|
Name |
Accession |
Description |
Interval |
E-value |
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1589-1848 |
1.40e-105 |
|
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: 338.62 E-value: 1.40e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1589 TMNIN-LTGPLPAPYKILYGLENTTQELKHLLSPQRAPERLIQLAEGNVNTLVMETNELLTRATKVTADGEQTGQDAERT 1667
Cdd:pfam06008 1 LLSLNsLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1668 NSRAESLEEFIKGLVQDAEAINEKAVQLNEtlgNQDKTAERNLEELQKEIDRMLKELRSKDLQTQKEVAEDELVAAEGLL 1747
Cdd:pfam06008 81 LGHAKELAEAIKNLIDNIKEINEKVATLGE---NDFALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQDLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1748 KRVNKLFGEPRAQNEDMEKDLQQKLAEYKNKLDDAWDLLREATDKTRDANRLSAANQKNMTILETKKEAIEGSKRQIENT 1827
Cdd:pfam06008 158 SRIQTWFQSPQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEET 237
|
250 260
....*....|....*....|.
gi 117647249 1828 LKEGNDILDEANRLLGEINSV 1848
Cdd:pfam06008 238 LKTARDSLDAANLLLQEIDDA 258
|
|
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
29-281 |
5.71e-93 |
|
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related protein such as Unc-6/ netrins.
Pssm-ID: 214532 Cd Length: 238 Bit Score: 301.59 E-value: 5.71e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 29 AHQQRGLFPAVLNLASNALITTNATCGEKGPEMYCKLVEHVpgqpVRNPQCRICNQNssNPYQRHPITNAIDGKN----T 104
Cdd:smart00136 1 AGRPRSCYPPFVNLAFGREVTATSTCGEPGPERYCKLVGHT----EQGKKCDYCDAR--NPRRSHPAENLTDGNNpnnpT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 105 WWQSPSIKNGVeyHYVTITLDLQQVFQIAYVIVKAAnSPRPGNWILERSLDDVEYKPWQYHAvtdTECLTLYNIyPRTGP 184
Cdd:smart00136 75 WWQSEPLSNGP--QNVNLTLDLGKEFHVTYVILKFC-SPRPSLWILERSDFGKTWQPWQYFS---SDCRRTFGR-PPRGP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 185 PSYAKDDEVICTSFYSKIHPLENGEIHISLINGRPSADDP--SPELLEFTSARYIRLRFQRIRTLNADLMMfahkdpreI 262
Cdd:smart00136 148 ITKGNEDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDFdnSPVLQEWVTATNIRVRLTRLRTLGDELMD--------D 219
|
250
....*....|....*....
gi 117647249 263 DPIVTRRYYYSVKDISVGG 281
Cdd:smart00136 220 RPEVTRRYYYAISDIAVGG 238
|
|
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
35-281 |
6.13e-88 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 286.79 E-value: 6.13e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 35 LFPAVLNLASNALITTNATCGEKGPEMYCKLVEHVPGQpvrnpQCRICNqnSSNPYQRHPITNAIDGKN----TWWQSPS 110
Cdd:pfam00055 1 CYPAFGNLAFGREVSATSTCGLNGPERYCILSGLEGGK-----KCFICD--SRDPHNSHPPSNLTDSNNgtneTWWQSET 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 111 IKngVEYHYVTITLDLQQVFQIAYVIVKAAnSPRPGNWILERSLD-DVEYKPWQYHAvtdTECLTLYNIypRTGPPSYAK 189
Cdd:pfam00055 74 GV--IQYENVNLTLDLGKEFHFTYLILKFK-SPRPAAMVLERSTDfGKTWQPYQYFA---SDCRRTFGR--PSGPSRGIK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 190 DDEVICTSFYSKIHPLENGEIHISLINGRPSA--DDPSPELLEFTSARYIRLRFQRIRTLNadlmmfahkDPREIDPIVT 267
Cdd:pfam00055 146 DDEVICTSEYSDISPLTGGEVIFSTLEGRPSAniFDYSPELQDWLTATNIRIRLLRLHTLG---------DELLDDPSVL 216
|
250
....*....|....
gi 117647249 268 RRYYYSVKDISVGG 281
Cdd:pfam00055 217 RKYYYAISDISVGG 230
|
|
| Laminin_II |
pfam06009 |
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 ... |
2033-2168 |
2.95e-54 |
|
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: 186.54 E-value: 2.95e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2033 VKEKAREANDTAKAVLAQVKDLHQNLDGLKQNYNKLADSVAKTNAVVKDpsKNKIIADAGTSVRNLEQEADRLIDKLKPI 2112
Cdd:pfam06009 1 SKELAREANETAKEVLEQLAPLSQNLENTSEKLSGINRSLEETNELVND--ANKALDDAGRSVKKLEELAPDLLDKLKPL 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 117647249 2113 KELEDN---LKKNISEIKELINQARKQANSIKVSVSSGGDCVRTYRPEIKKGSYNNIVV 2168
Cdd:pfam06009 79 KQLEVNsssLSDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTS 137
|
|
| LamB |
smart00281 |
Laminin B domain; |
1225-1360 |
5.37e-47 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 165.51 E-value: 5.37e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1225 HLEPFYWKLPQQFEGKKLMAYGGKLKYAIYFEARDEtGFATYKPQVIIRGGtptHARIITRHMAAPLIGQLTRHEIEMTE 1304
Cdd:smart00281 1 DNEPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRRG-GTHVSAPDVILEGN---GLRISHPAEGPPLPDELTTVEVRFRE 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 117647249 1305 KEWKYYGddpriSRTVTREDFLDILYDIHYILIKATYGNVVRQSRISEISMEVAEP 1360
Cdd:smart00281 77 ENWQYYG-----GRPVTREDLMMVLANLTAILIRATYSQQMAGSRLSDVSLEVAVP 127
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2789-2917 |
2.21e-45 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 160.95 E-value: 2.21e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2789 VRTEAESGLLFYMARINHADFATVQLRNGFPYFSYDLGSGDTSTMIPTKINDGQWHKIKIVRVKQEGILYVDD-ASSQTI 2867
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGeARPTGE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 117647249 2868 SPKKADI-LDVVGILYVGGLPINYTTRRIGPVTYSLDGCVRNLHMEQAPVD 2917
Cdd:pfam00054 81 SPLGATTdLDVDGPLYVGGLPSLGVKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
1230-1374 |
1.18e-44 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 158.97 E-value: 1.18e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1230 YWKLPQQFEGKKLMAYGGKLKYAIYFEARDETGFATYKPQVIIRGGtptHARIITRHMA--APLIGQLTRHEIEMTEKEW 1307
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGGGSLNSEPDVILEGN---GLRLSYSSPDqpPPDPGQEQTYSVRLHEENW 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 117647249 1308 KYygddpRISRTVTREDFLDILYDIHYILIKATYGNVVRQSRISEISMEVAEPGhvlAGSPPAHLIE 1374
Cdd:pfam00052 78 RD-----SDGAPVSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSAVPG---GSGPPASWVE 136
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
579-718 |
3.54e-39 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 143.56 E-value: 3.54e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 579 YWSAPPPYLGNRLPAVGGQLSFTISYDLEEEEDDTekILQLMIIFEGNDLRISTAYKE-VYLEPSEEHIEEVSLKEEAFT 657
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGGGSL--NSEPDVILEGNGLRLSYSSPDqPPPDPGQEQTYSVRLHEENWR 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 117647249 658 iHGTNLPVTRKDFMIVLTNLERVLMQITYNLGMDAIfRLSSVNLESAVPYPTDRRiATDVE 718
Cdd:pfam00052 79 -DSDGAPVSREDFMMVLANLTAILIRATYSTGSGQV-SLSNVSLDSAVPGGSGPP-ASWVE 136
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2364-2503 |
4.19e-39 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 142.84 E-value: 4.19e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2364 FRTFSSSALLMYLATRDLKDFMSVELSDGHVKVSYDLGSGMTSVVSNQNHNDGKWKAFTLSRIQKQANISIVDIdsnqEE 2443
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGE----AR 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2444 NVATSSSGNNFglDLKADDKIYFGGLPtlrNLSMKARPEVNVKKYSGCLKDIEISRTPYN 2503
Cdd:pfam00054 77 PTGESPLGATT--DLDVDGPLYVGGLP---SLGVKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2762-2911 |
2.58e-37 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 138.71 E-value: 2.58e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2762 FGLSRNSHIAIAFDDTKvKNRLTIELEVRTEAESGLLFYMARINHADFATVQLRNGFPYFSYDLGSGDTSTMIPTKINDG 2841
Cdd:cd00110 2 VSFSGSSYVRLPTLPAP-RTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 117647249 2842 QWHKIKIVRVKQEGILYVDDASS-QTISPKKADILDVVGILYVGGLPINYTTRRIgPVTYSLDGCVRNLHM 2911
Cdd:cd00110 81 QWHSVSVERNGRSVTLSVDGERVvESGSPGGSALLNLDGPLYLGGLPEDLKSPGL-PVSPGFVGCIRDLKV 150
|
|
| LamG |
smart00282 |
Laminin G domain; |
2784-2911 |
1.67e-36 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 135.54 E-value: 1.67e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2784 TIELEVRTEAESGLLFYMARINHADFATVQLRNGFPYFSYDLGSGDTSTMI-PTKINDGQWHKIKIVRVKQEGILYVDDA 2862
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSdPTPLNDGQWHRVAVERNGRSVTLSVDGG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 117647249 2863 SSQTI-SPKKADILDVVGILYVGGLPINYtTRRIGPVTYSLDGCVRNLHM 2911
Cdd:smart00282 81 NRVSGeSPGGLTILNLDGPLYLGGLPEDL-KLPPLPVTPGFRGCIRNLKV 129
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2170-2310 |
4.64e-34 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 128.59 E-value: 4.64e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2170 VKTAVADNLLFYLGSAKFIDFLAIEMRKGKVSFLWDVGSGVGRVEYPDlTIDDSYWYRIEASRTGRNGSISVRALDGPKA 2249
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGD-KLNDGKWHSVELERNGRSGTLSVDGEARPTG 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 117647249 2250 SmvpstyhsvSPPGYTIlDVDANAMLFVGGLTGKI-KKADAVRVITFTGCMGETYFDNKPIG 2310
Cdd:pfam00054 80 E---------SPLGATT-DLDVDGPLYVGGLPSLGvKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| LamB |
smart00281 |
Laminin B domain; |
578-706 |
2.82e-33 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 126.22 E-value: 2.82e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 578 YYWSAPPPYLGNRLPAVGGQLSFTISYdleEEEDDTEKILQLMIIFEGNDLRISTAYkEVYLEPSEEHIEEVSLKEEAFT 657
Cdd:smart00281 5 VYWVAPEQFLGDKVTSYGGKLRYTLSF---DGRRGGTHVSAPDVILEGNGLRISHPA-EGPPLPDELTTVEVRFREENWQ 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 117647249 658 IHGTNlPVTRKDFMIVLTNLERVLMQITYNLGMDAIfRLSSVNLESAVP 706
Cdd:smart00281 81 YYGGR-PVTREDLMMVLANLTAILIRATYSQQMAGS-RLSDVSLEVAVP 127
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2937-3089 |
3.87e-33 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 126.76 E-value: 3.87e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2937 GTYFDGTGFAKAVGGFKVGLDLLVEFEFRTTRPTGVLLGVSSQ-KMDGMGIEMIDEKLMFHVDNGAGRFTAIYdagiPGH 3015
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQnGGDFLALELEDGRLVLRYDLGSGSLVLSS----KTP 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 117647249 3016 MCNGQWHKVTAKKIKNRLELVVDGNQVDAQSPNSASTSADTNDPVFVGGFPGGLNQFGLTTNIRFRGCIRSLKL 3089
Cdd:cd00110 77 LNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKV 150
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2336-2497 |
2.28e-32 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 124.45 E-value: 2.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2336 TIQFDGEGYALVSRPIRWYPNiSTVMFKFRTFSSSALLMYLATRDLKDFMSVELSDGHVKVSYDLGSGMTSVVSNQNHND 2415
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRTR-LSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLND 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2416 GKWKAFTLSRIQKQANISIvdidsNQEENVATSSSGNNFGLDLkaDDKIYFGGLPTlrnlSMKARPEVNVKKYSGCLKDI 2495
Cdd:cd00110 80 GQWHSVSVERNGRSVTLSV-----DGERVVESGSPGGSALLNL--DGPLYLGGLPE----DLKSPGLPVSPGFVGCIRDL 148
|
..
