Interval |
E-value |
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
38-290 |
1.95e-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: 300.05 E-value: 1.95e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 38 AHQQRGLFPAVLNLASNAYITTNATCGEKGPEMYCKLVEHVpgqpVRDPQCRICNQNssNPNQRHPITNAIDGKN----T 113
Cdd:smart00136 1 AGRPRSCYPPFVNLAFGREVTATSTCGEPGPERYCKLVGHT----EQGKKCDYCDAR--NPRRSHPAENLTDGNNpnnpT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 114 WWQSPSIKNGIeyHYVTITLDLQQVFQIAYVIVKAAnSPRPGNWILERSLDDVEYKPWQYHAvtdTECLTLYNIyPRTGP 193
Cdd:smart00136 75 WWQSEPLSNGP--QNVNLTLDLGKEFHVTYVILKFC-SPRPSLWILERSDFGKTWQPWQYFS---SDCRRTFGR-PPRGP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 194 PSYSKDDEVICTSFYSKIHPLENGEIHISLINGRPSADDP--SPELLEFTSARYIRLRFQRIRTLNADLMMfahkdpreI 271
Cdd:smart00136 148 ITKGNEDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDFdnSPVLQEWVTATNIRVRLTRLRTLGDELMD--------D 219
|
250
....*....|....*....
gi 1911235092 272 DPIVTRRYYYSVKDISVGG 290
Cdd:smart00136 220 RPEVTRRYYYAISDIAVGG 238
|
|
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
44-290 |
1.03e-87 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 286.40 E-value: 1.03e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 44 LFPAVLNLASNAYITTNATCGEKGPEMYCKLVEHVPGQpvrdpQCRICNqnSSNPNQRHPITNAIDGKN----TWWQSPS 119
Cdd:pfam00055 1 CYPAFGNLAFGREVSATSTCGLNGPERYCILSGLEGGK-----KCFICD--SRDPHNSHPPSNLTDSNNgtneTWWQSET 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 120 IKngIEYHYVTITLDLQQVFQIAYVIVKAAnSPRPGNWILERSLD-DVEYKPWQYHAvtdTECLTLYNIypRTGPPSYSK 198
Cdd:pfam00055 74 GV--IQYENVNLTLDLGKEFHFTYLILKFK-SPRPAAMVLERSTDfGKTWQPYQYFA---SDCRRTFGR--PSGPSRGIK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 199 DDEVICTSFYSKIHPLENGEIHISLINGRPSA--DDPSPELLEFTSARYIRLRFQRIRTLNadlmmfahkDPREIDPIVT 276
Cdd:pfam00055 146 DDEVICTSEYSDISPLTGGEVIFSTLEGRPSAniFDYSPELQDWLTATNIRIRLLRLHTLG---------DELLDDPSVL 216
|
250
....*....|....
gi 1911235092 277 RRYYYSVKDISVGG 290
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 ... |
1573-1830 |
7.76e-86 |
|
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: 281.99 E-value: 7.76e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1573 SIN-LTGPLPAPYKMLYDLENRTQELKHLLSPQRAPERLIQLAEGNLNTLVTEMNELLTRATKVTADGEQTGQDAERTSR 1651
Cdd:pfam06008 3 SLNsLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1652 RANSLGDFIKGLVRDAEAVNEKAKEVNETlgiQDKAFERNMQGLQKEIDQMMRELRRKNLDTQKEVAEDELVAAEGLLKK 1731
Cdd:pfam06008 83 HAKELAEAIKNLIDNIKEINEKVATLGEN---DFALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQDLLSR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1732 VQKVFGEPRGKNEKMEKDLGEKLTDHKNKLDDAWDLLREATDKTREANRLAAANQQNMTALEEKKEAIESGKRQTENTLK 1811
Cdd:pfam06008 160 IQTWFQSPQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEETLK 239
|
250
....*....|....*....
gi 1911235092 1812 EGNDILDEANRLADEINSV 1830
Cdd:pfam06008 240 TARDSLDAANLLLQEIDDA 258
|
|
| Laminin_II |
pfam06009 |
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 ... |
2015-2151 |
3.86e-50 |
|
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: 174.98 E-value: 3.86e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2015 AKNKARQANDTAKDVLAQVKDLHQDLDGLKKSYNQLADSVAKTNAVVKDplKNKIIADADATVKNLEQEADRLIDKLKPI 2094
Cdd:pfam06009 1 SKELAREANETAKEVLEQLAPLSQNLENTSEKLSGINRSLEETNELVND--ANKALDDAGRSVKKLEELAPDLLDKLKPL 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2095 KELEDN---LKKNISEIKELINQARKQANSIKVSVSSGGDCIRTYKPEIKKGSYNNIIVN 2151
Cdd:pfam06009 79 KQLEVNsssLSDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTSL 138
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2768-2896 |
1.96e-46 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 164.03 E-value: 1.96e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2768 VRTEAESGLLFYMARINHADFATVQLRNGFPYFSYDLGSGDTNTMIPTKINDGQWHKIKITRIKQEGILYVDD-ASNRTI 2846
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGeARPTGE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1911235092 2847 SPKKADI-LDVVGLLYVGGLPINYTTRRIGPVTYSIDGCIRNLHMAEAPVD 2896
Cdd:pfam00054 81 SPLGATTdLDVDGPLYVGGLPSLGVKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| LamB |
smart00281 |
Laminin B domain; |
1253-1388 |
3.82e-46 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 162.82 E-value: 3.82e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1253 RFEPFYWKLPEQFEGKKLMAYGGKLKYAIYFEAREEtGVSTYKPQVIIRGGtpsHARIIVRHTAAPLIGQLTRHEIEMTE 1332
Cdd:smart00281 1 DNEPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRRG-GTHVSAPDVILEGN---GLRISHPAEGPPLPDELTTVEVRFRE 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1911235092 1333 REWKYYGddprvSRTVTREDFLDVLYDIHYILIKATYGNVIRQSRISEISMEVAEQ 1388
Cdd:smart00281 77 ENWQYYG-----GRPVTREDLMMVLANLTAILIRATYSQQMAGSRLSDVSLEVAVP 127
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
1258-1402 |
1.85e-44 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 158.59 E-value: 1.85e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1258 YWKLPEQFEGKKLMAYGGKLKYAIYFEAREETGVSTYKPQVIIRGGtpsHARIIVRHTA--APLIGQLTRHEIEMTEREW 1335
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGGGSLNSEPDVILEGN---GLRLSYSSPDqpPPDPGQEQTYSVRLHEENW 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1911235092 1336 KYygddpRVSRTVTREDFLDVLYDIHYILIKATYGNVIRQSRISEISMEVAEQGPvtaLTPPAHLIE 1402
Cdd:pfam00052 78 RD-----SDGAPVSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSAVPGG---SGPPASWVE 136
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2346-2485 |
4.65e-40 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 145.54 E-value: 4.65e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2346 FRTFSSSALLMYLATKDLKDFMSVELTDGHIKVSYDLGSGMASVVSNQNHNDGKWKSFTLSRIQKQANISiidIDTNQEE 2425
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLS---VDGEARP 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2426 NIATSSSGNNfglDLKADDKIYFGGLPtlrNLSMKARPEVNLKKYSGCLKDIEISRTPYN 2485
Cdd:pfam00054 78 TGESPLGATT---DLDVDGPLYVGGLP---SLGVKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2741-2890 |
9.08e-38 |
|
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: 139.86 E-value: 9.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2741 FGLSKNSHIAIAFDDTKvKNRLTIEFEVRTEAESGLLFYMARINHADFATVQLRNGFPYFSYDLGSGDTNTMIPTKINDG 2820
Cdd:cd00110 2 VSFSGSSYVRLPTLPAP-RTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1911235092 2821 QWHKIKITRIKQEGILYVDD-ASNRTISPKKADILDVVGLLYVGGLPINYTTRRIgPVTYSIDGCIRNLHM 2890
Cdd:cd00110 81 QWHSVSVERNGRSVTLSVDGeRVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGL-PVSPGFVGCIRDLKV 150
|
|
| LamG |
smart00282 |
Laminin G domain; |
2763-2890 |
2.37e-36 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 135.16 E-value: 2.37e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2763 TIEFEVRTEAESGLLFYMARINHADFATVQLRNGFPYFSYDLGSGDTNTMI-PTKINDGQWHKIKITRIKQEGILYVDD- 2840
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSdPTPLNDGQWHRVAVERNGRSVTLSVDGg 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2841 ASNRTISPKKADILDVVGLLYVGGLPINYtTRRIGPVTYSIDGCIRNLHM 2890
Cdd:smart00282 81 NRVSGESPGGLTILNLDGPLYLGGLPEDL-KLPPLPVTPGFRGCIRNLKV 129
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
587-728 |
1.20e-35 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 133.16 E-value: 1.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 587 FWSAPAPYLGNKLTAAGGQLTFTISYDLEEEEEEeetaRVLQLMIILEGKDLRISTAQEE-VELRPSEDYIHALPLKEDS 665
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGGGS----LNSEPDVILEGNGLRLSYSSPDqPPPDPGQEQTYSVRLHEEN 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1911235092 666 FTiHGTDFPVSRKEFMTVLVDLKRILIQITDSLGVDAIyRLSSVGLASAVPYRTdGGFASAVE 728
Cdd:pfam00052 77 WR-DSDGAPVSREDFMMVLANLTAILIRATYSTGSGQV-SLSNVSLDSAVPGGS-GPPASWVE 136
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2916-3068 |
2.52e-35 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 132.93 E-value: 2.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2916 GTYFDGTGFAKAVGGFKVGLDLLVEFEFRTTRTTGVLLGISSQ-KMDGMGIEMIDEKIMFHVDNGAGRFTAvydaGVPGH 2994
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQnGGDFLALELEDGRLVLRYDLGSGSLVL----SSKTP 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1911235092 2995 LCDGQWHTVRANKIKHRIELTVDGNQVEAQSPNPASTSADTNDPVFVGGFPDGLNQFGLTINVPFRGCIRSLKL 3068
Cdd:cd00110 77 LNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKV 150
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2152-2292 |
4.79e-34 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 128.59 E-value: 4.79e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2152 VKTPVADNLLFYLGSAKFIDFLAIEMRKGKVSFLWDVGSGVGRVEYPDlTIDDSYWYRIEASRTGRNGSISVRALDGPka 2231
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGD-KLNDGKWHSVELERNGRSGTLSVDGEARP-- 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1911235092 2232 sivpstyHSASPPGYTIlDVDANAMLFVGGLTG-KLKKADAVRVITFTGCMGETYFDGKPIG 2292
Cdd:pfam00054 78 -------TGESPLGATT-DLDVDGPLYVGGLPSlGVKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| LamG |
smart00282 |
Laminin G domain; |
2939-3068 |
1.49e-32 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 124.37 E-value: 1.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2939 VEFEFRTTRTTGVLLGISS-QKMDGMGIEMIDEKIMFHVDNGAGRFTAVYDagvPGHLCDGQWHTVRANKIKHRIELTVD 3017
Cdd:smart00282 2 ISFSFRTTSPNGLLLYAGSkGGGDYLALELRDGRLVLRYDLGSGPARLTSD---PTPLNDGQWHRVAVERNGRSVTLSVD 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1911235092 3018 G-NQVEAQSPnPASTSADTNDPVFVGGFPDGLNQFGLTINVPFRGCIRSLKL 3068
Cdd:smart00282 79 GgNRVSGESP-GGLTILNLDGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKV 129
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2318-2479 |
3.78e-32 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 123.68 E-value: 3.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2318 TIQFDGEGYAMVSRPIRWYPNiSTVMFKFRTFSSSALLMYLATKDLKDFMSVELTDGHIKVSYDLGSGMASVVSNQNHND 2397
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRTR-LSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLND 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2398 GKWKSFTLSRIQKQANISIididtNQEENIATSSSGNNFGLDLkaDDKIYFGGLPTlrnlSMKARPEVNLKKYSGCLKDI 2477
Cdd:cd00110 80 GQWHSVSVERNGRSVTLSV-----DGERVVESGSPGGSALLNL--DGPLYLGGLPE----DLKSPGLPVSPGFVGCIRDL 148
|
..
gi 1911235092 2478 EI 2479
Cdd:cd00110 149 KV 150
|
|
| LamB |
smart00281 |
Laminin B domain; |
582-716 |
5.01e-31 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 119.67 E-value: 5.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 582 LPQEYFWSAPAPYLGNKLTAAGGQLTFTISYDLeeeeeEEETARVLQLMIILEGKDLRISTAQEEvELRPSEDYIHALPL 661
Cdd:smart00281 1 DNEPVYWVAPEQFLGDKVTSYGGKLRYTLSFDG-----RRGGTHVSAPDVILEGNGLRISHPAEG-PPLPDELTTVEVRF 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1911235092 662 KEDSFTIHGtDFPVSRKEFMTVLVDLKRILIQITDSLGVDAIYrLSSVGLASAVP 716
Cdd:smart00281 75 REENWQYYG-GRPVTREDLMMVLANLTAILIRATYSQQMAGSR-LSDVSLEVAVP 127
|
|
| LamG |
smart00282 |
Laminin G domain; |
2341-2481 |
2.20e-30 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 118.21 E-value: 2.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2341 TVMFKFRTFSSSALLMYLATKDLKDFMSVELTDGHIKVSYDLGSGMASVVSNQNH-NDGKWKSFTLSRIQKQANISIidi 2419
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPlNDGQWHRVAVERNGRSVTLSV--- 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1911235092 2420 dtNQEENIATSSSGNNFGLDLkaDDKIYFGGLPTlrnlSMKARPEVNLKKYSGCLKDIEISR 2481
Cdd:smart00282 78 --DGGNRVSGESPGGLTILNL--DGPLYLGGLPE----DLKLPPLPVTPGFRGCIRNLKVNG 131
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2532-2670 |
1.54e-28 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 112.80 E-value: 1.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2532 FSTKNESGIILLGSggalrrkrRQTGQAYYAIFLNKGRLEVHLSTGARimRKIVVKPEPslFHDGREHSVHVERARGIFT 2611
Cdd:pfam00054 1 FRTTEPSGLLLYNG--------TQTERDFLALELRDGRLEVSYDLGSG--AAVVRSGDK--LNDGKWHSVELERNGRSGT 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1911235092 2612 VQVDEDRRHM--QNLTADQAIEV-KKLFVGGAPPE-FQPSPLRNIPPFEGCVWNLVINSVPMD 2670
Cdd:pfam00054 69 LSVDGEARPTgeSPLGATTDLDVdGPLYVGGLPSLgVKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2506-2665 |
8.10e-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: 8.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2506 TVSFPKPGFVELA-PVSISVGTEINLSFSTKNESGIILLGSGgalrrkrrQTGQAYYAIFLNKGRLEVHLSTGARimrKI 2584
Cdd:cd00110 1 GVSFSGSSYVRLPtLPAPRTRLSISFSFRTTSPNGLLLYAGS--------QNGGDFLALELEDGRLVLRYDLGSG---SL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2585 VVKPEPSLfHDGREHSVHVERARGIFTVQVDEDR--RHMQNLTADQAIEVKKLFVGGAPPEFQPSPLRNIPPFEGCVWNL 2662
Cdd:cd00110 70 VLSSKTPL-NDGQWHSVSVERNGRSVTLSVDGERvvESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDL 148
|
...
gi 1911235092 2663 VIN 2665
Cdd:cd00110 149 KVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
2147-2289 |
5.34e-27 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 108.58 E-value: 5.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2147 NIIVNVKTPVADNLLFYLGSAKFIDFLAIEMRKGKVSFLWDVGSGVGRVEYPDLTIDDSYWYRIEASRTGRNGSISVral 2226
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLNDGQWHRVAVERNGRSVTLSV--- 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1911235092 2227 DGPKASIVPstyhsaSPPGYTILDVDANamLFVGGLTGKLKKADAVRVITFTGCMGETYFDGK 2289
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 ... |
2943-3068 |
3.07e-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: 105.96 E-value: 3.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2943 FRTTRTTGVLLGISSQKMDGMGIEMIDEKIMFHVDNGAGRFTAVYdagVPGHLCDGQWHTVRANKIKHRIELTVDGNQVE 3022
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDFLALELVNGRLVLRYDLGSGPESLLS---SGKNLNDGQWHSVRVERNGNTLTLSVDGQTVV 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1911235092 3023 AQSPNPASTSADTNDPVFVGGFPDGLNQFGLTINVPFRGCIRSLKL 3068
Cdd:pfam02210 78 SSLPPGESLLLNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRV 123
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2128-2287 |
2.94e-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: 104.04 E-value: 2.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2128 SGGDCIRtYKPEIKKGSYNNIIVNVKTPVADNLLFYLGSAKFIDFLAIEMRKGKVSFLWDVGSGVGRVEYPDlTIDDSYW 2207
Cdd:cd00110 5 SGSSYVR-LPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKT-PLNDGQW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2208 YRIEASRTGRNGSISVralDGPKasivpsTYHSASPPGYTILDVDANamLFVGGLTGKLKKADAVRVITFTGCMGETYFD 2287
Cdd:cd00110 83 HSVSVERNGRSVTLSV---DGER------VVESGSPGGSALLNLDGP--LYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
2527-2667 |
2.59e-22 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 95.10 E-value: 2.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2527 EINLSFSTKNESGIILLGSGGAlrrkrrqtGQAYYAIFLNKGRLEVHLSTGARimrKIVVKPEPSLFHDGREHSVHVERA 2606
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKG--------GGDYLALELRDGRLVLRYDLGSG---PARLTSDPTPLNDGQWHRVAVERN 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1911235092 2607 RGIFTVQVD-EDRRHMQNLTADQAIEVK-KLFVGGAPPEFQPSPLRNIPPFEGCVWNLVINSV 2667
Cdd:smart00282 70 GRSVTLSVDgGNRVSGESPGGLTILNLDgPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1660-2127 |
1.31e-16 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 87.04 E-value: 1.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1660 IKGLVRDAEavnEKAKEVNETLGIQD--KAFErNMQGLQKEIDQMMREL-----RRKNLDTQKEVAEDELVAAEGLLKKV 1732
Cdd:PRK03918 137 IDAILESDE---SREKVVRQILGLDDyeNAYK-NLGEVIKEIKRRIERLekfikRTENIEELIKEKEKELEEVLREINEI 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1733 QKVFGEPRGKNEKMEKDLGE----------------KLTDHKNKLDDAWDLLREATDKTREANRLAAANQQNMTALEEKK 1796
Cdd:PRK03918 213 SSELPELREELEKLEKEVKEleelkeeieelekeleSLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKA 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1797 EAIESGKRQTENTLKEGNDILDEANRLADEINSVIDYVTDIQTK---LPPMSEELKDKIDDLSREMKDRKLAERVYQAEN 1873
Cdd:PRK03918 293 EEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKeerLEELKKKLKELEKRLEELEERHELYEEAKAKKE 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1874 HAAQLNASSAVL--DGILDEAKSISFNATAAFKAYSNIKDYIDEADKIAKEAKgLAHEATKLATG--P--QGSLKDGAKG 1947
Cdd:PRK03918 373 ELERLKKRLTGLtpEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELK-KAIEELKKAKGkcPvcGRELTEEHRK 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1948 SLQKSFgiLNEAKKLANNVKENDDDLNSLQTRLEKAD-VRNGELR-RALNDTLAKLSAIPNDT----AAKLQAAKNKARQ 2021
Cdd:PRK03918 452 ELLEEY--TAELKRIEKELKEIEEKERKLRKELRELEkVLKKESElIKLKELAEQLKELEEKLkkynLEELEKKAEEYEK 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2022 ANDTAKDVLAQVKDLHQDLDGLKKSYNQLA------DSVAKTNAVVKDPLKN---KIIADADATVKNLEQEADRLI---- 2088
Cdd:PRK03918 530 LKEKLIKLKGEIKSLKKELEKLEELKKKLAelekklDELEEELAELLKELEElgfESVEELEERLKELEPFYNEYLelkd 609
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1911235092 2089 ------DKLKPIKELEDNLKK---NISEIKELINQARKQANSIKVSVS 2127
Cdd:PRK03918 610 aekeleREEKELKKLEEELDKafeELAETEKRLEELRKELEELEKKYS 657
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
941-989 |
1.97e-14 |
|
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: 69.69 E-value: 1.97e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1911235092 941 PCRCHANGSFSEVCHTQTGQCECRPNVQGRRCDECKPETFGLQS-PRGCV 989
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSqGGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
942-988 |
7.93e-14 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 67.76 E-value: 7.93e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1911235092 942 CRCHANGSFSEVCHTQTGQCECRPNVQGRRCDECKPETFGLQ--SPRGC 988
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPsdPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
942-988 |
1.10e-13 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 67.34 E-value: 1.10e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1911235092 942 CRCHANGSFSEVCHTQTGQCECRPNVQGRRCDECKPETFGlQSPRGC 988
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYG-DGPPGC 46
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1660-2153 |
2.09e-13 |
|
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: 76.60 E-value: 2.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1660 IKGLVRDAEAVNEKAKEVN---ETLGIQDKAFERNMQGLQKEIDQMMRELRRKNLdtqkevaedelvaaegLLKKVQKvf 1736
Cdd:TIGR04523 147 IKKKEKELEKLNNKYNDLKkqkEELENELNLLEKEKLNIQKNIDKIKNKLLKLEL----------------LLSNLKK-- 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1737 geprgKNEKmEKDLGEKLTDHKNK---LDDAWDLLR-EATDKTREANR-------LAAANQQNMTALEEKKEAIESGKR- 1804
Cdd:TIGR04523 209 -----KIQK-NKSLESQISELKKQnnqLKDNIEKKQqEINEKTTEISNtqtqlnqLKDEQNKIKKQLSEKQKELEQNNKk 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1805 --QTENTLKEGNDILDEAN---------RLADEINSVIDYVTDIQTKLPPMSE---ELKDKIDDLSREM---------KD 1861
Cdd:TIGR04523 283 ikELEKQLNQLKSEISDLNnqkeqdwnkELKSELKNQEKKLEEIQNQISQNNKiisQLNEQISQLKKELtnsesenseKQ 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1862 RKLAERVYQAENHAAQlNASSavLDGILDEAKSISfnataafkaysNIKDYIDEADKIAKEakglaheatklatgpqgsl 1941
Cdd:TIGR04523 363 RELEEKQNEIEKLKKE-NQSY--KQEIKNLESQIN-----------DLESKIQNQEKLNQQ------------------- 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1942 KDGAKGSLQKSFGIL-NEAKKL-ANNVKEND--DDLN----SLQTRLEKADVRNGELRRALNDTLAKLSAIPNDTAAKLQ 2013
Cdd:TIGR04523 410 KDEQIKKLQQEKELLeKEIERLkETIIKNNSeiKDLTnqdsVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQK 489
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2014 AAKNKARQA---NDTAKDVLAQVKDLHQDLDGLKKSYNQLADSVAKTNAVVKDpLKNKIIA-DADATVKNLEQEADRLID 2089
Cdd:TIGR04523 490 ELKSKEKELkklNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISD-LEDELNKdDFELKKENLEKEIDEKNK 568
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1911235092 2090 KLKPIKELEDNLKKNISEIKELINQARKQANSIK-------VSVSSGGDCIRTYKPEIKKgsYNNIIVNVK 2153
Cdd:TIGR04523 569 EIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIkeieekeKKISSLEKELEKAKKENEK--LSSIIKNIK 637
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1655-2118 |
6.80e-13 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 74.80 E-value: 6.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1655 SLGDFIKGLVRDaeavnEKAKEVNETLGIQDKAFERNMQGLqKEIDQMMRELRRKNLDTQKevAEDELVAAEGLLKKVQK 1734
Cdd:COG4717 38 TLLAFIRAMLLE-----RLEKEADELFKPQGRKPELNLKEL-KELEEELKEAEEKEEEYAE--LQEELEELEEELEELEA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1735 VFGEPRGKNEKMEKDLG--------EKLTDHKNKLDDAWDLLREATDKTREA-NRLAAANQQnmtaLEEKKEAIESGKRQ 1805
Cdd:COG4717 110 ELEELREELEKLEKLLQllplyqelEALEAELAELPERLEELEERLEELRELeEELEELEAE----LAELQEELEELLEQ 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1806 TEN-TLKEGNDILDEANRLADEINSVIDYVTDIQTKLppmsEELKDKIDDLSREMKDRKLAERVYQAENHAAQLnASSAV 1884
Cdd:COG4717 186 LSLaTEEELQDLAEELEELQQRLAELEEELEEAQEEL----EELEEELEQLENELEAAALEERLKEARLLLLIA-AALLA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1885 LDGILDEAKSISFNATAAFKAYSNIkdYIDEADKIAKEAKGLAHEATKLATGP-QGSLKDGAKGSLQKSFGILNEAKKla 1963
Cdd:COG4717 261 LLGLGGSLLSLILTIAGVLFLVLGL--LALLFLLLAREKASLGKEAEELQALPaLEELEEEELEELLAALGLPPDLSP-- 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1964 NNVKENDDDLNSLQTRLEKADVRNGELRRA-LNDTLAKLSAIPN-DTAAKLQAAKNKARQANDTakdvLAQVKDLHQDLD 2041
Cdd:COG4717 337 EELLELLDRIEELQELLREAEELEEELQLEeLEQEIAALLAEAGvEDEEELRAALEQAEEYQEL----KEELEELEEQLE 412
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1911235092 2042 GLKKSYNQLADsvaktnavvkdplknkiiadaDATVKNLEQEADRLIDKLKPIKELEDNLKKNISEIKELINQARKQ 2118
Cdd:COG4717 413 ELLGELEELLE---------------------ALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEED 468
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
991-1035 |
1.19e-12 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 64.64 E-value: 1.19e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1911235092 991 CNCNSFGSKSFDCE-ESGQCWCQPGVTGKKCDHCAHGYFNFQEGGC 1035
Cdd:smart00180 1 CDCDPGGSASGTCDpDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
990-1036 |
1.68e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 61.22 E-value: 1.68e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1911235092 990 PCNCNSFGSKSFDCE-ESGQCWCQPGVTGKKCDHCAHGYFNF--QEGGCT 1036
Cdd:cd00055 1 PCDCNGHGSLSGQCDpGTGQCECKPNTTGRRCDRCAPGYYGLpsQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
888-940 |
1.99e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 61.22 E-value: 1.99e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1911235092 888 PCQCNDNldFSIPGSCDSLSGACLiCKPGTTGRYCELCADGYFGDAVDARNCQ 940
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. |
1130-1187 |
2.02e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 61.22 E-value: 2.02e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1911235092 1130 CNCFLPGTDDATCDSETkkcacmdqtGQCTCKVNVEGVHCDRCQPGTFGLDAKNPLGC 1187
Cdd:pfam00053 1 CDCNPHGSLSDTCDPET---------GQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1084-1132 |
2.20e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 60.83 E-value: 2.20e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1911235092 1084 CNCSTVGSLDFQCNINTGQCNCHPKFAGAKCTECSRGYWNYPHCDPCNC 1132
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1129-1187 |
8.95e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 59.29 E-value: 8.95e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1911235092 1129 PCNCFLPGTDDATCDSETkkcacmdqtGQCTCKVNVEGVHCDRCQPGTFGlDAKNPLGC 1187
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGT---------GQCECKPNTTGRRCDRCAPGYYG-LPSQGGGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1444-1490 |
9.82e-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: 9.82e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1444 CQCNGHSSL---CDPETSICQnCQHHTAGDFCERCALGYYGIVKGLPNDC 1490
Cdd:pfam00053 1 CDCNPHGSLsdtCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
419-476 |
1.38e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 58.52 E-value: 1.38e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1911235092 419 CHCDPVGSLSEVCVkdekhaprgLAPGSCHCKPGFGGERCDRCVRGYTGYPDCKPCNC 476
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. |
991-1038 |
2.13e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 58.13 E-value: 2.13e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1911235092 991 CNCNSFGSKSFDCE-ESGQCWCQPGVTGKKCDHCAHGYFNFQEGGCTAC 1038
Cdd:pfam00053 1 CDCNPHGSLSDTCDpETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1130-1187 |
2.73e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 57.71 E-value: 2.73e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1911235092 1130 CNCFLPGTDDATCDSETkkcacmdqtGQCTCKVNVEGVHCDRCQPGTFGldaKNPLGC 1187
Cdd:smart00180 1 CDCDPGGSASGTCDPDT---------GQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1083-1125 |
3.52e-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: 3.52e-10
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1911235092 1083 ACNCSTVGSLDFQCNINTGQCNCHPKFAGAKCTECSRGYWNYP 1125
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1839-2142 |
3.93e-10 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 63.78 E-value: 3.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1839 TKLPPMSEELKDKIDDLSREMKD--RKLAERVYQAENHAAQLNASSAVLDGILDEAKSI-----SFNAtaafkaysNIKD 1911
Cdd:COG1340 4 DELSSSLEELEEKIEELREEIEElkEKRDELNEELKELAEKRDELNAQVKELREEAQELrekrdELNE--------KVKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1912 YIDEADKIAKEAKGLAHEATKLatgpqgslkdgakgslQKSFGILNEAKKLANNVKEnddDLNSLQTRLEKADVrNGELR 1991
Cdd:COG1340 76 LKEERDELNEKLNELREELDEL----------------RKELAELNKAGGSIDKLRK---EIERLEWRQQTEVL-SPEEE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1992 RALNDTLAKLsaipndtAAKLQAAKnKARQANDTAKDVLAQVKDLHQDLDGLKKSYNQLADSVAKtnavvkdpLKNKIIa 2071
Cdd:COG1340 136 KELVEKIKEL-------EKELEKAK-KALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQE--------LHEEMI- 198
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1911235092 2072 dadatvkNLEQEADRLIDKLKPIKELEDNLKKNISEIKELINQARKQANSIKVSVSSggdcIRTYKPEIKK 2142
Cdd:COG1340 199 -------ELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKK----LRKKQRALKR 258
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1443-1491 |
4.00e-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: 57.36 E-value: 4.00e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1911235092 1443 PCQCNGHSSL---CDPETSICQnCQHHTAGDFCERCALGYYGIVKGlPNDCQ 1491
Cdd:cd00055 1 PCDCNGHGSLsgqCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQ-GGGCQ 50
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1589-1997 |
6.71e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 65.06 E-value: 6.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1589 DLENRTQELKHLLSPQRAPerlIQLAEGNLNTLVTEMNELLTRATKV---TADGEQTGQDAERTSR-RANSLgdfikglv 1664
Cdd:PRK02224 318 ELEDRDEELRDRLEECRVA---AQAHNEEAESLREDADDLEERAEELreeAAELESELEEAREAVEdRREEI-------- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1665 rdaEAVNEKAKEVNETLGIQDKAFErNMQGLQKEIDQMMRELR--RKNLDTQKEVAEDELVAAEGLLKK------VQKVF 1736
Cdd:PRK02224 387 ---EELEEEIEELRERFGDAPVDLG-NAEDFLEELREERDELRerEAELEATLRTARERVEEAEALLEAgkcpecGQPVE 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1737 GEP--------RGKNEKME---KDLGEKLTDHKNKLDDAWDLLREATDKTREANRLAAANQ---QNMTALEEKKEAIESG 1802
Cdd:PRK02224 463 GSPhvetieedRERVEELEaelEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEEliaERRETIEEKRERAEEL 542
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1803 KRQTENTLKEGNDILDEANRLADEINSVIDYVTDIQTKLppmsEELKDKIDDLSR----------------EMKDRK--L 1864
Cdd:PRK02224 543 RERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKL----AELKERIESLERirtllaaiadaedeieRLREKReaL 618
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1865 AERVYQAENHAAQLNASSAVLDGILDEAksisfNATAAFKAYSNIKDYIDEADKiakeakglaheatKLATgpqgslKDG 1944
Cdd:PRK02224 619 AELNDERRERLAEKRERKRELEAEFDEA-----RIEEAREDKERAEEYLEQVEE-------------KLDE------LRE 674
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1911235092 1945 AKGSLQKSFG-ILNEAKKLaNNVKENDDDLNSLQTRLE----------------KADVRN---GELRRALNDT 1997
Cdd:PRK02224 675 ERDDLQAEIGaVENELEEL-EELRERREALENRVEALEalydeaeelesmygdlRAELRQrnvETLERMLNET 746
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
780-829 |
7.40e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 56.59 E-value: 7.40e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1911235092 780 PCQCFGHAD---SCDDITAECLnCRDHTGGPYCNQCLPGFYGDPTKGtaEDCQ 829
Cdd:cd00055 1 PCDCNGHGSlsgQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQG--GGCQ 50
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1583-2111 |
9.82e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 64.68 E-value: 9.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1583 PYKMLYDLENRTQELKHLLSpqRAPERLIQLAE--GNLNTLVTEMNELLTRATKVTADGEQTGQDAERTSRRANSLGDFI 1660
Cdd:PRK02224 204 LHERLNGLESELAELDEEIE--RYEEQREQAREtrDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEV 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1661 KGLVRDAEAVNEKAKEVNETLGIQD---KAFERNMQGLQKEIDQMMRELRRKNLDTQKEVAEdelvaAEGLLKKVQKVFG 1737
Cdd:PRK02224 282 RDLRERLEELEEERDDLLAEAGLDDadaEAVEARREELEDRDEELRDRLEECRVAAQAHNEE-----AESLREDADDLEE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1738 EPRGKNEK---MEKDL---GEKLTDHKNKLDDawdlLREATDKTREANRLAAANQQNMTA----LEEKKEAIESGKRQTE 1807
Cdd:PRK02224 357 RAEELREEaaeLESELeeaREAVEDRREEIEE----LEEEIEELRERFGDAPVDLGNAEDfleeLREERDELREREAELE 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1808 NTLKEGNDILDEANRLADEinsvidyvtdiqTKLPPMSEELKD------------KIDDLSREMKDRKLA-ERVYQAENH 1874
Cdd:PRK02224 433 ATLRTARERVEEAEALLEA------------GKCPECGQPVEGsphvetieedreRVEELEAELEDLEEEvEEVEERLER 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1875 AAQLNASSAVLDGILDEAKsisfnataafkaysNIKDYIDEADKIAKE----AKGLAHEATKLATGPQGSLKDGAKGSLq 1950
Cdd:PRK02224 501 AEDLVEAEDRIERLEERRE--------------DLEELIAERRETIEEkrerAEELRERAAELEAEAEEKREAAAEAEE- 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1951 ksfgilnEAKKLANNVKENDDDLNSLQTRLEkadvrngelrrALNDTLAKLSAIPN--DTAAKLQAaKNKARQA-NDTAK 2027
Cdd:PRK02224 566 -------EAEEAREEVAELNSKLAELKERIE-----------SLERIRTLLAAIADaeDEIERLRE-KREALAElNDERR 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2028 DVLAQVKDLHQDLDglkksynqladsvaktnavvkDPLKNKIIADADATVKNLEQEADRLIDKLKPIKELEDNLKKNI-- 2105
Cdd:PRK02224 627 ERLAEKRERKRELE---------------------AEFDEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIga 685
|
....*...