gi 117647249 2496 EI 2497
Cdd:cd00110 149 KV 150
|
|
| LamG |
smart00282 |
Laminin G domain; |
2359-2499 |
1.38e-30 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 118.60 E-value: 1.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2359 TVMFKFRTFSSSALLMYLATRDLKDFMSVELSDGHVKVSYDLGSGMTSVVSNQNH-NDGKWKAFTLSRIQKQANISIvdi 2437
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPlNDGQWHRVAVERNGRSVTLSV--- 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 117647249 2438 dsNQEENVATSSSGNNFGLDLkaDDKIYFGGLPTlrnlSMKARPEVNVKKYSGCLKDIEISR 2499
Cdd:smart00282 78 --DGGNRVSGESPGGLTILNL--DGPLYLGGLPE----DLKLPPLPVTPGFRGCIRNLKVNG 131
|
|
| LamG |
smart00282 |
Laminin G domain; |
2960-3089 |
2.96e-30 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 117.83 E-value: 2.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2960 VEFEFRTTRPTGVLLGVSS-QKMDGMGIEMIDEKLMFHVDNGAGRFTAIYDagiPGHMCNGQWHKVTAKKIKNRLELVVD 3038
Cdd:smart00282 2 ISFSFRTTSPNGLLLYAGSkGGGDYLALELRDGRLVLRYDLGSGPARLTSD---PTPLNDGQWHRVAVERNGRSVTLSVD 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 117647249 3039 G-NQVDAQSPnSASTSADTNDPVFVGGFPGGLNQFGLTTNIRFRGCIRSLKL 3089
Cdd:smart00282 79 GgNRVSGESP-GGLTILNLDGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKV 129
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2524-2686 |
1.26e-27 |
|
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: 110.97 E-value: 1.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2524 TVSFPKPGFVELAAVSID-VGTEINLSFSTRNESGIILLGSGGTLTPprrkrrqttqaYYAIFLNKGRLEVHLSSGTRTm 2602
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPrTRLSISFSFRTTSPNGLLLYAGSQNGGD-----------FLALELEDGRLVLRYDLGSGS- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2603 rkIVIKPePNLFHDGREHSVHVERTRGIFTVQIDEDR--RHMQNLTEEQPIEVKKLFVGGAPPEFQPSPLRNIPAFQGCV 2680
Cdd:cd00110 69 --LVLSS-KTPLNDGQWHSVSVERNGRSVTLSVDGERvvESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCI 145
|
....*.
gi 117647249 2681 WNLVIN 2686
Cdd:cd00110 146 RDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
2165-2307 |
5.70e-27 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 108.20 E-value: 5.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2165 NIVVHVKTAVADNLLFYLGSAKFIDFLAIEMRKGKVSFLWDVGSGVGRVEYPDLTIDDSYWYRIEASRTGRNGSISVral 2244
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLNDGQWHRVAVERNGRSVTLSV--- 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 117647249 2245 DGPKASMVpstyhsVSPPGYTILDVDANamLFVGGLTGKIKKADAVRVITFTGCMGETYFDNK 2307
Cdd:smart00282 78 DGGNRVSG------ESPGGLTILNLDGP--LYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2146-2305 |
2.85e-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: 2.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2146 SGGDCVRtYRPEIKKGSYNNIVVHVKTAVADNLLFYLGSAKFIDFLAIEMRKGKVSFLWDVGSGVGRVEYPDlTIDDSYW 2225
Cdd:cd00110 5 SGSSYVR-LPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKT-PLNDGQW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2226 YRIEASRTGRNGSISVralDGPKasmvpsTYHSVSPPGYTILDVDANamLFVGGLTGKIKKADAVRVITFTGCMGETYFD 2305
Cdd:cd00110 83 HSVSVERNGRSVTLSV---DGER------VVESGSPGGSALLNLDGP--LYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2550-2691 |
4.58e-25 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 102.78 E-value: 4.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2550 FSTRNESGIILlgSGGTLTPPrrkrrqttqAYYAIFLNKGRLEVHLSSGTRtmrKIVIKPEPNLfHDGREHSVHVERTRG 2629
Cdd:pfam00054 1 FRTTEPSGLLL--YNGTQTER---------DFLALELRDGRLEVSYDLGSG---AAVVRSGDKL-NDGKWHSVELERNGR 65
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 117647249 2630 IFTVQIDEDRRHM--QNLTEEQ-PIEVKKLFVGGAPPE-FQPSPLRNIPAFQGCVWNLVINSIPMD 2691
Cdd:pfam00054 66 SGTLSVDGEARPTgeSPLGATTdLDVDGPLYVGGLPSLgVKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2964-3089 |
2.41e-24 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 100.57 E-value: 2.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2964 FRTTRPTGVLLGVSSQKMDGMGIEMIDEKLMFHVDNGAGRFTAIYdagIPGHMCNGQWHKVTAKKIKNRLELVVDGNQVD 3043
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDFLALELVNGRLVLRYDLGSGPESLLS---SGKNLNDGQWHSVRVERNGNTLTLSVDGQTVV 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 117647249 3044 AQSPNSASTSADTNDPVFVGGFPGGLNQFGLTTNIRFRGCIRSLKL 3089
Cdd:pfam02210 78 SSLPPGESLLLNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRV 123
|
|
| LamG |
smart00282 |
Laminin G domain; |
2545-2687 |
3.76e-23 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 97.41 E-value: 3.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2545 EINLSFSTRNESGIILLGSGGTLTPprrkrrqttqaYYAIFLNKGRLEVHLSSGTRTmrkIVIKPEPNLFHDGREHSVHV 2624
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGD-----------YLALELRDGRLVLRYDLGSGP---ARLTSDPTPLNDGQWHRVAV 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 117647249 2625 ERTRGIFTVQID-EDRRHMQNLTEEQPIEVK-KLFVGGAPPEFQPSPLRNIPAFQGCVWNLVINS 2687
Cdd:smart00282 67 ERNGRSVTLSVDgGNRVSGESPGGLTILNLDgPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNG 131
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1665-2143 |
3.54e-17 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 88.92 E-value: 3.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1665 ERTNSRAESLEEFIKGLVQDAEAINEKAVQLNETLGNQDKTAERnLEELQKEIDR----------MLKELRSK--DLQTQ 1732
Cdd:TIGR04523 225 KQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQ-LSEKQKELEQnnkkikelekQLNQLKSEisDLNNQ 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1733 KEvaedelvaaEGLLKRVNKLFGEPRAQNEDMEKDL---QQKLAEYKNKLDDawdLLREATDKTRDanrlsaaNQKnmti 1809
Cdd:TIGR04523 304 KE---------QDWNKELKSELKNQEKKLEEIQNQIsqnNKIISQLNEQISQ---LKKELTNSESE-------NSE---- 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1810 letKKEAIEGSKRQIENTLKEGNDILDEANRLLGEINSVIDYVDDIKTKlppmSEELSDKI-------DDLAQEIKdrRL 1882
Cdd:TIGR04523 361 ---KQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKL----NQQKDEQIkklqqekELLEKEIE--RL 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1883 AEKVFQAESHAAQLNDSSAVLDGILDEAKNISfnataafraySNIKDYIDEAEKVAREAK-ELAQGATKLATSPQGLLKe 1961
Cdd:TIGR04523 432 KETIIKNNSEIKDLTNQDSVKELIIKNLDNTR----------ESLETQLKVLSRSINKIKqNLEQKQKELKSKEKELKK- 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1962 dakgslqksfrILNEAKKLANDVKgnhndlnDLKTRLETadlrnsgllgaLNDTMDKLSAITNDTAAKLQAVKEKAREAN 2041
Cdd:TIGR04523 501 -----------LNEEKKELEEKVK-------DLTKKISS-----------LKEKIEKLESEKKEKESKISDLEDELNKDD 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2042 DT-AKAVLAQVKD-LHQNLDGLKQNYNKLADSVAKTNAVVKDPSKNKI-----IADAGTSVRNLEQEADRLIDKLKPIKE 2114
Cdd:TIGR04523 552 FElKKENLEKEIDeKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKdlikeIEEKEKKISSLEKELEKAKKENEKLSS 631
|
490 500
....*....|....*....|....*....
gi 117647249 2115 LEDNLKKNISEIKELINQARKQANSIKVS 2143
Cdd:TIGR04523 632 IIKNIKSKKNKLKQEVKQIKETIKEIRNK 660
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1609-2145 |
2.99e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 79.34 E-value: 2.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1609 ENTTQELKHLLSPQRAPERLIQlAEGNVNTLVMETNELLTRATKVTADGEQtgqDAERTNSRAESLEEFIKGLVQDAEAI 1688
Cdd:PRK03918 165 KNLGEVIKEIKRRIERLEKFIK-RTENIEELIKEKEKELEEVLREINEISS---ELPELREELEKLEKEVKELEELKEEI 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1689 NEKAVQLNETLGNQdktaeRNLEELQKEIDRMLKELRSKDLQTQKEVAE-DELvaaEGLLKRVNKLfGEPRAQNEDMEKD 1767
Cdd:PRK03918 241 EELEKELESLEGSK-----RKLEEKIRELEERIEELKKEIEELEEKVKElKEL---KEKAEEYIKL-SEFYEEYLDELRE 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1768 LQQKLAEYKNKLDDAWDLLREATDKTRDANRLSaanqKNMTILETKKEAIEGSKRQIEnTLKEgndILDEANRL------ 1841
Cdd:PRK03918 312 IEKRLSRLEEEINGIEERIKELEEKEERLEELK----KKLKELEKRLEELEERHELYE-EAKA---KKEELERLkkrltg 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1842 --LGEINSVIDYVDDIKTKLPPMSEELSDKIDDLAQEIKDRRLA-EKVFQAESH----AAQLNDssavldgilDEAKNIs 1914
Cdd:PRK03918 384 ltPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAiEELKKAKGKcpvcGRELTE---------EHRKEL- 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1915 fnataafraysnIKDYIDEAEKVAREAKELAQGATKLATSPQGLLKEDAKGS-LQKSFRILNEAKKLANDVKG-NHNDLN 1992
Cdd:PRK03918 454 ------------LEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESeLIKLKELAEQLKELEEKLKKyNLEELE 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1993 DLKTRLETADLRNSGLLG---ALNDTMDKLSAITNdtaaKLQAVKEKAREANDTAKAVLAQ--------VKDLHQNLDGL 2061
Cdd:PRK03918 522 KKAEEYEKLKEKLIKLKGeikSLKKELEKLEELKK----KLAELEKKLDELEEELAELLKEleelgfesVEELEERLKEL 597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2062 KQNYNKLadsvaktnavvkdpsknkiiadagTSVRNLEQEADRLIDKLKPIKELEDNLKKNISEIKELINQARKQANSIK 2141
Cdd:PRK03918 598 EPFYNEY------------------------LELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELE 653
|
....
gi 117647249 2142 VSVS 2145
Cdd:PRK03918 654 KKYS 657
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
913-960 |
5.03e-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: 68.53 E-value: 5.03e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 117647249 913 PCRCNINGSFSEICHTRTGQCECRPNVQGRHCDECKPETFGLQL-GRGC 960
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSqGGGC 49
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1694-2054 |
3.43e-13 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 74.17 E-value: 3.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1694 QLNETLGNQDKTAERNLEELQKEIDRMLKELRskDLQTQKEVAEDELvaaegllkrvnklfgepraqnedmeKDLQQKLA 1773
Cdd:COG4372 17 GLRPKTGILIAALSEQLRKALFELDKLQEELE--QLREELEQAREEL-------------------------EQLEEELE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1774 EYKNKLDDAWDLLREATDKTRDANRLSAANQKNMTILETKKEAIEgskRQIENTLKEGNDILDEANRLLGEINSVIDYVD 1853
Cdd:COG4372 70 QARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQ---EELEELQKERQDLEQQRKQLEAQIAELQSEIA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1854 DIKTKLppmsEELSDKIDDLAQEIKDrrlaekvFQAESHAAQLNDSSAVLDGILDEAKNISFNATAAFRAYSNIKDYIDE 1933
Cdd:COG4372 147 EREEEL----KELEEQLESLQEELAA-------LEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1934 AEKVAREAK---ELAQGATKLATSPQGLLKEDAKGSLQKSFRILNEAKKLANDVKGNHNDLNDLKTRLETADLRNSGLLG 2010
Cdd:COG4372 216 LAEELLEAKdslEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALEL 295
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 117647249 2011 ALNDTMDKLSAITNDTAAKLQAVKEKAREANDTAKAVLAQVKDL 2054
Cdd:COG4372 296 KLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAEL 339
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
914-960 |
5.47e-13 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 65.45 E-value: 5.47e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 117647249 914 CRCNINGSFSEICHTRTGQCECRPNVQGRHCDECKPETFGLQ--LGRGC 960
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPsdPPQGC 49
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1642-2129 |
6.76e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 75.08 E-value: 6.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1642 ETNELLTRATKVTADgeQTGQDAERTNSRAESLEEFIKGLVQD-AEAINEKavqlnETLGNQDKTAERNLEELQKEIDRM 1720
Cdd:PRK02224 226 EEQREQARETRDEAD--EVLEEHEERREELETLEAEIEDLRETiAETERER-----EELAEEVRDLRERLEELEEERDDL 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1721 LKE------------LRSKDLQTQKEVAEDELV-----------AAEGLLKRVNKLfgEPRAQN-----EDMEKDLQ--- 1769
Cdd:PRK02224 299 LAEaglddadaeaveARREELEDRDEELRDRLEecrvaaqahneEAESLREDADDL--EERAEElreeaAELESELEear 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1770 QKLAEYKNKLDDAWDLLREATDKTRDAN-RLSAANQKNMTILETKkEAIEGSKRQIENTLKEGNDILDEANRLLGEIN-- 1846
Cdd:PRK02224 377 EAVEDRREEIEELEEEIEELRERFGDAPvDLGNAEDFLEELREER-DELREREAELEATLRTARERVEEAEALLEAGKcp 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1847 ---------SVIDYVDDIKTKLppmsEELSDKIDDLAQEIKDrrLAEKVFQAEShaaqLNDSSAVLDGILDEAKNISfna 1917
Cdd:PRK02224 456 ecgqpvegsPHVETIEEDRERV----EELEAELEDLEEEVEE--VEERLERAED----LVEAEDRIERLEERREDLE--- 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1918 taafraySNIKDYIDEAEKVAREAKELAQGATKLATSPQGllKEDAKGSLQKsfrilnEAKKLANDVKGNHNDLNDLKTR 1997
Cdd:PRK02224 523 -------ELIAERRETIEEKRERAEELRERAAELEAEAEE--KREAAAEAEE------EAEEAREEVAELNSKLAELKER 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1998 LEtadlrnsgllgALNDTMDKLSAITN--DTAAKLQAVKEKAREANDTAKAVLAQVKDLHQNLDGlkqnynKLadsvakt 2075
Cdd:PRK02224 588 IE-----------SLERIRTLLAAIADaeDEIERLREKREALAELNDERRERLAEKRERKRELEA------EF------- 643
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 117647249 2076 navvkDPSKnkiIADAGTSVRNLEQEADRLIDKLKPIKELEDNLKKNI----SEIKEL 2129
Cdd:PRK02224 644 -----DEAR---IEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIgaveNELEEL 693
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
914-960 |
9.87e-13 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 64.64 E-value: 9.87e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 117647249 914 CRCNINGSFSEICHTRTGQCECRPNVQGRHCDECKPETFGLQlGRGC 960
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG-PPGC 46
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1644-2146 |
1.17e-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: 73.90 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1644 NELLTRATKVTADGEQTGQDAERTNSraesLEEFIKGLVQDAEAINEKAV-------QLNETL---GNQDKTAERNLEEL 1713
Cdd:TIGR04523 47 NELKNKEKELKNLDKNLNKDEEKINN----SNNKIKILEQQIKDLNDKLKknkdkinKLNSDLskiNSEIKNDKEQKNKL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1714 QKEIDRMLKELRSKDlQTQKEVAeDELVAAEGLLKRVNKLFGEPRAQNEDMEKdlqqklaeYKNKLDDAWDLLREATDKT 1793
Cdd:TIGR04523 123 EVELNKLEKQKKENK-KNIDKFL-TEIKKKEKELEKLNNKYNDLKKQKEELEN--------ELNLLEKEKLNIQKNIDKI 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1794 RdaNRLSAANQKnMTILETKKEAIEGSKRQIENtLKEGNDIL-DEANRLLGEINsvidyvdDIKTKLPPMSEELSDKIDD 1872
Cdd:TIGR04523 193 K--NKLLKLELL-LSNLKKKIQKNKSLESQISE-LKKQNNQLkDNIEKKQQEIN-------EKTTEISNTQTQLNQLKDE 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1873 LaQEIKDRrLAEKVFQAESHAAQLNDSSAVLdgildeaknisfnataafraySNIKDYIDEAEKVareaKElaQGATKLa 1952
Cdd:TIGR04523 262 Q-NKIKKQ-LSEKQKELEQNNKKIKELEKQL---------------------NQLKSEISDLNNQ----KE--QDWNKE- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1953 tspqglLKEDAKgSLQKSFRI----LNEAKKLANDVKgnhNDLNDLKTRLETADLRNSGLLGALNDTMDKLSAITNDTAA 2028
Cdd:TIGR04523 312 ------LKSELK-NQEKKLEEiqnqISQNNKIISQLN---EQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQS 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2029 KLQAVKEKAREANDTaKAVLAQVKDLHQNLD----GLKQNYNK-------LADSVAKTNAVVKD-----PSKNKIIADAG 2092
Cdd:TIGR04523 382 YKQEIKNLESQINDL-ESKIQNQEKLNQQKDeqikKLQQEKELlekeierLKETIIKNNSEIKDltnqdSVKELIIKNLD 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2093 TSVRNLEQEADRLIDKLKPIK-ELEDN---------------------------LKKNISEIKELINQARKQANSIKVSV 2144
Cdd:TIGR04523 461 NTRESLETQLKVLSRSINKIKqNLEQKqkelkskekelkklneekkeleekvkdLTKKISSLKEKIEKLESEKKEKESKI 540
|
..
gi 117647249 2145 SS 2146
Cdd:TIGR04523 541 SD 542
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
963-1007 |
3.73e-12 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 63.10 E-value: 3.73e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 117647249 963 CNCNSFGSKSFDCEA-SGQCWCQPGVAGKKCDRCAHGYFNFQEGGC 1007
Cdd:smart00180 1 CDCDPGGSASGTCDPdTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1056-1104 |
1.74e-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: 1.74e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 117647249 1056 CNCSTVGSLASQCNVNTGQCSCHPKFSGMKCSECSRGHWNYPLCTLCDC 1104
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
962-1007 |
4.55e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 60.06 E-value: 4.55e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 117647249 962 PCNCNSFGSKSFDCEA-SGQCWCQPGVAGKKCDRCAHGYFNF--QEGGC 1007
Cdd:cd00055 1 PCDCNGHGSLSGQCDPgTGQCECKPNTTGRRCDRCAPGYYGLpsQGGGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1416-1462 |
4.80e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 60.06 E-value: 4.80e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 117647249 1416 CQCNGHSS---QCDPETSVCQnCQHHTAGDFCERCALGYYGIVRGLPNDC 1462
Cdd:pfam00053 1 CDCNPHGSlsdTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
860-912 |
4.97e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 60.06 E-value: 4.97e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 117647249 860 PCQCNDNldYSIPGSCDSLSGSCLiCKPGTTGRYCELCADGYFGDAVNAKNCQ 912
Cdd:cd00055 1 PCDCNGH--GSLSGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1635-1912 |
6.44e-11 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 66.09 E-value: 6.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1635 NVNTLVMETNELLTRATKVTadgEQTGQDAERTNSRAESLEEF----------IKGLVQDAEAINEKAVQLNETLgnQDK 1704
Cdd:COG1340 2 KTDELSSSLEELEEKIEELR---EEIEELKEKRDELNEELKELaekrdelnaqVKELREEAQELREKRDELNEKV--KEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1705 TAERNleELQKEIDRMLKELRSKDLQTQKEVAEDELVAAegLLKRVNKLfgEPRAQNEDM----EKDLQQKLAEYKNKLD 1780
Cdd:COG1340 77 KEERD--ELNEKLNELREELDELRKELAELNKAGGSIDK--LRKEIERL--EWRQQTEVLspeeEKELVEKIKELEKELE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1781 DAwdllREATDKTRDANRLSAAnqknmtiLETKKEAIEGSKRQIENTLKEGNDILDEANRLLGEINSVIDYVDDIKTKLP 1860
Cdd:COG1340 151 KA----KKALEKNEKLKELRAE-------LKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIV 219
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 117647249 1861 PMSE---ELSDKIDDLAQEIKDRRLAEKVFQAESHAAQLNDSSAVLDGILDEAKN 1912
Cdd:COG1340 220 EAQEkadELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAEEIFE 274
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1102-1159 |
1.09e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 58.90 E-value: 1.09e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 117647249 1102 CDCFLPGTDATTCDLETrkcscsdqtGQCSCKVNVEGVHCDRCRPGKFGLDAKNPLGC 1159
Cdd:pfam00053 1 CDCNPHGSLSDTCDPET---------GQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1415-1463 |
1.51e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 58.52 E-value: 1.51e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 117647249 1415 PCQCNGHSS---QCDPETSVCQnCQHHTAGDFCERCALGYYGIvRGLPNDCQ 1463
Cdd:cd00055 1 PCDCNGHGSlsgQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGL-PSQGGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
963-1010 |
2.41e-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: 2.41e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 117647249 963 CNCNSFGSKSFDCEAS-GQCWCQPGVAGKKCDRCAHGYFNFQEGGCIAC 1010
Cdd:pfam00053 1 CDCNPHGSLSDTCDPEtGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1009-1054 |
2.94e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 57.75 E-value: 2.94e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 117647249 1009 ACDCSHLG---NNCDPKTGQCICPPNTTGEKCSECLPNTWGH-SIVTGCK 1054
Cdd:cd00055 1 PCDCNGHGslsGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLpSQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1056-1098 |
3.51e-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: 3.51e-10
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 117647249 1056 CNCSTVGSLASQCNVNTGQCSCHPKFSGMKCSECSRGHWNYPL 1098
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1010-1048 |
5.56e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.94 E-value: 5.56e-10