gi 1911235092 2106 --SEIKEL 2111
Cdd:PRK02224 686 veNELEEL 693
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1038-1076 |
1.13e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.17 E-value: 1.13e-09
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1911235092 1038 CDCS---HLGNNCDPKTGRCICPPNTIGDQCSQCVPNTWGHS 1076
Cdd:smart00180 1 CDCDpggSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1037-1082 |
1.16e-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: 56.21 E-value: 1.16e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1037 ACDCSHLG---NNCDPKTGRCICPPNTIGDQCSQCVPNTWGHSII-SGCK 1082
Cdd:cd00055 1 PCDCNGHGslsGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQgGGCQ 50
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1684-1922 |
1.73e-09 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 61.85 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1684 QDKAFERNMQGLQKEIDQM---MRELRRKNLDTQKEVAEdelVAAE--GLLKKVQKVFGEPRGKNEKMeKDLGEKLTDHK 1758
Cdd:COG1340 2 KTDELSSSLEELEEKIEELreeIEELKEKRDELNEELKE---LAEKrdELNAQVKELREEAQELREKR-DELNEKVKELK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1759 NKLDDAWDLLREATDKTREANRLAAANQQNMTALEEKKEAIES--GKRQTEN-TLKEGNDILDEANRL------ADEINS 1829
Cdd:COG1340 78 EERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERleWRQQTEVlSPEEEKELVEKIKELekelekAKKALE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1830 VIDYVTDIQTKLppmsEELKDKIDDLSREMKdrKLAErvyQAENHAAQLNASSAVLDGILDEAKSisfnataafkAYSNI 1909
Cdd:COG1340 158 KNEKLKELRAEL----KELRKEAEEIHKKIK--ELAE---EAQELHEEMIELYKEADELRKEADE----------LHKEI 218
|
250
....*....|...
gi 1911235092 1910 KDYIDEADKIAKE 1922
Cdd:COG1340 219 VEAQEKADELHEE 231
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
889-932 |
2.85e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 55.01 E-value: 2.85e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1911235092 889 CQCNdnLDFSIPGSCDSLSGACLiCKPGTTGRYCELCADGYFGD 932
Cdd:smart00180 1 CDCD--PGGSASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD 41
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
418-470 |
3.00e-09 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 55.05 E-value: 3.00e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1911235092 418 PCHCDPVGSLSEVCVKDEkhaprglapGSCHCKPGFGGERCDRCVRGYTGYPD 470
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. |
474-520 |
3.77e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 54.67 E-value: 3.77e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1911235092 474 CNCSGEGSANE--DPCFGPCHCKENVEGGDCSRCKSGFFNLQESNQKGC 520
Cdd:pfam00053 1 CDCNPHGSLSDtcDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
889-938 |
4.16e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 54.67 E-value: 4.16e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1911235092 889 CQCNDNLdfSIPGSCDSLSGACLiCKPGTTGRYCELCADGYFGDAVDARN 938
Cdd:pfam00053 1 CDCNPHG--SLSDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQ 47
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1697-2162 |
5.85e-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: 62.38 E-value: 5.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1697 KEIDQMMRELRRKNLDTQKEVaEDELVAAEGLLKKVQK--VFGEPRGKNEKM--EKDLGE---KLTDHKNKLddawdLLR 1769
Cdd:TIGR01612 1361 KKIIDEVKEYTKEIEENNKNI-KDELDKSEKLIKKIKDdiNLEECKSKIESTldDKDIDEcikKIKELKNHI-----LSE 1434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1770 EATDKT-----REANRLAAANQQNMTALEEKKEAIESGKRQTE--------NTLKEGND----ILDEA--NRLADEINSV 1830
Cdd:TIGR01612 1435 ESNIDTyfknaDENNENVLLLFKNIEMADNKSQHILKIKKDNAtndhdfniNELKEHIDkskgCKDEAdkNAKAIEKNKE 1514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1831 I--DYVTDIQTKLPPMSE-ELKDKIDD-------LSREMKDRKlAERVYQAENHAAQLNASSAVLDGILDEAKSISFNAT 1900
Cdd:TIGR01612 1515 LfeQYKKDVTELLNKYSAlAIKNKFAKtkkdseiIIKEIKDAH-KKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNK 1593
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1901 AAFKAYSNIKDYIDEADKIakeakglaheaTKLATGPQGSLKDGAkgSLQK---SFGILNEAKKLannvKENDDDLNSLQ 1977
Cdd:TIGR01612 1594 AAIDIQLSLENFENKFLKI-----------SDIKKKINDCLKETE--SIEKkisSFSIDSQDTEL----KENGDNLNSLQ 1656
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1978 TRLE--KADVRNGE-LRRALNDTLAKLSAIPNDTAaklQAAKN-------KARQANDTAKDVLAQVKDLHQ--------- 2038
Cdd:TIGR01612 1657 EFLEslKDQKKNIEdKKKELDELDSEIEKIEIDVD---QHKKNyeigiieKIKEIAIANKEEIESIKELIEptienliss 1733
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2039 ----DLDGLK--------------------KSYNQLA---DSVAKtNAVVKDPLKNKIIADADATVKNLEQEadrlidkl 2091
Cdd:TIGR01612 1734 fntnDLEGIDpnekleeynteigdiyeefiELYNIIAgclETVSK-EPITYDEIKNTRINAQNEFLKIIEIE-------- 1804
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1911235092 2092 KPIKELEDNLKknISEIKELINQARKQANSIKVSVSsggdciRTYKpEIKKGsYNNI---IVNVKTPVADNLLF 2162
Cdd:TIGR01612 1805 KKSKSYLDDIE--AKEFDRIINHFKKKLDHVNDKFT------KEYS-KINEG-FDDIsksIENVKNSTDENLLF 1868
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1084-1127 |
6.56e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 53.85 E-value: 6.56e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1911235092 1084 CNCSTVGSLDFQCNINTGQCNCHPKFAGAKCTECSRGYW--NYPHC 1127
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYgdGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1038-1081 |
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 1911235092 1038 CDCSHLG---NNCDPKTGRCICPPNTIGDQCSQCVPNTWGHSIISGC 1081
Cdd:pfam00053 1 CDCNPHGslsDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQ 47
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1955-2124 |
1.33e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 59.92 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1955 ILNEAKKLANNVKENDDDLNSLQTRLEKAdvrNGELRRA------LNDTLAKLSAIPNDTAAKLQAAKNKARQANDTAKD 2028
Cdd:COG4372 43 LQEELEQLREELEQAREELEQLEEELEQA---RSELEQLeeeleeLNEQLQAAQAELAQAQEELESLQEEAEELQEELEE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2029 VLAQVKDLHQDLDGLKKSYNQLadsvaktnavvkdplkNKIIADADATVKNLEQEADRLIDKLKPIKELEDNLKKN--IS 2106
Cdd:COG4372 120 LQKERQDLEQQRKQLEAQIAEL----------------QSEIAEREEELKELEEQLESLQEELAALEQELQALSEAeaEQ 183
|
170
....*....|....*...
gi 1911235092 2107 EIKELINQARKQANSIKV 2124
Cdd:COG4372 184 ALDELLKEANRNAEKEEE 201
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
419-471 |
1.63e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 52.70 E-value: 1.63e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1911235092 419 CHCDPVGSLSEVCVKDEkhaprglapGSCHCKPGFGGERCDRCVRGYTG--YPDC 471
Cdd:smart00180 1 CDCDPGGSASGTCDPDT---------GQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
781-828 |
1.67e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 52.74 E-value: 1.67e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1911235092 781 CQCFGHA---DSCDDITAECLnCRDHTGGPYCNQCLPGFYGDPtKGTAEDC 828
Cdd:pfam00053 1 CDCNPHGslsDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLP-SDPPQGC 49
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1672-2122 |
4.44e-08 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 58.93 E-value: 4.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1672 EKAKEVNETLGIQDK------------AFERNMQGLQKEIDQMMRELRRknLDTQKEvaeDELVAAEGLLKKVQkvfgEP 1739
Cdd:pfam05622 29 EKNSLQQENKKLQERldqlesgddsgtPGGKKYLLLQKQLEQLQEENFR--LETARD---DYRIKCEELEKEVL----EL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1740 RGKNEKMEKdlgekLTDHKNKLDDAWDLLREATDKtreANRLaaanQQNMTALEEKKEAIESGKRQTEnTLKEGN----- 1814
Cdd:pfam05622 100 QHRNEELTS-----LAEEAQALKDEMDILRESSDK---VKKL----EATVETYKKKLEDLGDLRRQVK-LLEERNaeymq 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1815 ---DILDEANRLADEINSVIDY---VTDIQTKLppmSEE-------------LKDKIDDLSREmKDRKLAER--VYQA-- 1871
Cdd:pfam05622 167 rtlQLEEELKKANALRGQLETYkrqVQELHGKL---SEEskkadklefeykkLEEKLEALQKE-KERLIIERdtLRETne 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1872 ENHAAQLNASSAVLDGILDEAKSISFNATAAFKAYSNIKDYIDEadkiakeakgLAHEaTKLatgpqgsLKDGAKGSlqk 1951
Cdd:pfam05622 243 ELRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIR----------LQHE-NKM-------LRLGQEGS--- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1952 sfgilneakklannvkeNDDDLNSLQTRLEKADVRNGELR---RALNDTLAKLSAIPNDTAAKLQAAKNKARQANDTAKD 2028
Cdd:pfam05622 302 -----------------YRERLTELQQLLEDANRRKNELEtqnRLANQRILELQQQVEELQKALQEQGSKAEDSSLLKQK 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2029 VLAQVKDLHQDLDGLKKSYNQLADSVAK--TNAVVK-DPLKNKIIAdADATVKNLEQEADRLIDKLKP-IKELEDnlKKN 2104
Cdd:pfam05622 365 LEEHLEKLHEAQSELQKKKEQIEELEPKqdSNLAQKiDELQEALRK-KDEDMKAMEERYKKYVEKAKSvIKTLDP--KQN 441
|
490 500
....*....|....*....|.
gi 1911235092 2105 ---ISEIKELINQARKQANSI 2122
Cdd:pfam05622 442 pasPPEIQALKNQLLEKDKKI 462
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1884-2124 |
6.22e-08 |
|
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: 57.38 E-value: 6.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1884 VLDGILDEAKSIS-FNATAAFKA---YSNIKDYIDEADKIAKEAKglaheatklatgpQGSLKDGAKGSLQKsfgILNEA 1959
Cdd:cd22656 67 TYPSIVSLAGDIYnYAQNAGGTIdsyYAEILELIDDLADATDDEE-------------LEEAKKTIKALLDD---LLKEA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1960 KKLANNVKENDDDLNSLQTRLEKADVRNGELRRALNDTL-AKLSAIPNDTAAKLQAAKNKARQAndtakdvlaQVKDLHQ 2038
Cdd:cd22656 131 KKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLLtDEGGAIARKEIKDLQKELEKLNEE---------YAAKLKA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2039 DLDGLKKSYNQLADSVAKTNAVVKDplknkiIADADATVKNLEQEADRLIDKLKPIKELEDNLKKNISEIKELINQARKQ 2118
Cdd:cd22656 202 KIDELKALIADDEAKLAAALRLIAD------LTAADTDLDNLLALIGPAIPALEKLQGAWQAIATDLDSLKDLLEDDISK 275
|
....*.
gi 1911235092 2119 ANSIKV 2124
Cdd:cd22656 276 IPAAIL 281
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1444-1490 |
5.71e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 48.46 E-value: 5.71e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1444 CQCN--GHSSL-CDPETSICQnCQHHTAGDFCERCALGYYGIVkglPNDC 1490
Cdd:smart00180 1 CDCDpgGSASGtCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDG---PPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
473-520 |
6.12e-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: 6.12e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1911235092 473 PCNCSGEGSANE--DPCFGPCHCKENVEGGDCSRCKSGFFNLQeSNQKGC 520
Cdd:cd00055 1 PCDCNGHGSLSGqcDPGTGQCECKPNTTGRRCDRCAPGYYGLP-SQGGGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
292-339 |
1.08e-06 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 47.73 E-value: 1.08e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1911235092 292 CICFGHA---RACplDPVTnkSRCECEHNTCGDSCDQCCPGFHQKPWRAGT 339
Cdd:cd00055 2 CDCNGHGslsGQC--DPGT--GQCECKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
781-823 |
1.38e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 47.31 E-value: 1.38e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1911235092 781 CQC--FGHAD-SCDDITAECLnCRDHTGGPYCNQCLPGFYGDPTKG 823
Cdd:smart00180 1 CDCdpGGSASgTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
474-511 |
4.10e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 45.77 E-value: 4.10e-06
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1911235092 474 CNCSGEGSANE--DPCFGPCHCKENVEGGDCSRCKSGFFN 511
Cdd:smart00180 1 CDCDPGGSASGtcDPDTGQCECKPNVTGRRCDRCAPGYYG 40
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1663-1863 |
4.69e-06 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 50.14 E-value: 4.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1663 LVRDAEAV----NEKAKEVNETLGIQD-----------KAFERNMQGLQKEIDQMMrelrrknlDTQKEVAEDELVAAEG 1727
Cdd:cd00176 5 FLRDADELeawlSEKEELLSSTDYGDDlesveallkkhEALEAELAAHEERVEALN--------ELGEQLIEEGHPDAEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1728 LLKKVQKVfgeprgknEKMEKDLGEKLTDHKNKLDDAWDLLREATDKTREANRL-----AAANQQNMTALEEKKEAIESG 1802
Cdd:cd00176 77 IQERLEEL--------NQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLeekeaALASEDLGKDLESVEELLKKH 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1911235092 1803 KrQTENTLKEGNDILDEANRLADE-INSVIDYVTD-IQTKLppmsEELKDKIDDLSREMKDRK 1863
Cdd:cd00176 149 K-ELEEELEAHEPRLKSLNELAEElLEEGHPDADEeIEEKL----EELNERWEELLELAEERQ 206
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1493-1548 |
4.73e-06 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 45.81 E-value: 4.73e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1911235092 1493 CACPLISSSnnfSPSCVMEGlddYRCTaCPRGYEGQYCERCAPGYTGSPSSPGGSC 1548
Cdd:pfam00053 1 CDCNPHGSL---SDTCDPET---GQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
831-886 |
6.29e-06 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 45.42 E-value: 6.29e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1911235092 831 CACPLNIPSnnfSPTCHldrSLGLICDeCPVGYAGPRCERCAEGYFGQPSVAGGSC 886
Cdd:pfam00053 1 CDCNPHGSL---SDTCD---PETGQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1590-1861 |
7.83e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.99 E-value: 7.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1590 LENRTQELKHLLSPQRAPERLIqlaEGNLNTLVTEMNELLTRATKVTADGEQTGQDAERTSRRANSLGDFIKGLVRDAEA 1669
Cdd:TIGR02169 679 LRERLEGLKRELSSLQSELRRI---ENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIEN 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1670 VNEKAKEVNETLG---------------IQDKAFERNMQGLQKEIDQMMRELRR------------KNLDTQKEVAEDE- 1721
Cdd:TIGR02169 756 VKSELKELEARIEeleedlhkleealndLEARLSHSRIPEIQAELSKLEEEVSRiearlreieqklNRLTLEKEYLEKEi 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1722 ------LVAAEGLLKKVQKVFGEPRGKNEKME----------KDLGEKLTDHKNKLDDAWDLLREATDKTREANRLAAAN 1785
Cdd:TIGR02169 836 qelqeqRIDLKEQIKSIEKEIENLNGKKEELEeeleeleaalRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKK 915
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1786 QQNMTALEEKKEAIESGKRQTENTLKEGNDI-----------------------LDEANRLA-DEINSVIDYVTDIQTKL 1841
Cdd:TIGR02169 916 RKRLSELKAKLEALEEELSEIEDPKGEDEEIpeeelsledvqaelqrveeeiraLEPVNMLAiQEYEEVLKRLDELKEKR 995
|
330 340
....*....|....*....|...
gi 1911235092 1842 PPMSEE---LKDKIDDLSREMKD 1861
Cdd:TIGR02169 996 AKLEEErkaILERIEEYEKKKRE 1018
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
830-887 |
9.18e-06 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 45.04 E-value: 9.18e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1911235092 830 PCACPLNIpsnNFSPTCHLDrslGLICdECPVGYAGPRCERCAEGYFGQPSVAGGsCQ 887
Cdd:cd00055 1 PCDCNGHG---SLSGQCDPG---TGQC-ECKPNTTGRRCDRCAPGYYGLPSQGGG-CQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
831-879 |
2.38e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 43.84 E-value: 2.38e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1911235092 831 CACPlniPSNNFSPTCHLDrslGLICdECPVGYAGPRCERCAEGYFGQP 879
Cdd:smart00180 1 CDCD---PGGSASGTCDPD---TGQC-ECKPNVTGRRCDRCAPGYYGDG 42
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1608-1837 |
4.58e-05 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 49.44 E-value: 4.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1608 ERLIQLAEGNLNTLVTEMNElltRATKVTADGEQTG--------QDAERTSRRA----NSL--------GDFIKGLVRDA 1667
Cdd:NF041483 1040 DTLITEAAAEADQLTAKAQE---EALRTTTEAEAQAdtmvgaarKEAERIVAEAtvegNSLvekartdaDELLVGARRDA 1116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1668 EAVNEKAKEVNETLgiqdkafernmqglQKEIDQMMRELRRKNLDTQKEVAE--DELV-AAEgllkkvqkvfgEPRGKNE 1744
Cdd:NF041483 1117 TAIRERAEELRDRI--------------TGEIEELHERARRESAEQMKSAGErcDALVkAAE-----------EQLAEAE 1171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1745 KMEKDLGEKLTDHKNKL-----DDAWDLLREATDK----TREANRLAAanqqnmTALEEKKEAIESGKRQtentlkegnd 1815
Cdd:NF041483 1172 AKAKELVSDANSEASKVriaavKKAEGLLKEAEQKkaelVREAEKIKA------EAEAEAKRTVEEGKRE---------- 1235
|
250 260
....*....|....*....|..
gi 1911235092 1816 iLDEANRLADEINSVIDYVTDI 1837
Cdd:NF041483 1236 -LDVLVRRREDINAEISRVQDV 1256
|
|
| alph_xenorhab_A |
NF033928 |
alpha-xenorhabdolysin family binary toxin subunit A; Alpha-xenorhabdolysin was the founding ... |
1825-2123 |
4.71e-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: 48.45 E-value: 4.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1825 DEINSVIDYVTDIQ---TKLPPMSEELK-DKIDDLSREMKDrklAERVYQAENHAAQlnaS-SAVLDGILDEAKSISfNA 1899
Cdd:NF033928 6 EDWISIQKYVQAALalpTTLEEVESYLGyPKDGIPGLEPKD---LLDLFQNIRNHAR---SwSNLEPKIKQLANDLA-NY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1900 TAAFKAYSN-IKDYIDEADkIAKEAKGLAHEATKLATGPQGSLKDGAKGSLQKsfgILneaKKLANNVKENDDDLNSLQT 1978
Cdd:NF033928 79 ARNIVVTGNpIIDLINEMP-IIKRGDLTEEELSELPPIPLSSDDKEIVKELKE---IL---EDLKNDIKDYQQKADDVKK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1979 RLekadvrnGELRRALNDTLakLSAIpndtAAKLQAAKNKarQANDTAKDVLAQVKDLHQDLDGLKKSYNQLADSVAKTn 2058
Cdd:NF033928 152 EL-------DDFENDLREEL--LPQL----KLKKKLYDDN--LGSDSIEELREKIDQLEKEIEQLNKEYDDYVKLSFTG- 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1911235092 2059 aVVKDPLKNKIIA--------DADATVKNLEQEADRLIDKLK---PIKELEDNLKKNISEIKELINQARKQANSIK 2123
Cdd:NF033928 216 -LAGGPIGLAITGgifgskaeKIRKEKNALIQEIDELQEQLKkknALLGSLERLQTSLDDILTRMEDALPALKKLK 290
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1493-1549 |
1.77e-04 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 41.57 E-value: 1.77e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1911235092 1493 CACPLISSSNnfsPSCVMEGLddyRCTaCPRGYEGQYCERCAPGYTGSPSSPGGsCQ 1549
Cdd:cd00055 2 CDCNGHGSLS---GQCDPGTG---QCE-CKPNTTGRRCDRCAPGYYGLPSQGGG-CQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
311-335 |
2.49e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 40.76 E-value: 2.49e-04
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1403-1431 |
3.14e-04 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 40.80 E-value: 3.14e-04
10 20
....*....|....*....|....*....
gi 1911235092 1403 RCDCPPGYSGLSCETCLPGFYRLRSGPGV 1431
Cdd:pfam00053 19 QCLCKPGVTGRHCDRCKPGYYGLPSDPPQ 47
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1493-1541 |
6.03e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 39.99 E-value: 6.03e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1911235092 1493 CACPLissSNNFSPSCVmegLDDYRCTaCPRGYEGQYCERCAPGYTGSP 1541
Cdd:smart00180 1 CDCDP---GGSASGTCD---PDTGQCE-CKPNVTGRRCDRCAPGYYGDG 42
|
|
| TNFRSF16 |
cd13416 |
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 ... |
795-943 |
6.81e-04 |
|
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 neurotrophin receptor (p75NTR) or CD271; TNFRSF16 (also known as nerve growth factor receptor (NGFR) or p75 neurotrophin receptor (p75NTR or p75(NTR)), CD271, Gp80-LNGFR) is a common receptor for both neurotrophins and proneurotrophins, and plays a diverse role in many tissues, including the nervous system. It has been shown to be expressed in various types of stem cells and has been used to prospectively isolate stem cells with different degrees of potency. p75NTR owes its signaling to the recruitment of intracellular binding proteins, leading to the activation of different signaling pathways. It binds nerve growth factor (NGF) and the complex can initiate a signaling cascade which has been associated with both neuronal apoptosis and neuronal survival of discrete populations of neurons, depending on the presence or absence of intracellular signaling molecules downstream of p75NTR (e.g. NF-kB, JNK, or p75NTR intracellular death domain). p75NTR can also bind NGF in concert with the neurotrophic tyrosine kinase receptor type 1 (TrkA) protein where it is thought to modulate the formation of the high-affinity neurotrophin binding complex. On melanoma cell, p75NTR is an immunosuppressive factor, induced by interferon (IFN)-gamma, and mediates down-regulation of melanoma antigens. It can interact with the aggregated form of amyloid beta (Abeta) peptides, and plays an important role in etiopathogenesis of Alzheimer's disease by influencing protein tau hyper-phosphorylation. p75(NTR) is involved in the formation and progression of retina diseases; its expression is induced in retinal pigment epithelium (RPE) cells and its knockdown rescues RPE cell proliferation activity and inhibits RPE apoptosis induced by hypoxia. It can therefore be a potential therapeutic target for RPE hypoxia or oxidative stress diseases.
Pssm-ID: 276921 [Multi-domain] Cd Length: 159 Bit Score: 42.67 E-value: 6.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 795 AECLNCRDHTGGPYCNQCLPGFyGDPTKGTAED--CQPCacplnIPSNNFSPT-CHLDRSlgLICDECPvGYAGPRCE-- 869
Cdd:cd13416 1 EACPSGQYTSSGECCEQCPPGE-GVARPCGDNQtvCEPC-----LDGVTFSDVvSHTEPC--QPCTRCP-GLMSMRAPct 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 870 -------RCAEGYFgqPSVAGGSCQPCQcndnldfsipgSCDSLSGACLICKPGTTGRyCELCADGYFGDAVDARN-CQP 941
Cdd:cd13416 72 athdtvcECAYGYY--LDEDSGTCEPCT-----------VCPPGQGVVQSCGPNQDTV-CEACPEGTYSDEDSSTDpCLP 137
|
..
gi 1911235092 942 CR 943
Cdd:cd13416 138 CT 139
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1403-1430 |
1.44e-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: 38.87 E-value: 1.44e-03
10 20
....*....|....*....|....*...
gi 1911235092 1403 RCDCPPGYSGLSCETCLPGFYRLRSGPG 1430
Cdd:cd00055 20 QCECKPNTTGRRCDRCAPGYYGLPSQGG 47
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1403-1424 |
9.60e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 36.52 E-value: 9.60e-03
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
38-290 |
1.95e-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: 300.05 E-value: 1.95e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 38 AHQQRGLFPAVLNLASNAYITTNATCGEKGPEMYCKLVEHVpgqpVRDPQCRICNQNssNPNQRHPITNAIDGKN----T 113
Cdd:smart00136 1 AGRPRSCYPPFVNLAFGREVTATSTCGEPGPERYCKLVGHT----EQGKKCDYCDAR--NPRRSHPAENLTDGNNpnnpT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 114 WWQSPSIKNGIeyHYVTITLDLQQVFQIAYVIVKAAnSPRPGNWILERSLDDVEYKPWQYHAvtdTECLTLYNIyPRTGP 193
Cdd:smart00136 75 WWQSEPLSNGP--QNVNLTLDLGKEFHVTYVILKFC-SPRPSLWILERSDFGKTWQPWQYFS---SDCRRTFGR-PPRGP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 194 PSYSKDDEVICTSFYSKIHPLENGEIHISLINGRPSADDP--SPELLEFTSARYIRLRFQRIRTLNADLMMfahkdpreI 271
Cdd:smart00136 148 ITKGNEDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDFdnSPVLQEWVTATNIRVRLTRLRTLGDELMD--------D 219
|
250
....*....|....*....
gi 1911235092 272 DPIVTRRYYYSVKDISVGG 290
Cdd:smart00136 220 RPEVTRRYYYAISDIAVGG 238
|
|
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
44-290 |
1.03e-87 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 286.40 E-value: 1.03e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 44 LFPAVLNLASNAYITTNATCGEKGPEMYCKLVEHVPGQpvrdpQCRICNqnSSNPNQRHPITNAIDGKN----TWWQSPS 119
Cdd:pfam00055 1 CYPAFGNLAFGREVSATSTCGLNGPERYCILSGLEGGK-----KCFICD--SRDPHNSHPPSNLTDSNNgtneTWWQSET 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 120 IKngIEYHYVTITLDLQQVFQIAYVIVKAAnSPRPGNWILERSLD-DVEYKPWQYHAvtdTECLTLYNIypRTGPPSYSK 198
Cdd:pfam00055 74 GV--IQYENVNLTLDLGKEFHFTYLILKFK-SPRPAAMVLERSTDfGKTWQPYQYFA---SDCRRTFGR--PSGPSRGIK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 199 DDEVICTSFYSKIHPLENGEIHISLINGRPSA--DDPSPELLEFTSARYIRLRFQRIRTLNadlmmfahkDPREIDPIVT 276
Cdd:pfam00055 146 DDEVICTSEYSDISPLTGGEVIFSTLEGRPSAniFDYSPELQDWLTATNIRIRLLRLHTLG---------DELLDDPSVL 216
|
250
....*....|....
gi 1911235092 277 RRYYYSVKDISVGG 290
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 ... |
1573-1830 |
7.76e-86 |
|
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: 281.99 E-value: 7.76e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1573 SIN-LTGPLPAPYKMLYDLENRTQELKHLLSPQRAPERLIQLAEGNLNTLVTEMNELLTRATKVTADGEQTGQDAERTSR 1651
Cdd:pfam06008 3 SLNsLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1652 RANSLGDFIKGLVRDAEAVNEKAKEVNETlgiQDKAFERNMQGLQKEIDQMMRELRRKNLDTQKEVAEDELVAAEGLLKK 1731
Cdd:pfam06008 83 HAKELAEAIKNLIDNIKEINEKVATLGEN---DFALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQDLLSR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1732 VQKVFGEPRGKNEKMEKDLGEKLTDHKNKLDDAWDLLREATDKTREANRLAAANQQNMTALEEKKEAIESGKRQTENTLK 1811
Cdd:pfam06008 160 IQTWFQSPQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEETLK 239
|
250
....*....|....*....