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 117647249 1010 CDCS---HLGNNCDPKTGQCICPPNTTGEKCSECLPNTWGHS 1048
Cdd:smart00180 1 CDCDpggSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
752-801 |
8.22e-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: 8.22e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 117647249 752 PCQCFAHA---EACDDITGECLnCKDHTGGPYCNECLPGFYGDPTRgsPEDCQ 801
Cdd:cd00055 1 PCDCNGHGslsGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQ--GGGCQ 50
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1653-2119 |
1.04e-09 |
|
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: 63.94 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1653 VTADGEQTGQDAERTNSRAESLEEFIKGLVQDAEAINEKAVQLnETLGNQDKTAERNLEELQKEIDRMLKELrskdlqTQ 1732
Cdd:pfam05622 5 AQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQL-ESGDDSGTPGGKKYLLLQKQLEQLQEEN------FR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1733 KEVAEDEL-VAAEGLLKRVnklfGEPRAQNEDMekdlqQKLAEYKNKLDDAWDLLREATDKtrdANRLSAAnqknmtiLE 1811
Cdd:pfam05622 78 LETARDDYrIKCEELEKEV----LELQHRNEEL-----TSLAEEAQALKDEMDILRESSDK---VKKLEAT-------VE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1812 TKKEAIEGS---KRQIEnTLKEGN-----------DILDEANRLLGEINSVIDYVDDIKTKLppmSEE------------ 1865
Cdd:pfam05622 139 TYKKKLEDLgdlRRQVK-LLEERNaeymqrtlqleEELKKANALRGQLETYKRQVQELHGKL---SEEskkadklefeyk 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1866 -LSDKIDDLAQEiKDRRLAE----KVFQAESHAAQLNDSSAVLDGILDEAKNISFNATAAFRAYSNIKDYID--EAE-KV 1937
Cdd:pfam05622 215 kLEEKLEALQKE-KERLIIErdtlRETNEELRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIrlQHEnKM 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1938 AREAKElAQGATKLATSpQGLLkEDAKGSLQKsfriLNEAKKLAND-VKGNHNDLNDLKTRLETADLRN--SGLLGA-LN 2013
Cdd:pfam05622 294 LRLGQE-GSYRERLTEL-QQLL-EDANRRKNE----LETQNRLANQrILELQQQVEELQKALQEQGSKAedSSLLKQkLE 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2014 DTMDKLSaitndtaaKLQAVKEKAREA-NDTAKAVLAQvkdLHQNLDGLKQNYNKLADS-----------VAKTNAVVK- 2080
Cdd:pfam05622 367 EHLEKLH--------EAQSELQKKKEQiEELEPKQDSN---LAQKIDELQEALRKKDEDmkameerykkyVEKAKSVIKt 435
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 117647249 2081 -DPSKNKIIADAGTSVRNLEQEADRLID-------KLKPIKELEDNL 2119
Cdd:pfam05622 436 lDPKQNPASPPEIQALKNQLLEKDKKIEhlerdfeKSKLQREQEEKL 482
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
465-511 |
1.07e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 56.21 E-value: 1.07e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 117647249 465 CNCSGLGSTNE--DPCVGPCSCKENVEGEDCSRCKSGFFNLQEDNQKGC 511
Cdd:pfam00053 1 CDCNPHGSLSDtcDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1010-1053 |
1.23e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 56.21 E-value: 1.23e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 117647249 1010 CDCSHLG---NNCDPKTGQCICPPNTTGEKCSECLPNTWGHSIVTGC 1053
Cdd:pfam00053 1 CDCNPHGslsDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQ 47
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
410-467 |
1.26e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 55.82 E-value: 1.26e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 117647249 410 CHCDPTGSLSEVCVKDekyaqrglkPGSCHCKTGFGGVNCDRCVRGYHGYPDCQPCNC 467
Cdd:pfam00053 1 CDCNPHGSLSDTCDPE---------TGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
753-800 |
2.33e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 55.05 E-value: 2.33e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 117647249 753 CQCFAHA---EACDDITGECLnCKDHTGGPYCNECLPGFYGDPTrGSPEDC 800
Cdd:pfam00053 1 CDCNPHGslsDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPS-DPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1102-1159 |
2.99e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 55.01 E-value: 2.99e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 117647249 1102 CDCFLPGTDATTCDLETrkcscsdqtGQCSCKVNVEGVHCDRCRPGKFGldaKNPLGC 1159
Cdd:smart00180 1 CDCDPGGSASGTCDPDT---------GQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1523-1566 |
3.36e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 54.62 E-value: 3.36e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 117647249 1523 CECDPYGSLPVPCDRVTGLCTCRPGATGRKCDGCEHWHAREGAE 1566
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPP 44
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1523-1560 |
3.43e-09 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 54.67 E-value: 3.43e-09
10 20 30
....*....|....*....|....*....|....*...
gi 117647249 1523 CECDPYGSLPVPCDRVTGLCTCRPGATGRKCDGCEHWH 1560
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGY 39
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1056-1097 |
3.64e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 54.62 E-value: 3.64e-09
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 117647249 1056 CNCSTVGSLASQCNVNTGQCSCHPKFSGMKCSECSRGHWNYP 1097
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1523-1558 |
6.02e-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: 6.02e-09
10 20 30
....*....|....*....|....*....|....*.
gi 117647249 1523 CECDPYGSLPVPCDRVTGLCTCRPGATGRKCDGCEH 1558
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKP 36
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1102-1159 |
6.29e-09 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 53.90 E-value: 6.29e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 117647249 1102 CDCFLPGTDATTCDLETrkcscsdqtGQCSCKVNVEGVHCDRCRPGKFGlDAKNPLGC 1159
Cdd:cd00055 2 CDCNGHGSLSGQCDPGT---------GQCECKPNTTGRRCDRCAPGYYG-LPSQGGGC 49
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1853-2142 |
6.33e-09 |
|
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: 60.46 E-value: 6.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1853 DDIKTKLPpmseELSDKIDDLAQEIKDRRLAEKVFQaeSHAAQLNDSsaVLDGILDEAKNISFNATAA----FRAYSNIK 1928
Cdd:cd22656 26 EEYRKRLG----ISSDIDDKLSSDFDPLLDAYKSIK--DHCTDFKDD--TYPSIVSLAGDIYNYAQNAggtiDSYYAEIL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1929 DYIDEA-----EKVAREAKELAQGATKLatspqglLKEDAKgslqksfRILNEAKKLANDVKGNHNDLNDLKTRLETADL 2003
Cdd:cd22656 98 ELIDDLadatdDEELEEAKKTIKALLDD-------LLKEAK-------KYQDKAAKVVDKLTDFENQTEKDQTALETLEK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2004 RNSGLLGalndtmDKLSAITNDTAAKLQAVKEKAREandtakavlAQVKDLHQNLDGLKQNYNKLADSVAKTNAVVKDps 2083
Cdd:cd22656 164 ALKDLLT------DEGGAIARKEIKDLQKELEKLNE---------EYAAKLKAKIDELKALIADDEAKLAAALRLIAD-- 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 117647249 2084 knkiIADAGTSVRNLEQEADRLIDKLKPIKELEDNLKKNISEIKELINQARKQANSIKV 2142
Cdd:cd22656 227 ----LTAADTDLDNLLALIGPAIPALEKLQGAWQAIATDLDSLKDLLEDDISKIPAAIL 281
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
861-904 |
7.36e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 53.85 E-value: 7.36e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 117647249 861 CQCNdnLDYSIPGSCDSLSGSCLiCKPGTTGRYCELCADGYFGD 904
Cdd:smart00180 1 CDCD--PGGSASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD 41
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
409-461 |
2.76e-08 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 52.36 E-value: 2.76e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 117647249 409 PCHCDPTGSLSEVCVKDEkyaqrglkpGSCHCKTGFGGVNCDRCVRGYHGYPD 461
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. |
861-907 |
3.95e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 51.59 E-value: 3.95e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 117647249 861 CQCNDNLDYSipGSCDSLSGSCLiCKPGTTGRYCELCADGYFGDAVN 907
Cdd:pfam00053 1 CDCNPHGSLS--DTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSD 44
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1416-1462 |
6.47e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 51.16 E-value: 6.47e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 117647249 1416 CQCN--GH-SSQCDPETSVCQnCQHHTAGDFCERCALGYYGIVrglPNDC 1462
Cdd:smart00180 1 CDCDpgGSaSGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDG---PPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
410-462 |
2.24e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 49.62 E-value: 2.24e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 117647249 410 CHCDPTGSLSEVCVKDEkyaqrglkpGSCHCKTGFGGVNCDRCVRGYHG--YPDC 462
Cdd:smart00180 1 CDCDPGGSASGTCDPDT---------GQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
464-512 |
2.84e-07 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 49.27 E-value: 2.84e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 117647249 464 PCNCSGLGSTNE--DPCVGPCSCKENVEGEDCSRCKSGFFNLQEDNQkGCE 512
Cdd:cd00055 1 PCDCNGHGSLSGqcDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGG-GCQ 50
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1682-1881 |
3.36e-07 |
|
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: 53.60 E-value: 3.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1682 VQDAEA-INEKAVQLNETLGNQDktaERNLEELQKEIDRMLKEL-----RSKDLQTQ-KEVAEDELVAAEGLLKRVNKLf 1754
Cdd:cd00176 9 ADELEAwLSEKEELLSSTDYGDD---LESVEALLKKHEALEAELaaheeRVEALNELgEQLIEEGHPDAEEIQERLEEL- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1755 gepraqnEDMEKDLQQKLAEYKNKLDDAWDLLRE----------ATDKTRDANRLSAAnqKNMTILETKKEAIEGSKRQI 1824
Cdd:cd00176 85 -------NQRWEELRELAEERRQRLEEALDLQQFfrdaddleqwLEEKEAALASEDLG--KDLESVEELLKKHKELEEEL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 117647249 1825 ENTLKEGNDILDEANRLLGEINSviDYVDDIKTKLppmsEELSDKIDDLAQEIKDRR 1881
Cdd:cd00176 156 EAHEPRLKSLNELAEELLEEGHP--DADEEIEEKL----EELNERWEELLELAEERQ 206
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1929-2142 |
3.79e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 55.29 E-value: 3.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1929 DYIDEAEKVAREAKELAQGATKLATSpqgLLKEDAKGSLQKSFRILNEAKKLANDVKGNHNDLNDLKTRLETAD---LRN 2005
Cdd:COG4372 2 DRLGEKVGKARLSLFGLRPKTGILIA---ALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARselEQL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2006 SGLLGALNDTMDKLSAITNDTAAKLQAVKEKAREANDTAKAVLAQVKDLHQNLDGLKQNYNKLADSVAktnavvkdpSKN 2085
Cdd:COG4372 79 EEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIA---------ERE 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 117647249 2086 KIIADAGTSVRNLEQEADRLIDKLKPIKElednlKKNISEIKELINQARKQANSIKV 2142
Cdd:COG4372 150 EELKELEEQLESLQEELAALEQELQALSE-----AEAEQALDELLKEANRNAEKEEE 201
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
753-795 |