gi 1911235092 1812 EGNDILDEANRLADEINSV 1830
Cdd:pfam06008 240 TARDSLDAANLLLQEIDDA 258
|
|
| Laminin_II |
pfam06009 |
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 ... |
2015-2151 |
3.86e-50 |
|
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: 174.98 E-value: 3.86e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2015 AKNKARQANDTAKDVLAQVKDLHQDLDGLKKSYNQLADSVAKTNAVVKDplKNKIIADADATVKNLEQEADRLIDKLKPI 2094
Cdd:pfam06009 1 SKELAREANETAKEVLEQLAPLSQNLENTSEKLSGINRSLEETNELVND--ANKALDDAGRSVKKLEELAPDLLDKLKPL 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2095 KELEDN---LKKNISEIKELINQARKQANSIKVSVSSGGDCIRTYKPEIKKGSYNNIIVN 2151
Cdd:pfam06009 79 KQLEVNsssLSDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTSL 138
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2768-2896 |
1.96e-46 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 164.03 E-value: 1.96e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2768 VRTEAESGLLFYMARINHADFATVQLRNGFPYFSYDLGSGDTNTMIPTKINDGQWHKIKITRIKQEGILYVDD-ASNRTI 2846
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGeARPTGE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1911235092 2847 SPKKADI-LDVVGLLYVGGLPINYTTRRIGPVTYSIDGCIRNLHMAEAPVD 2896
Cdd:pfam00054 81 SPLGATTdLDVDGPLYVGGLPSLGVKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| LamB |
smart00281 |
Laminin B domain; |
1253-1388 |
3.82e-46 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 162.82 E-value: 3.82e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1253 RFEPFYWKLPEQFEGKKLMAYGGKLKYAIYFEAREEtGVSTYKPQVIIRGGtpsHARIIVRHTAAPLIGQLTRHEIEMTE 1332
Cdd:smart00281 1 DNEPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRRG-GTHVSAPDVILEGN---GLRISHPAEGPPLPDELTTVEVRFRE 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1911235092 1333 REWKYYGddprvSRTVTREDFLDVLYDIHYILIKATYGNVIRQSRISEISMEVAEQ 1388
Cdd:smart00281 77 ENWQYYG-----GRPVTREDLMMVLANLTAILIRATYSQQMAGSRLSDVSLEVAVP 127
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
1258-1402 |
1.85e-44 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 158.59 E-value: 1.85e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1258 YWKLPEQFEGKKLMAYGGKLKYAIYFEAREETGVSTYKPQVIIRGGtpsHARIIVRHTA--APLIGQLTRHEIEMTEREW 1335
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGGGSLNSEPDVILEGN---GLRLSYSSPDqpPPDPGQEQTYSVRLHEENW 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1911235092 1336 KYygddpRVSRTVTREDFLDVLYDIHYILIKATYGNVIRQSRISEISMEVAEQGPvtaLTPPAHLIE 1402
Cdd:pfam00052 78 RD-----SDGAPVSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSAVPGG---SGPPASWVE 136
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2346-2485 |
4.65e-40 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 145.54 E-value: 4.65e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2346 FRTFSSSALLMYLATKDLKDFMSVELTDGHIKVSYDLGSGMASVVSNQNHNDGKWKSFTLSRIQKQANISiidIDTNQEE 2425
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLS---VDGEARP 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2426 NIATSSSGNNfglDLKADDKIYFGGLPtlrNLSMKARPEVNLKKYSGCLKDIEISRTPYN 2485
Cdd:pfam00054 78 TGESPLGATT---DLDVDGPLYVGGLP---SLGVKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2741-2890 |
9.08e-38 |
|
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: 139.86 E-value: 9.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2741 FGLSKNSHIAIAFDDTKvKNRLTIEFEVRTEAESGLLFYMARINHADFATVQLRNGFPYFSYDLGSGDTNTMIPTKINDG 2820
Cdd:cd00110 2 VSFSGSSYVRLPTLPAP-RTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1911235092 2821 QWHKIKITRIKQEGILYVDD-ASNRTISPKKADILDVVGLLYVGGLPINYTTRRIgPVTYSIDGCIRNLHM 2890
Cdd:cd00110 81 QWHSVSVERNGRSVTLSVDGeRVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGL-PVSPGFVGCIRDLKV 150
|
|
| LamG |
smart00282 |
Laminin G domain; |
2763-2890 |
2.37e-36 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 135.16 E-value: 2.37e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2763 TIEFEVRTEAESGLLFYMARINHADFATVQLRNGFPYFSYDLGSGDTNTMI-PTKINDGQWHKIKITRIKQEGILYVDD- 2840
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSdPTPLNDGQWHRVAVERNGRSVTLSVDGg 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2841 ASNRTISPKKADILDVVGLLYVGGLPINYtTRRIGPVTYSIDGCIRNLHM 2890
Cdd:smart00282 81 NRVSGESPGGLTILNLDGPLYLGGLPEDL-KLPPLPVTPGFRGCIRNLKV 129
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
587-728 |
1.20e-35 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 133.16 E-value: 1.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 587 FWSAPAPYLGNKLTAAGGQLTFTISYDLEEEEEEeetaRVLQLMIILEGKDLRISTAQEE-VELRPSEDYIHALPLKEDS 665
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGGGS----LNSEPDVILEGNGLRLSYSSPDqPPPDPGQEQTYSVRLHEEN 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1911235092 666 FTiHGTDFPVSRKEFMTVLVDLKRILIQITDSLGVDAIyRLSSVGLASAVPYRTdGGFASAVE 728
Cdd:pfam00052 77 WR-DSDGAPVSREDFMMVLANLTAILIRATYSTGSGQV-SLSNVSLDSAVPGGS-GPPASWVE 136
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2916-3068 |
2.52e-35 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 132.93 E-value: 2.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2916 GTYFDGTGFAKAVGGFKVGLDLLVEFEFRTTRTTGVLLGISSQ-KMDGMGIEMIDEKIMFHVDNGAGRFTAvydaGVPGH 2994
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQnGGDFLALELEDGRLVLRYDLGSGSLVL----SSKTP 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1911235092 2995 LCDGQWHTVRANKIKHRIELTVDGNQVEAQSPNPASTSADTNDPVFVGGFPDGLNQFGLTINVPFRGCIRSLKL 3068
Cdd:cd00110 77 LNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKV 150
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2152-2292 |
4.79e-34 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 128.59 E-value: 4.79e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2152 VKTPVADNLLFYLGSAKFIDFLAIEMRKGKVSFLWDVGSGVGRVEYPDlTIDDSYWYRIEASRTGRNGSISVRALDGPka 2231
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGD-KLNDGKWHSVELERNGRSGTLSVDGEARP-- 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1911235092 2232 sivpstyHSASPPGYTIlDVDANAMLFVGGLTG-KLKKADAVRVITFTGCMGETYFDGKPIG 2292
Cdd:pfam00054 78 -------TGESPLGATT-DLDVDGPLYVGGLPSlGVKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| LamG |
smart00282 |
Laminin G domain; |
2939-3068 |
1.49e-32 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 124.37 E-value: 1.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2939 VEFEFRTTRTTGVLLGISS-QKMDGMGIEMIDEKIMFHVDNGAGRFTAVYDagvPGHLCDGQWHTVRANKIKHRIELTVD 3017
Cdd:smart00282 2 ISFSFRTTSPNGLLLYAGSkGGGDYLALELRDGRLVLRYDLGSGPARLTSD---PTPLNDGQWHRVAVERNGRSVTLSVD 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1911235092 3018 G-NQVEAQSPnPASTSADTNDPVFVGGFPDGLNQFGLTINVPFRGCIRSLKL 3068
Cdd:smart00282 79 GgNRVSGESP-GGLTILNLDGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKV 129
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2318-2479 |
3.78e-32 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 123.68 E-value: 3.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2318 TIQFDGEGYAMVSRPIRWYPNiSTVMFKFRTFSSSALLMYLATKDLKDFMSVELTDGHIKVSYDLGSGMASVVSNQNHND 2397
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRTR-LSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLND 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2398 GKWKSFTLSRIQKQANISIididtNQEENIATSSSGNNFGLDLkaDDKIYFGGLPTlrnlSMKARPEVNLKKYSGCLKDI 2477
Cdd:cd00110 80 GQWHSVSVERNGRSVTLSV-----DGERVVESGSPGGSALLNL--DGPLYLGGLPE----DLKSPGLPVSPGFVGCIRDL 148
|
..
gi 1911235092 2478 EI 2479
Cdd:cd00110 149 KV 150
|
|
| LamB |
smart00281 |
Laminin B domain; |
582-716 |
5.01e-31 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 119.67 E-value: 5.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 582 LPQEYFWSAPAPYLGNKLTAAGGQLTFTISYDLeeeeeEEETARVLQLMIILEGKDLRISTAQEEvELRPSEDYIHALPL 661
Cdd:smart00281 1 DNEPVYWVAPEQFLGDKVTSYGGKLRYTLSFDG-----RRGGTHVSAPDVILEGNGLRISHPAEG-PPLPDELTTVEVRF 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1911235092 662 KEDSFTIHGtDFPVSRKEFMTVLVDLKRILIQITDSLGVDAIYrLSSVGLASAVP 716
Cdd:smart00281 75 REENWQYYG-GRPVTREDLMMVLANLTAILIRATYSQQMAGSR-LSDVSLEVAVP 127
|
|
| LamG |
smart00282 |
Laminin G domain; |
2341-2481 |
2.20e-30 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 118.21 E-value: 2.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2341 TVMFKFRTFSSSALLMYLATKDLKDFMSVELTDGHIKVSYDLGSGMASVVSNQNH-NDGKWKSFTLSRIQKQANISIidi 2419
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPlNDGQWHRVAVERNGRSVTLSV--- 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1911235092 2420 dtNQEENIATSSSGNNFGLDLkaDDKIYFGGLPTlrnlSMKARPEVNLKKYSGCLKDIEISR 2481
Cdd:smart00282 78 --DGGNRVSGESPGGLTILNL--DGPLYLGGLPE----DLKLPPLPVTPGFRGCIRNLKVNG 131
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2532-2670 |
1.54e-28 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 112.80 E-value: 1.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2532 FSTKNESGIILLGSggalrrkrRQTGQAYYAIFLNKGRLEVHLSTGARimRKIVVKPEPslFHDGREHSVHVERARGIFT 2611
Cdd:pfam00054 1 FRTTEPSGLLLYNG--------TQTERDFLALELRDGRLEVSYDLGSG--AAVVRSGDK--LNDGKWHSVELERNGRSGT 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1911235092 2612 VQVDEDRRHM--QNLTADQAIEV-KKLFVGGAPPE-FQPSPLRNIPPFEGCVWNLVINSVPMD 2670
Cdd:pfam00054 69 LSVDGEARPTgeSPLGATTDLDVdGPLYVGGLPSLgVKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2506-2665 |
8.10e-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: 8.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2506 TVSFPKPGFVELA-PVSISVGTEINLSFSTKNESGIILLGSGgalrrkrrQTGQAYYAIFLNKGRLEVHLSTGARimrKI 2584
Cdd:cd00110 1 GVSFSGSSYVRLPtLPAPRTRLSISFSFRTTSPNGLLLYAGS--------QNGGDFLALELEDGRLVLRYDLGSG---SL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2585 VVKPEPSLfHDGREHSVHVERARGIFTVQVDEDR--RHMQNLTADQAIEVKKLFVGGAPPEFQPSPLRNIPPFEGCVWNL 2662
Cdd:cd00110 70 VLSSKTPL-NDGQWHSVSVERNGRSVTLSVDGERvvESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDL 148
|
...
gi 1911235092 2663 VIN 2665
Cdd:cd00110 149 KVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
2147-2289 |
5.34e-27 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 108.58 E-value: 5.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2147 NIIVNVKTPVADNLLFYLGSAKFIDFLAIEMRKGKVSFLWDVGSGVGRVEYPDLTIDDSYWYRIEASRTGRNGSISVral 2226
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLNDGQWHRVAVERNGRSVTLSV--- 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1911235092 2227 DGPKASIVPstyhsaSPPGYTILDVDANamLFVGGLTGKLKKADAVRVITFTGCMGETYFDGK 2289
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 ... |
2768-2890 |
9.88e-27 |
|
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: 107.51 E-value: 9.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2768 VRTEAESGLLFYMARINHaDFATVQLRNGFPYFSYDLGSGDTNTM-IPTKINDGQWHKIKITRIKQEGILYVDDASNRTI 2846
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGS-DFLALELVNGRLVLRYDLGSGPESLLsSGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSS 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1911235092 2847 S-PKKADILDVVGLLYVGGLPINYTTRRIgPVTYSIDGCIRNLHM 2890
Cdd:pfam02210 80 LpPGESLLLNLNGPLYLGGLPPLLLLPAL-PVRAGFVGCIRDVRV 123
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2943-3068 |
3.07e-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: 105.96 E-value: 3.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2943 FRTTRTTGVLLGISSQKMDGMGIEMIDEKIMFHVDNGAGRFTAVYdagVPGHLCDGQWHTVRANKIKHRIELTVDGNQVE 3022
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDFLALELVNGRLVLRYDLGSGPESLLS---SGKNLNDGQWHSVRVERNGNTLTLSVDGQTVV 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1911235092 3023 AQSPNPASTSADTNDPVFVGGFPDGLNQFGLTINVPFRGCIRSLKL 3068
Cdd:pfam02210 78 SSLPPGESLLLNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRV 123
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2128-2287 |
2.94e-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: 104.04 E-value: 2.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2128 SGGDCIRtYKPEIKKGSYNNIIVNVKTPVADNLLFYLGSAKFIDFLAIEMRKGKVSFLWDVGSGVGRVEYPDlTIDDSYW 2207
Cdd:cd00110 5 SGSSYVR-LPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKT-PLNDGQW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2208 YRIEASRTGRNGSISVralDGPKasivpsTYHSASPPGYTILDVDANamLFVGGLTGKLKKADAVRVITFTGCMGETYFD 2287
Cdd:cd00110 83 HSVSVERNGRSVTLSV---DGER------VVESGSPGGSALLNLDGP--LYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2943-3077 |
1.02e-23 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 98.93 E-value: 1.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2943 FRTTRTTGVLLGISSQ-KMDGMGIEMIDEKIMFHVDNGAGRFTAVYdagvPGHLCDGQWHTVRANKIKHRIELTVDGNQV 3021
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQtERDFLALELRDGRLEVSYDLGSGAAVVRS----GDKLNDGKWHSVELERNGRSGTLSVDGEAR 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1911235092 3022 E-AQSPNPASTSADTNDPVFVGGFP-DGLNQFGLTINVPFRGCIRSLKLtkgTGKPLE 3077
Cdd:pfam00054 77 PtGESPLGATTDLDVDGPLYVGGLPsLGVKKRRLAISPSFDGCIRDVIV---NGKPLD 131
|
|
| LamG |
smart00282 |
Laminin G domain; |
2527-2667 |
2.59e-22 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 95.10 E-value: 2.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2527 EINLSFSTKNESGIILLGSGGAlrrkrrqtGQAYYAIFLNKGRLEVHLSTGARimrKIVVKPEPSLFHDGREHSVHVERA 2606
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKG--------GGDYLALELRDGRLVLRYDLGSG---PARLTSDPTPLNDGQWHRVAVERN 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1911235092 2607 RGIFTVQVD-EDRRHMQNLTADQAIEVK-KLFVGGAPPEFQPSPLRNIPPFEGCVWNLVINSV 2667
Cdd:smart00282 70 GRSVTLSVDgGNRVSGESPGGLTILNLDgPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2346-2479 |
1.34e-21 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 92.87 E-value: 1.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2346 FRTFSSSALLMYLATKDlKDFMSVELTDGHIKVSYDLGSG-MASVVSNQNHNDGKWKSFTLSRIQKQANISIididtNQE 2424
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGG-SDFLALELVNGRLVLRYDLGSGpESLLSSGKNLNDGQWHSVRVERNGNTLTLSV-----DGQ 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1911235092 2425 ENIATSSSGNNFGLDLKADdkIYFGGLPTLRNLSmkarPEVNLKKYSGCLKDIEI 2479
Cdd:pfam02210 75 TVVSSLPPGESLLLNLNGP--LYLGGLPPLLLLP----ALPVRAGFVGCIRDVRV 123
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2532-2667 |
3.98e-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: 80.16 E-value: 3.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2532 FSTKNESGIILLGSGGalrrkrrqtGQAYYAIFLNKGRLEVHLSTGARimrKIVVKPEPSLFHDGREHSVHVERARGIFT 2611
Cdd:pfam02210 1 FRTRQPNGLLLYAGGG---------GSDFLALELVNGRLVLRYDLGSG---PESLLSSGKNLNDGQWHSVRVERNGNTLT 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1911235092 2612 VQVDEDRRHMQNLTADQAI--EVKKLFVGGAPPEFQPSPLRNIPPFEGCVWNLVINSV 2667
Cdd:pfam02210 69 LSVDGQTVVSSLPPGESLLlnLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2152-2289 |
1.22e-16 |
|
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: 78.62 E-value: 1.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2152 VKTPVADNLLFYLGSAKfIDFLAIEMRKGKVSFLWDVGSGVGRVEYPDLTIDDSYWYRIEASRTGRNGSISVralDGpka 2231
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGG-SDFLALELVNGRLVLRYDLGSGPESLLSSGKNLNDGQWHSVRVERNGNTLTLSV---DG--- 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1911235092 2232 sivpsTYHSASPPGYTILDVDANAMLFVGGLTGKLKKADAVRVITFTGCMGETYFDGK 2289
Cdd:pfam02210 74 -----QTVVSSLPPGESLLLNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1660-2127 |
1.31e-16 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 87.04 E-value: 1.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1660 IKGLVRDAEavnEKAKEVNETLGIQD--KAFErNMQGLQKEIDQMMREL-----RRKNLDTQKEVAEDELVAAEGLLKKV 1732
Cdd:PRK03918 137 IDAILESDE---SREKVVRQILGLDDyeNAYK-NLGEVIKEIKRRIERLekfikRTENIEELIKEKEKELEEVLREINEI 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1733 QKVFGEPRGKNEKMEKDLGE----------------KLTDHKNKLDDAWDLLREATDKTREANRLAAANQQNMTALEEKK 1796
Cdd:PRK03918 213 SSELPELREELEKLEKEVKEleelkeeieelekeleSLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKA 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1797 EAIESGKRQTENTLKEGNDILDEANRLADEINSVIDYVTDIQTK---LPPMSEELKDKIDDLSREMKDRKLAERVYQAEN 1873
Cdd:PRK03918 293 EEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKeerLEELKKKLKELEKRLEELEERHELYEEAKAKKE 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1874 HAAQLNASSAVL--DGILDEAKSISFNATAAFKAYSNIKDYIDEADKIAKEAKgLAHEATKLATG--P--QGSLKDGAKG 1947
Cdd:PRK03918 373 ELERLKKRLTGLtpEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELK-KAIEELKKAKGkcPvcGRELTEEHRK 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1948 SLQKSFgiLNEAKKLANNVKENDDDLNSLQTRLEKAD-VRNGELR-RALNDTLAKLSAIPNDT----AAKLQAAKNKARQ 2021
Cdd:PRK03918 452 ELLEEY--TAELKRIEKELKEIEEKERKLRKELRELEkVLKKESElIKLKELAEQLKELEEKLkkynLEELEKKAEEYEK 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2022 ANDTAKDVLAQVKDLHQDLDGLKKSYNQLA------DSVAKTNAVVKDPLKN---KIIADADATVKNLEQEADRLI---- 2088
Cdd:PRK03918 530 LKEKLIKLKGEIKSLKKELEKLEELKKKLAelekklDELEEELAELLKELEElgfESVEELEERLKELEPFYNEYLelkd 609
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1911235092 2089 ------DKLKPIKELEDNLKK---NISEIKELINQARKQANSIKVSVS 2127
Cdd:PRK03918 610 aekeleREEKELKKLEEELDKafeELAETEKRLEELRKELEELEKKYS 657
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1590-2123 |
1.95e-16 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 86.66 E-value: 1.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1590 LENRTQELKHLLSPQRAPERLIQLAEGNLNTLVTEMNELLTRATKVTADGEQtgqdAERTSRRANSLGDFIKGLVRDAEA 1669
Cdd:PRK03918 174 IKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEK----LEKEVKELEELKEEIEELEKELES 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1670 VNEKAKEVNETLgiqdKAFERNMQGLQKEIDQM-------------------MRELRRKNLDTQKEVaEDELVAAEGLLK 1730
Cdd:PRK03918 250 LEGSKRKLEEKI----RELEERIEELKKEIEELeekvkelkelkekaeeyikLSEFYEEYLDELREI-EKRLSRLEEEIN 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1731 KVQKVFGEPRGKNEKME--KDLGEKLTDHKNKLDDAWDLLREATDKTREANRLAAANQQNmtALEEKKEAIESGKRQTEN 1808
Cdd:PRK03918 325 GIEERIKELEEKEERLEelKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGL--TPEKLEKELEELEKAKEE 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1809 TLKEGNDILDEANRLADEINSVIDYVTDIQT---KLP----PMSEE-LKDKIDDLSREMKDrkLAERVYQAENHAAQLNA 1880
Cdd:PRK03918 403 IEEEISKITARIGELKKEIKELKKAIEELKKakgKCPvcgrELTEEhRKELLEEYTAELKR--IEKELKEIEEKERKLRK 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1881 SSAVLDGILDEAKSISFNATAA---FKAYSNIKDY-IDEADKIAKEAKGLAHEATKLAtGPQGSLKDgakgSLQKSFGIL 1956
Cdd:PRK03918 481 ELRELEKVLKKESELIKLKELAeqlKELEEKLKKYnLEELEKKAEEYEKLKEKLIKLK-GEIKSLKK----ELEKLEELK 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1957 NEAKKLANNVKENDDDLNSLQTRLEKA--------DVRNGELRRALNDTLaKLSAIPND---TAAKLQAAKNKARQANDT 2025
Cdd:PRK03918 556 KKLAELEKKLDELEEELAELLKELEELgfesveelEERLKELEPFYNEYL-ELKDAEKElerEEKELKKLEEELDKAFEE 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2026 AKDVLAQVKDLHQDLDGLKKSYNQlADSVAKTNAVVKdplKNKIIADADATVKNLE---QEADRLIDKLKP--------I 2094
Cdd:PRK03918 635 LAETEKRLEELRKELEELEKKYSE-EEYEELREEYLE---LSRELAGLRAELEELEkrrEEIKKTLEKLKEeleerekaK 710
|
570 580
....*....|....*....|....*....
gi 1911235092 2095 KELEdNLKKNISEIKELINQARKQANSIK 2123
Cdd:PRK03918 711 KELE-KLEKALERVEELREKVKKYKALLK 738
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1608-2148 |
1.94e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 80.11 E-value: 1.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1608 ERLIQLAE--GNLNTLVTEMNELLTRATKVTADGEQTGQDAERTSRRANSLGDFIKGLVRDAEAVNEKAKEVNEtlgIQD 1685
Cdd:PRK03918 214 SELPELREelEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKE---LKE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1686 KAFE-RNMQGLQKEIDQMMREL--RRKNLDTQKEVAEDELVAAEgllKKVQKVfGEPRGKNEKMEKDLGEKLTDHKnKLD 1762
Cdd:PRK03918 291 KAEEyIKLSEFYEEYLDELREIekRLSRLEEEINGIEERIKELE---EKEERL-EELKKKLKELEKRLEELEERHE-LYE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1763 DAWDLLREATD-KTREANRlaaanqqnmtALEEKKEAIESGKRQTENTLKEGNDILDEANRLADEINSVIDYVTDIQT-- 1839
Cdd:PRK03918 366 EAKAKKEELERlKKRLTGL----------TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKak 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1840 -KLP----PMSEE-LKDKIDDLSREMKDrkLAERVYQAENHAAQLNASSAVLDGILDEAKSISFNATAA---FKAYSNIK 1910
Cdd:PRK03918 436 gKCPvcgrELTEEhRKELLEEYTAELKR--IEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAeqlKELEEKLK 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1911 DY-IDEADKIAKEAKGLAHEATKLAtGPQGSLKDgakgSLQKSFGILNEAKKLANNVKENDDDLNSLQTRLEKA------ 1983
Cdd:PRK03918 514 KYnLEELEKKAEEYEKLKEKLIKLK-GEIKSLKK----ELEKLEELKKKLAELEKKLDELEEELAELLKELEELgfesve 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1984 --DVRNGELRRALNDTLaKLSAIPND---TAAKLQAAKNKARQANDTAKDVLAQVKDLHQDLDGLKKSYNQladsvaktn 2058
Cdd:PRK03918 589 elEERLKELEPFYNEYL-ELKDAEKElerEEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE--------- 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2059 avvkDPLKNKiiadADATVKnLEQEADRLIDKLKPIKELEDNLKKNISEIK---ELINQARKQANSIKVSVSSGGDC--- 2132
Cdd:PRK03918 659 ----EEYEEL----REEYLE-LSRELAGLRAELEELEKRREEIKKTLEKLKeelEEREKAKKELEKLEKALERVEELrek 729
|
570
....*....|....*.
gi 1911235092 2133 IRTYKPEIKKGSYNNI 2148
Cdd:PRK03918 730 VKKYKALLKERALSKV 745
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
941-989 |
1.97e-14 |
|
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: 69.69 E-value: 1.97e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1911235092 941 PCRCHANGSFSEVCHTQTGQCECRPNVQGRRCDECKPETFGLQS-PRGCV 989
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSqGGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
942-988 |
7.93e-14 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 67.76 E-value: 7.93e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1911235092 942 CRCHANGSFSEVCHTQTGQCECRPNVQGRRCDECKPETFGLQ--SPRGC 988
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPsdPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
942-988 |
1.10e-13 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 67.34 E-value: 1.10e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1911235092 942 CRCHANGSFSEVCHTQTGQCECRPNVQGRRCDECKPETFGlQSPRGC 988
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYG-DGPPGC 46
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1628-2119 |
1.56e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 77.00 E-value: 1.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1628 LLTRATKVTADGEQTGQ----DAERTSRRANSLGDFIKGLVR-DAEA-VN---EKAKEVNETlgIQDKAFERnmqglQKE 1698
Cdd:PRK02224 82 HIERRVRLSGDRATTAKcvleTPEGTIDGARDVREEVTELLRmDAEAfVNcayVRQGEVNKL--INATPSDR-----QDM 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1699 IDQMmreLRRKNLDTQKEVAEDELVAAEGLLKKVQKVFGEPRGK-NEKMEKDLGEKLTDHKNKLDDawdllreatdktre 1777
Cdd:PRK02224 155 IDDL---LQLGKLEEYRERASDARLGVERVLSDQRGSLDQLKAQiEEKEEKDLHERLNGLESELAE-------------- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1778 anrlaaanqqnmtaLEEKKEAIESGKRQTENTLKEGNDILDEANRLADEINSVIDYVTDIQTKLppmsEELKDKIDDLSR 1857
Cdd:PRK02224 218 --------------LDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETI----AETEREREELAE 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1858 EMKDRKlaERVYQAENHAAQLNASSAV--------------LDGILDEAK-SISFNATAAFKAYSNIKDYIDEADKIAKE 1922
Cdd:PRK02224 280 EVRDLR--ERLEELEEERDDLLAEAGLddadaeavearreeLEDRDEELRdRLEECRVAAQAHNEEAESLREDADDLEER 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1923 AKGLAHEATKLATGPQGSLKDGAKGSlqksfgilNEAKKLANNVKENDDDLNSLQTRLEKADVRNGELRRALNDTLAKLs 2002
Cdd:PRK02224 358 AEELREEAAELESELEEAREAVEDRR--------EEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRERE- 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2003 aipNDTAAKLQAAKNKARQAN---------------------DTAKDVLAQVKDLHQDLDGLKKSYNQLADSVAKTNAVV 2061
Cdd:PRK02224 429 ---AELEATLRTARERVEEAEalleagkcpecgqpvegsphvETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLV 505
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1911235092 2062 KdplknkiiadadatvknLEQEADRLIDKLKPIKELEDNLKKNISEIKELINQARKQA 2119
Cdd:PRK02224 506 E-----------------AEDRIERLEERREDLEELIAERRETIEEKRERAEELRERA 546
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1660-2153 |
2.09e-13 |
|
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: 76.60 E-value: 2.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1660 IKGLVRDAEAVNEKAKEVN---ETLGIQDKAFERNMQGLQKEIDQMMRELRRKNLdtqkevaedelvaaegLLKKVQKvf 1736
Cdd:TIGR04523 147 IKKKEKELEKLNNKYNDLKkqkEELENELNLLEKEKLNIQKNIDKIKNKLLKLEL----------------LLSNLKK-- 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1737 geprgKNEKmEKDLGEKLTDHKNK---LDDAWDLLR-EATDKTREANR-------LAAANQQNMTALEEKKEAIESGKR- 1804
Cdd:TIGR04523 209 -----KIQK-NKSLESQISELKKQnnqLKDNIEKKQqEINEKTTEISNtqtqlnqLKDEQNKIKKQLSEKQKELEQNNKk 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1805 --QTENTLKEGNDILDEAN---------RLADEINSVIDYVTDIQTKLPPMSE---ELKDKIDDLSREM---------KD 1861
Cdd:TIGR04523 283 ikELEKQLNQLKSEISDLNnqkeqdwnkELKSELKNQEKKLEEIQNQISQNNKiisQLNEQISQLKKELtnsesenseKQ 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1862 RKLAERVYQAENHAAQlNASSavLDGILDEAKSISfnataafkaysNIKDYIDEADKIAKEakglaheatklatgpqgsl 1941
Cdd:TIGR04523 363 RELEEKQNEIEKLKKE-NQSY--KQEIKNLESQIN-----------DLESKIQNQEKLNQQ------------------- 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1942 KDGAKGSLQKSFGIL-NEAKKL-ANNVKEND--DDLN----SLQTRLEKADVRNGELRRALNDTLAKLSAIPNDTAAKLQ 2013
Cdd:TIGR04523 410 KDEQIKKLQQEKELLeKEIERLkETIIKNNSeiKDLTnqdsVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQK 489
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2014 AAKNKARQA---NDTAKDVLAQVKDLHQDLDGLKKSYNQLADSVAKTNAVVKDpLKNKIIA-DADATVKNLEQEADRLID 2089
Cdd:TIGR04523 490 ELKSKEKELkklNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISD-LEDELNKdDFELKKENLEKEIDEKNK 568
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1911235092 2090 KLKPIKELEDNLKKNISEIKELINQARKQANSIK-------VSVSSGGDCIRTYKPEIKKgsYNNIIVNVK 2153
Cdd:TIGR04523 569 EIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIkeieekeKKISSLEKELEKAKKENEK--LSSIIKNIK 637
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1585-2117 |
2.87e-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: 2.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1585 KMLYDLENRTQELK-HLLSPQRAPERLIQLAEGNLntlvtemnelltratkVTADGEQTGQDAERT--SRRANSLGDFIK 1661
Cdd:pfam15921 317 RQLSDLESTVSQLRsELREAKRMYEDKIEELEKQL----------------VLANSELTEARTERDqfSQESGNLDDQLQ 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1662 GLVRDaeaVNEKAKEVNETLGIQDKAFERNMqGLQKEIDQMMRELRRKNLDTQKevaedelvaAEGLLK--------KVQ 1733
Cdd:pfam15921 381 KLLAD---LHKREKELSLEKEQNKRLWDRDT-GNSITIDHLRRELDDRNMEVQR---------LEALLKamksecqgQME 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1734 KVFGEPRGKNEKMekdlgEKLTDHKNKLDDAWDLLREATDKTrEANRLAAANQQN-----MTALEEKKEAIESGKRQTeN 1808
Cdd:pfam15921 448 RQMAAIQGKNESL-----EKVSSLTAQLESTKEMLRKVVEEL-TAKKMTLESSERtvsdlTASLQEKERAIEATNAEI-T 520
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1809 TLKEGNDI-LDEANRLADEinsvIDYVTDIQTKLPPMSEEL--KDKIDDLSREMKDrKLAERVYQAENHAAQLNASSAVL 1885
Cdd:pfam15921 521 KLRSRVDLkLQELQHLKNE----GDHLRNVQTECEALKLQMaeKDKVIEILRQQIE-NMTQLVGQHGRTAGAMQVEKAQL 595
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1886 DGILDEAKsisfnatAAFKAYSNIKDYIDEadKIAK-EAK--GLAHEATKLATGpqGSLKdgakgsLQKSFGILNEAKKL 1962
Cdd:pfam15921 596 EKEINDRR-------LELQEFKILKDKKDA--KIRElEARvsDLELEKVKLVNA--GSER------LRAVKDIKQERDQL 658
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1963 ANNVKENDDDLNSLQTRLEKadvrngeLRRALNDTLAKLSAIPNDTAAKLQAAKNKARQANDTAKDVlaQVKDLHqdldG 2042
Cdd:pfam15921 659 LNEVKTSRNELNSLSEDYEV-------LKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSM--EGSDGH----A 725
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2043 LKKSYNQLADSVAKTNAVvkDPLKNKI------IADADATVKNLEQEADRLIDKLKPIKElEDNlkKNISEIKELINQAR 2116
Cdd:pfam15921 726 MKVAMGMQKQITAKRGQI--DALQSKIqfleeaMTNANKEKHFLKEEKNKLSQELSTVAT-EKN--KMAGELEVLRSQER 800
|
.
gi 1911235092 2117 K 2117
Cdd:pfam15921 801 R 801
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1686-2123 |
4.84e-13 |
|
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: 75.44 E-value: 4.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1686 KAFERNMQGLQKEIDQmmRELRRKNLDtqkevaedelvaaEGLLKKVQKVfgeprgKN--------EKMEKDLGEKLTDH 1757
Cdd:TIGR04523 36 KQLEKKLKTIKNELKN--KEKELKNLD-------------KNLNKDEEKI------NNsnnkikilEQQIKDLNDKLKKN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1758 KNKLD--DAwDLLREATD-KTreanrlaaaNQQNMTALEE-----KKEAIESGKRQT---------ENTLKEGNDILDEA 1820
Cdd:TIGR04523 95 KDKINklNS-DLSKINSEiKN---------DKEQKNKLEVelnklEKQKKENKKNIDkflteikkkEKELEKLNNKYNDL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1821 NR----LADEINSVIDYVTDIQTKLPPM-SEELKD--KIDDL-SREMKDRKLAERVYQAENHAAQLNassavlDGILDEA 1892
Cdd:TIGR04523 165 KKqkeeLENELNLLEKEKLNIQKNIDKIkNKLLKLelLLSNLkKKIQKNKSLESQISELKKQNNQLK------DNIEKKQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1893 KSISFNATAAFKAYSNIKDYIDEADKIAKE----------AKGLAHEATKLATGPQGSLKDGAKgslQKSFGILNEAK-- 1960
Cdd:TIGR04523 239 QEINEKTTEISNTQTQLNQLKDEQNKIKKQlsekqkeleqNNKKIKELEKQLNQLKSEISDLNN---QKEQDWNKELKse 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1961 -------------KLANNVK---ENDDDLNSLQTRLEKADVRNGELRRALNDTLAKLSAIPNDTAAKLQAAKNKARQAND 2024
Cdd:TIGR04523 316 lknqekkleeiqnQISQNNKiisQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQIND 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2025 ----------TAKDVLAQVKDLHQDLDGLKKSYNQLADSVAKTNAVVKDpLKNKI------IADADATVKNLEQEADRLI 2088
Cdd:TIGR04523 396 leskiqnqekLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKD-LTNQDsvkeliIKNLDNTRESLETQLKVLS 474
|
490 500 510
....*....|....*....|....*....|....*....
gi 1911235092 2089 DKLKPIK-ELEDN---LKKNISEIKELINQARKQANSIK 2123
Cdd:TIGR04523 475 RSINKIKqNLEQKqkeLKSKEKELKKLNEEKKELEEKVK 513
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1655-2118 |
6.80e-13 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 74.80 E-value: 6.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1655 SLGDFIKGLVRDaeavnEKAKEVNETLGIQDKAFERNMQGLqKEIDQMMRELRRKNLDTQKevAEDELVAAEGLLKKVQK 1734
Cdd:COG4717 38 TLLAFIRAMLLE-----RLEKEADELFKPQGRKPELNLKEL-KELEEELKEAEEKEEEYAE--LQEELEELEEELEELEA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1735 VFGEPRGKNEKMEKDLG--------EKLTDHKNKLDDAWDLLREATDKTREA-NRLAAANQQnmtaLEEKKEAIESGKRQ 1805
Cdd:COG4717 110 ELEELREELEKLEKLLQllplyqelEALEAELAELPERLEELEERLEELRELeEELEELEAE----LAELQEELEELLEQ 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1806 TEN-TLKEGNDILDEANRLADEINSVIDYVTDIQTKLppmsEELKDKIDDLSREMKDRKLAERVYQAENHAAQLnASSAV 1884
Cdd:COG4717 186 LSLaTEEELQDLAEELEELQQRLAELEEELEEAQEEL----EELEEELEQLENELEAAALEERLKEARLLLLIA-AALLA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1885 LDGILDEAKSISFNATAAFKAYSNIkdYIDEADKIAKEAKGLAHEATKLATGP-QGSLKDGAKGSLQKSFGILNEAKKla 1963
Cdd:COG4717 261 LLGLGGSLLSLILTIAGVLFLVLGL--LALLFLLLAREKASLGKEAEELQALPaLEELEEEELEELLAALGLPPDLSP-- 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1964 NNVKENDDDLNSLQTRLEKADVRNGELRRA-LNDTLAKLSAIPN-DTAAKLQAAKNKARQANDTakdvLAQVKDLHQDLD 2041
Cdd:COG4717 337 EELLELLDRIEELQELLREAEELEEELQLEeLEQEIAALLAEAGvEDEEELRAALEQAEEYQEL----KEELEELEEQLE 412
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1911235092 2042 GLKKSYNQLADsvaktnavvkdplknkiiadaDATVKNLEQEADRLIDKLKPIKELEDNLKKNISEIKELINQARKQ 2118
Cdd:COG4717 413 ELLGELEELLE---------------------ALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEED 468
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1676-2119 |
1.05e-12 |
|
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: 74.33 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1676 EVNETL---GIQDKAFERNMQGLQKEIDQMMRELRRK---------NLDTQKEVAEDELVAAEGLLKKVQKVFGEprgKN 1743
Cdd:TIGR02169 121 EIHDFLaaaGIYPEGYNVVLQGDVTDFISMSPVERRKiideiagvaEFDRKKEKALEELEEVEENIERLDLIIDE---KR 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1744 EKMEKDLGEKltDHKNKLDDAWDLLREatdktREANRLAAANQqnmtALEEKKEAIEsgkRQTENTLKEGNDILDEANRL 1823
Cdd:TIGR02169 198 QQLERLRRER--EKAERYQALLKEKRE-----YEGYELLKEKE----ALERQKEAIE---RQLASLEEELEKLTEEISEL 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1824 ADEINSVIDYVTDIQTKLPPMSEE----LKDKIDDLSREMK--DRKLAERVYQAENHAAQLnassavldgildeaksisf 1897
Cdd:TIGR02169 264 EKRLEEIEQLLEELNKKIKDLGEEeqlrVKEKIGELEAEIAslERSIAEKERELEDAEERL------------------- 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1898 nataafkaysniKDYIDEADKIAKEAKGLaheatklatgpqgslkDGAKGSLQKsfgilnEAKKLANNVKENDDDLNSLQ 1977
Cdd:TIGR02169 325 ------------AKLEAEIDKLLAEIEEL----------------EREIEEERK------RRDKLTEEYAELKEELEDLR 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1978 TRLEKADVRNGELRRALNDTLAKLSaipnDTAAKLQAAKNKARQANDTAKDVLAQVKDLHQDLDGLKKSYNQLADSVAKT 2057
Cdd:TIGR02169 371 AELEEVDKEFAETRDELKDYREKLE----KLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDK 446
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1911235092 2058 NAVVKdplknKIIADADATVKNLEQEADRLIDKLKPIKELEDNLKKNISEIKELinQARKQA 2119
Cdd:TIGR02169 447 ALEIK-----KQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEA--EAQARA 501
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
991-1035 |
1.19e-12 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 64.64 E-value: 1.19e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1911235092 991 CNCNSFGSKSFDCE-ESGQCWCQPGVTGKKCDHCAHGYFNFQEGGC 1035
Cdd:smart00180 1 CDCDPGGSASGTCDpDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1713-2093 |
1.26e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 74.32 E-value: 1.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1713 TQKEVAEDELVAAEGLLKKVQKVFGEPRGKNEKMEK--DLGEKLTDHKNKLDDA-WDLLreATDKTREANRLAAANQQnM 1789
Cdd:TIGR02168 172 ERRKETERKLERTRENLDRLEDILNELERQLKSLERqaEKAERYKELKAELRELeLALL--VLRLEELREELEELQEE-L 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1790 TALEEKKEAIESGKRQTENTLKEGNDILDEANRLADEINSVIDYVTDIQTKLPPMSEELKDKIDDLSREMKdrKLAERVY 1869
Cdd:TIGR02168 249 KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLE--ELEAQLE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1870 QAENHAAQLNASSAVLDGILDEAKsisfnataafKAYSNIKDYIDEADKIAKEAKGLAHEATKLATgpqgSLKDgakgsl 1949
Cdd:TIGR02168 327 ELESKLDELAEELAELEEKLEELK----------EELESLEAELEELEAELEELESRLEELEEQLE----TLRS------ 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1950 qKSFGILNEAKKLANNVKENDDDLNSLQTRLEKADVRN-------------------GELRRALNDTLAKLSAIpNDTAA 2010
Cdd:TIGR02168 387 -KVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIeellkkleeaelkelqaelEELEEELEELQEELERL-EEALE 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2011 KLQAAKNKARQANDTAKDVLAQV-------KDLHQDLDGLKKSYNQLADSvAKTNAVVKDPLKNKIIADA---------- 2073
Cdd:TIGR02168 465 ELREELEEAEQALDAAERELAQLqarldslERLQENLEGFSEGVKALLKN-QSGLSGILGVLSELISVDEgyeaaieaal 543
|
410 420
....*....|....*....|....*
gi 1911235092 2074 -----DATVKNLEQeADRLIDKLKP 2093
Cdd:TIGR02168 544 ggrlqAVVVENLNA-AKKAIAFLKQ 567
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1682-2074 |
1.48e-12 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 72.24 E-value: 1.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1682 GIQDKAFERNMQGLQKEIDQMMRELRRKNldTQKEVAEDELVAAEgllkkvqkvfgeprgknekmekdlgEKLTDHKNKL 1761
Cdd:COG4372 23 GILIAALSEQLRKALFELDKLQEELEQLR--EELEQAREELEQLE-------------------------EELEQARSEL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1762 DDAWDLLREATDKTREANRLAAANQQNMTALEEKKEAIEsgkRQTENTLKEGNDILDEANRLADEINSVIDYVTDIQTKL 1841
Cdd:COG4372 76 EQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQ---EELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEEL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1842 ppmsEELKDKIDDLSREMKDRklaervyQAENHAAQLNASSAVLDGILDEAKSISFNATAAFKAYSNIKDYIDEADKIAK 1921
Cdd:COG4372 153 ----KELEEQLESLQEELAAL-------EQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1922 EAK-GLAHEATKLATGPQGSLKDGAKGSLQKSFGILNEAKKlanNVKENDDDLNSLQTRLEKADVRNGELRRALNDTLAK 2000
Cdd:COG4372 222 EAKdSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEE---LELAILVEKDTEEEELEIAALELEALEEAALELKLL 298
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1911235092 2001 LSAIPNDTAAKLQAAKNKARQANDTAKdvlAQVKDLHQDLDGLKKSYNQLADSVAKTNAVVKDPLKNKIIADAD 2074
Cdd:COG4372 299 ALLLNLAALSLIGALEDALLAALLELA---KKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVAD 369
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1586-2103 |
3.12e-12 |
|
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: 72.90 E-value: 3.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1586 MLYDLENRTQELKHLLSpQRAPERLIQLAE-----GNLNTL-------VTEMNELLTRAtkvtadgEQTGQDAERTSRR- 1652
Cdd:pfam01576 142 LLEDQNSKLSKERKLLE-ERISEFTSNLAEeeekaKSLSKLknkheamISDLEERLKKE-------EKGRQELEKAKRKl 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1653 ---ANSLGDFIKGL-VRDAEAVNEKAKEVNETLGIQDKAFERNMQ--GLQKEIdqmmRELRRKNLDTQKEVaEDELVAae 1726
Cdd:pfam01576 214 egeSTDLQEQIAELqAQIAELRAQLAKKEEELQAALARLEEETAQknNALKKI----RELEAQISELQEDL-ESERAA-- 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1727 gllkkvqkvfgepRGKNEKMEKDLGEKLTDHKNKLDDAWD-----------------LLREATD---KTREAnRLAAANQ 1786
Cdd:pfam01576 287 -------------RNKAEKQRRDLGEELEALKTELEDTLDttaaqqelrskreqevtELKKALEeetRSHEA-QLQEMRQ 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1787 QNMTALEEKKEAIESGKRQTENTLKEGNDILDEANRLADEINSVIDYVTDIQT---KLPPMSEELKDKIDDLSREMKDrk 1863
Cdd:pfam01576 353 KHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHkrkKLEGQLQELQARLSESERQRAE-- 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1864 LAERVYQAENhaaQLNASSAVLDGIldEAKSISFNATAAfKAYSNIKDyideadkiakeAKGLAHEATKlatgpqgslkd 1943
Cdd:pfam01576 431 LAEKLSKLQS---ELESVSSLLNEA--EGKNIKLSKDVS-SLESQLQD-----------TQELLQEETR----------- 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1944 gakgslQKsfgiLNeakkLANNVKENDDDLNSLQTRLEKADVRNGELRRALNDTLAKLSaipnDTAAKLQAAKNKARQAN 2023
Cdd:pfam01576 483 ------QK----LN----LSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLS----DMKKKLEEDAGTLEALE 544
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2024 DTAKDVLAQVKDLHQDLDGLKKSYNQLadsvaktnavvkdplknkiiadaDATVKNLEQEADRLIDKLKPIKELEDNLKK 2103
Cdd:pfam01576 545 EGKKRLQRELEALTQQLEEKAAAYDKL-----------------------EKTKNRLQQELDDLLVDLDHQRQLVSNLEK 601
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1668-2142 |
5.23e-12 |
|
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: 71.98 E-value: 5.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1668 EAVNEKAK----EVNEtLGIQDKAFERNMQGLQKEIDQMMRELRR------------KNLDTQKEVAEDELVAAEGLLKK 1731
Cdd:TIGR04523 207 KKKIQKNKslesQISE-LKKQNNQLKDNIEKKQQEINEKTTEISNtqtqlnqlkdeqNKIKKQLSEKQKELEQNNKKIKE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1732 VQKVFGEPRG-----KNEKME---KDLGEKLTDHKNKLDDAW-----------DLLREATDKTREANRLAAANQQNMTAL 1792
Cdd:TIGR04523 286 LEKQLNQLKSeisdlNNQKEQdwnKELKSELKNQEKKLEEIQnqisqnnkiisQLNEQISQLKKELTNSESENSEKQREL 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1793 EEKKEAIESGKRQTENTLKEGNDILDEANRL------ADEINSVIDyvTDIQTK------LPPMSEELKDKIDDLSREMK 1860
Cdd:TIGR04523 366 EEKQNEIEKLKKENQSYKQEIKNLESQINDLeskiqnQEKLNQQKD--EQIKKLqqekelLEKEIERLKETIIKNNSEIK 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1861 DrkLAERVYQAENHAAQLNASSAVLDGILDEAkSISFNataafKAYSNIKDYIDEADKIAKEAKGLAHEATKLatgpQGS 1940
Cdd:TIGR04523 444 D--LTNQDSVKELIIKNLDNTRESLETQLKVL-SRSIN-----KIKQNLEQKQKELKSKEKELKKLNEEKKEL----EEK 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1941 LKDGAKgslQKSFGILNEaKKLANNVKENDDDLNSLQTRLEKadvrngelrraLNDTLAKlsaipndtaAKLQAAKNKAR 2020
Cdd:TIGR04523 512 VKDLTK---KISSLKEKI-EKLESEKKEKESKISDLEDELNK-----------DDFELKK---------ENLEKEIDEKN 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2021 QandtakdvlaQVKDLHQDLDGLKKSYNQLADSVAKTNAVVKDpLKNKIiADADATVKNLEQEAD-------RLIDKLKP 2093
Cdd:TIGR04523 568 K----------EIEELKQTQKSLKKKQEEKQELIDQKEKEKKD-LIKEI-EEKEKKISSLEKELEkakkeneKLSSIIKN 635
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1911235092 2094 IKELEDNLKKNISEIKELINQAR-KQAN---SIKVSVSSGGDCIRT-----------YKPEIKK 2142
Cdd:TIGR04523 636 IKSKKNKLKQEVKQIKETIKEIRnKWPEiikKIKESKTKIDDIIELmkdwlkelslhYKKYITR 699
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1664-2123 |
6.11e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 72.10 E-value: 6.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1664 VRDAEAVNEKAKEVNETlgiqdkAFERNMQGLQKEIDQMMRELRRKNLDTQKEVAE--DELVAAEGLLKKVQKVFGEPRG 1741
Cdd:PTZ00121 1229 VKKAEEAKKDAEEAKKA------EEERNNEEIRKFEEARMAHFARRQAAIKAEEARkaDELKKAEEKKKADEAKKAEEKK 1302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1742 KNEKMEKDLGE--KLTDHKNKLDDAWDLLREATDKTREANRLAAANQQNMTALEEKKEAIESGKRQTENTLKEGNDILDE 1819
Cdd:PTZ00121 1303 KADEAKKKAEEakKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADA 1382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1820 ANRLADEINSVidyvtdiqTKLPPMSEELKDKIDDLSREMKDRKLAERVYQA--ENHAAQLNASSAVLDGILDEAKSISF 1897
Cdd:PTZ00121 1383 AKKKAEEKKKA--------DEAKKKAEEDKKKADELKKAAAAKKKADEAKKKaeEKKKADEAKKKAEEAKKADEAKKKAE 1454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1898 NATAA---------------FKAYSNIKDYIDEADKIAKEAKGLAHEATK----------LATGPQGSLKDGAKGSLQKS 1952
Cdd:PTZ00121 1455 EAKKAeeakkkaeeakkadeAKKKAEEAKKADEAKKKAEEAKKKADEAKKaaeakkkadeAKKAEEAKKADEAKKAEEAK 1534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1953 FGilNEAKKL-----------ANNVKENDDDLNSLQTRLEKADvRNGELRRALNDTLAKLSAIPNDTAAKLQAAKNKARQ 2021
Cdd:PTZ00121 1535 KA--DEAKKAeekkkadelkkAEELKKAEEKKKAEEAKKAEED-KNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEE 1611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2022 AN--DTAKDVLAQVKDLHQDLDGLKKSYNQLADSVAKTNAVVKDPLKNKIIAdadATVKNLEQEADRLIDKLKpiKELED 2099
Cdd:PTZ00121 1612 AKkaEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKA---AEEAKKAEEDKKKAEEAK--KAEED 1686
|
490 500
....*....|....*....|....
gi 1911235092 2100 NLKKNISEIKEliNQARKQANSIK 2123
Cdd:PTZ00121 1687 EKKAAEALKKE--AEEAKKAEELK 1708
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
990-1036 |
1.68e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 61.22 E-value: 1.68e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1911235092 990 PCNCNSFGSKSFDCE-ESGQCWCQPGVTGKKCDHCAHGYFNF--QEGGCT 1036
Cdd:cd00055 1 PCDCNGHGSLSGQCDpGTGQCECKPNTTGRRCDRCAPGYYGLpsQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
888-940 |
1.99e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 61.22 E-value: 1.99e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1911235092 888 PCQCNDNldFSIPGSCDSLSGACLiCKPGTTGRYCELCADGYFGDAVDARNCQ 940
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. |
1130-1187 |
2.02e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 61.22 E-value: 2.02e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1911235092 1130 CNCFLPGTDDATCDSETkkcacmdqtGQCTCKVNVEGVHCDRCQPGTFGLDAKNPLGC 1187
Cdd:pfam00053 1 CDCNPHGSLSDTCDPET---------GQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1084-1132 |
2.20e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 60.83 E-value: 2.20e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1911235092 1084 CNCSTVGSLDFQCNINTGQCNCHPKFAGAKCTECSRGYWNYPHCDPCNC 1132
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1689-2091 |
3.32e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 69.70 E-value: 3.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1689 ERNMQGLQKEIDQMMRELRrkNLDTQKEVAEDELVAAEGLLKKVQKVFGEPRGKNEKMEKDLGEKLTDHKNKLDDAWDLL 1768
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIA--ELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1769 REATDKTREANRLAAANQQNMTAL---EEKKEAIESGKRQTENTLKEGNDILDEANrlaDEINSVIDYVTDIQTKLppms 1845
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELaeaEAEIEELEAQIEQLKEELKALREALDELR---AELTLLNEEAANLRERL---- 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1846 EELKDKIDDLSREMKDrkLAERVYQAENHAAQLNASsavldgILDEAKSISfNATAAFKAYSNIKDYIDEADKIAKEAKG 1925
Cdd:TIGR02168 827 ESLERRIAATERRLED--LEEQIEELSEDIESLAAE------IEELEELIE-ELESELEALLNERASLEEALALLRSELE 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1926 LAheatklatgpQGSLKDgakgslqksfgILNEAKKLANNVKENDDDLNSLQTRLEKADVR----NGELRRALNDTLAKL 2001
Cdd:TIGR02168 898 EL----------SEELRE-----------LESKRSELRRELEELREKLAQLELRLEGLEVRidnlQERLSEEYSLTLEEA 956
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2002 SAIPNDTAAKLQAAKNKARQA----------NDTAKDVLAQVKDLHQDLDG----LKKSYNQLADSVAKTNAVVKDPLKn 2067
Cdd:TIGR02168 957 EALENKIEDDEEEARRRLKRLenkikelgpvNLAAIEEYEELKERYDFLTAqkedLTEAKETLEEAIEEIDREARERFK- 1035
|
410 420
....*....|....*....|....
gi 1911235092 2068 kiiadadATVKNLEQEADRLIDKL 2091
Cdd:TIGR02168 1036 -------DTFDQVNENFQRVFPKL 1052
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1129-1187 |
8.95e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 59.29 E-value: 8.95e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1911235092 1129 PCNCFLPGTDDATCDSETkkcacmdqtGQCTCKVNVEGVHCDRCQPGTFGlDAKNPLGC 1187
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGT---------GQCECKPNTTGRRCDRCAPGYYG-LPSQGGGC 49
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1591-2153 |
9.67e-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: 67.82 E-value: 9.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1591 ENRTQELKHLLSPQRAPERLIQLAEGNLNTLVTEmnelltratkvtadGEQTGQDAERTSRRANSLGDFIK-GLVRDAEA 1669
Cdd:pfam05483 105 ENKLQENRKIIEAQRKAIQELQFENEKVSLKLEE--------------EIQENKDLIKENNATRHLCNLLKeTCARSAEK 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1670 VNEKAKEVNETLGIqdkafernMQGLQKEIDQMM---RELR----RKNLDTQKEVAEDElvaaegllKKVQKVFGEPRGK 1742
Cdd:pfam05483 171 TKKYEYEREETRQV--------YMDLNNNIEKMIlafEELRvqaeNARLEMHFKLKEDH--------EKIQHLEEEYKKE 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1743 NEKMEKDLGEKL---TDHKNKLDDAWDLLREATDKTREANRLAAANQQNMTALEEKKEAIE--------SGKR--QTENT 1809
Cdd:pfam05483 235 INDKEKQVSLLLiqiTEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTkeledikmSLQRsmSTQKA 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1810 LKEGNDI---------------LDEANRlADEINSVIdyVTDIQTKLPPMSEELK----------DKIDDLSREM--KDR 1862
Cdd:pfam05483 315 LEEDLQIatkticqlteekeaqMEELNK-AKAAHSFV--VTEFEATTCSLEELLRteqqrlekneDQLKIITMELqkKSS 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1863 KLAERVYQAENHAAQLNASSAVL---DGILDEAKSIsfnataafkaysnikdyideaDKIAKEAKGLAHEATKLATGPQG 1939
Cdd:pfam05483 392 ELEEMTKFKNNKEVELEELKKILaedEKLLDEKKQF---------------------EKIAEELKGKEQELIFLLQAREK 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1940 SLKDgakgsLQKSFGILNEAKK-LANNVKEndddlnsLQTRLEKADVRNGELRRALNDTLAKLSAIPNDTAAKLQAAKNK 2018
Cdd:pfam05483 451 EIHD-----LEIQLTAIKTSEEhYLKEVED-------LKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKH 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2019 ARQANDTAKD---VLAQVKDLHQ-------DLDGLKKSYNQLADSV------AKTNAVVKD---PLKNKIIADADATVKN 2079
Cdd:pfam05483 519 QEDIINCKKQeerMLKQIENLEEkemnlrdELESVREEFIQKGDEVkckldkSEENARSIEyevLKKEKQMKILENKCNN 598
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2080 LEQEADrliDKLKPIKELEDN---LKKNISEIKELINQARKQANSIKVSVSSG----GDCIRTYKPEI--KKGSYNNIIV 2150
Cdd:pfam05483 599 LKKQIE---NKNKNIEELHQEnkaLKKKGSAENKQLNAYEIKVNKLELELASAkqkfEEIIDNYQKEIedKKISEEKLLE 675
|
...
gi 1911235092 2151 NVK 2153
Cdd:pfam05483 676 EVE 678
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1444-1490 |
9.82e-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: 9.82e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1444 CQCNGHSSL---CDPETSICQnCQHHTAGDFCERCALGYYGIVKGLPNDC 1490
Cdd:pfam00053 1 CDCNPHGSLsdtCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
419-476 |
1.38e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 58.52 E-value: 1.38e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1911235092 419 CHCDPVGSLSEVCVkdekhaprgLAPGSCHCKPGFGGERCDRCVRGYTGYPDCKPCNC 476
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. |
991-1038 |
2.13e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 58.13 E-value: 2.13e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1911235092 991 CNCNSFGSKSFDCE-ESGQCWCQPGVTGKKCDHCAHGYFNFQEGGCTAC 1038
Cdd:pfam00053 1 CDCNPHGSLSDTCDpETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1130-1187 |
2.73e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 57.71 E-value: 2.73e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1911235092 1130 CNCFLPGTDDATCDSETkkcacmdqtGQCTCKVNVEGVHCDRCQPGTFGldaKNPLGC 1187
Cdd:smart00180 1 CDCDPGGSASGTCDPDT---------GQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1083-1125 |
3.52e-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: 3.52e-10
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1911235092 1083 ACNCSTVGSLDFQCNINTGQCNCHPKFAGAKCTECSRGYWNYP 1125
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1839-2142 |
3.93e-10 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 63.78 E-value: 3.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1839 TKLPPMSEELKDKIDDLSREMKD--RKLAERVYQAENHAAQLNASSAVLDGILDEAKSI-----SFNAtaafkaysNIKD 1911
Cdd:COG1340 4 DELSSSLEELEEKIEELREEIEElkEKRDELNEELKELAEKRDELNAQVKELREEAQELrekrdELNE--------KVKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1912 YIDEADKIAKEAKGLAHEATKLatgpqgslkdgakgslQKSFGILNEAKKLANNVKEnddDLNSLQTRLEKADVrNGELR 1991
Cdd:COG1340 76 LKEERDELNEKLNELREELDEL----------------RKELAELNKAGGSIDKLRK---EIERLEWRQQTEVL-SPEEE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1992 RALNDTLAKLsaipndtAAKLQAAKnKARQANDTAKDVLAQVKDLHQDLDGLKKSYNQLADSVAKtnavvkdpLKNKIIa 2071
Cdd:COG1340 136 KELVEKIKEL-------EKELEKAK-KALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQE--------LHEEMI- 198
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1911235092 2072 dadatvkNLEQEADRLIDKLKPIKELEDNLKKNISEIKELINQARKQANSIKVSVSSggdcIRTYKPEIKK 2142
Cdd:COG1340 199 -------ELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKK----LRKKQRALKR 258
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1443-1491 |
4.00e-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: 57.36 E-value: 4.00e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1911235092 1443 PCQCNGHSSL---CDPETSICQnCQHHTAGDFCERCALGYYGIVKGlPNDCQ 1491
Cdd:cd00055 1 PCDCNGHGSLsgqCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQ-GGGCQ 50
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1589-1997 |
6.71e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 65.06 E-value: 6.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1589 DLENRTQELKHLLSPQRAPerlIQLAEGNLNTLVTEMNELLTRATKV---TADGEQTGQDAERTSR-RANSLgdfikglv 1664
Cdd:PRK02224 318 ELEDRDEELRDRLEECRVA---AQAHNEEAESLREDADDLEERAEELreeAAELESELEEAREAVEdRREEI-------- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1665 rdaEAVNEKAKEVNETLGIQDKAFErNMQGLQKEIDQMMRELR--RKNLDTQKEVAEDELVAAEGLLKK------VQKVF 1736
Cdd:PRK02224 387 ---EELEEEIEELRERFGDAPVDLG-NAEDFLEELREERDELRerEAELEATLRTARERVEEAEALLEAgkcpecGQPVE 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1737 GEP--------RGKNEKME---KDLGEKLTDHKNKLDDAWDLLREATDKTREANRLAAANQ---QNMTALEEKKEAIESG 1802
Cdd:PRK02224 463 GSPhvetieedRERVEELEaelEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEEliaERRETIEEKRERAEEL 542
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1803 KRQTENTLKEGNDILDEANRLADEINSVIDYVTDIQTKLppmsEELKDKIDDLSR----------------EMKDRK--L 1864
Cdd:PRK02224 543 RERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKL----AELKERIESLERirtllaaiadaedeieRLREKReaL 618
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1865 AERVYQAENHAAQLNASSAVLDGILDEAksisfNATAAFKAYSNIKDYIDEADKiakeakglaheatKLATgpqgslKDG 1944
Cdd:PRK02224 619 AELNDERRERLAEKRERKRELEAEFDEA-----RIEEAREDKERAEEYLEQVEE-------------KLDE------LRE 674
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1911235092 1945 AKGSLQKSFG-ILNEAKKLaNNVKENDDDLNSLQTRLE----------------KADVRN---GELRRALNDT 1997
Cdd:PRK02224 675 ERDDLQAEIGaVENELEEL-EELRERREALENRVEALEalydeaeelesmygdlRAELRQrnvETLERMLNET 746
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
780-829 |
7.40e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 56.59 E-value: 7.40e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1911235092 780 PCQCFGHAD---SCDDITAECLnCRDHTGGPYCNQCLPGFYGDPTKGtaEDCQ 829
Cdd:cd00055 1 PCDCNGHGSlsgQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQG--GGCQ 50
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1583-2111 |
9.82e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 64.68 E-value: 9.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1583 PYKMLYDLENRTQELKHLLSpqRAPERLIQLAE--GNLNTLVTEMNELLTRATKVTADGEQTGQDAERTSRRANSLGDFI 1660
Cdd:PRK02224 204 LHERLNGLESELAELDEEIE--RYEEQREQAREtrDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEV 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1661 KGLVRDAEAVNEKAKEVNETLGIQD---KAFERNMQGLQKEIDQMMRELRRKNLDTQKEVAEdelvaAEGLLKKVQKVFG 1737
Cdd:PRK02224 282 RDLRERLEELEEERDDLLAEAGLDDadaEAVEARREELEDRDEELRDRLEECRVAAQAHNEE-----AESLREDADDLEE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1738 EPRGKNEK---MEKDL---GEKLTDHKNKLDDawdlLREATDKTREANRLAAANQQNMTA----LEEKKEAIESGKRQTE 1807
Cdd:PRK02224 357 RAEELREEaaeLESELeeaREAVEDRREEIEE----LEEEIEELRERFGDAPVDLGNAEDfleeLREERDELREREAELE 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1808 NTLKEGNDILDEANRLADEinsvidyvtdiqTKLPPMSEELKD------------KIDDLSREMKDRKLA-ERVYQAENH 1874
Cdd:PRK02224 433 ATLRTARERVEEAEALLEA------------GKCPECGQPVEGsphvetieedreRVEELEAELEDLEEEvEEVEERLER 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1875 AAQLNASSAVLDGILDEAKsisfnataafkaysNIKDYIDEADKIAKE----AKGLAHEATKLATGPQGSLKDGAKGSLq 1950
Cdd:PRK02224 501 AEDLVEAEDRIERLEERRE--------------DLEELIAERRETIEEkrerAEELRERAAELEAEAEEKREAAAEAEE- 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1951 ksfgilnEAKKLANNVKENDDDLNSLQTRLEkadvrngelrrALNDTLAKLSAIPN--DTAAKLQAaKNKARQA-NDTAK 2027
Cdd:PRK02224 566 -------EAEEAREEVAELNSKLAELKERIE-----------SLERIRTLLAAIADaeDEIERLRE-KREALAElNDERR 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2028 DVLAQVKDLHQDLDglkksynqladsvaktnavvkDPLKNKIIADADATVKNLEQEADRLIDKLKPIKELEDNLKKNI-- 2105
Cdd:PRK02224 627 ERLAEKRERKRELE---------------------AEFDEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIga 685
|
....*...