4.16e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 48.85 E-value: 4.16e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 117647249 753 CQCF---AHAEACDDITGECLnCKDHTGGPYCNECLPGFYGDPTRG 795
Cdd:smart00180 1 CDCDpggSASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1613-1980 |
5.70e-07 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 55.60 E-value: 5.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1613 QELKHLLSPQRaperliQLAEGNVNTLVMETNELLTRatkvtadgeqTGQDAER--TNSRAESlEEFIKGLVQDAEAINE 1690
Cdd:NF041483 130 QQLDQELAERR------QTVESHVNENVAWAEQLRAR----------TESQARRllDESRAEA-EQALAAARAEAERLAE 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1691 KAVQlneTLGNQDKTAERNLEEL----QKEIDRMLKELrskdlQTQKEVAEDElvaAEGLLKRVNKLFGEPRAQNEDMEK 1766
Cdd:NF041483 193 EARQ---RLGSEAESARAEAEAIlrraRKDAERLLNAA-----STQAQEATDH---AEQLRSSTAAESDQARRQAAELSR 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1767 DLQQKLAEYKNKLD----DAWDLLREAtdKTRDANRLSAANQKNMTILETKKEAIegsKRQIENTLKEGNDILDEANRLL 1842
Cdd:NF041483 262 AAEQRMQEAEEALRearaEAEKVVAEA--KEAAAKQLASAESANEQRTRTAKEEI---ARLVGEATKEAEALKAEAEQAL 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1843 GeinsvidyvdDIKTKLPPMSEELSDKIDDLAqeikdrrlaekvfqAESHAAQLNDSSAVLDGILDEAkniSFNATAAFR 1922
Cdd:NF041483 337 A----------DARAEAEKLVAEAAEKARTVA--------------AEDTAAQLAKAARTAEEVLTKA---SEDAKATTR 389
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 117647249 1923 AYSnikdyiDEAEKVAREAK----ELAQGATKLATSPQGLLKEDAKGSLQKSFRILNEAKKL 1980
Cdd:NF041483 390 AAA------EEAERIRREAEaeadRLRGEAADQAEQLKGAAKDDTKEYRAKTVELQEEARRL 445
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
802-859 |
2.19e-06 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 46.96 E-value: 2.19e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 117647249 802 PCACPLNIpsnNFSPTCHLDrslGLICdECPIGYTGPRCERCAEGYFGQPSIPGGsCQ 859
Cdd:cd00055 1 PCDCNGHG---SLSGQCDPG---TGQC-ECKPNTTGRRCDRCAPGYYGLPSQGGG-CQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
283-330 |
2.41e-06 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 46.58 E-value: 2.41e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 117647249 283 CICYGHA---RACplDPATnkSRCECEHNTCGESCDRCCPGFHQKPWRAGT 330
Cdd:cd00055 2 CDCNGHGslsGQC--DPGT--GQCECKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
803-858 |
4.63e-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: 4.63e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 117647249 803 CACPLNIPSnnfSPTCHldrSLGLICDeCPIGYTGPRCERCAEGYFGQPSIPGGSC 858
Cdd:pfam00053 1 CDCNPHGSL---SDTCD---PETGQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| alph_xenorhab_A |
NF033928 |
alpha-xenorhabdolysin family binary toxin subunit A; Alpha-xenorhabdolysin was the founding ... |
1664-1944 |
5.07e-06 |
|
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: 51.53 E-value: 5.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1664 AERTNSRAESLEEFIKGLvQDAEAINEKAVQLNE----TLGNQDKTAERN----LEELQKEIDRMLKELR--SKDLQT-Q 1732
Cdd:NF033928 79 ARNIVVTGNPIIDLINEM-PIIKRGDLTEEELSElppiPLSSDDKEIVKElkeiLEDLKNDIKDYQQKADdvKKELDDfE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1733 KEVAEDELVAAEGLLKRVNKLFGEP-----RAQNEDMEKDLQQKLAEYKNKLDDAWdllreatdktrdanrlSAANQKN- 1806
Cdd:NF033928 158 NDLREELLPQLKLKKKLYDDNLGSDsieelREKIDQLEKEIEQLNKEYDDYVKLSF----------------TGLAGGPi 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1807 -----MTILETKKEAIEGSKRQIENTLKEGNDILDEANRLLGEINSVIDYVDDIKTKlppMSEELS--DKIDDLAQEIkd 1879
Cdd:NF033928 222 glaitGGIFGSKAEKIRKEKNALIQEIDELQEQLKKKNALLGSLERLQTSLDDILTR---MEDALPalKKLKGVWQSL-- 296
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 117647249 1880 rrlaekvfqaeshAAQLNDSSAVLDGILDEAKNISFNAtaafraysNIKDYIDEAEKVAREAKEL 1944
Cdd:NF033928 297 -------------LTDIDSSINALKEIDDADSLRLFKL--------EFEQVIAPWKEIQDYAKQL 340
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
803-851 |
8.45e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 44.99 E-value: 8.45e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 117647249 803 CACPlniPSNNFSPTCHLDrslGLICdECPIGYTGPRCERCAEGYFGQP 851
Cdd:smart00180 1 CDCD---PGGSASGTCDPD---TGQC-ECKPNVTGRRCDRCAPGYYGDG 42
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
465-511 |
1.03e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 44.99 E-value: 1.03e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 117647249 465 CNCSGLGSTNE--DPCVGPCSCKENVEGEDCSRCKSGFFNlqeDNQKGC 511
Cdd:smart00180 1 CDCDPGGSASGtcDPDTGQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1465-1520 |
1.49e-05 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 44.65 E-value: 1.49e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 117647249 1465 CACPLISPSnnfSPSCVLEGledYRCTaCPRGYEGQYCERCAPGYTGSPSSPGGSC 1520
Cdd:pfam00053 1 CDCNPHGSL---SDTCDPET---GQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
1822-2062 |
2.17e-05 |
|
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo reversible methylation in response to attractants or repellants during bacterial chemotaxis.
Pssm-ID: 214599 [Multi-domain] Cd Length: 262 Bit Score: 48.82 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1822 RQIENTLKEGNDILDEANRLLGEINSVIDYVDDIKTKLPPMSE------ELSDKIDDLAQEIKDR--RLAEKVFQAESHA 1893
Cdd:smart00283 4 EAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAAtaqsaaEAAEEGREAVEDAITAmdQIREVVEEAVSAV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1894 AQLNDSSAVLDGILDEAKNISF-------NAT--AAfRAysnikdyiDEAEK----VAREAKELAQGATKLATSPQGLLK 1960
Cdd:smart00283 84 EELEESSDEIGEIVSVIDDIADqtnllalNAAieAA-RA--------GEAGRgfavVADEVRKLAERSAESAKEIESLIK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1961 E------DAKGSLQKSFRILNEAKKLANDVKGNHNDLNDL---------KTRLETADLRNSglLGALNDTMDKLSAITND 2025
Cdd:smart00283 155 EiqeetnEAVAAMEESSSEVEEGVELVEETGDALEEIVDSveeiadlvqEIAAATDEQAAG--SEEVNAAIDEIAQVTQE 232
|
250 260 270
....*....|....*....|....*....|....*..
gi 117647249 2026 TAAKLQavkekarEANDTAKAVLAQVKDLHQNLDGLK 2062
Cdd:smart00283 233 TAAMSE-------EISAAAEELSGLAEELDELVERFK 262
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1464-1521 |
2.41e-04 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 41.19 E-value: 2.41e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 117647249 1464 PCACPLISpsnNFSPSCVLEGLedyRCTaCPRGYEGQYCERCAPGYTGSPSSPGGsCQ 1521
Cdd:cd00055 1 PCDCNGHG---SLSGQCDPGTG---QCE-CKPNTTGRRCDRCAPGYYGLPSQGGG-CQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1375-1403 |
2.88e-04 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 40.80 E-value: 2.88e-04
10 20
....*....|....*....|....*....
gi 117647249 1375 RCDCPPGYSGLSCETCAPGFYRLRSEPGG 1403
Cdd:cd00055 20 QCECKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1465-1513 |
3.30e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 40.76 E-value: 3.30e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 117647249 1465 CACPlisPSNNFSPSCVLEGLedyRCTaCPRGYEGQYCERCAPGYTGSP 1513
Cdd:smart00180 1 CDCD---PGGSASGTCDPDTG---QCE-CKPNVTGRRCDRCAPGYYGDG 42
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
302-326 |
3.61e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 40.37 E-value: 3.61e-04
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1375-1403 |
3.93e-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: 40.41 E-value: 3.93e-04
10 20
....*....|....*....|....*....
gi 117647249 1375 RCDCPPGYSGLSCETCAPGFYRLRSEPGG 1403
Cdd:pfam00053 19 QCLCKPGVTGRHCDRCKPGYYGLPSDPPQ 47
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1375-1396 |
5.00e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 37.29 E-value: 5.00e-03
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
1972-2099 |
5.09e-03 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 42.02 E-value: 5.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1972 RILNEAKKLANDVKGNHNDLNDLKTRLETADLRNSGLLGALNDTMDKLSAITNDTAAKLQAVKekareandTAKAVLAQV 2051
Cdd:TIGR04320 237 YIADGNKFDKTPIPNPPNSLAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALA--------TAQKELANA 308
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 117647249 2052 KDlhQNLDGLKQNYNKLADSVAKTNAVVKDPSKNK--IIADAGTSVRNLE 2099
Cdd:TIGR04320 309 QA--QALQTAQNNLATAQAALANAEARLAKAKEALanLNADLAKKQAALD 356
|
|
| ClyA-like |
cd21116 |
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ... |
1983-2143 |
8.55e-03 |
|
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including Bacillus cereus HblB, Aeromonas hydrophila AhlB, Bacillus thuringiensis Cry6Aa and similar proteins; This family belongs to the ClyA family of alpha-PFT bacterial toxins. PFTs form the major group of virulence factors in many pathogenic bacteria and in general are critical components of the molecular offensive and defensive machinery of cells in all kingdoms of life. Bacterial PFTs facilitate the takeover of host resources by puncturing holes in the membrane. PFTs can be classified as alpha-PFTs and beta-PFTs depending on the secondary structures of their membrane component. Alpha-PFTs use a ring of amphipathic helices while beta-PFTs use a beta-barrel to construct the pore. Members of this family include the toxins: Bacillus cereus hemolysin binding component B (HblB or HBL-B) of the diarrheal enterotoxin hemolysin BL, Aeromonas hydrophila hemolytic (Ahl) component B (AhlB) of the tripartite AhlABC toxin, Vibrio cholerae cytotoxin motility associated killing factor A (MakA) cytotoxin, Xenorhabdus nematophila alpha-xenorhabdolysin (XaxA), Bacillus thuringiensis crystal 6Aa (Cry6Aa) parasporal crystal (Cry) toxin, and Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA) of the non-hemolytic enterotoxin Nhe, which, despite its name, is hemolytic, among others. In solution, ClyA proteins have an elongated, almost entirely alpha-helical structure, except for a short hydrophobic beta-hairpin known as the beta-tongue. Pore formation by ClyA requires circular oligomerization of the toxin by a sequential mechanism. This, in turn, concentrates the amphipathic helices in the center of the ring-like structure, forming a helical barrel that inserts into the membrane by a wedge-like mechanism. Compared with ClyA, NheA is almost entirely alpha-helical with an enlarged "head" domain, and an enlarged beta-tongue; it has been proposed that NheA could even form beta-barrel pores. Alpha-PFTs with similar structures are increasingly being found in eukaryotes, in particular as components of the immune systems of animals. This family may be distantly related to Escherichia coli alpha-PFT hemolysin E (HlyE, also known as ClyA or SheA).