gi 1911235092 2106 --SEIKEL 2111
Cdd:PRK02224 686 veNELEEL 693
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1038-1076 |
1.13e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.17 E-value: 1.13e-09
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1911235092 1038 CDCS---HLGNNCDPKTGRCICPPNTIGDQCSQCVPNTWGHS 1076
Cdd:smart00180 1 CDCDpggSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1037-1082 |
1.16e-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: 56.21 E-value: 1.16e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1037 ACDCSHLG---NNCDPKTGRCICPPNTIGDQCSQCVPNTWGHSII-SGCK 1082
Cdd:cd00055 1 PCDCNGHGslsGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQgGGCQ 50
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1584-2122 |
1.65e-09 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 64.08 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1584 YKMLYDLENRTQELKHLLSPQRAPERLIQLAEGNLNTLVtemnelltraTKVTADGEqtgqdaerTSRRANSLGDFIKGL 1663
Cdd:PTZ00440 449 DEKINELKKSINQLKTLISIMKSFYDLIISEKDSMDSKE----------KKESSDSN--------YQEKVDELLQIINSI 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1664 VRDAEAVNEKAKEVnetlgiqdKAFERNMQGLQKEIDQMMrELRRKNLDTQKEVAEDElvaaegllkkvqkvfgeprGKN 1743
Cdd:PTZ00440 511 KEKNNIVNNNFKNI--------EDYYITIEGLKNEIEGLI-ELIKYYLQSIETLIKDE-------------------KLK 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1744 EKMEKDLGEKL---TDHKNKLDDAWDLLREATDKTREANRLAAANQQNMTALEEKKEAIESGKRQTENTLKEGN--DILD 1818
Cdd:PTZ00440 563 RSMKNDIKNKIkyiEENVDHIKDIISLNDEIDNIIQQIEELINEALFNKEKFINEKNDLQEKVKYILNKFYKGDlqELLD 642
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1819 EANRLADEINSVI---DYVTDIQTKLPPMSEE-----------LKDKIDDLSREMKDRKLAERVYQAENHAAQLNASSAV 1884
Cdd:PTZ00440 643 ELSHFLDDHKYLYheaKSKEDLQTLLNTSKNEyeklefmksdnIDNIIKNLKKELQNLLSLKENIIKKQLNNIEQDISNS 722
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1885 LDGILDEAKSISfNATAAFKAYSN-IKDYIDEADKIAKEAKGLAHEATKlaTGPQG--------SLKDGAkgsLQKSFGI 1955
Cdd:PTZ00440 723 LNQYTIKYNDLK-SSIEEYKEEEEkLEVYKHQIINRKNEFILHLYENDK--DLPDGkntyeeflQYKDTI---LNKENKI 796
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1956 LNEAKKLANNVKENDDDLNSLQTRLEKADVRNGELRRALNDTLAKLSAipNDTAAKLQAAKNKARQANDTAKDVLAQVKD 2035
Cdd:PTZ00440 797 SNDINILKENKKNNQDLLNSYNILIQKLEAHTEKNDEELKQLLQKFPT--EDENLNLKELEKEFNENNQIVDNIIKDIEN 874
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2036 LHQDLDGLKK---------SYNQLADSVAKTnavvKDPLKNKIiadaDATVKNLEQeaDRLIDKLKPIKeLEDNLKKNIS 2106
Cdd:PTZ00440 875 MNKNINIIKTlniainrsnSNKQLVEHLLNN----KIDLKNKL----EQHMKIINT--DNIIQKNEKLN-LLNNLNKEKE 943
|
570 580
....*....|....*....|.
gi 1911235092 2107 EIKE-----LINQARKQANSI 2122
Cdd:PTZ00440 944 KIEKqlsdtKINNLKMQIEKT 964
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1684-1922 |
1.73e-09 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 61.85 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1684 QDKAFERNMQGLQKEIDQM---MRELRRKNLDTQKEVAEdelVAAE--GLLKKVQKVFGEPRGKNEKMeKDLGEKLTDHK 1758
Cdd:COG1340 2 KTDELSSSLEELEEKIEELreeIEELKEKRDELNEELKE---LAEKrdELNAQVKELREEAQELREKR-DELNEKVKELK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1759 NKLDDAWDLLREATDKTREANRLAAANQQNMTALEEKKEAIES--GKRQTEN-TLKEGNDILDEANRL------ADEINS 1829
Cdd:COG1340 78 EERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERleWRQQTEVlSPEEEKELVEKIKELekelekAKKALE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1830 VIDYVTDIQTKLppmsEELKDKIDDLSREMKdrKLAErvyQAENHAAQLNASSAVLDGILDEAKSisfnataafkAYSNI 1909
Cdd:COG1340 158 KNEKLKELRAEL----KELRKEAEEIHKKIK--ELAE---EAQELHEEMIELYKEADELRKEADE----------LHKEI 218
|
250
....*....|...
gi 1911235092 1910 KDYIDEADKIAKE 1922
Cdd:COG1340 219 VEAQEKADELHEE 231
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
889-932 |
2.85e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 55.01 E-value: 2.85e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1911235092 889 CQCNdnLDFSIPGSCDSLSGACLiCKPGTTGRYCELCADGYFGD 932
Cdd:smart00180 1 CDCD--PGGSASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD 41
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
418-470 |
3.00e-09 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 55.05 E-value: 3.00e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1911235092 418 PCHCDPVGSLSEVCVKDEkhaprglapGSCHCKPGFGGERCDRCVRGYTGYPD 470
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. |
474-520 |
3.77e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 54.67 E-value: 3.77e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1911235092 474 CNCSGEGSANE--DPCFGPCHCKENVEGGDCSRCKSGFFNLQESNQKGC 520
Cdd:pfam00053 1 CDCNPHGSLSDtcDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1672-2096 |
3.89e-09 |
|
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: 62.28 E-value: 3.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1672 EKAKEVNETLGIQdKAFERNMQGLQKEIDQmmrelrrknldtqkevaEDELvaaEGLLKKVQKVFGEPRGKNEKMEKDLG 1751
Cdd:COG5185 223 EKAKEIINIEEAL-KGFQDPESELEDLAQT-----------------SDKL---EKLVEQNTDLRLEKLGENAESSKRLN 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1752 EKLTDHKNKLDDAWDLLREATDK------TREANRLAAANQQNmTALEEKKEAIESG-KRQTENTLKEGNDILDEANRLA 1824
Cdd:COG5185 282 ENANNLIKQFENTKEKIAEYTKSidikkaTESLEEQLAAAEAE-QELEESKRETETGiQNLTAEIEQGQESLTENLEAIK 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1825 DEINSVIDYVtdIQTKLPPMSEELKDKIDDLSRemkdrklaervyqaENHAAQLNASSAVLDGILDEAKSISFNATAAFK 1904
Cdd:COG5185 361 EEIENIVGEV--ELSKSSEELDSFKDTIESTKE--------------SLDEIPQNQRGYAQEILATLEDTLKAADRQIEE 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1905 AYSNIKDYIDEADKIAKEAKGLAHEATKLATgpqgSLKDGAKGSLQksfgilNEAKKLANNVKENDDDLNSLQTRLEKad 1984
Cdd:COG5185 425 LQRQIEQATSSNEEVSKLLNELISELNKVMR----EADEESQSRLE------EAYDEINRSVRSKKEDLNEELTQIES-- 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1985 vRNGELRRALNDTLAKLSaipndtaAKLQAAKNKARQANDTAKDVLAQVKDLHqdldgLKKSYNQLADSVAKTNavvkDP 2064
Cdd:COG5185 493 -RVSTLKATLEKLRAKLE-------RQLEGVRSKLDQVAESLKDFMRARGYAH-----ILALENLIPASELIQA----SN 555
|
410 420 430
....*....|....*....|....*....|..
gi 1911235092 2065 LKNKIIADADATVKNLEQEADRLIDKLKPIKE 2096
Cdd:COG5185 556 AKTDGQAANLRTAVIDELTQYLSTIESQQARE 587
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
889-938 |
4.16e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 54.67 E-value: 4.16e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1911235092 889 CQCNDNLdfSIPGSCDSLSGACLiCKPGTTGRYCELCADGYFGDAVDARN 938
Cdd:pfam00053 1 CDCNPHG--SLSDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQ 47
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1697-2162 |
5.85e-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: 62.38 E-value: 5.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1697 KEIDQMMRELRRKNLDTQKEVaEDELVAAEGLLKKVQK--VFGEPRGKNEKM--EKDLGE---KLTDHKNKLddawdLLR 1769
Cdd:TIGR01612 1361 KKIIDEVKEYTKEIEENNKNI-KDELDKSEKLIKKIKDdiNLEECKSKIESTldDKDIDEcikKIKELKNHI-----LSE 1434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1770 EATDKT-----REANRLAAANQQNMTALEEKKEAIESGKRQTE--------NTLKEGND----ILDEA--NRLADEINSV 1830
Cdd:TIGR01612 1435 ESNIDTyfknaDENNENVLLLFKNIEMADNKSQHILKIKKDNAtndhdfniNELKEHIDkskgCKDEAdkNAKAIEKNKE 1514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1831 I--DYVTDIQTKLPPMSE-ELKDKIDD-------LSREMKDRKlAERVYQAENHAAQLNASSAVLDGILDEAKSISFNAT 1900
Cdd:TIGR01612 1515 LfeQYKKDVTELLNKYSAlAIKNKFAKtkkdseiIIKEIKDAH-KKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNK 1593
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1901 AAFKAYSNIKDYIDEADKIakeakglaheaTKLATGPQGSLKDGAkgSLQK---SFGILNEAKKLannvKENDDDLNSLQ 1977
Cdd:TIGR01612 1594 AAIDIQLSLENFENKFLKI-----------SDIKKKINDCLKETE--SIEKkisSFSIDSQDTEL----KENGDNLNSLQ 1656
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1978 TRLE--KADVRNGE-LRRALNDTLAKLSAIPNDTAaklQAAKN-------KARQANDTAKDVLAQVKDLHQ--------- 2038
Cdd:TIGR01612 1657 EFLEslKDQKKNIEdKKKELDELDSEIEKIEIDVD---QHKKNyeigiieKIKEIAIANKEEIESIKELIEptienliss 1733
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2039 ----DLDGLK--------------------KSYNQLA---DSVAKtNAVVKDPLKNKIIADADATVKNLEQEadrlidkl 2091
Cdd:TIGR01612 1734 fntnDLEGIDpnekleeynteigdiyeefiELYNIIAgclETVSK-EPITYDEIKNTRINAQNEFLKIIEIE-------- 1804
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1911235092 2092 KPIKELEDNLKknISEIKELINQARKQANSIKVSVSsggdciRTYKpEIKKGsYNNI---IVNVKTPVADNLLF 2162
Cdd:TIGR01612 1805 KKSKSYLDDIE--AKEFDRIINHFKKKLDHVNDKFT------KEYS-KINEG-FDDIsksIENVKNSTDENLLF 1868
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1084-1127 |
6.56e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 53.85 E-value: 6.56e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1911235092 1084 CNCSTVGSLDFQCNINTGQCNCHPKFAGAKCTECSRGYW--NYPHC 1127
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYgdGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1038-1081 |
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 1911235092 1038 CDCSHLG---NNCDPKTGRCICPPNTIGDQCSQCVPNTWGHSIISGC 1081
Cdd:pfam00053 1 CDCNPHGslsDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQ 47
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1639-1987 |
8.32e-09 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 60.30 E-value: 8.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1639 GEQTGQDAERTSRRANSLGDFIKGLVRDAEAVNEKAKEVNETLgiqdKAFERNMQGLQKEIDQMMRELRRKN-----LDT 1713
Cdd:COG4372 5 GEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEEL----EQLREELEQAREELEQLEEELEQARseleqLEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1714 QKEVAEDELVAAEGLLKKVQKVFGEPRGKNEKMEKDL------GEKLTDHKNKLDDAWDLLREA-TDKTREANRLaaanQ 1786
Cdd:COG4372 81 ELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELeelqkeRQDLEQQRKQLEAQIAELQSEiAEREEELKEL----E 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1787 QNMTALEEKKEAIESGKRQ--TENTLKEGNDILDEANRLAdeinsvidYVTDIQTKLPPMSEELKDKIDDLSREMKDRKL 1864
Cdd:COG4372 157 EQLESLQEELAALEQELQAlsEAEAEQALDELLKEANRNA--------EKEEELAEAEKLIESLPRELAEELLEAKDSLE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1865 AERVYqaeNHAAQLNASSAVLDGILDEAKSISFNATAAFKAYSNIKDYIDEADKIAKEAKGLAHEATKLATGPQGSLKDG 1944
Cdd:COG4372 229 AKLGL---ALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLA 305
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1911235092 1945 A-----KGSLQKSFGILNEAKKLANNVKENDDDLNSLQTRLEKADVRN 1987
Cdd:COG4372 306 AlsligALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDN 353
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1955-2124 |
1.33e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 59.92 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1955 ILNEAKKLANNVKENDDDLNSLQTRLEKAdvrNGELRRA------LNDTLAKLSAIPNDTAAKLQAAKNKARQANDTAKD 2028
Cdd:COG4372 43 LQEELEQLREELEQAREELEQLEEELEQA---RSELEQLeeeleeLNEQLQAAQAELAQAQEELESLQEEAEELQEELEE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2029 VLAQVKDLHQDLDGLKKSYNQLadsvaktnavvkdplkNKIIADADATVKNLEQEADRLIDKLKPIKELEDNLKKN--IS 2106
Cdd:COG4372 120 LQKERQDLEQQRKQLEAQIAEL----------------QSEIAEREEELKELEEQLESLQEELAALEQELQALSEAeaEQ 183
|
170
....*....|....*...
gi 1911235092 2107 EIKELINQARKQANSIKV 2124
Cdd:COG4372 184 ALDELLKEANRNAEKEEE 201
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
419-471 |
1.63e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 52.70 E-value: 1.63e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1911235092 419 CHCDPVGSLSEVCVKDEkhaprglapGSCHCKPGFGGERCDRCVRGYTG--YPDC 471
Cdd:smart00180 1 CDCDPGGSASGTCDPDT---------GQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
781-828 |
1.67e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 52.74 E-value: 1.67e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1911235092 781 CQCFGHA---DSCDDITAECLnCRDHTGGPYCNQCLPGFYGDPtKGTAEDC 828
Cdd:pfam00053 1 CDCNPHGslsDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLP-SDPPQGC 49
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1683-2048 |
1.76e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.46 E-value: 1.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1683 IQDKAFE--RNMQGL--QKEIDQMMRELRRKNLDTQKEVAEDELVAAEGLLKKVQKVFgeprgknEKMEKDLgEKLTDHK 1758
Cdd:TIGR02168 191 LEDILNEleRQLKSLerQAEKAERYKELKAELRELELALLVLRLEELREELEELQEEL-------KEAEEEL-EELTAEL 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1759 NKLDDAWDLLR----EATDKTREANR--LAAANQQNmtALEEKKEAIESGKRQTENTLKEGNDILDEA----NRLADEIN 1828
Cdd:TIGR02168 263 QELEEKLEELRlevsELEEEIEELQKelYALANEIS--RLEQQKQILRERLANLERQLEELEAQLEELesklDELAEELA 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1829 SVIDYVTDIQTKLppmsEELKDKIDDLSREMKDRKLAERVYQaenhaAQLNASSAVLDGILDEAKSIsfNATaafkaysn 1908
Cdd:TIGR02168 341 ELEEKLEELKEEL----ESLEAELEELEAELEELESRLEELE-----EQLETLRSKVAQLELQIASL--NNE-------- 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1909 ikdyIDEADkiaKEAKGLAHEATKLATGPQGSLKDGAKGSLQKSFGILNEAKKLANNVKEnddDLNSLQTRLEKADVRNG 1988
Cdd:TIGR02168 402 ----IERLE---ARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQE---ELERLEEALEELREELE 471
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1989 ELRRALNDTLAKLSAIPNDTAAkLQAAKNKARQANDTAKDVLAQVKDLHQDLDGLKKSYN 2048
Cdd:TIGR02168 472 EAEQALDAAERELAQLQARLDS-LERLQENLEGFSEGVKALLKNQSGLSGILGVLSELIS 530
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1776-2126 |
2.56e-08 |
|
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: 60.08 E-value: 2.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1776 REANRLAAANQQNMTALEEKKEAIESGKRQTENTLKEGNDILDEANRLADEInsvidyvTDIQTKLppmsEELKDKIDDL 1855
Cdd:TIGR02169 688 RELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERL-------EELEEDL----SSLEQEIENV 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1856 SREMKD--RKLAERVYQAENHAAQLNASSAVLDG-ILDEAKsisfnataafKAYSNIKDYIDEADKIAKEAKGLAHEATK 1932
Cdd:TIGR02169 757 KSELKEleARIEELEEDLHKLEEALNDLEARLSHsRIPEIQ----------AELSKLEEEVSRIEARLREIEQKLNRLTL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1933 LatgpqgslkdgaKGSLQKSF-GILNEAKKLANNVKENDDDLNSLQTRLEKADVRNGELRRALND---TLAKLSAIPNDT 2008
Cdd:TIGR02169 827 E------------KEYLEKEIqELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDlesRLGDLKKERDEL 894
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2009 AAKLQAAKNKARQANDTAKDVLAQVKDLHQDLDGLKKSYNQLADSVAktnAVVKDPLKNKIIADADATVKNLE------- 2081
Cdd:TIGR02169 895 EAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKG---EDEEIPEEELSLEDVQAELQRVEeeirale 971
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1911235092 2082 -------QEADRLIDKLKPIKELEDNLKKNISEIKELINQARKQANSIKVSV 2126
Cdd:TIGR02169 972 pvnmlaiQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREVFMEA 1023
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1618-2123 |
3.68e-08 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 59.20 E-value: 3.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1618 LNTLVTEMNELLTRATKVTadGEQTGQDAERTSRRANSLGDFIKGLVRDAEAVNEKAKEVNETLGIQDKAFERNM--QGL 1695
Cdd:COG5185 49 LGISRDSLRVTLRSVINVL--DGLNYQNDVKKSESSVKARKFLKEKKLDTKILQEYVNSLIKLPNYEWSADILISllYLY 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1696 QKEIDQMMRELR--RKNldtqKEVAEDELVAAEGLLKKVQKVFGE-PRGKNEKMEKDLGEKLTDhknklddawdLLREAT 1772
Cdd:COG5185 127 KSEIVALKDELIkvEKL----DEIADIEASYGEVETGIIKDIFGKlTQELNQNLKKLEIFGLTL----------GLLKGI 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1773 DKTREANRLAAANQQnMTALEEKkeaiESGKRQTENTLKEGNDILdEANRLADEINSVIDYVTDIQTKLppmsEELKDKI 1852
Cdd:COG5185 193 SELKKAEPSGTVNSI-KESETGN----LGSESTLLEKAKEIINIE-EALKGFQDPESELEDLAQTSDKL----EKLVEQN 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1853 DDLsREMKDRKLAERVYQA-ENHAAQLNASSAVLDGILDEAKSISfnataAFKAYSNIKDYIDEADKIAKEAKGLAHEAT 1931
Cdd:COG5185 263 TDL-RLEKLGENAESSKRLnENANNLIKQFENTKEKIAEYTKSID-----IKKATESLEEQLAAAEAEQELEESKRETET 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1932 KLATGPQGSLKDgaKGSLQKSFGILNEAKK---LANNVKENDDDLNSLQTRLEKADVRNGELRRALndtlaklsaipndt 2008
Cdd:COG5185 337 GIQNLTAEIEQG--QESLTENLEAIKEEIEnivGEVELSKSSEELDSFKDTIESTKESLDEIPQNQ-------------- 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2009 aakLQAAKNKARQANDTAKDVLAQVKDLHQDLDGLKKSY-------NQLADSVAKTNAVVKDPLKNKIIADADATVKNLE 2081
Cdd:COG5185 401 ---RGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNeevskllNELISELNKVMREADEESQSRLEEAYDEINRSVR 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1911235092 2082 QEADRLIDKLKPIK-----------ELEDNLKKNISEIKELINQarkQANSIK 2123
Cdd:COG5185 478 SKKEDLNEELTQIEsrvstlkatleKLRAKLERQLEGVRSKLDQ---VAESLK 527
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1672-2122 |
4.44e-08 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 58.93 E-value: 4.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1672 EKAKEVNETLGIQDK------------AFERNMQGLQKEIDQMMRELRRknLDTQKEvaeDELVAAEGLLKKVQkvfgEP 1739
Cdd:pfam05622 29 EKNSLQQENKKLQERldqlesgddsgtPGGKKYLLLQKQLEQLQEENFR--LETARD---DYRIKCEELEKEVL----EL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1740 RGKNEKMEKdlgekLTDHKNKLDDAWDLLREATDKtreANRLaaanQQNMTALEEKKEAIESGKRQTEnTLKEGN----- 1814
Cdd:pfam05622 100 QHRNEELTS-----LAEEAQALKDEMDILRESSDK---VKKL----EATVETYKKKLEDLGDLRRQVK-LLEERNaeymq 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1815 ---DILDEANRLADEINSVIDY---VTDIQTKLppmSEE-------------LKDKIDDLSREmKDRKLAER--VYQA-- 1871
Cdd:pfam05622 167 rtlQLEEELKKANALRGQLETYkrqVQELHGKL---SEEskkadklefeykkLEEKLEALQKE-KERLIIERdtLRETne 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1872 ENHAAQLNASSAVLDGILDEAKSISFNATAAFKAYSNIKDYIDEadkiakeakgLAHEaTKLatgpqgsLKDGAKGSlqk 1951
Cdd:pfam05622 243 ELRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIR----------LQHE-NKM-------LRLGQEGS--- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1952 sfgilneakklannvkeNDDDLNSLQTRLEKADVRNGELR---RALNDTLAKLSAIPNDTAAKLQAAKNKARQANDTAKD 2028
Cdd:pfam05622 302 -----------------YRERLTELQQLLEDANRRKNELEtqnRLANQRILELQQQVEELQKALQEQGSKAEDSSLLKQK 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2029 VLAQVKDLHQDLDGLKKSYNQLADSVAK--TNAVVK-DPLKNKIIAdADATVKNLEQEADRLIDKLKP-IKELEDnlKKN 2104
Cdd:pfam05622 365 LEEHLEKLHEAQSELQKKKEQIEELEPKqdSNLAQKiDELQEALRK-KDEDMKAMEERYKKYVEKAKSvIKTLDP--KQN 441
|
490 500
....*....|....*....|.
gi 1911235092 2105 ---ISEIKELINQARKQANSI 2122
Cdd:pfam05622 442 pasPPEIQALKNQLLEKDKKI 462
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1617-2131 |
5.59e-08 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 59.07 E-value: 5.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1617 NLNTLVT--EMNELLTRATKVTADGEQTGQDAERTSRRANSLgdfIKGLVRDAEAVNEKAKEVNETLgiQDKAFERNMQG 1694
Cdd:PTZ00440 1286 NMYEFLIsiDSEKILKEILNSTKKAEEFSNDAKKELEKTDNL---IKQVEAKIEQAKEHKNKIYGSL--EDKQIDDEIKK 1360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1695 L---QKEI----DQMMRELrrKNLDTQKEVAEDELVAAE------GLLKKvqkvfGEPRGKNEKMEKDLGeKLTDHKNKL 1761
Cdd:PTZ00440 1361 IeqiKEEIsnkrKEINKYL--SNIKSNKEKCDLHVRNASrgkdkiDFLNK-----HEAIEPSNSKEVNII-KITDNINKC 1432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1762 DDawdLLREATDKTREANrlaaANQQNMTALEEK-----KEAIESGKRQT-ENTLKEGNDILDEANRLADEINSVidyVT 1835
Cdd:PTZ00440 1433 KQ---YSNEAMETENKAD----ENNDSIIKYEKEitnilNNSSILGKKTKlEKKKKEATNIMDDINGEHSIIKTK---LT 1502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1836 DIQTKLPPMSEE--LKDKIDDLSREMKdrKLAERVYQAENHAAQLNASSavLDGILDEAKSISFNATAAFKAYSNIK--- 1910
Cdd:PTZ00440 1503 KSSEKLNQLNEQpnIKREGDVLNNDKS--TIAYETIQYNLGRVKHNLLN--ILNIKDEIETILNKAQDLMRDISKISkiv 1578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1911 -------------DYIDEADKIAKEAKGLAHEATKLatGPQGSLKDGAKGSLQKS-----FGILNEAKKLANNVK----E 1968
Cdd:PTZ00440 1579 enknlenlndkeaDYVKYLDNILKEKQLMEAEYKKL--NEIYSDVDNIEKELKKHkknyeIGLLEKVIEINKNIKlymdS 1656
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1969 NDDDLNSL----QTRLEKADVRNGELRRALNDTLAKLSAIPNDTAAKLQAAKNKARQANDTAKDvLAQVKDLHQDLdglK 2044
Cdd:PTZ00440 1657 TKESLNSLvnnfSSLFNNFYLNKYNINENLEKYKKKLNEIYNEFMESYNIIQEKMKEVSNDDVD-YNEAKTLREEA---Q 1732
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2045 KSYNQLADSVAKTNAVVKDplknkiiadadatVKNleQEADRLIDKlkpIKELEDNLKKNISEIKELINQARKQANSIKV 2124
Cdd:PTZ00440 1733 KEEVNLNNKEEEAKKYLND-------------IKK--QESFRFILY---MKEKLDELSKMCKQQYNIVDEGYNYIKKKIE 1794
|
....*..
gi 1911235092 2125 SVSSGGD 2131
Cdd:PTZ00440 1795 YIKTLND 1801
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1647-2127 |
5.72e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 58.76 E-value: 5.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1647 ERTSRRANSLGDFIKGL---VRDAEAVNEKAKEVNETLGIQDKAFE----------RNMQGLQKEIDQMMRELRR----- 1708
Cdd:PRK01156 162 NSLERNYDKLKDVIDMLraeISNIDYLEEKLKSSNLELENIKKQIAddekshsitlKEIERLSIEYNNAMDDYNNlksal 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1709 KNLDTQKEVA---EDELVAAEGLLKKVQKVFGEPRGKNEKMEKDLGEKLTDHKNKLDDAWDLLREATDKTREANRLAAaN 1785
Cdd:PRK01156 242 NELSSLEDMKnryESEIKTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDA-E 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1786 QQNMTALEEKKEAIESGKRQTENTLKEGNDILDEANRLADEINSVIDYVTDIqtklppmsEELKDKIDDLSREMKD--RK 1863
Cdd:PRK01156 321 INKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSI--------ESLKKKIEEYSKNIERmsAF 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1864 LAERVYQAENHAAQLNASSAVLDGILDEAKSISFNATAAFKAYSNIKDYIDEADKIAKEAKGLAHEATKLatGPQGSlKD 1943
Cdd:PRK01156 393 ISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPVCGTTL--GEEKS-NH 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1944 GAKGSLQKSFGILNEAKKLANNVKENDD---DLNSLQTRLEKADVRNGE--------LRRALNDTLAKLSAIpNDTAAKL 2012
Cdd:PRK01156 470 IINHYNEKKSRLEEKIREIEIEVKDIDEkivDLKKRKEYLESEEINKSIneynkiesARADLEDIKIKINEL-KDKHDKY 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2013 QAAKNKAR--------QANDTAKDVLAQVKDLhqDLDGLKKSYN----QLADSVAKTNAVVKD--PLKNKIiadaDATVK 2078
Cdd:PRK01156 549 EEIKNRYKslkledldSKRTSWLNALAVISLI--DIETNRSRSNeikkQLNDLESRLQEIEIGfpDDKSYI----DKSIR 622
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1911235092 2079 NLEQEADRLIDKLKPIKELE----------DNLKKNISEIKELI-----------------NQARKQANSIKVSVS 2127
Cdd:PRK01156 623 EIENEANNLNNKYNEIQENKilieklrgkiDNYKKQIAEIDSIIpdlkeitsrindiednlKKSRKALDDAKANRA 698
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1589-2113 |
6.07e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.91 E-value: 6.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1589 DLENRTQELKHLLSPQRAPERLIQLAEGNLNTLVTEMNELLTRATKVTADGEQTGQDAERTSRRANSLGDFIKGLvrDAE 1668
Cdd:TIGR02168 352 ELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEEL--LKK 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1669 AVNEKAKEVNETLGIQDKAFErnmqGLQKEIDQMMRELRRknLDTQKEVAEDELVAAEGLLKKVQ-KVFGEPRGKNEKME 1747
Cdd:TIGR02168 430 LEEAELKELQAELEELEEELE----ELQEELERLEEALEE--LREELEEAEQALDAAERELAQLQaRLDSLERLQENLEG 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1748 KDLGEK-LTDHKNKLDD----AWDLLReaTDKTREANrLAAANQQNMTAL-----EEKKEAIES------GKR------- 1804
Cdd:TIGR02168 504 FSEGVKaLLKNQSGLSGilgvLSELIS--VDEGYEAA-IEAALGGRLQAVvvenlNAAKKAIAFlkqnelGRVtflplds 580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1805 --------QTENTLKEGNDILDEANRL---ADEINSVIDY-------VTDIQTKLppmseELKDKID------------- 1853
Cdd:TIGR02168 581 ikgteiqgNDREILKNIEGFLGVAKDLvkfDPKLRKALSYllggvlvVDDLDNAL-----ELAKKLRpgyrivtldgdlv 655
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1854 ----------------DLSREMKDRKLAERVYQAENHAAQLNASSAVLDGILDEAKSisfNATAAFKAYSNIKDYIDEAD 1917
Cdd:TIGR02168 656 rpggvitggsaktnssILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEE---ELEQLRKELEELSRQISALR 732
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1918 KIAKEAKGLAHEATKLATGPQGSLKD------GAKGSLQKSFGILNEAK----KLANNVKENDDDLNSLQTRLEKADVRN 1987
Cdd:TIGR02168 733 KDLARLEAEVEQLEERIAQLSKELTEleaeieELEERLEEAEEELAEAEaeieELEAQIEQLKEELKALREALDELRAEL 812
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1988 GELRRALNDTLAKLSAIPNDTAAKLQAAKNKARQANDTAKDVL---AQVKDLHQDLDGLKKSYNQLADSVAKTN---AVV 2061
Cdd:TIGR02168 813 TLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIEslaAEIEELEELIEELESELEALLNERASLEealALL 892
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 1911235092 2062 KDPLKNKI--IADADATVKNLEQEADRLIDKLKPIKELEDNLKKNISEIKELIN 2113
Cdd:TIGR02168 893 RSELEELSeeLRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLS 946
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1884-2124 |
6.22e-08 |
|
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: 57.38 E-value: 6.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1884 VLDGILDEAKSIS-FNATAAFKA---YSNIKDYIDEADKIAKEAKglaheatklatgpQGSLKDGAKGSLQKsfgILNEA 1959
Cdd:cd22656 67 TYPSIVSLAGDIYnYAQNAGGTIdsyYAEILELIDDLADATDDEE-------------LEEAKKTIKALLDD---LLKEA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1960 KKLANNVKENDDDLNSLQTRLEKADVRNGELRRALNDTL-AKLSAIPNDTAAKLQAAKNKARQAndtakdvlaQVKDLHQ 2038
Cdd:cd22656 131 KKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLLtDEGGAIARKEIKDLQKELEKLNEE---------YAAKLKA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2039 DLDGLKKSYNQLADSVAKTNAVVKDplknkiIADADATVKNLEQEADRLIDKLKPIKELEDNLKKNISEIKELINQARKQ 2118
Cdd:cd22656 202 KIDELKALIADDEAKLAAALRLIAD------LTAADTDLDNLLALIGPAIPALEKLQGAWQAIATDLDSLKDLLEDDISK 275
|
....*.
gi 1911235092 2119 ANSIKV 2124
Cdd:cd22656 276 IPAAIL 281
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1660-2149 |
1.35e-07 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 57.92 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1660 IKGLVRDAEAVNEKA---KEVNETLGIQDKAFErNMQGLQKEIDQMMRELRR-KNLDTQKEVAEDELVA---------AE 1726
Cdd:PTZ00440 1233 IEELTTEAKGLKGEAnrsTNVDELKEIKLQVFS-YLQQVIKENNKMENALHEiKNMYEFLISIDSEKILkeilnstkkAE 1311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1727 GLLKKVQKVFGEPRGKNEKMEKDLgEKLTDHKNKLDDAwdLLREATDKtrEANRLAAANQQNMTALEEKKEAIESGKRQT 1806
Cdd:PTZ00440 1312 EFSNDAKKELEKTDNLIKQVEAKI-EQAKEHKNKIYGS--LEDKQIDD--EIKKIEQIKEEISNKRKEINKYLSNIKSNK 1386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1807 ENTLKEgndiLDEANRLADeinsVIDYVTDIQTKLPPMSEELK-DKIDDLSREMKdrKLAERVYQAENHAaqlnasSAVL 1885
Cdd:PTZ00440 1387 EKCDLH----VRNASRGKD----KIDFLNKHEAIEPSNSKEVNiIKITDNINKCK--QYSNEAMETENKA------DENN 1450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1886 DGILDEAKSIS--FNATAAFKAYSNIKDYIDEADKIAKEAKGLAHE-ATKLAtgpqgslkdgakgSLQKSFGILNEAKkl 1962
Cdd:PTZ00440 1451 DSIIKYEKEITniLNNSSILGKKTKLEKKKKEATNIMDDINGEHSIiKTKLT-------------KSSEKLNQLNEQP-- 1515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1963 anNVKENDDDLNSLQTRLEKADVR--NGELRRALNDTlaklsaipNDTAAKLQAAKNKArqaNDTAKDVLAQVK-DLHQD 2039
Cdd:PTZ00440 1516 --NIKREGDVLNNDKSTIAYETIQynLGRVKHNLLNI--------LNIKDEIETILNKA---QDLMRDISKISKiVENKN 1582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2040 LDGLKKSYN---QLADSVAKTNAVVKDPLK--NKIIADADATVKNLEQEADRL-IDKLKPIKELEDNLKKNISEIKELIN 2113
Cdd:PTZ00440 1583 LENLNDKEAdyvKYLDNILKEKQLMEAEYKklNEIYSDVDNIEKELKKHKKNYeIGLLEKVIEINKNIKLYMDSTKESLN 1662
|
490 500 510
....*....|....*....|....*....|....*.
gi 1911235092 2114 QARKQANSIKVSVSsggdcIRTYKPEIKKGSYNNII 2149
Cdd:PTZ00440 1663 SLVNNFSSLFNNFY-----LNKYNINENLEKYKKKL 1693
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1665-2123 |
1.38e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.84 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1665 RDAEAVNE---KAKEVNETLGIQDKAFERNMQGLQKEIDQMMRELRRKNLDTQKevAEDELVAAEGLLKKVQKVFGEPRG 1741
Cdd:PTZ00121 1088 RADEATEEafgKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARK--AEEARKAEDAKRVEIARKAEDARK 1165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1742 KNEKMEKDLGEKLTDHKNKLDdawdlLREATD--KTREANRLAAANQ-QNMTALEEKKEAIESGKRQTENTLKEGNDILD 1818
Cdd:PTZ00121 1166 AEEARKAEDAKKAEAARKAEE-----VRKAEElrKAEDARKAEAARKaEEERKAEEARKAEDAKKAEAVKKAEEAKKDAE 1240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1819 EANRlADEINSVIDYVTDIQTKLPPMSEELKDKIDDLSREMKDRKLAERVYQAEnhaaQLNASSAVLDgiLDEAKSisfN 1898
Cdd:PTZ00121 1241 EAKK-AEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAD----EAKKAEEKKK--ADEAKK---K 1310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1899 ATAAFKAySNIKDYIDEADKIAKEAKGLAHEATKLATGPQGSLKDGAKgSLQKSFGILNEAKKLANNVKENDDDLNSLQT 1978
Cdd:PTZ00121 1311 AEEAKKA-DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAAD-EAEAAEEKAEAAEKKKEEAKKKADAAKKKAE 1388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1979 RLEKADvrngELRRALNDTLAKLsaipnDTAAKLQAAKNKARQANDTAKDVlaqvkdlhQDLDGLKKSynqlADSVAKTn 2058
Cdd:PTZ00121 1389 EKKKAD----EAKKKAEEDKKKA-----DELKKAAAAKKKADEAKKKAEEK--------KKADEAKKK----AEEAKKA- 1446
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2059 avvkDPLKNKiiADADATVKNLEQEAD--RLIDKLKPIKELE---DNLKKNISEIKELINQARKQANSIK 2123
Cdd:PTZ00121 1447 ----DEAKKK--AEEAKKAEEAKKKAEeaKKADEAKKKAEEAkkaDEAKKKAEEAKKKADEAKKAAEAKK 1510
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1665-2142 |
1.67e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 57.22 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1665 RDAEAVNEKAKEVNetlgiqdKAFERNMQGLQKEIdqmmrelrRKNLDTQKEVAEDELVAaeGLLKKVQKVFGE-----P 1739
Cdd:PRK01156 101 KDGSIIAEGFDDTT-------KYIEKNILGISKDV--------FLNSIFVGQGEMDSLIS--GDPAQRKKILDEileinS 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1740 RGKNEKMEKDLGEKLTDHKNKLDDAWDLLREATDKTREANRLAAANQQNMTALEEKKEAIESGKRQTENTLKEGNDILDE 1819
Cdd:PRK01156 164 LERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNE 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1820 ANRLADEINSVIDYVTDIQTKLpPMSEELKDKIDDLSREMK----DRKLAERVYQAE--NHAAQLNASSAVLDGILDEAK 1893
Cdd:PRK01156 244 LSSLEDMKNRYESEIKTAESDL-SMELEKNNYYKELEERHMkiinDPVYKNRNYINDyfKYKNDIENKKQILSNIDAEIN 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1894 SISfnatAAFKAYSNIKDYIDEADKIAKEAKGLAHEATKLATGP---QGSLKDgakgslqksfgILNEAKKLANNVKEND 1970
Cdd:PRK01156 323 KYH----AIIKKLSVLQKDYNDYIKKKSRYDDLNNQILELEGYEmdyNSYLKS-----------IESLKKKIEEYSKNIE 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1971 DDLNSLQTRLEKADVRNGELRRALNDTLAKLSAIPNDTAAkLQAAKNKARQANDTAKDVLAQ------------------ 2032
Cdd:PRK01156 388 RMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSS-LNQRIRALRENLDELSRNMEMlngqsvcpvcgttlgeek 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2033 ----VKDLHQDLDGLKKSYNQLADSVAKTNAVVKDPLK----------NKIIADaDATVKNLEQEADRLIDKLKPIKELE 2098
Cdd:PRK01156 467 snhiINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKrkeyleseeiNKSINE-YNKIESARADLEDIKIKINELKDKH 545
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1911235092 2099 DNLKKNISEIK----ELINQARKQANSIKVSVSS-GGDCIRTYKPEIKK 2142
Cdd:PRK01156 546 DKYEEIKNRYKslklEDLDSKRTSWLNALAVISLiDIETNRSRSNEIKK 594
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1634-1942 |
1.96e-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: 56.89 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1634 KVTADGEQTGQDAERTSRRANSLGDFIKGLVRDAEAVN-EKAKEVNETLGIQDKAFERnmqgLQKEIDQMMRELRRKNLD 1712
Cdd:COG5185 236 KGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENaESSKRLNENANNLIKQFEN----TKEKIAEYTKSIDIKKAT 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1713 TQKEvaedELVAAEGLLKKVQKVFGEPrgknEKMEKDLGEKLTDHKNKLDDAWDLLREATDKTREANRL----AAANQQN 1788
Cdd:COG5185 312 ESLE----EQLAAAEAEQELEESKRET----ETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELskssEELDSFK 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1789 MTaLEEKKEAIESGKRQTENTLKEGNDILDEANRLAD-EINSVIDYVTDIQTKLPPMSEELKDKIDDLSREMK--DRKLA 1865
Cdd:COG5185 384 DT-IESTKESLDEIPQNQRGYAQEILATLEDTLKAADrQIEELQRQIEQATSSNEEVSKLLNELISELNKVMReaDEESQ 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1866 ERVYQAENHAAQ-LNASSAVLDGILDEAKS--------ISFNATAAFKAYSNIKDYIDEADKIAKEAKGLAHEATKLATG 1936
Cdd:COG5185 463 SRLEEAYDEINRsVRSKKEDLNEELTQIESrvstlkatLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALE 542
|
....*.
gi 1911235092 1937 PQGSLK 1942
Cdd:COG5185 543 NLIPAS 548
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1782-2015 |
2.67e-07 |
|
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: 55.93 E-value: 2.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1782 AAANQQNMTALEEKKEAIESGKRQTENTLKEGNDILDEANRLADEINSVIDYVTDIQTKLPPMSEELKD---KIDDLSRE 1858
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAElekEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1859 MKDRK--LAERVYqaenhAAQLNASSAVLDGILdeaKSISFNATAAFKAYSNikdYIDEADKiaKEAKGLAHEATKLATg 1936
Cdd:COG4942 99 LEAQKeeLAELLR-----ALYRLGRQPPLALLL---SPEDFLDAVRRLQYLK---YLAPARR--EQAEELRADLAELAA- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1937 pqgsLKDGAKGSLQKSFGILNEA----KKLANNVKENDDDLNSLQTRLEKADVRNGELRRA---LNDTLAKLSAIPNDTA 2009
Cdd:COG4942 165 ----LRAELEAERAELEALLAELeeerAALEALKAERQKLLARLEKELAELAAELAELQQEaeeLEALIARLEAEAAAAA 240
|
....*.
gi 1911235092 2010 AKLQAA 2015
Cdd:COG4942 241 ERTPAA 246
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1587-2140 |
2.87e-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: 56.98 E-value: 2.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1587 LYDLENRTQELKHLLSP-QRAPERLIQlaegNLNTLvTEMNELLtratKVTadgEQTGQDAERTSRRANSLGdfikglvr 1665
Cdd:TIGR01612 885 LNDYEKKFNDSKSLINEiNKSIEEEYQ----NINTL-KKVDEYI----KIC---ENTKESIEKFHNKQNILK-------- 944
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1666 daEAVNEKAKEVNETLGIQDK---AFERNMQGLQKEIDQMMRELRRKNLdtqkEVAEDELVAAEGLLKKVqkvFGEPRG- 1741
Cdd:TIGR01612 945 --EILNKNIDTIKESNLIEKSykdKFDNTLIDKINELDKAFKDASLNDY----EAKNNELIKYFNDLKAN---LGKNKEn 1015
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1742 -------KNEKMEKDLGEKLTD-HKNKLDDAWDLLREATDKTREANRLAAANQQ--NMTALEEKKEAIESGKRQTENtLK 1811
Cdd:TIGR01612 1016 mlyhqfdEKEKATNDIEQKIEDaNKNIPNIEIAIHTSIYNIIDEIEKEIGKNIEllNKEILEEAEINITNFNEIKEK-LK 1094
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1812 EGN--DILDEAN-RLADEINSVIDyvtDIQTklppmseeLKDKIDDLSREMKDRKlaervYQAENHAAQLNASSAVLDGI 1888
Cdd:TIGR01612 1095 HYNfdDFGKEENiKYADEINKIKD---DIKN--------LDQKIDHHIKALEEIK-----KKSENYIDEIKAQINDLEDV 1158
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1889 LDEAKSiSFNATAAFKAYSNIKDYIDEADKIAKEAKGLAHEATKLATGpQGSLKD--GAKGSLQKSFGIL------NEAK 1960
Cdd:TIGR01612 1159 ADKAIS-NDDPEEIEKKIENIVTKIDKKKNIYDEIKKLLNEIAEIEKD-KTSLEEvkGINLSYGKNLGKLflekidEEKK 1236
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1961 KLANNVKEND---DDLNSLQTRLEKADVRNGeLRRALNDTLAKLSAIPNDTAAKLQAAKNKARQANDTAKDVLAQVKDLH 2037
Cdd:TIGR01612 1237 KSEHMIKAMEayiEDLDEIKEKSPEIENEMG-IEMDIKAEMETFNISHDDDKDHHIISKKHDENISDIREKSLKIIEDFS 1315
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2038 Q--DLDGLKKSYNQLADSVAKTNAVVKDPLkNKIiadadATVKNleqeadrlIDKLkpikeleDNLKKNISEIKELINQA 2115
Cdd:TIGR01612 1316 EesDINDIKKELQKNLLDAQKHNSDINLYL-NEI-----ANIYN--------ILKL-------NKIKKIIDEVKEYTKEI 1374
|
570 580
....*....|....*....|....*
gi 1911235092 2116 RKQANSIKVSVSSGGDCIRTYKPEI 2140
Cdd:TIGR01612 1375 EENNKNIKDELDKSEKLIKKIKDDI 1399
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1667-2142 |
5.03e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 55.75 E-value: 5.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1667 AEAVNEKAKEVNETLGIQDKAFERNMQGLQKEIDQMMRElrrkNLDTQKEVAEDelvaaeglLKKVQKVfgeprGKNEKM 1746
Cdd:TIGR00618 122 AAKKSETEEVIHDLLKLDYKTFTRVVLLPQGEFAQFLKA----KSKEKKELLMN--------LFPLDQY-----TQLALM 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1747 EKDLGEKLTDHKNKLDDAWDLLreaTDKTREANRLAAANQQNMTALEEKKEAIESGKRQTENTLKEGNDILDEANRLADE 1826
Cdd:TIGR00618 185 EFAKKKSLHGKAELLTLRSQLL---TLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQL 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1827 INSVIDYVTDIQTKLPPMsEELKDKIDDLSREMKDRKLAERVYQAENHAAQLNAssavldgildEAKSISFNATAAFKAY 1906
Cdd:TIGR00618 262 LKQLRARIEELRAQEAVL-EETQERINRARKAAPLAAHIKAVTQIEQQAQRIHT----------ELQSKMRSRAKLLMKR 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1907 SNI-KDYIDEADKIAKEAKGLA-HEATKLATGPQGSLKDgakgSLQKSFGILNEAKKLANNVKENDDDLNSLQTRLEKAD 1984
Cdd:TIGR00618 331 AAHvKQQSSIEEQRRLLQTLHSqEIHIRDAHEVATSIRE----ISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQ 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1985 VRNGEL------RRALNDTLAKL---------------SAIPNDTAAKLQA--AKNKARQANDTAKDVLAQVKDLHQDld 2041
Cdd:TIGR00618 407 REQATIdtrtsaFRDLQGQLAHAkkqqelqqryaelcaAAITCTAQCEKLEkiHLQESAQSLKEREQQLQTKEQIHLQ-- 484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2042 glKKSYNQLADSVAKTNAVVKDPLKNKIIADADATVKNLEQEAD-----RLIDKLKPIKELEDNLKKNISEIKELINQAR 2116
Cdd:TIGR00618 485 --ETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLtrrmqRGEQTYAQLETSEEDVYHQLTSERKQRASLK 562
|
490 500
....*....|....*....|....*.
gi 1911235092 2117 KQANSIKVSVSSGGDCIRTYKPEIKK 2142
Cdd:TIGR00618 563 EQMQEIQQSFSILTQCDNRSKEDIPN 588
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1444-1490 |
5.71e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 48.46 E-value: 5.71e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1444 CQCN--GHSSL-CDPETSICQnCQHHTAGDFCERCALGYYGIVkglPNDC 1490
Cdd:smart00180 1 CDCDpgGSASGtCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDG---PPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
473-520 |
6.12e-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: 6.12e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1911235092 473 PCNCSGEGSANE--DPCFGPCHCKENVEGGDCSRCKSGFFNLQeSNQKGC 520
Cdd:cd00055 1 PCDCNGHGSLSGqcDPGTGQCECKPNTTGRRCDRCAPGYYGLP-SQGGGC 49
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1671-1908 |
7.48e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.45 E-value: 7.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1671 NEKAKEVNETLGIQDKAfERNMQGLQKEIDQMMRELRRknLDTQKEVAEDELVAAEGLLKKVQKvfgeprgKNEKMEKDL 1750
Cdd:COG3883 19 QAKQKELSELQAELEAA-QAELDALQAELEELNEEYNE--LQAELEALQAEIDKLQAEIAEAEA-------EIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1751 GEKLTDHKNK--LDDAWDLLREAT------DKTREANRLAAANQQNMTALEEKKEAIESGKRQTENTLKEGNDILDEANR 1822
Cdd:COG3883 89 GERARALYRSggSVSYLDVLLGSEsfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1823 LADEINSVIdyvtdiqtklppmsEELKDKIDDLSREMKDRKLAERVYQAENHAAQLNASSAVLDGILDEAKSISFNATAA 1902
Cdd:COG3883 169 AKAELEAQQ--------------AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAA 234
|
....*.
gi 1911235092 1903 FKAYSN 1908
Cdd:COG3883 235 AAAAAA 240
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1634-2154 |
9.21e-07 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 55.22 E-value: 9.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1634 KVTADGEQTGQdAERTSRRANSLGDF---IKGLVRDAEAVNE---KAKEVNETLGIQDKAFernmqglqkeIDQMMRELR 1707
Cdd:PTZ00440 1111 VVNADKEKNKQ-TEHYNKKKKSLEKIykqMEKTLKELENMNLediTLNEVNEIEIEYERIL----------IDHIVEQIN 1179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1708 RKNLDTQKEVAEDELVAAEGLLKKVqKVFGEPRGKNEKME-KDLGEKLTDHKNKLDDawdLLREATDKTREANRlaaanQ 1786
Cdd:PTZ00440 1180 NEAKKSKTIMEEIESYKKDIDQVKK-NMSKERNDHLTTFEyNAYYDKATASYENIEE---LTTEAKGLKGEANR-----S 1250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1787 QNMTALEEKKEAIESGKRQT-------ENTLKE---GNDILDEANrladeINSVIDYVTDIQTKLPPMSEELK---DKID 1853
Cdd:PTZ00440 1251 TNVDELKEIKLQVFSYLQQVikennkmENALHEiknMYEFLISID-----SEKILKEILNSTKKAEEFSNDAKkelEKTD 1325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1854 DLSREMKdrklaERVYQAENHAAQLNASsaVLDGILDE--------AKSISFNATAAFKAYSNIKDYIDEAD-KIAKEAK 1924
Cdd:PTZ00440 1326 NLIKQVE-----AKIEQAKEHKNKIYGS--LEDKQIDDeikkieqiKEEISNKRKEINKYLSNIKSNKEKCDlHVRNASR 1398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1925 GLA-------HEATKLATGPQGSLkDGAKGSLQKSFGILNEAKKLANNVKENDDDLNSLQTrlekadvrngELRRALNDT 1997
Cdd:PTZ00440 1399 GKDkidflnkHEAIEPSNSKEVNI-IKITDNINKCKQYSNEAMETENKADENNDSIIKYEK----------EITNILNNS 1467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1998 LakLSAIPNDTAAKLQAAKNKARQANDTAKDVLAQVKDLHQDLDGLKKSYN-----QLADSVAKTNAVVKDPLKNKIIAD 2072
Cdd:PTZ00440 1468 S--ILGKKTKLEKKKKEATNIMDDINGEHSIIKTKLTKSSEKLNQLNEQPNikregDVLNNDKSTIAYETIQYNLGRVKH 1545
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2073 ADATVKNLEQEADRLIDK----LKPIKELEDNL---------------KKNISEI---KELINQARKQANSIKVSVSSGG 2130
Cdd:PTZ00440 1546 NLLNILNIKDEIETILNKaqdlMRDISKISKIVenknlenlndkeadyVKYLDNIlkeKQLMEAEYKKLNEIYSDVDNIE 1625
|
570 580
....*....|....*....|....
gi 1911235092 2131 DCIRTYKPEIKKGSYNNIIVNVKT 2154
Cdd:PTZ00440 1626 KELKKHKKNYEIGLLEKVIEINKN 1649
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1660-1893 |
1.07e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 53.38 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1660 IKGLVRDAEAVNEKAKEVNETlgIQDKAFERNmqglqkEIDQMMRELRRKnLDTQKEVAeDELVAAEGLLKKVQKvfgep 1739
Cdd:COG1340 52 VKELREEAQELREKRDELNEK--VKELKEERD------ELNEKLNELREE-LDELRKEL-AELNKAGGSIDKLRK----- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1740 rgKNEKMEKDL-GEKLT-DHKNKLDDAWDLLREATDKTREANRLAAANQQNMTALEEKKEAIESGKRQTENTLKEGN--- 1814
Cdd:COG1340 117 --EIERLEWRQqTEVLSpEEEKELVEKIKELEKELEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQelh 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1815 DILDEANRLADEINSVID----YVTDIQTKLppmsEELKDKIDDLSREMKDRKLAERVYQAENHAAQLNASSAVLDGILD 1890
Cdd:COG1340 195 EEMIELYKEADELRKEADelhkEIVEAQEKA----DELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAE 270
|
...
gi 1911235092 1891 EAK 1893
Cdd:COG1340 271 EIF 273
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
292-339 |
1.08e-06 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 47.73 E-value: 1.08e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1911235092 292 CICFGHA---RACplDPVTnkSRCECEHNTCGDSCDQCCPGFHQKPWRAGT 339
Cdd:cd00055 2 CDCNGHGslsGQC--DPGT--GQCECKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
781-823 |
1.38e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 47.31 E-value: 1.38e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1911235092 781 CQC--FGHAD-SCDDITAECLnCRDHTGGPYCNQCLPGFYGDPTKG 823
Cdd:smart00180 1 CDCdpGGSASgTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1790-2026 |
1.44e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 53.30 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1790 TALEEKKEAIESGKRQTENTLKEGNDILDEANRLADEINSVIDYVTDIQTKLppmsEELKDKIDDLSREMKDRK--LAER 1867
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEI----DKLQAEIAEAEAEIEERReeLGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1868 VyqaenHAAQLNASSAVLDGILDEAKSISfnataafkaysnikDYIDEA---DKIAKEAKGLAHEATKLatgpQGSLKDg 1944
Cdd:COG3883 92 A-----RALYRSGGSVSYLDVLLGSESFS--------------DFLDRLsalSKIADADADLLEELKAD----KAELEA- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1945 AKGSLQKsfgilnEAKKLANNVKENDDDLNSLQTRLEKADVRNGELRRALNDTLAKLSAIPNDTAAKLQAAKNKARQAND 2024
Cdd:COG3883 148 KKAELEA------KLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
..
gi 1911235092 2025 TA 2026
Cdd:COG3883 222 AA 223
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1664-2030 |
2.12e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.99 E-value: 2.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1664 VRDAEAVnEKAKEVNetlgiqdKAFERNMQGLQKEIDQMMRELRRKNLDTQKevAEDELVAAEGLLKKVQKVFGEPRG-- 1741
Cdd:PTZ00121 1539 AKKAEEK-KKADELK-------KAEELKKAEEKKKAEEAKKAEEDKNMALRK--AEEAKKAEEARIEEVMKLYEEEKKmk 1608
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1742 ----KNEKMEKDLGEKLTDHKNKLDDAWDLLREATDKTREANRLAAANQQNMTALEEKKEAIESGKRQTENTLKEGNDIL 1817
Cdd:PTZ00121 1609 aeeaKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEK 1688
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1818 ---------DEANRLADEINSVIDYVTDIQTKLPPMSEELKDKIDDLSREM-KDRKLAE--RVYQAE-NHAAQLNAS--- 1881
Cdd:PTZ00121 1689 kaaealkkeAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAeEDKKKAEeaKKDEEEkKKIAHLKKEeek 1768
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1882 ---------SAVLDGIL---DEAKSISFNATA--AFKAYSNIKDYIDEADKIAKEAKGLAHEATKLATGPQGSLKDGAKG 1947
Cdd:PTZ00121 1769 kaeeirkekEAVIEEELdeeDEKRRMEVDKKIkdIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADA 1848
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1948 SLQKSFGILNEAKKLAN---NVKENDDDLNSLQTRLEKADvrngELRRALNDTLAklSAIPNDTAA---------KLQAA 2015
Cdd:PTZ00121 1849 FEKHKFNKNNENGEDGNkeaDFNKEKDLKEDDEEEIEEAD----EIEKIDKDDIE--REIPNNNMAgknndiiddKLDKD 1922
|
410
....*....|....*
gi 1911235092 2016 KNKARQANDTAKDVL 2030
Cdd:PTZ00121 1923 EYIKRDAEETREEII 1937
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1671-2132 |
2.16e-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: 53.90 E-value: 2.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1671 NEKAKEVNETLGIQDKAFERNMQGLQKEI---DQMMRELRRKNLDTQKEVAEDELvAAEGLLKKVQKVFGEPRGKNEKME 1747
Cdd:TIGR00606 300 DEQLNDLYHNHQRTVREKERELVDCQRELeklNKERRLLNQEKTELLVEQGRLQL-QADRHQEHIRARDSLIQSLATRLE 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1748 KDLGEKLTDHKNKLDDAWDLLREA-TDKTREANRLAAANQQNMT------------------ALEEKKEAIESGKRQTEN 1808
Cdd:TIGR00606 379 LDGFERGPFSERQIKNFHTLVIERqEDEAKTAAQLCADLQSKERlkqeqadeirdekkglgrTIELKKEILEKKQEELKF 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1809 TLKEGNDI---------LDEANRLADEINSVIDYVTDIQTKLppmSEELKDKIDDLSREMKDRKLAERVYQAENHAAQLN 1879
Cdd:TIGR00606 459 VIKELQQLegssdrileLDQELRKAERELSKAEKNSLTETLK---KEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRT 535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1880 assavldgildEAKSISFNATAAFKAYSNIKdyideadkiAKEAKGLAHEATKLATGPQgslkdgakgsLQKSFgilnea 1959
Cdd:TIGR00606 536 -----------QMEMLTKDKMDKDEQIRKIK---------SRHSDELTSLLGYFPNKKQ----------LEDWL------ 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1960 KKLANNVKENDDDLNSLQTRLEKADVRNGELRRALNDTLAKLSAIPN---------DTAAKLQAAKNKARQANDTaKDVL 2030
Cdd:TIGR00606 580 HSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDklfdvcgsqDEESDLERLKEEIEKSSKQ-RAML 658
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2031 AQVKDLH----QDLDGLKKSYNQLADSVAKT----NAVVKDpLKNKIIADAD------ATVKNLEQEADRLIDKL----- 2091
Cdd:TIGR00606 659 AGATAVYsqfiTQLTDENQSCCPVCQRVFQTeaelQEFISD-LQSKLRLAPDklksteSELKKKEKRRDEMLGLApgrqs 737
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2092 ------KPIKELEDNLKK---NISEIKELINQARKQANSIKVSVSSGGDC 2132
Cdd:TIGR00606 738 iidlkeKEIPELRNKLQKvnrDIQRLKNDIEEQETLLGTIMPEEESAKVC 787
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1684-2154 |
2.22e-06 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 54.07 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1684 QDKAFERNMQGLQKEIDQMMRELRRKN--LDTQKEVAEDELVAAEGLLKKVQKVFGEPRGKNEKMEKDLGekltdhknkl 1761
Cdd:PTZ00440 1071 KNPKIKEEIKLLEEKVEALLKKIDENKnkLIEIKNKSHEHVVNADKEKNKQTEHYNKKKKSLEKIYKQME---------- 1140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1762 ddawDLLREATDKTREANRLAAANQQNMtalEEKKEAIESGKRQTENTLKEGNDILdeanrlaDEINSVIDYVTDIQTKl 1841
Cdd:PTZ00440 1141 ----KTLKELENMNLEDITLNEVNEIEI---EYERILIDHIVEQINNEAKKSKTIM-------EEIESYKKDIDQVKKN- 1205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1842 ppMSEELKDKIDdlsrEMKDRKLAERVYQAENHAAQLNASSAVLDGILDEAKSISFNATAAFKAYSNIKDYIDEADKIAK 1921
Cdd:PTZ00440 1206 --MSKERNDHLT----TFEYNAYYDKATASYENIEELTTEAKGLKGEANRSTNVDELKEIKLQVFSYLQQVIKENNKMEN 1279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1922 EAKglaheatklatgpqgSLKDgakgslQKSFGILNEAKKLANNVkendddLNSLQTRLEKADVRNGELrralndtlakl 2001
Cdd:PTZ00440 1280 ALH---------------EIKN------MYEFLISIDSEKILKEI------LNSTKKAEEFSNDAKKEL----------- 1321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2002 saipNDTAAKLQAAKNKARQANDTAKDVLAQVKD--LHQDLDGLKKSYNQLADSVAKTNAVVKDPLKNKiiADADATVKN 2079
Cdd:PTZ00440 1322 ----EKTDNLIKQVEAKIEQAKEHKNKIYGSLEDkqIDDEIKKIEQIKEEISNKRKEINKYLSNIKSNK--EKCDLHVRN 1395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2080 LEQEADrLIDKLKPIKELEDNLKK--NISEIKELINQARK---QANSIKVSVSSGGDCIRTYKPEIKKGSYNNIIVNVKT 2154
Cdd:PTZ00440 1396 ASRGKD-KIDFLNKHEAIEPSNSKevNIIKITDNINKCKQysnEAMETENKADENNDSIIKYEKEITNILNNSSILGKKT 1474
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1675-2153 |
3.08e-06 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 53.30 E-value: 3.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1675 KEVNETLGIQDKAFERN---MQGLQKEIDQMMRELRRKNLDTQKEVAEDELVAA--EGLLKKVQKVFGEPRGKNEKMEKD 1749
Cdd:PTZ00440 357 KFSLEMLSMLDSLLIKKekiLNNLFNKLFGDLKEKIETLLDSEYFISKYTNIISlsEHTLKAAEDVLKENSQKIADYALY 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1750 LGEKLTDHKNKLDDAWDLLREATDKT-------REANRLAAANQQNMTALEEKKEAIESGKRQTENTLKEGNDILDEANR 1822
Cdd:PTZ00440 437 SNLEIIEIKKKYDEKINELKKSINQLktlisimKSFYDLIISEKDSMDSKEKKESSDSNYQEKVDELLQIINSIKEKNNI 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1823 LADEINSVIDYVTDIqtklppmsEELKDKIDDLSREMKDRKLA-ERVYQAENHAAQLNassavlDGILDEAKSISFNATA 1901
Cdd:PTZ00440 517 VNNNFKNIEDYYITI--------EGLKNEIEGLIELIKYYLQSiETLIKDEKLKRSMK------NDIKNKIKYIEENVDH 582
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1902 afkaysnIKDYI---DEADKIAKEAKGLAHEAtklatgpqgslkdgakgsLQKSFGILNEAKKLANNVKENDDDLNslqt 1978
Cdd:PTZ00440 583 -------IKDIIslnDEIDNIIQQIEELINEA------------------LFNKEKFINEKNDLQEKVKYILNKFY---- 633
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1979 rlekadvrNGELRRALNDtlakLSAIPNDTAAKLQAAKNKarqandtakdvlaqvKDLHQDLDGLKKSYNQLadsvaktn 2058
Cdd:PTZ00440 634 --------KGDLQELLDE----LSHFLDDHKYLYHEAKSK---------------EDLQTLLNTSKNEYEKL-------- 678
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2059 avvkDPLKNKIIadaDATVKNLEQEADRLID-KLKPIKELEDNLKKNISEIkelINQARKQANSIKVSVSSggdcirtYK 2137
Cdd:PTZ00440 679 ----EFMKSDNI---DNIIKNLKKELQNLLSlKENIIKKQLNNIEQDISNS---LNQYTIKYNDLKSSIEE-------YK 741
|
490
....*....|....*..
gi 1911235092 2138 PEIKK-GSYNNIIVNVK 2153
Cdd:PTZ00440 742 EEEEKlEVYKHQIINRK 758
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1753-2160 |
3.24e-06 |
|
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: 53.52 E-value: 3.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1753 KLTDHKNKLDDAWDLLreatdktreanrlaaanqQNMtaleeKKEAIESGKRQTENTLKEGNDILDEANR-----LADEI 1827
Cdd:TIGR01612 697 KLDDLKSKIDKEYDKI------------------QNM-----ETATVELHLSNIENKKNELLDIIVEIKKhihgeINKDL 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1828 NSVIDyvtDIQTKlppmSEELKDKIDDLSREmKDR--KLAERVYQAENHaaqLNASSAVlDGILDEAKSISFNATAAFKA 1905
Cdd:TIGR01612 754 NKILE---DFKNK----EKELSNKINDYAKE-KDElnKYKSKISEIKNH---YNDQINI-DNIKDEDAKQNYDKSKEYIK 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1906 YSNIKDyiDEADKIAKEAKGLAHEatklatgpqgslkdgakgslqksfgILNEAKK---LANNVKENDDDLNSLQTRLE- 1981
Cdd:TIGR01612 822 TISIKE--DEIFKIINEMKFMKDD-------------------------FLNKVDKfinFENNCKEKIDSEHEQFAELTn 874
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1982 --KADVRNGEL---RRALNDTLAKLSAIPNDTAAKLQAAkNKARQAND---TAKDVLAQVKDLHQDLDGLKKSYNQLADS 2053
Cdd:TIGR01612 875 kiKAEISDDKLndyEKKFNDSKSLINEINKSIEEEYQNI-NTLKKVDEyikICENTKESIEKFHNKQNILKEILNKNIDT 953
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2054 VAKTNAVVK-------DPLKNKII----ADADATVKNLEQEADRLIdklKPIKELEDNLKKNISE-IKELINQARKQANS 2121
Cdd:TIGR01612 954 IKESNLIEKsykdkfdNTLIDKINeldkAFKDASLNDYEAKNNELI---KYFNDLKANLGKNKENmLYHQFDEKEKATND 1030
|
410 420 430
....*....|....*....|....*....|....*....