Pssm-ID: 439149 [Multi-domain] Cd Length: 224 Bit Score: 40.47 E-value: 8.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1983 DVKGNHND-LNDLKTRLE---TADLRNSGLLGALNDTMDKL--SAITNDTAAK------LQAVKEKAREANDTAKAVLAQ 2050
Cdd:cd21116 41 LARAHALEwLNEIKPKLLslpNDIIGYNNTFQSYYPDLIELadNLIKGDQGAKqqllqgLEALQSQVTKKQTSVTSFINE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2051 VKDLHQNLDGLKQNYNKLADSVAKTNAVVKDPSKNkiiadagtsVRNLEQEADRLIDKLKPIKELEDNLKKNISEIKELI 2130
Cdd:cd21116 121 LTTFKNDLDDDSRNLQTDATKAQAQVAVLNALKNQ---------LNSLAEQIDAAIDALEKLSNDWQTLDSDIKELITDL 191
|
170
....*....|...
gi 117647249 2131 NQARKQANSIKVS 2143
Cdd:cd21116 192 EDAESSIDAAFLQ 204
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1589-1848 |
1.40e-105 |
|
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: 338.62 E-value: 1.40e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1589 TMNIN-LTGPLPAPYKILYGLENTTQELKHLLSPQRAPERLIQLAEGNVNTLVMETNELLTRATKVTADGEQTGQDAERT 1667
Cdd:pfam06008 1 LLSLNsLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1668 NSRAESLEEFIKGLVQDAEAINEKAVQLNEtlgNQDKTAERNLEELQKEIDRMLKELRSKDLQTQKEVAEDELVAAEGLL 1747
Cdd:pfam06008 81 LGHAKELAEAIKNLIDNIKEINEKVATLGE---NDFALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQDLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1748 KRVNKLFGEPRAQNEDMEKDLQQKLAEYKNKLDDAWDLLREATDKTRDANRLSAANQKNMTILETKKEAIEGSKRQIENT 1827
Cdd:pfam06008 158 SRIQTWFQSPQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEET 237
|
250 260
....*....|....*....|.
gi 117647249 1828 LKEGNDILDEANRLLGEINSV 1848
Cdd:pfam06008 238 LKTARDSLDAANLLLQEIDDA 258
|
|
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
29-281 |
5.71e-93 |
|
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related protein such as Unc-6/ netrins.
Pssm-ID: 214532 Cd Length: 238 Bit Score: 301.59 E-value: 5.71e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 29 AHQQRGLFPAVLNLASNALITTNATCGEKGPEMYCKLVEHVpgqpVRNPQCRICNQNssNPYQRHPITNAIDGKN----T 104
Cdd:smart00136 1 AGRPRSCYPPFVNLAFGREVTATSTCGEPGPERYCKLVGHT----EQGKKCDYCDAR--NPRRSHPAENLTDGNNpnnpT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 105 WWQSPSIKNGVeyHYVTITLDLQQVFQIAYVIVKAAnSPRPGNWILERSLDDVEYKPWQYHAvtdTECLTLYNIyPRTGP 184
Cdd:smart00136 75 WWQSEPLSNGP--QNVNLTLDLGKEFHVTYVILKFC-SPRPSLWILERSDFGKTWQPWQYFS---SDCRRTFGR-PPRGP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 185 PSYAKDDEVICTSFYSKIHPLENGEIHISLINGRPSADDP--SPELLEFTSARYIRLRFQRIRTLNADLMMfahkdpreI 262
Cdd:smart00136 148 ITKGNEDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDFdnSPVLQEWVTATNIRVRLTRLRTLGDELMD--------D 219
|
250
....*....|....*....
gi 117647249 263 DPIVTRRYYYSVKDISVGG 281
Cdd:smart00136 220 RPEVTRRYYYAISDIAVGG 238
|
|
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
35-281 |
6.13e-88 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 286.79 E-value: 6.13e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 35 LFPAVLNLASNALITTNATCGEKGPEMYCKLVEHVPGQpvrnpQCRICNqnSSNPYQRHPITNAIDGKN----TWWQSPS 110
Cdd:pfam00055 1 CYPAFGNLAFGREVSATSTCGLNGPERYCILSGLEGGK-----KCFICD--SRDPHNSHPPSNLTDSNNgtneTWWQSET 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 111 IKngVEYHYVTITLDLQQVFQIAYVIVKAAnSPRPGNWILERSLD-DVEYKPWQYHAvtdTECLTLYNIypRTGPPSYAK 189
Cdd:pfam00055 74 GV--IQYENVNLTLDLGKEFHFTYLILKFK-SPRPAAMVLERSTDfGKTWQPYQYFA---SDCRRTFGR--PSGPSRGIK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 190 DDEVICTSFYSKIHPLENGEIHISLINGRPSA--DDPSPELLEFTSARYIRLRFQRIRTLNadlmmfahkDPREIDPIVT 267
Cdd:pfam00055 146 DDEVICTSEYSDISPLTGGEVIFSTLEGRPSAniFDYSPELQDWLTATNIRIRLLRLHTLG---------DELLDDPSVL 216
|
250
....*....|....
gi 117647249 268 RRYYYSVKDISVGG 281
Cdd:pfam00055 217 RKYYYAISDISVGG 230
|
|
| Laminin_II |
pfam06009 |
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 ... |
2033-2168 |
2.95e-54 |
|
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: 186.54 E-value: 2.95e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2033 VKEKAREANDTAKAVLAQVKDLHQNLDGLKQNYNKLADSVAKTNAVVKDpsKNKIIADAGTSVRNLEQEADRLIDKLKPI 2112
Cdd:pfam06009 1 SKELAREANETAKEVLEQLAPLSQNLENTSEKLSGINRSLEETNELVND--ANKALDDAGRSVKKLEELAPDLLDKLKPL 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 117647249 2113 KELEDN---LKKNISEIKELINQARKQANSIKVSVSSGGDCVRTYRPEIKKGSYNNIVV 2168
Cdd:pfam06009 79 KQLEVNsssLSDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTS 137
|
|
| LamB |
smart00281 |
Laminin B domain; |
1225-1360 |
5.37e-47 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 165.51 E-value: 5.37e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1225 HLEPFYWKLPQQFEGKKLMAYGGKLKYAIYFEARDEtGFATYKPQVIIRGGtptHARIITRHMAAPLIGQLTRHEIEMTE 1304
Cdd:smart00281 1 DNEPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRRG-GTHVSAPDVILEGN---GLRISHPAEGPPLPDELTTVEVRFRE 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 117647249 1305 KEWKYYGddpriSRTVTREDFLDILYDIHYILIKATYGNVVRQSRISEISMEVAEP 1360
Cdd:smart00281 77 ENWQYYG-----GRPVTREDLMMVLANLTAILIRATYSQQMAGSRLSDVSLEVAVP 127
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2789-2917 |
2.21e-45 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 160.95 E-value: 2.21e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2789 VRTEAESGLLFYMARINHADFATVQLRNGFPYFSYDLGSGDTSTMIPTKINDGQWHKIKIVRVKQEGILYVDD-ASSQTI 2867
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGeARPTGE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 117647249 2868 SPKKADI-LDVVGILYVGGLPINYTTRRIGPVTYSLDGCVRNLHMEQAPVD 2917
Cdd:pfam00054 81 SPLGATTdLDVDGPLYVGGLPSLGVKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
1230-1374 |
1.18e-44 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 158.97 E-value: 1.18e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1230 YWKLPQQFEGKKLMAYGGKLKYAIYFEARDETGFATYKPQVIIRGGtptHARIITRHMA--APLIGQLTRHEIEMTEKEW 1307
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGGGSLNSEPDVILEGN---GLRLSYSSPDqpPPDPGQEQTYSVRLHEENW 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 117647249 1308 KYygddpRISRTVTREDFLDILYDIHYILIKATYGNVVRQSRISEISMEVAEPGhvlAGSPPAHLIE 1374
Cdd:pfam00052 78 RD-----SDGAPVSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSAVPG---GSGPPASWVE 136
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
579-718 |
3.54e-39 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 143.56 E-value: 3.54e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 579 YWSAPPPYLGNRLPAVGGQLSFTISYDLEEEEDDTekILQLMIIFEGNDLRISTAYKE-VYLEPSEEHIEEVSLKEEAFT 657
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGGGSL--NSEPDVILEGNGLRLSYSSPDqPPPDPGQEQTYSVRLHEENWR 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 117647249 658 iHGTNLPVTRKDFMIVLTNLERVLMQITYNLGMDAIfRLSSVNLESAVPYPTDRRiATDVE 718
Cdd:pfam00052 79 -DSDGAPVSREDFMMVLANLTAILIRATYSTGSGQV-SLSNVSLDSAVPGGSGPP-ASWVE 136
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2364-2503 |
4.19e-39 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 142.84 E-value: 4.19e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2364 FRTFSSSALLMYLATRDLKDFMSVELSDGHVKVSYDLGSGMTSVVSNQNHNDGKWKAFTLSRIQKQANISIVDIdsnqEE 2443
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGE----AR 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2444 NVATSSSGNNFglDLKADDKIYFGGLPtlrNLSMKARPEVNVKKYSGCLKDIEISRTPYN 2503
Cdd:pfam00054 77 PTGESPLGATT--DLDVDGPLYVGGLP---SLGVKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2762-2911 |
2.58e-37 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 138.71 E-value: 2.58e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2762 FGLSRNSHIAIAFDDTKvKNRLTIELEVRTEAESGLLFYMARINHADFATVQLRNGFPYFSYDLGSGDTSTMIPTKINDG 2841
Cdd:cd00110 2 VSFSGSSYVRLPTLPAP-RTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 117647249 2842 QWHKIKIVRVKQEGILYVDDASS-QTISPKKADILDVVGILYVGGLPINYTTRRIgPVTYSLDGCVRNLHM 2911
Cdd:cd00110 81 QWHSVSVERNGRSVTLSVDGERVvESGSPGGSALLNLDGPLYLGGLPEDLKSPGL-PVSPGFVGCIRDLKV 150
|
|
| LamG |
smart00282 |
Laminin G domain; |
2784-2911 |
1.67e-36 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 135.54 E-value: 1.67e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2784 TIELEVRTEAESGLLFYMARINHADFATVQLRNGFPYFSYDLGSGDTSTMI-PTKINDGQWHKIKIVRVKQEGILYVDDA 2862
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSdPTPLNDGQWHRVAVERNGRSVTLSVDGG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 117647249 2863 SSQTI-SPKKADILDVVGILYVGGLPINYtTRRIGPVTYSLDGCVRNLHM 2911
Cdd:smart00282 81 NRVSGeSPGGLTILNLDGPLYLGGLPEDL-KLPPLPVTPGFRGCIRNLKV 129
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2170-2310 |
4.64e-34 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 128.59 E-value: 4.64e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2170 VKTAVADNLLFYLGSAKFIDFLAIEMRKGKVSFLWDVGSGVGRVEYPDlTIDDSYWYRIEASRTGRNGSISVRALDGPKA 2249
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGD-KLNDGKWHSVELERNGRSGTLSVDGEARPTG 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 117647249 2250 SmvpstyhsvSPPGYTIlDVDANAMLFVGGLTGKI-KKADAVRVITFTGCMGETYFDNKPIG 2310
Cdd:pfam00054 80 E---------SPLGATT-DLDVDGPLYVGGLPSLGvKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| LamB |
smart00281 |
Laminin B domain; |
578-706 |
2.82e-33 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 126.22 E-value: 2.82e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 578 YYWSAPPPYLGNRLPAVGGQLSFTISYdleEEEDDTEKILQLMIIFEGNDLRISTAYkEVYLEPSEEHIEEVSLKEEAFT 657
Cdd:smart00281 5 VYWVAPEQFLGDKVTSYGGKLRYTLSF---DGRRGGTHVSAPDVILEGNGLRISHPA-EGPPLPDELTTVEVRFREENWQ 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 117647249 658 IHGTNlPVTRKDFMIVLTNLERVLMQITYNLGMDAIfRLSSVNLESAVP 706
Cdd:smart00281 81 YYGGR-PVTREDLMMVLANLTAILIRATYSQQMAGS-RLSDVSLEVAVP 127
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2937-3089 |
3.87e-33 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 126.76 E-value: 3.87e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2937 GTYFDGTGFAKAVGGFKVGLDLLVEFEFRTTRPTGVLLGVSSQ-KMDGMGIEMIDEKLMFHVDNGAGRFTAIYdagiPGH 3015
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQnGGDFLALELEDGRLVLRYDLGSGSLVLSS----KTP 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 117647249 3016 MCNGQWHKVTAKKIKNRLELVVDGNQVDAQSPNSASTSADTNDPVFVGGFPGGLNQFGLTTNIRFRGCIRSLKL 3089
Cdd:cd00110 77 LNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKV 150
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2336-2497 |
2.28e-32 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 124.45 E-value: 2.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2336 TIQFDGEGYALVSRPIRWYPNiSTVMFKFRTFSSSALLMYLATRDLKDFMSVELSDGHVKVSYDLGSGMTSVVSNQNHND 2415
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRTR-LSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLND 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2416 GKWKAFTLSRIQKQANISIvdidsNQEENVATSSSGNNFGLDLkaDDKIYFGGLPTlrnlSMKARPEVNVKKYSGCLKDI 2495
Cdd:cd00110 80 GQWHSVSVERNGRSVTLSV-----DGERVVESGSPGGSALLNL--DGPLYLGGLPE----DLKSPGLPVSPGFVGCIRDL 148
|
..
gi 117647249 2496 EI 2497
Cdd:cd00110 149 KV 150
|
|
| LamG |
smart00282 |
Laminin G domain; |
2359-2499 |
1.38e-30 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 118.60 E-value: 1.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2359 TVMFKFRTFSSSALLMYLATRDLKDFMSVELSDGHVKVSYDLGSGMTSVVSNQNH-NDGKWKAFTLSRIQKQANISIvdi 2437
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPlNDGQWHRVAVERNGRSVTLSV--- 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 117647249 2438 dsNQEENVATSSSGNNFGLDLkaDDKIYFGGLPTlrnlSMKARPEVNVKKYSGCLKDIEISR 2499
Cdd:smart00282 78 --DGGNRVSGESPGGLTILNL--DGPLYLGGLPE----DLKLPPLPVTPGFRGCIRNLKVNG 131
|
|
| LamG |
smart00282 |
Laminin G domain; |
2960-3089 |
2.96e-30 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 117.83 E-value: 2.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2960 VEFEFRTTRPTGVLLGVSS-QKMDGMGIEMIDEKLMFHVDNGAGRFTAIYDagiPGHMCNGQWHKVTAKKIKNRLELVVD 3038
Cdd:smart00282 2 ISFSFRTTSPNGLLLYAGSkGGGDYLALELRDGRLVLRYDLGSGPARLTSD---PTPLNDGQWHRVAVERNGRSVTLSVD 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 117647249 3039 G-NQVDAQSPnSASTSADTNDPVFVGGFPGGLNQFGLTTNIRFRGCIRSLKL 3089
Cdd:smart00282 79 GgNRVSGESP-GGLTILNLDGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKV 129
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2524-2686 |
1.26e-27 |
|
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: 110.97 E-value: 1.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2524 TVSFPKPGFVELAAVSID-VGTEINLSFSTRNESGIILLGSGGTLTPprrkrrqttqaYYAIFLNKGRLEVHLSSGTRTm 2602
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPrTRLSISFSFRTTSPNGLLLYAGSQNGGD-----------FLALELEDGRLVLRYDLGSGS- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2603 rkIVIKPePNLFHDGREHSVHVERTRGIFTVQIDEDR--RHMQNLTEEQPIEVKKLFVGGAPPEFQPSPLRNIPAFQGCV 2680
Cdd:cd00110 69 --LVLSS-KTPLNDGQWHSVSVERNGRSVTLSVDGERvvESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCI 145
|
....*.
gi 117647249 2681 WNLVIN 2686
Cdd:cd00110 146 RDLKVN 151
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2789-2911 |
1.40e-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: 109.82 E-value: 1.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2789 VRTEAESGLLFYMARINHaDFATVQLRNGFPYFSYDLGSGDTSTM-IPTKINDGQWHKIKIVRVKQEGILYVDDASSQTI 2867
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGS-DFLALELVNGRLVLRYDLGSGPESLLsSGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSS 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 117647249 2868 S-PKKADILDVVGILYVGGLPINYTTRRIgPVTYSLDGCVRNLHM 2911
Cdd:pfam02210 80 LpPGESLLLNLNGPLYLGGLPPLLLLPAL-PVRAGFVGCIRDVRV 123
|
|
| LamG |
smart00282 |
Laminin G domain; |
2165-2307 |
5.70e-27 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 108.20 E-value: 5.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2165 NIVVHVKTAVADNLLFYLGSAKFIDFLAIEMRKGKVSFLWDVGSGVGRVEYPDLTIDDSYWYRIEASRTGRNGSISVral 2244
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLNDGQWHRVAVERNGRSVTLSV--- 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 117647249 2245 DGPKASMVpstyhsVSPPGYTILDVDANamLFVGGLTGKIKKADAVRVITFTGCMGETYFDNK 2307
Cdd:smart00282 78 DGGNRVSG------ESPGGLTILNLDGP--LYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2146-2305 |
2.85e-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: 2.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2146 SGGDCVRtYRPEIKKGSYNNIVVHVKTAVADNLLFYLGSAKFIDFLAIEMRKGKVSFLWDVGSGVGRVEYPDlTIDDSYW 2225
Cdd:cd00110 5 SGSSYVR-LPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKT-PLNDGQW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2226 YRIEASRTGRNGSISVralDGPKasmvpsTYHSVSPPGYTILDVDANamLFVGGLTGKIKKADAVRVITFTGCMGETYFD 2305
Cdd:cd00110 83 HSVSVERNGRSVTLSV---DGER------VVESGSPGGSALLNLDGP--LYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2550-2691 |
4.58e-25 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 102.78 E-value: 4.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2550 FSTRNESGIILlgSGGTLTPPrrkrrqttqAYYAIFLNKGRLEVHLSSGTRtmrKIVIKPEPNLfHDGREHSVHVERTRG 2629
Cdd:pfam00054 1 FRTTEPSGLLL--YNGTQTER---------DFLALELRDGRLEVSYDLGSG---AAVVRSGDKL-NDGKWHSVELERNGR 65
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 117647249 2630 IFTVQIDEDRRHM--QNLTEEQ-PIEVKKLFVGGAPPE-FQPSPLRNIPAFQGCVWNLVINSIPMD 2691
Cdd:pfam00054 66 SGTLSVDGEARPTgeSPLGATTdLDVDGPLYVGGLPSLgVKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2964-3089 |
2.41e-24 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 100.57 E-value: 2.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2964 FRTTRPTGVLLGVSSQKMDGMGIEMIDEKLMFHVDNGAGRFTAIYdagIPGHMCNGQWHKVTAKKIKNRLELVVDGNQVD 3043
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDFLALELVNGRLVLRYDLGSGPESLLS---SGKNLNDGQWHSVRVERNGNTLTLSVDGQTVV 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 117647249 3044 AQSPNSASTSADTNDPVFVGGFPGGLNQFGLTTNIRFRGCIRSLKL 3089
Cdd:pfam02210 78 SSLPPGESLLLNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRV 123
|
|
| LamG |
smart00282 |
Laminin G domain; |
2545-2687 |
3.76e-23 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 97.41 E-value: 3.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2545 EINLSFSTRNESGIILLGSGGTLTPprrkrrqttqaYYAIFLNKGRLEVHLSSGTRTmrkIVIKPEPNLFHDGREHSVHV 2624
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGD-----------YLALELRDGRLVLRYDLGSGP---ARLTSDPTPLNDGQWHRVAV 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 117647249 2625 ERTRGIFTVQID-EDRRHMQNLTEEQPIEVK-KLFVGGAPPEFQPSPLRNIPAFQGCVWNLVINS 2687
Cdd:smart00282 67 ERNGRSVTLSVDgGNRVSGESPGGLTILNLDgPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNG 131
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2364-2497 |
1.97e-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: 92.48 E-value: 1.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2364 FRTFSSSALLMYlATRDLKDFMSVELSDGHVKVSYDLGSGMTSVVSNQNH-NDGKWKAFTLSRIQKQANISIvdidsNQE 2442
Cdd:pfam02210 1 FRTRQPNGLLLY-AGGGGSDFLALELVNGRLVLRYDLGSGPESLLSSGKNlNDGQWHSVRVERNGNTLTLSV-----DGQ 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 117647249 2443 ENVATSSSGNNFGLDLKADdkIYFGGLPTLRNLSMKARPEVnvkkYSGCLKDIEI 2497
Cdd:pfam02210 75 TVVSSLPPGESLLLNLNGP--LYLGGLPPLLLLPALPVRAG----FVGCIRDVRV 123
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2964-3098 |
1.31e-19 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 87.37 E-value: 1.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2964 FRTTRPTGVLLGVSSQ-KMDGMGIEMIDEKLMFHVDNGAGRFTAiydaGIPGHMCNGQWHKVTAKKIKNRLELVVDGNQV 3042
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQtERDFLALELRDGRLEVSYDLGSGAAVV----RSGDKLNDGKWHSVELERNGRSGTLSVDGEAR 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 117647249 3043 -DAQSPNSASTSADTNDPVFVGGFPG-GLNQFGLTTNIRFRGCIRSLKLtkgTGKPLE 3098
Cdd:pfam00054 77 pTGESPLGATTDLDVDGPLYVGGLPSlGVKKRRLAISPSFDGCIRDVIV---NGKPLD 131
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2550-2688 |
4.57e-18 |
|
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: 82.85 E-value: 4.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2550 FSTRNESGIILLGSGGTltpprrkrrqttQAYYAIFLNKGRLEVHLSSGTRTMRKIVIKpepNLFHDGREHSVHVERTRG 2629
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGG------------SDFLALELVNGRLVLRYDLGSGPESLLSSG---KNLNDGQWHSVRVERNGN 65
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 117647249 2630 IFTVQIDEDRRHMQNLTEEQPI--EVKKLFVGGAPPEFQPSPLRNIPAFQGCVWNLVINSI 2688
Cdd:pfam02210 66 TLTLSVDGQTVVSSLPPGESLLlnLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1665-2143 |
3.54e-17 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 88.92 E-value: 3.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1665 ERTNSRAESLEEFIKGLVQDAEAINEKAVQLNETLGNQDKTAERnLEELQKEIDR----------MLKELRSK--DLQTQ 1732
Cdd:TIGR04523 225 KQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQ-LSEKQKELEQnnkkikelekQLNQLKSEisDLNNQ 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1733 KEvaedelvaaEGLLKRVNKLFGEPRAQNEDMEKDL---QQKLAEYKNKLDDawdLLREATDKTRDanrlsaaNQKnmti 1809
Cdd:TIGR04523 304 KE---------QDWNKELKSELKNQEKKLEEIQNQIsqnNKIISQLNEQISQ---LKKELTNSESE-------NSE---- 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1810 letKKEAIEGSKRQIENTLKEGNDILDEANRLLGEINSVIDYVDDIKTKlppmSEELSDKI-------DDLAQEIKdrRL 1882
Cdd:TIGR04523 361 ---KQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKL----NQQKDEQIkklqqekELLEKEIE--RL 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1883 AEKVFQAESHAAQLNDSSAVLDGILDEAKNISfnataafraySNIKDYIDEAEKVAREAK-ELAQGATKLATSPQGLLKe 1961
Cdd:TIGR04523 432 KETIIKNNSEIKDLTNQDSVKELIIKNLDNTR----------ESLETQLKVLSRSINKIKqNLEQKQKELKSKEKELKK- 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1962 dakgslqksfrILNEAKKLANDVKgnhndlnDLKTRLETadlrnsgllgaLNDTMDKLSAITNDTAAKLQAVKEKAREAN 2041
Cdd:TIGR04523 501 -----------LNEEKKELEEKVK-------DLTKKISS-----------LKEKIEKLESEKKEKESKISDLEDELNKDD 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2042 DT-AKAVLAQVKD-LHQNLDGLKQNYNKLADSVAKTNAVVKDPSKNKI-----IADAGTSVRNLEQEADRLIDKLKPIKE 2114
Cdd:TIGR04523 552 FElKKENLEKEIDeKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKdlikeIEEKEKKISSLEKELEKAKKENEKLSS 631
|
490 500
....*....|....*....|....*....