gi 1911235092 2122 IKVSVSSGGDCIRTYKPEIKKGSYnNIIVNVKTPVADNL 2160
Cdd:TIGR01612 1031 IEQKIEDANKNIPNIEIAIHTSIY-NIIDEIEKEIGKNI 1068
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
474-511 |
4.10e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 45.77 E-value: 4.10e-06
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1911235092 474 CNCSGEGSANE--DPCFGPCHCKENVEGGDCSRCKSGFFN 511
Cdd:smart00180 1 CDCDPGGSASGtcDPDTGQCECKPNVTGRRCDRCAPGYYG 40
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1958-2123 |
4.23e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.14 E-value: 4.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1958 EAKKLANNVKENDDDLNSLQTRLEKADVRNGELRRALNDTLAKLSAIpNDTAAKLQAAKNKARQANDTAKDVLAQ-VKDL 2036
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEAL-QAEIDKLQAEIAEAEAEIEERREELGErARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2037 HQDLDGLK--------KSYNQLADSVAKTNAVVKDplKNKIIADADATVKNLEQEADRLIDKLKPIKELEDNLKKNISEI 2108
Cdd:COG3883 96 YRSGGSVSyldvllgsESFSDFLDRLSALSKIADA--DADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170
....*....|....*
gi 1911235092 2109 KELINQARKQANSIK 2123
Cdd:COG3883 174 EAQQAEQEALLAQLS 188
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1683-2159 |
4.38e-06 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 52.91 E-value: 4.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1683 IQDKAFERNMQGLQKEIDQMMRELRRKNLDTQKEVAEDelvaaegLLKKVQKVFgeprgkneKMEKDLGEKLTDHKNKld 1762
Cdd:PTZ00440 655 YHEAKSKEDLQTLLNTSKNEYEKLEFMKSDNIDNIIKN-------LKKELQNLL--------SLKENIIKKQLNNIEQ-- 717
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1763 DAWDLLREATDKTREANrlaaanqQNMTALEEKKEAIESGKRQTEN-------TLKEGNDILDEANRLADEINSVIDYVT 1835
Cdd:PTZ00440 718 DISNSLNQYTIKYNDLK-------SSIEEYKEEEEKLEVYKHQIINrknefilHLYENDKDLPDGKNTYEEFLQYKDTIL 790
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1836 DIQTKLPPMSEELKDKIDDLSREMKdrKLAERVYQAENHAAQLNASSAVL-DGILDEAKSIS-------FNatAAFKAYS 1907
Cdd:PTZ00440 791 NKENKISNDINILKENKKNNQDLLN--SYNILIQKLEAHTEKNDEELKQLlQKFPTEDENLNlkelekeFN--ENNQIVD 866
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1908 NIKDYIDEADKIAKEAKGL-----AHEATKLATGPQGSLKDGAKGSLQKSFGILNEAKKLANNVKEN-DDDLNSlqtrlE 1981
Cdd:PTZ00440 867 NIIKDIENMNKNINIIKTLniainRSNSNKQLVEHLLNNKIDLKNKLEQHMKIINTDNIIQKNEKLNlLNNLNK-----E 941
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1982 KAdvrngELRRALNDT-LAKLSAIPNDTAAKLQAAKNKARQANDTAKDVLAQVKD----LHQDLDGLKKSYNQLAdsvAK 2056
Cdd:PTZ00440 942 KE-----KIEKQLSDTkINNLKMQIEKTLEYYDKSKENINGNDGTHLEKLDKEKDewehFKSEIDKLNVNYNILN---KK 1013
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2057 TNAVVKDPlKNKIIADADATVKNLEQEADRLIDKLkpIKELEDnLKKNISEIKELINQARKQANSIKVSVSSGGDCIRTY 2136
Cdd:PTZ00440 1014 IDDLIKKQ-HDDIIELIDKLIKEKGKEIEEKVDQY--ISLLEK-MKTKLSSFHFNIDIKKYKNPKIKEEIKLLEEKVEAL 1089
|
490 500
....*....|....*....|...
gi 1911235092 2137 KPEIKKGsyNNIIVNVKTPVADN 2159
Cdd:PTZ00440 1090 LKKIDEN--KNKLIEIKNKSHEH 1110
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1663-1863 |
4.69e-06 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 50.14 E-value: 4.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1663 LVRDAEAV----NEKAKEVNETLGIQD-----------KAFERNMQGLQKEIDQMMrelrrknlDTQKEVAEDELVAAEG 1727
Cdd:cd00176 5 FLRDADELeawlSEKEELLSSTDYGDDlesveallkkhEALEAELAAHEERVEALN--------ELGEQLIEEGHPDAEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1728 LLKKVQKVfgeprgknEKMEKDLGEKLTDHKNKLDDAWDLLREATDKTREANRL-----AAANQQNMTALEEKKEAIESG 1802
Cdd:cd00176 77 IQERLEEL--------NQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLeekeaALASEDLGKDLESVEELLKKH 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1911235092 1803 KrQTENTLKEGNDILDEANRLADE-INSVIDYVTD-IQTKLppmsEELKDKIDDLSREMKDRK 1863
Cdd:cd00176 149 K-ELEEELEAHEPRLKSLNELAEElLEEGHPDADEeIEEKL----EELNERWEELLELAEERQ 206
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1493-1548 |
4.73e-06 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 45.81 E-value: 4.73e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1911235092 1493 CACPLISSSnnfSPSCVMEGlddYRCTaCPRGYEGQYCERCAPGYTGSPSSPGGSC 1548
Cdd:pfam00053 1 CDCNPHGSL---SDTCDPET---GQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
831-886 |
6.29e-06 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 45.42 E-value: 6.29e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1911235092 831 CACPLNIPSnnfSPTCHldrSLGLICDeCPVGYAGPRCERCAEGYFGQPSVAGGSC 886
Cdd:pfam00053 1 CDCNPHGSL---SDTCD---PETGQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1590-1861 |
7.83e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.99 E-value: 7.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1590 LENRTQELKHLLSPQRAPERLIqlaEGNLNTLVTEMNELLTRATKVTADGEQTGQDAERTSRRANSLGDFIKGLVRDAEA 1669
Cdd:TIGR02169 679 LRERLEGLKRELSSLQSELRRI---ENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIEN 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1670 VNEKAKEVNETLG---------------IQDKAFERNMQGLQKEIDQMMRELRR------------KNLDTQKEVAEDE- 1721
Cdd:TIGR02169 756 VKSELKELEARIEeleedlhkleealndLEARLSHSRIPEIQAELSKLEEEVSRiearlreieqklNRLTLEKEYLEKEi 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1722 ------LVAAEGLLKKVQKVFGEPRGKNEKME----------KDLGEKLTDHKNKLDDAWDLLREATDKTREANRLAAAN 1785
Cdd:TIGR02169 836 qelqeqRIDLKEQIKSIEKEIENLNGKKEELEeeleeleaalRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKK 915
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1786 QQNMTALEEKKEAIESGKRQTENTLKEGNDI-----------------------LDEANRLA-DEINSVIDYVTDIQTKL 1841
Cdd:TIGR02169 916 RKRLSELKAKLEALEEELSEIEDPKGEDEEIpeeelsledvqaelqrveeeiraLEPVNMLAiQEYEEVLKRLDELKEKR 995
|
330 340
....*....|....*....|...
gi 1911235092 1842 PPMSEE---LKDKIDDLSREMKD 1861
Cdd:TIGR02169 996 AKLEEErkaILERIEEYEKKKRE 1018
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
1666-1812 |
8.65e-06 |
|
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: 48.07 E-value: 8.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1666 DAEAVNEKAKEVNEtlgiQDKAFE-RNmqgLQKEidQMMRELRRKNldtqkEVAEDELVAAEGLLK--KVQKVFGEPRG- 1741
Cdd:pfam12718 8 EAENAQERAEELEE----KVKELEqEN---LEKE--QEIKSLTHKN-----QQLEEEVEKLEEQLKeaKEKAEESEKLKt 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1911235092 1742 -------KNEKMEKDLGEklTDHKnklddawdlLREATDKTREANRLAAANQQNMTALEEKKEAIESGKRQTENTLKE 1812
Cdd:pfam12718 74 nnenltrKIQLLEEELEE--SDKR---------LKETTEKLRETDVKAEHLERKVQALEQERDEWEKKYEELEEKYKE 140
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
830-887 |
9.18e-06 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 45.04 E-value: 9.18e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1911235092 830 PCACPLNIpsnNFSPTCHLDrslGLICdECPVGYAGPRCERCAEGYFGQPSVAGGsCQ 887
Cdd:cd00055 1 PCDCNGHG---SLSGQCDPG---TGQC-ECKPNTTGRRCDRCAPGYYGLPSQGGG-CQ 50
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1585-1876 |
1.11e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 50.67 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1585 KMLYDLENRTQELKHLLSPQRAPERLIQLAEGNLNTLVTEMNELLTRATKVTADGEQTGQDAERTSRRANSLGDFIKGLV 1664
Cdd:COG4372 42 KLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1665 RDAEAVNEKAKEVNET---LGIQDKAFERNMQGLQKEIDQMMRELRR--------KNLDTQKEVAEDELVAAEGLLKKVQ 1733
Cdd:COG4372 122 KERQDLEQQRKQLEAQiaeLQSEIAEREEELKELEEQLESLQEELAAleqelqalSEAEAEQALDELLKEANRNAEKEEE 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1734 KVFGEPRGKNEKMEKDLGEKLTDHKNKLDDAWDLLREATDKTREANRLAAANQQNMTALEEKKEAIESGKRQTENTLKEG 1813
Cdd:COG4372 202 LAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIA 281
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1911235092 1814 NDILDEANRLADEINSVIDYVTDIQTKLPPMSEE----LKDKIDDLSREMKDRKLAERVYQAENHAA 1876
Cdd:COG4372 282 ALELEALEEAALELKLLALLLNLAALSLIGALEDallaALLELAKKLELALAILLAELADLLQLLLV 348
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1730-2132 |
1.20e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 50.67 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1730 KKVQKVFGEpRGKNEKMEKDLGEKLTDHKNKLDDawdLLREATDKTREANRLAAANQQNMTALEEKKEAIEsgkrQTENT 1809
Cdd:COG4372 10 KARLSLFGL-RPKTGILIAALSEQLRKALFELDK---LQEELEQLREELEQAREELEQLEEELEQARSELE----QLEEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1810 LKEGNDILDEAnrladeinsvidyvtdiQTKLPPMSEELKdkidDLSREMKdrKLAERVYQAENHAAQLNASSAVLDGIL 1889
Cdd:COG4372 82 LEELNEQLQAA-----------------QAELAQAQEELE----SLQEEAE--ELQEELEELQKERQDLEQQRKQLEAQI 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1890 DEAKsisfnataafkaySNIKDYIDEADKIAKEAKGLAHEATKLATGPQGSLKDGAKGSLQKsfgILNEAKKLANNVKEN 1969
Cdd:COG4372 139 AELQ-------------SEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDE---LLKEANRNAEKEEEL 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1970 DDDLNSLQTRLEKADVRNGELRRALNDTLAKLSAIPNDTAAKLQAAKNKARQANDTAKDVLAQVKDLHQDLDGLKKSYNQ 2049
Cdd:COG4372 203 AEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAA 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2050 LADSVAKTNAVVKdpLKNKIIADADATVKNLEQEADRLIDKLKPIKELEDNLKKNISEIKELINQARKQANSIKVSVSSG 2129
Cdd:COG4372 283 LELEALEEAALEL--KLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLS 360
|
...
gi 1911235092 2130 GDC 2132
Cdd:COG4372 361 KGA 363
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1709-1883 |
1.77e-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: 48.87 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1709 KNLDTQKEVAEDELVAAEGLLKKvqkvfgeprgKNEKMEKDLGE--------KLTDHKnkLDDAWDLLREATDKTREANR 1780
Cdd:pfam00261 4 QQIKEELDEAEERLKEAMKKLEE----------AEKRAEKAEAEvaalnrriQLLEEE--LERTEERLAEALEKLEEAEK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1781 LAAANQQNMTALEEKKEAIESGKRQTENTLKEGNDILDEANRLADEinsvidyvtdIQTKLPPMSEELKDKID--DLSrE 1858
Cdd:pfam00261 72 AADESERGRKVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEE----------VARKLVVVEGDLERAEEraELA-E 140
|
170 180
....*....|....*....|....*
gi 1911235092 1859 MKDRKLAERVYQAENHAAQLNASSA 1883
Cdd:pfam00261 141 SKIVELEEELKVVGNNLKSLEASEE 165
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
831-879 |
2.38e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 43.84 E-value: 2.38e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1911235092 831 CACPlniPSNNFSPTCHLDrslGLICdECPVGYAGPRCERCAEGYFGQP 879
Cdd:smart00180 1 CDCD---PGGSASGTCDPD---TGQC-ECKPNVTGRRCDRCAPGYYGDG 42
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1809-2163 |
2.57e-05 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 50.22 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1809 TLKEGNDILDEANRLADEINSVIDYVTDIQT--KLPPMSE-ELKDKIDDLSREMKDRKLAERvyqaenHAAQLNASSAVL 1885
Cdd:PTZ00440 300 IQEEIGDIIKRYNFHLKKIEKGKEYIKRIQNnnIPPQVKKdELKKKYFESAKHYASFKFSLE------MLSMLDSLLIKK 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1886 DGILDEAKSISFN-ATAAFKAYSNIKDYIDEADKIAKEAKGLAHEATKLATGPQGSLKDGAKGSLQKsfgILNEAKKLAN 1964
Cdd:PTZ00440 374 EKILNNLFNKLFGdLKEKIETLLDSEYFISKYTNIISLSEHTLKAAEDVLKENSQKIADYALYSNLE---IIEIKKKYDE 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1965 NVKENDDDLNSLQT------------RLEKADVRNG-ELRRALNDTLAKLSAIPNdtaaKLQAAKNKARQANDTAKDVla 2031
Cdd:PTZ00440 451 KINELKKSINQLKTlisimksfydliISEKDSMDSKeKKESSDSNYQEKVDELLQ----IINSIKEKNNIVNNNFKNI-- 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2032 qvKDLHQDLDGLKKSYNQLADSVAK-----TNAVVKDPLKNKIIADADATVKNLEQEadrlIDKLKPIKELEDNLKKNIS 2106
Cdd:PTZ00440 525 --EDYYITIEGLKNEIEGLIELIKYylqsiETLIKDEKLKRSMKNDIKNKIKYIEEN----VDHIKDIISLNDEIDNIIQ 598
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1911235092 2107 EIKELINQARKQANSIKVSVSSGGDCIRTYKPEIKKGSYNNIIVNVKTPVADNLLFY 2163
Cdd:PTZ00440 599 QIEELINEALFNKEKFINEKNDLQEKVKYILNKFYKGDLQELLDELSHFLDDHKYLY 655
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1689-1883 |
3.67e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.99 E-value: 3.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1689 ERNMQGLQKEIDQMMREL-----RRKNLDTQKEVAEDELVAAEGLLKKVQKVFGEPRGK---NEKMEKDLGEKLTDHKNK 1760
Cdd:COG4942 26 EAELEQLQQEIAELEKELaalkkEEKALLKQLAALERRIAALARRIRALEQELAALEAElaeLEKEIAELRAELEAQKEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1761 L------------DDAWDLLREATDKTREANRL------AAANQQNMTALEEKKEAIESGKRQTENTLKEGNDILDEANR 1822
Cdd:COG4942 106 LaellralyrlgrQPPLALLLSPEDFLDAVRRLqylkylAPARREQAEELRADLAELAALRAELEAERAELEALLAELEE 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1911235092 1823 LADEINSVIDYVTDIQTKLPPMSEELKDKIDDLSREMKD-RKLAERVYQAENHAAQLNASSA 1883
Cdd:COG4942 186 ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEElEALIARLEAEAAAAAERTPAAG 247
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1695-1880 |
4.33e-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: 47.61 E-value: 4.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1695 LQkEIDQMMREL--RRKNLDTQKEVAEDELVAAEGLLKKVQKVFgeprgknekmeKDLGEKLTDHKNKLDDawdlLREAT 1772
Cdd:COG1579 12 LQ-ELDSELDRLehRLKELPAELAELEDELAALEARLEAAKTEL-----------EDLEKEIKRLELEIEE----VEARI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1773 DKTREanRLAAA-NQQNMTALEEKKEAIESGKRQTENTLKEGNDILDEANRLADEINSVIDyvtDIQTKLPPMSEELKDK 1851
Cdd:COG1579 76 KKYEE--QLGNVrNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELA---ELEAELEEKKAELDEE 150
|
170 180
....*....|....*....|....*....
gi 1911235092 1852 IDDLSREMKDRKlAERvyqaENHAAQLNA 1880
Cdd:COG1579 151 LAELEAELEELE-AER----EELAAKIPP 174
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1625-1879 |
4.41e-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: 49.12 E-value: 4.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1625 MNELLTraTKVTADGEQTGQDAERTSRRANSLGDFIKG-------LVRDAEAVNEKAKEVNETLGIQDKAFERNMQGLQK 1697
Cdd:pfam07888 3 LDELVT--LEEESHGEEGGTDMLLVVPRAELLQNRLEEclqeraeLLQAQEAANRQREKEKERYKRDREQWERQRRELES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1698 EIDQMMRELRRKNLDTQK-EVAEDELVAAEGLLKKVQKVFGEPRGKNEKMEKDLGEKLTDHKNKLDDAWDLLREATDKTR 1776
Cdd:pfam07888 81 RVAELKEELRQSREKHEElEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1777 EANRLAAANQQNMTALEEKKEAIESGKRQTENTLKEGNDILDE----ANRLADEINSVIDYVTDIQTK---LPPMSEELK 1849
Cdd:pfam07888 161 KAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQrdtqVLQLQDTITTLTQKLTTAHRKeaeNEALLEELR 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1911235092 1850 D----------KIDDLSREM------KDRKLAErVYQAENHAAQLN 1879
Cdd:pfam07888 241 SlqerlnaserKVEGLGEELssmaaqRDRTQAE-LHQARLQAAQLT 285
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1608-1837 |
4.58e-05 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 49.44 E-value: 4.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1608 ERLIQLAEGNLNTLVTEMNElltRATKVTADGEQTG--------QDAERTSRRA----NSL--------GDFIKGLVRDA 1667
Cdd:NF041483 1040 DTLITEAAAEADQLTAKAQE---EALRTTTEAEAQAdtmvgaarKEAERIVAEAtvegNSLvekartdaDELLVGARRDA 1116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1668 EAVNEKAKEVNETLgiqdkafernmqglQKEIDQMMRELRRKNLDTQKEVAE--DELV-AAEgllkkvqkvfgEPRGKNE 1744
Cdd:NF041483 1117 TAIRERAEELRDRI--------------TGEIEELHERARRESAEQMKSAGErcDALVkAAE-----------EQLAEAE 1171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1745 KMEKDLGEKLTDHKNKL-----DDAWDLLREATDK----TREANRLAAanqqnmTALEEKKEAIESGKRQtentlkegnd 1815
Cdd:NF041483 1172 AKAKELVSDANSEASKVriaavKKAEGLLKEAEQKkaelVREAEKIKA------EAEAEAKRTVEEGKRE---------- 1235
|
250 260
....*....|....*....|..
gi 1911235092 1816 iLDEANRLADEINSVIDYVTDI 1837
Cdd:NF041483 1236 -LDVLVRRREDINAEISRVQDV 1256
|
|
| alph_xenorhab_A |
NF033928 |
alpha-xenorhabdolysin family binary toxin subunit A; Alpha-xenorhabdolysin was the founding ... |
1825-2123 |
4.71e-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: 48.45 E-value: 4.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1825 DEINSVIDYVTDIQ---TKLPPMSEELK-DKIDDLSREMKDrklAERVYQAENHAAQlnaS-SAVLDGILDEAKSISfNA 1899
Cdd:NF033928 6 EDWISIQKYVQAALalpTTLEEVESYLGyPKDGIPGLEPKD---LLDLFQNIRNHAR---SwSNLEPKIKQLANDLA-NY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1900 TAAFKAYSN-IKDYIDEADkIAKEAKGLAHEATKLATGPQGSLKDGAKGSLQKsfgILneaKKLANNVKENDDDLNSLQT 1978
Cdd:NF033928 79 ARNIVVTGNpIIDLINEMP-IIKRGDLTEEELSELPPIPLSSDDKEIVKELKE---IL---EDLKNDIKDYQQKADDVKK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1979 RLekadvrnGELRRALNDTLakLSAIpndtAAKLQAAKNKarQANDTAKDVLAQVKDLHQDLDGLKKSYNQLADSVAKTn 2058
Cdd:NF033928 152 EL-------DDFENDLREEL--LPQL----KLKKKLYDDN--LGSDSIEELREKIDQLEKEIEQLNKEYDDYVKLSFTG- 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1911235092 2059 aVVKDPLKNKIIA--------DADATVKNLEQEADRLIDKLK---PIKELEDNLKKNISEIKELINQARKQANSIK 2123
Cdd:NF033928 216 -LAGGPIGLAITGgifgskaeKIRKEKNALIQEIDELQEQLKkknALLGSLERLQTSLDDILTRMEDALPALKKLK 290
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1644-1881 |
5.04e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 5.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1644 QDAERTSRRANSLGDFIKGLVRDAEAVNEKAkevNETLGIQDKAFER-NMQGLQKEIDQMMRELRRKNLDTQK-EVAEDE 1721
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQERR---EALQRLAEYSWDEiDVASAEREIAELEAELERLDASSDDlAALEEQ 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1722 LVAAEGLLKKVQKVFGEPRGKnekmEKDLGEKLTDHKNKLDDAWDLLREATDKTRE------ANRLAAANQQNMTA---- 1791
Cdd:COG4913 694 LEELEAELEELEEELDELKGE----IGRLEKELEQAEEELDELQDRLEAAEDLARLelrallEERFAAALGDAVERelre 769
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1792 -LEEKKEAIESGKRQTENTLkegNDILDEANR--------LADEINSVIDYV---TDIQT-KLPpmseELKDKIDDLSRE 1858
Cdd:COG4913 770 nLEERIDALRARLNRAEEEL---ERAMRAFNRewpaetadLDADLESLPEYLallDRLEEdGLP----EYEERFKELLNE 842
|
250 260 270
....*....|....*....|....*....|
gi 1911235092 1859 MKDRKLAE---RVYQAENHA----AQLNAS 1881
Cdd:COG4913 843 NSIEFVADllsKLRRAIREIkeriDPLNDS 872
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1621-2122 |
7.45e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.78 E-value: 7.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1621 LVTEMNELLTRATKVTADGEQTGQDAERTSRRanslgdfikglVRDAEAVNEKAKEVNETLGIQDKAFERNMQGLQKEID 1700
Cdd:COG1196 230 LLLKLRELEAELEELEAELEELEAELEELEAE-----------LAELEAELEELRLELEELELELEEAQAEEYELLAELA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1701 QMMRELRR--------------------------KNLDTQKEVAEDELVAAEGLLKKVQKVFGEPRGKNEKMEKDLGEKL 1754
Cdd:COG1196 299 RLEQDIARleerrreleerleeleeelaeleeelEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1755 TDHKNKLDDAWDLLREATDKTREANRLAAANQQNMTALEEKKEAIES-------GKRQTENTLKEGNDILDEANRLADEI 1827
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEEleealaeLEEEEEEEEEALEEAAEEEAELEEEE 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1828 NSVIDYVTDIQTKLppmsEELKDKIDDLSREMKDRKLAERVYQAENH----------AAQLNASSAVLDGILDEAKSISF 1897
Cdd:COG1196 459 EALLELLAELLEEA----ALLEAALAELLEELAEAAARLLLLLEAEAdyegflegvkAALLLAGLRGLAGAVAVLIGVEA 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1898 NATAAFKAY--SNIKDYIDEADKIAKEAKGLaheatklatgpqgsLKDGAKGSLqkSFGILNEAKKLANNVKENDDDLNS 1975
Cdd:COG1196 535 AYEAALEAAlaAALQNIVVEDDEVAAAAIEY--------------LKAAKAGRA--TFLPLDKIRARAALAAALARGAIG 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1976 LQTRLEKADVRNGELR-RALNDTLAKLSAIpndtAAKLQAAKNKARQANDTAKDVLAQVKDLHQDLDGLKKSYNQLADSV 2054
Cdd:COG1196 599 AAVDLVASDLREADARyYVLGDTLLGRTLV----AARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAAL 674
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1911235092 2055 AKTNAvvkdpLKNKIIADADATVKNLEQEADRLIDKLKPIKELEDNLKKNISEIKELINQARKQANSI 2122
Cdd:COG1196 675 LEAEA-----ELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREEL 737
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1976-2123 |
7.47e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.97 E-value: 7.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1976 LQTRLEKADVRNGELRRALNDTLAKLSAIPNDTAAKLQAAKNKARQANDTAKDVLAQVKDLHQDLDGLKKSYNQLADSVA 2055
Cdd:COG4372 4 LGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELE 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1911235092 2056 KTNAVVKDplKNKIIADADATVKNLEQEADRLIDKL----KPIKELE---DNLKKNISEIKELINQARKQANSIK 2123
Cdd:COG4372 84 ELNEQLQA--AQAELAQAQEELESLQEEAEELQEELeelqKERQDLEqqrKQLEAQIAELQSEIAEREEELKELE 156
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1591-1880 |
9.20e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 48.25 E-value: 9.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1591 ENRTQELKhLLSPQRAPERLIQL---AEGNLNTLVTEMNELLTRATKVtadGEQTgQDAERtSRRAnslgdfikgLVRDA 1667
Cdd:pfam01576 630 EAREKETR-ALSLARALEEALEAkeeLERTNKQLRAEMEDLVSSKDDV---GKNV-HELER-SKRA---------LEQQV 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1668 EAVNEKAKEVNETLGIQDKA---FERNMQGL--QKEIDQMMR----ELRRKNLDTQKEVAEDEL-------VAAEGLLKK 1731
Cdd:pfam01576 695 EEMKTQLEELEDELQATEDAklrLEVNMQALkaQFERDLQARdeqgEEKRRQLVKQVRELEAELederkqrAQAVAAKKK 774
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1732 VQKVFGE--------PRGKNE--KMEKDLGEKLTDHKNKLDDAWDLLREATDKTREANRLAAANQQNMTALEEKKEAIES 1801
Cdd:pfam01576 775 LELDLKEleaqidaaNKGREEavKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASER 854
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1802 GKRQTENtlkegndildEANRLADEINS-------VIDYVTDIQTKLPPMSEELKDkiDDLSREMKDRKLAERVYQAENH 1874
Cdd:pfam01576 855 ARRQAQQ----------ERDELADEIASgasgksaLQDEKRRLEARIAQLEEELEE--EQSNTELLNDRLRKSTLQVEQL 922
|
....*.
gi 1911235092 1875 AAQLNA 1880
Cdd:pfam01576 923 TTELAA 928
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
1590-1850 |
9.61e-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: 47.38 E-value: 9.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1590 LENRTQELKHLLSpqrAPERLIQLAEGNLNTLVTEMNELLTRATKVTADGEQTGQDAERTSrransLGDFIkglvrDAEA 1669
Cdd:pfam04108 47 LEKVREGLEKVLN---ELKKDFKQLLKDLDAALERLEETLDKLRNTPVEPALPPGEEKQKT-----LLDFI-----DEDS 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1670 VNEKAKEVNEtlgiQDKAFERNMQGLQKEIDQMMRELRrknlDTQKEVaeDELVAAEGLLKKVQKVFGEprgkNEKMEKD 1749
Cdd:pfam04108 114 VEILRDALKE----LIDELQAAQESLDSDLKRFDDDLR----DLQKEL--ESLSSPSESISLIPTLLKE----LESLEEE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1750 ---LGEKLTDHknklddawdllreaTDKTREANRLAAANQQNMTALEEKKEaiesgkRQTENTLKEGNDILDE------- 1819
Cdd:pfam04108 180 masLLESLTNH--------------YDQCVTAVKLTEGGRAEMLEVLENDA------RELDDVVPELQDRLDEmennyer 239
|
250 260 270
....*....|....*....|....*....|....*...
gi 1911235092 1820 ANRLADEINSVIDYVT-------DIQTKLPPMSEELKD 1850
Cdd:pfam04108 240 LQKLLEQKNSLIDELLsalqliaEIQSRLPEYLAALKE 277
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1785-2117 |
1.02e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 47.91 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1785 NQQNMTALEEKKEAIESG--------------KRQTENTL----KEGNDI-----------LDEANRLAD---------E 1826
Cdd:PRK04778 27 NYKRIDELEERKQELENLpvndelekvkklnlTGQSEEKFeewrQKWDEIvtnslpdieeqLFEAEELNDkfrfrkakhE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1827 INSVIDYVTDIQTKLPPMSEELKD----------KID---DLSREMKDRKLAERvyqaenhaAQLNASSAVLDGILDEAK 1893
Cdd:PRK04778 107 INEIESLLDLIEEDIEQILEELQElleseeknreEVEqlkDLYRELRKSLLANR--------FSFGPALDELEKQLENLE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1894 S--ISF-------NATAAFKAYSNIKDYIDEADKIAKEAKGLAHEATKlaTGPQ--GSLKDGAKGSLQKSF-----GILN 1957
Cdd:PRK04778 179 EefSQFveltesgDYVEAREILDQLEEELAALEQIMEEIPELLKELQT--ELPDqlQELKAGYRELVEEGYhldhlDIEK 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1958 EAKKLANNVKENDDDLNSLqtRLEKADVRNGELRRALN---DTLAKlsaipnDTAAKLQAAKNKARQANDTAKdVLAQVK 2034
Cdd:PRK04778 257 EIQDLKEQIDENLALLEEL--DLDEAEEKNEEIQERIDqlyDILER------EVKARKYVEKNSDTLPDFLEH-AKEQNK 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2035 DLHQDLDGLKKSYnQLADS-VAKTNAVVKDpLKNkIIADADATVKNLEQEADR---LIDKLKPIKELEDNLKKNISEIKE 2110
Cdd:PRK04778 328 ELKEEIDRVKQSY-TLNESeLESVRQLEKQ-LES-LEKQYDEITERIAEQEIAyseLQEELEEILKQLEEIEKEQEKLSE 404
|
....*..
gi 1911235092 2111 LINQARK 2117
Cdd:PRK04778 405 MLQGLRK 411
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1958-2117 |
1.53e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1958 EAKKLANNVKENDDDLNSLQTRLEKADVRNGELRRALNDTLAKLSAIPNDtaaKLQAAKNKARQANDTAKDVLAQVKDLH 2037
Cdd:COG4913 289 RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGD---RLEQLEREIERLERELEERERRRARLE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2038 QDLDGLKKSYNQLADSVAKTNAVVKDplknkIIADADATVKNLEQEADRLIDKLKPIKELEDNLKKnisEIKELinQARK 2117
Cdd:COG4913 366 ALLAALGLPLPASAEEFAALRAEAAA-----LLEALEEELEALEEALAEAEAALRDLRRELRELEA---EIASL--ERRK 435
|
|
| NtpE |
COG1390 |
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal ... |
1789-1925 |
1.56e-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: 45.32 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1789 MTALEEKKEAIEsgkrqtENTLKEGNDILDEANRLADEInsvidyVTDIQTKLppmsEELKDKIDDLSREMKDRKLAERV 1868
Cdd:COG1390 1 MMSLEKIIEEIL------EEAEAEAEEILEEAEEEAEKI------LEEAEEEA----EEIKEEILEKAEREAEREKRRII 64
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1911235092 1869 YQAENHA--AQLNASSAVLDGILDEAKS--ISFNATAAFKAYsnIKDYIDEADKIAKEAKG 1925
Cdd:COG1390 65 SSAELEArkELLEAKEELIEEVFEEALEklKNLPKDPEYKEL--LKKLLKEAAEELGSGDL 123
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1589-1800 |
1.61e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 47.73 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1589 DLENRTQELKhllspqrapERLIQLAEGNLNTLVTEMNELLTRATKVTADGEQTGQDAERTSRRANSLGDFIKGLVRdae 1668
Cdd:TIGR00606 959 DIENKIQDGK---------DDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKR--- 1026
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1669 avNEKAKEVNETLGIQDKAF--------ERNMQGLQKEIDQMMRElRRKNLDTQKEVaEDELVAAEGLLKKVQKVFGEPR 1740
Cdd:TIGR00606 1027 --ENELKEVEEELKQHLKEMgqmqvlqmKQEHQKLEENIDLIKRN-HVLALGRQKGY-EKEIKHFKKELREPQFRDAEEK 1102
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1741 GKNEKME----KDLGEKLTDHKNKLDDAwdLLREATDKTREANRL------AAANQQNMTALEEKKEAIE 1800
Cdd:TIGR00606 1103 YREMMIVmrttELVNKDLDIYYKTLDQA--IMKFHSMKMEEINKIirdlwrSTYRGQDIEYIEIRSDADE 1170
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1493-1549 |
1.77e-04 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 41.57 E-value: 1.77e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1911235092 1493 CACPLISSSNnfsPSCVMEGLddyRCTaCPRGYEGQYCERCAPGYTGSPSSPGGsCQ 1549
Cdd:cd00055 2 CDCNGHGSLS---GQCDPGTG---QCE-CKPNTTGRRCDRCAPGYYGLPSQGGG-CQ 50
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1608-1768 |
2.31e-04 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 46.21 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1608 ERLIQLAEGNLNTLVTEMNELLTRATKVtadgeqtgqdaertsrrANSLGDFIKGLVRDAEAVNEKAKEVNETLGIQDKA 1687
Cdd:cd22656 113 EEAKKTIKALLDDLLKEAKKYQDKAAKV-----------------VDKLTDFENQTEKDQTALETLEKALKDLLTDEGGA 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1688 FER-NMQGLQKEIDQMMRELRRKNLDTQKEVaEDELVAAEGLLKKVQKVFGEPRGKNEKMeKDLGEKLT---DHKNKLDD 1763
Cdd:cd22656 176 IARkEIKDLQKELEKLNEEYAAKLKAKIDEL-KALIADDEAKLAAALRLIADLTAADTDL-DNLLALIGpaiPALEKLQG 253
|
....*
gi 1911235092 1764 AWDLL 1768
Cdd:cd22656 254 AWQAI 258
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1849-2123 |
2.32e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1849 KDKIDDLSREMkdRKLAERVYQAENHAAQLNASSAVLDGILDeaksisfnataafkAYSNIKDYIDEADKIAKEAKGLAH 1928
Cdd:COG4913 609 RAKLAALEAEL--AELEEELAEAEERLEALEAELDALQERRE--------------ALQRLAEYSWDEIDVASAEREIAE 672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1929 EATKLAtgpqgSLKDGAKG--SLQKSfgiLNEAKKLANNVKENDDDLNSLQTRLEKadvRNGELRRALNDTLAKLSAIPN 2006
Cdd:COG4913 673 LEAELE-----RLDASSDDlaALEEQ---LEELEAELEELEEELDELKGEIGRLEK---ELEQAEEELDELQDRLEAAED 741
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2007 DTAAKLQAAKNKARQANDTAKDVLAQVKDLHQDLDGLKKSYNQLADSVAKT----NAVVKDPlknkiIADADATVKNLEQ 2082
Cdd:COG4913 742 LARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAmrafNREWPAE-----TADLDADLESLPE 816
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2083 --------EADRLIDKLKPIKELednLKKN-ISEIKELINQARKQANSIK 2123
Cdd:COG4913 817 ylalldrlEEDGLPEYEERFKEL---LNENsIEFVADLLSKLRRAIREIK 863
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
311-335 |
2.49e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 40.76 E-value: 2.49e-04
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1792-2123 |
2.58e-04 |
|
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: 46.77 E-value: 2.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1792 LEEKKEAIESGK-RQTENTLKEGNDILDEANRLADEINSVIDYVTDIQTKLPPMSEELKDKIDDLSREMkdrkLAERvYQ 1870
Cdd:pfam06160 69 LFEAEELNDKYRfKKAKKALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKYRELRKTL----LANR-FS 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1871 AENHAAQLNASSAVLDGILDEAKSISFNA--TAAFKAYSNIKDYIDEADKIAKEAKGLAHEATKLATGPQGSLKDG---- 1944
Cdd:pfam06160 144 YGPAIDELEKQLAEIEEEFSQFEELTESGdyLEAREVLEKLEEETDALEELMEDIPPLYEELKTELPDQLEELKEGyrem 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1945 -AKGSLQKSFGILNEAKKLANNVKENDDDLNSLqtRLEKADVRNGELrralNDTLAKL-SAIPNDTAAKLQAAKNKarqa 2022
Cdd:pfam06160 224 eEEGYALEHLNVDKEIQQLEEQLEENLALLENL--ELDEAEEALEEI----EERIDQLyDLLEKEVDAKKYVEKNL---- 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2023 nDTAKDVLAQVKDLHQDL----DGLKKSYnQLADSVAKTNAVVKDPLKNkIIADADATVKNLEQEA----------DRLI 2088
Cdd:pfam06160 294 -PEIEDYLEHAEEQNKELkeelERVQQSY-TLNENELERVRGLEKQLEE-LEKRYDEIVERLEEKEvayselqeelEEIL 370
|
330 340 350
....*....|....*....|....*....|....*
gi 1911235092 2089 DKLKPIKELEDNLKKNISEIKELINQARKQANSIK 2123
Cdd:pfam06160 371 EQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFK 405
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1908-2115 |
2.68e-04 |
|
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: 45.40 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1908 NIKDYIDEADKIAKEAKGLAHEATKLATGPQG---SLK----------DGAKGSLQKSFGILNEAKK-----------LA 1963
Cdd:pfam00261 5 QIKEELDEAEERLKEAMKKLEEAEKRAEKAEAevaALNrriqlleeelERTEERLAEALEKLEEAEKaadesergrkvLE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1964 NNVKENDDDLNSLQTRLEKADVRNGELRRALNDTLAKLSAIPND---TAAKLQAAKNKARQANDTAKDVLAQVKDLHQDL 2040
Cdd:pfam00261 85 NRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDlerAEERAELAESKIVELEEELKVVGNNLKSLEASE 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1911235092 2041 DglkkSYNQLADSVAKTNAVVKDPLKNKII--ADADATVKNLEQEADRLIDKLkpikELEdnlKKNISEIKELINQA 2115
Cdd:pfam00261 165 E----KASEREDKYEEQIRFLTEKLKEAETraEFAERSVQKLEKEVDRLEDEL----EAE---KEKYKAISEELDQT 230
|
|
| VSP |
pfam03302 |
Giardia variant-specific surface protein; |
809-1190 |
2.83e-04 |
|
Giardia variant-specific surface protein;
Pssm-ID: 146106 [Multi-domain] Cd Length: 397 Bit Score: 46.12 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 809 CNQCLPGFYGDPTKGTAEDCQPCAcplnipsNNFSPTCHLDRslgLICDECPVGYAGP-----RCERCAEGYFgqpsVAG 883
Cdd:pfam03302 39 CEECNSNNYLTPTSQCIDDCAKIG-------NYYYTTNANNK---KICKECTVANCKTcedqgQCQACNDGFY----KSG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 884 GSCQPCQcndnldfsipGSCDSLSGA----CLICKPGTTGRYCElcaDGyfgdavdarncqpcrchANGSFSEVCHTQTG 959
Cdd:pfam03302 105 DACSPCH----------ESCKTCSGGtasdCTECLTGKALRYGN---DG-----------------TKGTCGEGCTTGTG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 960 QCECRP---NVQGRR-CDECKPETfglQSPRGCVpcnCNSFGSKSfdceeSGQCWCQPGVTGkKCDHCAHGYFNfQEGGC 1035
Cdd:pfam03302 155 AGACKTcglTIDGTSyCSECATET---EYPQNGV---CTSTAARA-----TATCKASSVANG-MCSSCANGYFR-MNGGC 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1036 TacdcshlgnNCDPKTGRCICPPNTIGDQCSQCVPNTWGHS-----IISGCKACNCSTVgsldfqcnintgqcnchpkfa 1110
Cdd:pfam03302 222 Y---------ETTKFPGKSVCEEANSGGTCQKEAPGYKLNNgdlvtCSPGCKTCTSNTV--------------------- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1111 gakCTECSRGYwnYPHCDPCncflpgtddATCDSETKKCacmdqTGQCTckvnvegvHCDRCQPGTFgldaKNPLGCSSC 1190
Cdd:pfam03302 272 ---CTTCMDGY--VKTSDSC---------TKCDSSCETC-----TGATT--------TCKTCATGYY----KSGTGCVSC 320
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1403-1431 |
3.14e-04 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 40.80 E-value: 3.14e-04
10 20
....*....|....*....|....*....
gi 1911235092 1403 RCDCPPGYSGLSCETCLPGFYRLRSGPGV 1431
Cdd:pfam00053 19 QCLCKPGVTGRHCDRCKPGYYGLPSDPPQ 47
|
|
| ApoLp-III |
pfam07464 |
Apolipophorin-III precursor (apoLp-III); This family consists of several insect ... |
1693-1849 |
3.34e-04 |
|
Apolipophorin-III precursor (apoLp-III); This family consists of several insect apolipoprotein-III sequences. Exchangeable apolipoproteins constitute a functionally important family of proteins that play critical roles in lipid transport and lipoprotein metabolism. Apolipophorin III (apoLp-III) is a prototypical exchangeable apolipoprotein found in many insect species that functions in transport of diacylglycerol (DAG) from the fat body lipid storage depot to flight muscles in the adult life stage.
Pssm-ID: 462172 [Multi-domain] Cd Length: 143 Bit Score: 43.51 E-value: 3.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1693 QGLQKEIDQMMrelrrkNLDTQKEVAEDELVAAEGLLKKVQKVFGEprgknekmekdLGEKLTDHKNKLDDAWDLLR--- 1769
Cdd:pfam07464 3 EELQQSVQKQL------GLPSQQEVVETIKENTENLVDQLKQVQKS-----------LQEELKKASGEAEEALKELNtki 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1770 -EATDKTREANrlaAANQQNMTALEEK-KEAIESGKRQTENTLKEGNDILDEAN-RLADEINSVIDYVTDIQTKLppmSE 1846
Cdd:pfam07464 66 vETADKLSEAN---PEVVQKANELQEKfQSGVQSLVTESQKLAKSISENSQGATeKLQKATKQAYDDAVQAAQKL---AN 139
|
...
gi 1911235092 1847 ELK 1849
Cdd:pfam07464 140 QLQ 142
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1688-1893 |
4.39e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 4.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1688 FERNMQGLQKEIDQMMRELRRKNLDTQ--KEVAED-------ELVAAEGLLKKVQKVFgEPRGKNEKMEKDLgeKLTDHK 1758
Cdd:COG4717 293 LAREKASLGKEAEELQALPALEELEEEelEELLAAlglppdlSPEELLELLDRIEELQ-ELLREAEELEEEL--QLEELE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1759 NKLDDawdLLREATDKTREANRLAAANQQNMTALEEKKEAIESGKRQTENTLKEGNDILDEANrLADEINSVIDYVTDIQ 1838
Cdd:COG4717 370 QEIAA---LLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEE-LEEELEELEEELEELE 445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1911235092 1839 TKLppmsEELKDKIDDLSREMK----DRKLAERVYQAENHAAQLN------ASSAVLDGILDEAK 1893
Cdd:COG4717 446 EEL----EELREELAELEAELEqleeDGELAELLQELEELKAELRelaeewAALKLALELLEEAR 506
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1889-2096 |
5.31e-04 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 44.21 E-value: 5.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1889 LDEAKSISFNATAAFKAYSNIKDYIDEADKIAKEAKGLAheaTKLATGPQG---------SLKDGAKGSLQKSFGIL--- 1956
Cdd:pfam12795 5 LEKAKLDEAAKKKLLQDLQQALSLLDKIDASKQRAAAYQ---KALDDAPAElrelrqelaALQAKAEAAPKEILASLsle 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1957 ----------NEAKKLANNVKENDDDLNSLQTRLEKADVRNGELRRALNDTLAKLSAiPNDTAAKLQAAKNKARQANDTA 2026
Cdd:pfam12795 82 eleqrllqtsAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRNRLNG-PAPPGEPLSEAQRWALQAELAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2027 KDvlAQVKDLHQDLDG-------LKKSYNQLADSVAKTNAVVKDpLKNKI----IADADATVKNLEQEADRLIDKLKPIK 2095
Cdd:pfam12795 161 LK--AQIDMLEQELLSnnnrqdlLKARRDLLTLRIQRLEQQLQA-LQELLnekrLQEAEQAVAQTEQLAEEAAGDHPLVQ 237
|
.
gi 1911235092 2096 E 2096
Cdd:pfam12795 238 Q 238
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1493-1541 |
6.03e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 39.99 E-value: 6.03e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1911235092 1493 CACPLissSNNFSPSCVmegLDDYRCTaCPRGYEGQYCERCAPGYTGSP 1541
Cdd:smart00180 1 CDCDP---GGSASGTCD---PDTGQCE-CKPNVTGRRCDRCAPGYYGDG 42
|
|
| TNFRSF16 |
cd13416 |
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 ... |
795-943 |
6.81e-04 |
|
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 neurotrophin receptor (p75NTR) or CD271; TNFRSF16 (also known as nerve growth factor receptor (NGFR) or p75 neurotrophin receptor (p75NTR or p75(NTR)), CD271, Gp80-LNGFR) is a common receptor for both neurotrophins and proneurotrophins, and plays a diverse role in many tissues, including the nervous system. It has been shown to be expressed in various types of stem cells and has been used to prospectively isolate stem cells with different degrees of potency. p75NTR owes its signaling to the recruitment of intracellular binding proteins, leading to the activation of different signaling pathways. It binds nerve growth factor (NGF) and the complex can initiate a signaling cascade which has been associated with both neuronal apoptosis and neuronal survival of discrete populations of neurons, depending on the presence or absence of intracellular signaling molecules downstream of p75NTR (e.g. NF-kB, JNK, or p75NTR intracellular death domain). p75NTR can also bind NGF in concert with the neurotrophic tyrosine kinase receptor type 1 (TrkA) protein where it is thought to modulate the formation of the high-affinity neurotrophin binding complex. On melanoma cell, p75NTR is an immunosuppressive factor, induced by interferon (IFN)-gamma, and mediates down-regulation of melanoma antigens. It can interact with the aggregated form of amyloid beta (Abeta) peptides, and plays an important role in etiopathogenesis of Alzheimer's disease by influencing protein tau hyper-phosphorylation. p75(NTR) is involved in the formation and progression of retina diseases; its expression is induced in retinal pigment epithelium (RPE) cells and its knockdown rescues RPE cell proliferation activity and inhibits RPE apoptosis induced by hypoxia. It can therefore be a potential therapeutic target for RPE hypoxia or oxidative stress diseases.
Pssm-ID: 276921 [Multi-domain] Cd Length: 159 Bit Score: 42.67 E-value: 6.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 795 AECLNCRDHTGGPYCNQCLPGFyGDPTKGTAED--CQPCacplnIPSNNFSPT-CHLDRSlgLICDECPvGYAGPRCE-- 869
Cdd:cd13416 1 EACPSGQYTSSGECCEQCPPGE-GVARPCGDNQtvCEPC-----LDGVTFSDVvSHTEPC--QPCTRCP-GLMSMRAPct 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 870 -------RCAEGYFgqPSVAGGSCQPCQcndnldfsipgSCDSLSGACLICKPGTTGRyCELCADGYFGDAVDARN-CQP 941
Cdd:cd13416 72 athdtvcECAYGYY--LDEDSGTCEPCT-----------VCPPGQGVVQSCGPNQDTV-CEACPEGTYSDEDSSTDpCLP 137
|
..
gi 1911235092 942 CR 943
Cdd:cd13416 138 CT 139
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1703-2085 |
7.03e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.31 E-value: 7.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1703 MRELRR--KNLDTQKEVAEdelvaaegllkKVQKVfgeprgKNEKMEKDLGEKLtdhknkldDAWDLLREatDKTREANR 1780
Cdd:COG1196 195 LGELERqlEPLERQAEKAE-----------RYREL------KEELKELEAELLL--------LKLRELEA--ELEELEAE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1781 LAAANQQnmtaLEEKK---EAIESGKRQTENTLKEGNDILDEAN-RLADEINSVIDYVTDIQ-TKLppMSEELKDKIDDL 1855
Cdd:COG1196 248 LEELEAE----LEELEaelAELEAELEELRLELEELELELEEAQaEEYELLAELARLEQDIArLEE--RRRELEERLEEL 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1856 SREMkdRKLAERVYQAENHAAQLNASSAVLDGILDEAK-SISFNATAAFKAYSNIKDYIDEADKIAKEAKGLAHEATKLA 1934
Cdd:COG1196 322 EEEL--AELEEELEELEEELEELEEELEEAEEELEEAEaELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELA 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1935 TGpQGSLKDGAKGSLQKSFGILNEAKKLANNVKENDDDLNSLQTRLEKADVRNGELRRALNDTLAKLsaipndtaAKLQA 2014
Cdd:COG1196 400 AQ-LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL--------AELLE 470
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1911235092 2015 AKNKARQANDTAKDVLAQVKDLHQDLDGLKKSYNQLADSVAKTNAVVKDPLKNKIIADADATVKNLEQEAD 2085
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALE 541
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1955-2153 |
7.52e-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: 43.76 E-value: 7.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1955 ILNEAKKLANNVKENDDDLNSLQTRLEKADVRNGELRRALNDTLAKLSaipndtAAKLQAAKNKARQAN-DTAKDvlaqV 2033
Cdd:COG1579 22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIE------EVEARIKKYEEQLGNvRNNKE----Y 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2034 KDLHQDLDGLKKSYNQLADSVAKtnavvkdplKNKIIADADATVKNLEQEADRLIDKLkpiKELEDNLKKNISEIKELIN 2113
Cdd:COG1579 92 EALQKEIESLKRRISDLEDEILE---------LMERIEELEEELAELEAELAELEAEL---EEKKAELDEELAELEAELE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1911235092 2114 QARKQANSIKVSVSSggDCIRTYKpEIKKGSYNNIIVNVK 2153
Cdd:COG1579 160 ELEAEREELAAKIPP--ELLALYE-RIRKRKNGLAVVPVE 196
|
|
| V_Alix_like |
cd08915 |
Protein-interacting V-domain of mammalian Alix and related domains; This superfamily contains ... |
1857-2116 |
8.73e-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: 44.26 E-value: 8.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1857 REMKDRKLAERVyqaenhAAQLNASSAVLDGILDEaksisFNATAAFKA---YSNIKDYIDEADKIAKEaKGLAHeatkl 1933
Cdd:cd08915 12 NERQDDYVREHI------VEPIEALNKLLNSFLAE-----RNLPASIDDlqkPENLPDSIQHSQEIIEE-GGLDN----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1934 atgpqgslkdgakgsLQKSFgilNEAKKLANNVKENdddLNSLQTRLEKADVRNGELRRA---LNDTLAKLSAIPNDTAA 2010
Cdd:cd08915 75 ---------------IEQSF---KELSKLRQNVEEL---LQECEELLEEEAAEDDQLRAKfgtLRWRRPSSDEAAKELYE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2011 KLQAAKNKARQANDTAKDVLAQVKDLHQDLDGLKKSYNQLADSVAKTNaVVKDPLKNKIIADADATVKNLEqeadrlidk 2090
Cdd:cd08915 134 KVTKLRGYLEQASNSDNEVLQCYESIDPNLVLLCGGYKELKAFIPSPY-PALDPEVSEVVSSLRPLLNEVS--------- 203
|
250 260
....*....|....*....|....*.
gi 1911235092 2091 lkpikELEDNLKKNISEIKELINQAR 2116
Cdd:cd08915 204 -----ELEKERERFISELEIKSRNND 224
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1958-2128 |
1.11e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1958 EAKKLANNVKEN--DDDLNSLQTRLEKAdvrngelRRALNDTLAKLSAIPNDTAAKLQA--AKNKARQANDTAKDVLAQV 2033
Cdd:COG3206 149 LAAAVANALAEAylEQNLELRREEARKA-------LEFLEEQLPELRKELEEAEAALEEfrQKNGLVDLSEEAKLLLQQL 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2034 KDLHQ-------DLDGLKKSYNQLADSVAKTNAVVKDPLKNKIIADADATVKNLEQEADRLIDKLKP----IKELE---D 2099
Cdd:COG3206 222 SELESqlaearaELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPnhpdVIALRaqiA 301
|
170 180 190
....*....|....*....|....*....|
gi 1911235092 2100 NLKKNI-SEIKELINQARKQANSIKVSVSS 2128
Cdd:COG3206 302 ALRAQLqQEAQRILASLEAELEALQAREAS 331
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1403-1430 |
1.44e-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: 38.87 E-value: 1.44e-03
10 20
....*....|....*....|....*...
gi 1911235092 1403 RCDCPPGYSGLSCETCLPGFYRLRSGPG 1430
Cdd:cd00055 20 QCECKPNTTGRRCDRCAPGYYGLPSQGG 47
|
|
| PTZ00214 |
PTZ00214 |
high cysteine membrane protein Group 4; Provisional |
818-1158 |
1.83e-03 |
|
high cysteine membrane protein Group 4; Provisional
Pssm-ID: 173479 [Multi-domain] Cd Length: 800 Bit Score: 44.14 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 818 GDPTKGTAEDCQPCACplnipsnnfsptchldRSLGLICDECPVGYAGPRCERCAEGYFGQP-----SVAGGS------C 886
Cdd:PTZ00214 354 GDATNGGVSGCATCGY----------------NSGAVTCTRCSAGYLGVDGKSCSESCSGDTrgvctKVAEGSestevsC 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 887 QpCQCNDNLdFSIPGSCDSLSGACLICKPGT-TGryCELCADGYFGDAVDARNcQPCRCHANGSFSEVChtqtgqCECRP 965
Cdd:PTZ00214 418 R-CVCKPTF-YNSSGTCTPCTDSCAVCKDGTpTG--CQQCSPGKILEFSIVSS-ESADCVDQCSVGSEC------AECGI 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 966 NVQGRR-CDECK-PETFGLQSPrgCVP-------CNCNSFGSKSfDCEES-----GQCWCQ---PGVT------GKKCDH 1022
Cdd:PTZ00214 487 TIDGSRyCTRCKdASTYPFNGV--CIPntqrdayCTSTANGACT-TCSGAaflmnGGCYTTehyPGSTicdkqsNGKCTT 563
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1023 CAHGYFNFQEGGCTACDCSHLGNNCdPKTGRCI-CPPNTI-------------------------GDQCSQCVP---NTW 1073
Cdd:PTZ00214 564 TKKGYGISPDGKLLECDPTCLACTA-PGPGRCTrCPSDKLlkrasgaatgscvdpgacvdgyyadGDACLPCATpgcKTC 642
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1074 GHSiiSGCKACNCSTVGSLDFQCNIN--TGQCNCHPKFAGAKCTECSRGYwnYPHCDPCNCFLPgtddATCDSETKKCAC 1151
Cdd:PTZ00214 643 GHA--SFCTECAGELFVSLDGQSCLEecTGDKVVGEVSGGVRRCWCERGF--LPALDRSGCVLP----TECPPDMPSCAA 714
|
....*..
gi 1911235092 1152 MDQTGQC 1158
Cdd:PTZ00214 715 CDESGRC 721
|
|
| dnaK |
PRK00290 |
molecular chaperone DnaK; Provisional |
1793-1890 |
1.97e-03 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 234715 [Multi-domain] Cd Length: 627 Bit Score: 43.94 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1793 EEKKEAIEsgKR--------QTENTLKEGNDILDEANRlaDEINSVIDYV------TDIqtklppmsEELKDKIDDLSRE 1858
Cdd:PRK00290 520 KKRKELVE--ARnqadsliyQTEKTLKELGDKVPADEK--EKIEAAIKELkealkgEDK--------EAIKAKTEELTQA 587
|
90 100 110
....*....|....*....|....*....|..
gi 1911235092 1859 MKdrKLAERVYQAENHAAQLNASSAVLDGILD 1890
Cdd:PRK00290 588 SQ--KLGEAMYQQAQAAQGAAGAAAKDDDVVD 617
|
|
| DAHL |
pfam19443 |
DAHL domain; The DAHL (Double All-Helical Ligand-binding) domain is a novel periplasmic ... |
1754-1896 |
2.48e-03 |
|
DAHL domain; The DAHL (Double All-Helical Ligand-binding) domain is a novel periplasmic sensory domain, which is found in major types of bacterial signal transduction proteins: histidine kinases and diguanylate cyclases/phosphodiesterases, and, occasionally in chemoreceptors. The majority of the DAHL domain-containing proteins were found in alpha-, beta-, gamma- and epsilonproteobacteria. It is also present in some cyanobacterial species. Secondary structure prediction suggested that DAHL consists predominantly of alpha-helical regions. The DAHL domain was identified in the Tlp10 chemoreceptor from the human pathogen Campylobacter jejuni and in the VirA sensor histidine kinase from a plant pathogen Agrobacterium tumefaciens. This domain recognizes Asp, Ile, purine, fumarate, malate, alpha-ketoglutarate, mannose, rhamnose, fucose, sialic acid, Arg, thiamine and galactose (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1 https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 466085 [Multi-domain] Cd Length: 222 Bit Score: 42.04 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1754 LTDHKNKLDDAWDLLREATDKTR-EANRLAAANQQNMTALEEKKEAIESGKRQT---ENTL--------------KEGND 1815
Cdd:pfam19443 41 LVAALAELRRLLERLELPSFLLAgDSAELDAALAALRAALQEKEELVERFKSQNallRNSLayfptlvdellaasPAEPA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1816 ILDEANRLadeINSVIDYVTDiqtkLPPMSEELKDKIDDLSR-EMKDRKLAERVYQAENHAAQLNASSAVLDGILDEAKS 1894
Cdd:pfam19443 121 LAAALNEL---LRAVLLYNLS----SDPALAEIEALLERLEAlAESAPALRAALQLLLAHARLILRLLPQVDALLQEILA 193
|
..
gi 1911235092 1895 IS 1896
Cdd:pfam19443 194 LP 195
|
|
| F5_F8_type_C |
pfam00754 |
F5/8 type C domain; This domain is also known as the discoidin (DS) domain family. |
95-179 |
2.58e-03 |
|
F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.
Pssm-ID: 459925 [Multi-domain] Cd Length: 127 Bit Score: 40.51 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 95 SSNPNQRHPITNAIDGK-NTWWQSPSIKNGieyhyVTITLDLQQVFQIAYVIVKAANSPRPGN---WILERSLDDVEYKP 170
Cdd:pfam00754 5 SSSYSGEGPAAAALDGDpNTAWSAWSGDDP-----QWIQVDLGKPKKITGVVTQGRQDGSNGYvtsYKIEYSLDGENWTT 79
|
....*....
gi 1911235092 171 WQYHAVTDT 179
Cdd:pfam00754 80 VKDEKIPGN 88
|
|
| TNFRSF21 |
cd10583 |
Tumor necrosis factor receptor superfamily member 21 (TNFRSF21), also known as death receptor ... |
847-953 |
2.70e-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: 41.27 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 847 HLDRSLG--LICDECPVGYAGPR---------CERCAEGYFGQPSVAGGSCQPCQ--CNDNLDFSIPgsCDSLSGACLIC 913
Cdd:cd10583 4 HVDPATGtqLTCDKCPAGTYVSKhctetslreCSPCPNGTFTRHENGIEQCHRCRkpCPAPMIEKTP--CTALTDRECTC 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1911235092 914 KPGT--TGRYC---ELCADGYF-----GDAVDARnCQPCrchANGSFSEV 953
Cdd:cd10583 82 PPGTflSNDTCvphSVCPVGWGvrkkgTETEDVR-CKPC---PRGTFSDV 127
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
1688-1778 |
2.98e-03 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.
Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 39.61 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1688 FERNMQGLQKEIDQMMRELrrknldTQKEVAEDeLVAAEGLLKKVQKVFGEPRGKNEKMEK--DLGEKLTDHK------- 1758
Cdd:pfam00435 6 FFRDADDLESWIEEKEALL------SSEDYGKD-LESVQALLKKHKALEAELAAHQDRVEAlnELAEKLIDEGhyaseei 78
|
90 100
....*....|....*....|....
gi 1911235092 1759 ----NKLDDAWDLLREATDKTREA 1778
Cdd:pfam00435 79 qerlEELNERWEQLLELAAERKQK 102
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1612-1844 |
3.03e-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: 42.74 E-value: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1612 QLAEGNLNTLVTEMNELLTRATKVTADgeqtgQDAERTSRRANSLgdfIKGLVRDAEAVNEKAKEVNETLGiqdkAFERN 1691
Cdd:cd22656 83 QNAGGTIDSYYAEILELIDDLADATDD-----EELEEAKKTIKAL---LDDLLKEAKKYQDKAAKVVDKLT----DFENQ 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1692 MQGLQKEIDQmmrelRRKNLDTQ--KEVAEDELVAAEGLLKKVqkvfgeprgknEKMEKDLGEKLtdhKNKLDDAWDLLR 1769
Cdd:cd22656 151 TEKDQTALET-----LEKALKDLltDEGGAIARKEIKDLQKEL-----------EKLNEEYAAKL---KAKIDELKALIA 211
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1911235092 1770 EATDKTREANRLaaanQQNMTALeekKEAIESGKRQTENTLKEGNDILDEANRLADEINSVIDYVTDIQTKLPPM 1844
Cdd:cd22656 212 DDEAKLAAALRL----IADLTAA---DTDLDNLLALIGPAIPALEKLQGAWQAIATDLDSLKDLLEDDISKIPAA 279
|
|
| GvpP |
COG4980 |
Gas vesicle protein YhaH [General function prediction only]; |
1800-1882 |
3.73e-03 |
|
Gas vesicle protein YhaH [General function prediction only];
Pssm-ID: 444004 [Multi-domain] Cd Length: 106 Bit Score: 39.57 E-value: 3.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1800 ESGKRQTENTLKEGNDILDEANRLADEI-NSVIDYVTDIQTKLPPMSEELKDKIDDLSREMKDRKlaERVyqaENHAAQL 1878
Cdd:COG4980 27 KSGKETRKKLKDKADDLKDKAEDLKDELkEKASELSEEAKEKLDELIEEIKEKIEELKEEVEPKI--EEL---KEEAEKL 101
|
....
gi 1911235092 1879 NASS 1882
Cdd:COG4980 102 QKEV 105
|
|
| PLU-1 |
pfam08429 |
PLU-1-like protein; Sequences in this family bear similarity to the central region of PLU-1. ... |
1793-2056 |
3.75e-03 |
|
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: 42.20 E-value: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1793 EEK-KEAIESGKRQTENTLK----EGNDI--------------LDEANRLADEINSVI----------DYVTDIQTKLPP 1843
Cdd:pfam08429 3 AEKvEEALEEEPKPSLKELRallnEAEKIkfplpellqdlrafVQRANKWVEEAQQLLsrkqqtrrknEAEEDEREREKR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1844 MSEELK---DKIDDLS---REMKD-RKLAERVYQAENHAAQL------NASSAVLDGILDEAKSISFNATAafkaysnik 1910
Cdd:pfam08429 83 TVEELRkllEEADNLPfdcPEIEQlKELLEEIEEFQKRAREAlseeppSLSIEELEELLEEGKSFNVDLPE--------- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1911 dyIDEADKIAKEAKGLAhEATKLATGPQGSLKDgakgsLQKsfgILNEAKKLANNvKENDDDLNSLQTRLEKADVRNGEL 1990
Cdd:pfam08429 154 --LEELEKVLEQLKWLE-EVRETSRKKSLTLED-----VRE---LIEEGVELGIP-PPYEDLMAELQELLTAGERWEEKA 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1911235092 1991 RRALND---TLAKLSAIPN---------DTAAKLQAAKNKARqandtakDVLAQVKDLHQDLDGLKK-SYNQLADSVAK 2056
Cdd:pfam08429 222 KELLSRervSLAQLEALSKeaqeipvslPNLAALDEILKKAR-------EWQRQIEALYQRSDFGKRpTLDELEELLAK 293
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
1674-1764 |
6.09e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 39.48 E-value: 6.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 1674 AKEVNETLGIQDKAFERNMQGLQKEIDQMMRELRRKN--LDTQKEVAEDELVAAEGLLKKVQKVFgepRGKNEKMEKDLG 1751
Cdd:pfam03938 17 GKAAQAQLEKKFKKRQAELEAKQKELQKLYEELQKDGalLEEEREEKEQELQKKEQELQQLQQKA---QQELQKKQQELL 93
|
90
....*....|...
gi 1911235092 1752 EKLTDhknKLDDA 1764
Cdd:pfam03938 94 QPIQD---KINKA 103
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2005-2123 |
7.79e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 7.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911235092 2005 PNDTAAKLQAAK------NKARQANDTAK---DVLAQVKDLHQDLDGLKKSYNQLADSVAKTN---AVVKDPLKNKIIAD 2072
Cdd:COG4913 220 EPDTFEAADALVehfddlERAHEALEDAReqiELLEPIRELAERYAAARERLAELEYLRAALRlwfAQRRLELLEAELEE 299
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1911235092 2073 ADATVKNLEQEADRLIDKLKPIKELEDNLK--------KNISEIKELINQARKQANSIK 2123
Cdd:COG4913 300 LRAELARLEAELERLEARLDALREELDELEaqirgnggDRLEQLEREIERLERELEERE 358
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1403-1424 |
9.60e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 36.52 E-value: 9.60e-03
|
| |