gi 117647249 2115 LEDNLKKNISEIKELINQARKQANSIKVS 2143
Cdd:TIGR04523 632 IIKNIKSKKNKLKQEVKQIKETIKEIRNK 660
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1674-2141 |
1.33e-16 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 87.00 E-value: 1.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1674 LEEFIKgLVQDAEAINEKAVQLN---ETLGNQDKTAERNLEELQKEIDRMLKELRSKDL---------QTQKEvaedelv 1741
Cdd:TIGR04523 144 LTEIKK-KEKELEKLNNKYNDLKkqkEELENELNLLEKEKLNIQKNIDKIKNKLLKLELllsnlkkkiQKNKS------- 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1742 aaegLLKRVNKLfgepRAQNEDMEKD---LQQKLAEYKNKLDDAWDLLREATDK-TRDANRLSAANQ---KNMTILETKK 1814
Cdd:TIGR04523 216 ----LESQISEL----KKQNNQLKDNiekKQQEINEKTTEISNTQTQLNQLKDEqNKIKKQLSEKQKeleQNNKKIKELE 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1815 EAIEGSKRQIENTLKEGNDILDeaNRLLGEINSVIDYVDDIKTKLPPMSE---ELSDKIDDLAQEI---------KDRRL 1882
Cdd:TIGR04523 288 KQLNQLKSEISDLNNQKEQDWN--KELKSELKNQEKKLEEIQNQISQNNKiisQLNEQISQLKKELtnsesenseKQREL 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1883 AEKVFQAESHAAQlNDSSavldgiLDEAKNISfnataafraySNIKDYIDEAEKVAREAKELAQGATKLATSPQGLLKEd 1962
Cdd:TIGR04523 366 EEKQNEIEKLKKE-NQSY------KQEIKNLE----------SQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKE- 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1963 akgslQKsfRILNEAKKLANDVKGNHNDLNDLKTRLETADLRNSGLLGALNDTMDKLSAITNDTAAKLQAVKEKAREA-- 2040
Cdd:TIGR04523 428 -----IE--RLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELkk 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2041 -NDTAKAVLAQVKDLHQNLDGLKQNYNKLADSVAKTNAVVKDPSKNKIIADAGTSVRNLEQEADRLIDKLKPIKELEDNL 2119
Cdd:TIGR04523 501 lNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSL 580
|
490 500
....*....|....*....|..
gi 117647249 2120 KKNISEIKELINQARKQANSIK 2141
Cdd:TIGR04523 581 KKKQEEKQELIDQKEKEKKDLI 602
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2170-2307 |
8.68e-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: 76.30 E-value: 8.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2170 VKTAVADNLLFYLGSAKfIDFLAIEMRKGKVSFLWDVGSGVGRVEYPDLTIDDSYWYRIEASRTGRNGSISVralDGpka 2249
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGG-SDFLALELVNGRLVLRYDLGSGPESLLSSGKNLNDGQWHSVRVERNGNTLTLSV---DG--- 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 117647249 2250 smvpSTYHSVSPPGYTiLDVDANAMLFVGGLTGKIKKADAVRVITFTGCMGETYFDNK 2307
Cdd:pfam02210 74 ----QTVVSSLPPGES-LLLNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1609-2145 |
2.99e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 79.34 E-value: 2.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1609 ENTTQELKHLLSPQRAPERLIQlAEGNVNTLVMETNELLTRATKVTADGEQtgqDAERTNSRAESLEEFIKGLVQDAEAI 1688
Cdd:PRK03918 165 KNLGEVIKEIKRRIERLEKFIK-RTENIEELIKEKEKELEEVLREINEISS---ELPELREELEKLEKEVKELEELKEEI 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1689 NEKAVQLNETLGNQdktaeRNLEELQKEIDRMLKELRSKDLQTQKEVAE-DELvaaEGLLKRVNKLfGEPRAQNEDMEKD 1767
Cdd:PRK03918 241 EELEKELESLEGSK-----RKLEEKIRELEERIEELKKEIEELEEKVKElKEL---KEKAEEYIKL-SEFYEEYLDELRE 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1768 LQQKLAEYKNKLDDAWDLLREATDKTRDANRLSaanqKNMTILETKKEAIEGSKRQIEnTLKEgndILDEANRL------ 1841
Cdd:PRK03918 312 IEKRLSRLEEEINGIEERIKELEEKEERLEELK----KKLKELEKRLEELEERHELYE-EAKA---KKEELERLkkrltg 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1842 --LGEINSVIDYVDDIKTKLPPMSEELSDKIDDLAQEIKDRRLA-EKVFQAESH----AAQLNDssavldgilDEAKNIs 1914
Cdd:PRK03918 384 ltPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAiEELKKAKGKcpvcGRELTE---------EHRKEL- 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1915 fnataafraysnIKDYIDEAEKVAREAKELAQGATKLATSPQGLLKEDAKGS-LQKSFRILNEAKKLANDVKG-NHNDLN 1992
Cdd:PRK03918 454 ------------LEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESeLIKLKELAEQLKELEEKLKKyNLEELE 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1993 DLKTRLETADLRNSGLLG---ALNDTMDKLSAITNdtaaKLQAVKEKAREANDTAKAVLAQ--------VKDLHQNLDGL 2061
Cdd:PRK03918 522 KKAEEYEKLKEKLIKLKGeikSLKKELEKLEELKK----KLAELEKKLDELEEELAELLKEleelgfesVEELEERLKEL 597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2062 KQNYNKLadsvaktnavvkdpsknkiiadagTSVRNLEQEADRLIDKLKPIKELEDNLKKNISEIKELINQARKQANSIK 2141
Cdd:PRK03918 598 EPFYNEY------------------------LELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELE 653
|
....
gi 117647249 2142 VSVS 2145
Cdd:PRK03918 654 KKYS 657
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1665-2164 |
4.72e-14 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 78.86 E-value: 4.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1665 ERTNSRAESLE--EFIKGlvqdaEAINEKAVQLNETLGNQDKTAERNLEELQKEIDRMLKELRSKDLQTQKEVAEDELva 1742
Cdd:pfam02463 154 RRLEIEEEAAGsrLKRKK-----KEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYL-- 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1743 aegLLKRVNKLFGEPRAQNEDMEKDLQQKLAEYKNKLDDAWDLLREATDKtrdaNRLSAANQKNMTILETKKEAIEGSKR 1822
Cdd:pfam02463 227 ---LYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKE----NKEEEKEKKLQEEELKLLAKEEEELK 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1823 QIENTLKEGNDILDEANRLLGEINSVIdyvdDIKTKLPPMSEELSDKIDDLAQEIKDRRLAEKVFQAESHAAQLNDSSAV 1902
Cdd:pfam02463 300 SELLKLERRKVDDEEKLKESEKEKKKA----EKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEEL 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1903 LDGILDEAKNISfnatAAFRAYSNIKDYIDEAEKVAREAKELAQgatklatspqgLLKEDAKGSLQKSFRILNEAKKLAN 1982
Cdd:pfam02463 376 LAKKKLESERLS----SAAKLKEEELELKSEEEKEAQLLLELAR-----------QLEDLLKEEKKEELEILEEEEESIE 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1983 DVKGNHN-------DLNDLKTRLETADLRNSGLLGALNDTMDKLSAITNDTAAKLQAVKEKAREANDTAKAVLAQVKDLH 2055
Cdd:pfam02463 441 LKQGKLTeekeeleKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGV 520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2056 QNLDGLKQNYNKL------ADSVAKTNAVVKDPSKNKIIADAGTSVRNLEQEADRLIDKLKPIKELEDNLKKNIS--EIK 2127
Cdd:pfam02463 521 GGRIISAHGRLGDlgvaveNYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAvlEID 600
|
490 500 510
....*....|....*....|....*....|....*..
gi 117647249 2128 ELINQARKQANSIKVSVSSGGDCVRTYRPEIKKGSYN 2164
Cdd:pfam02463 601 PILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKL 637
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
913-960 |
5.03e-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: 68.53 E-value: 5.03e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 117647249 913 PCRCNINGSFSEICHTRTGQCECRPNVQGRHCDECKPETFGLQL-GRGC 960
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSqGGGC 49
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1608-2031 |
7.54e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 78.16 E-value: 7.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1608 LENTTQELKHLLSPQRAPerlIQLAEGNVNTLVMETNELLTRATKVTADGEQTGQDAERTNSRAESLEEFIKGLVQDAEA 1687
Cdd:PRK02224 319 LEDRDEELRDRLEECRVA---AQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEE 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1688 INEKAVQLNETLGNqdktAERNLEELQKEIDRM---LKELRSkDLQTQKE-VAEDELVAAEGllK------------RVN 1751
Cdd:PRK02224 396 LRERFGDAPVDLGN----AEDFLEELREERDELrerEAELEA-TLRTARErVEEAEALLEAG--KcpecgqpvegspHVE 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1752 KLfGEPRAQNEDMEKDLQQ---KLAEYKNKLDDAWDLLREATDKTRDANRLSAANQknmtILETKKEAIEGSKRQIENTL 1828
Cdd:PRK02224 469 TI-EEDRERVEELEAELEDleeEVEEVEERLERAEDLVEAEDRIERLEERREDLEE----LIAERRETIEEKRERAEELR 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1829 KEGNDILDEA------------------------NRLLGEINSVIDYVDDIktklppmsEELSDKIDDLAQEIKDRR--- 1881
Cdd:PRK02224 544 ERAAELEAEAeekreaaaeaeeeaeeareevaelNSKLAELKERIESLERI--------RTLLAAIADAEDEIERLRekr 615
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1882 --LAEKVFQAESHAAQLNDSSAVLDGILDEAKnisfnataafraysnikdyIDEA-EKVAREAKELAQGATKLATspqgl 1958
Cdd:PRK02224 616 eaLAELNDERRERLAEKRERKRELEAEFDEAR-------------------IEEArEDKERAEEYLEQVEEKLDE----- 671
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1959 lKEDAKGSLQKSF-RILNEAKKLaNDVKGNHNDLNDLKTRLET----------------ADLR--NSGLLGA-LNDTMDK 2018
Cdd:PRK02224 672 -LREERDDLQAEIgAVENELEEL-EELRERREALENRVEALEAlydeaeelesmygdlrAELRqrNVETLERmLNETFDL 749
|
490
....*....|...
gi 117647249 2019 LsaITNDTAAKLQ 2031
Cdd:PRK02224 750 V--YQNDAYSHIE 760
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1602-2141 |
2.55e-13 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 76.55 E-value: 2.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1602 YKILYGLENTTQELKHLLSPQRAPERliqlaegnvntlvmETNELLTRATKVTADGEQTGQDAERTNSRAESLEEFIKGL 1681
Cdd:pfam02463 225 YLLYLDYLKLNEERIDLLQELLRDEQ--------------EEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1682 VQDAEAINEKAvqlNETLGNQDKTAERNLEELQKE--------------IDRMLKELRSKDLQTQ-----KEVAEDELVA 1742
Cdd:pfam02463 291 LAKEEEELKSE---LLKLERRKVDDEEKLKESEKEkkkaekelkkekeeIEELEKELKELEIKREaeeeeEEELEKLQEK 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1743 AEGLLKRVNKLFGEPRAQNEDMEKDLQQKLAEYKNKlddawdlLREATDKTRDANRLSAANQKNMTILETKKEAIEGSKR 1822
Cdd:pfam02463 368 LEQLEEELLAKKKLESERLSSAAKLKEEELELKSEE-------EKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIE 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1823 QIENTLKEGNDILDEANRLLGEINSVIDYVDDI-----KTKLPPMSEELSDKID---DLAQEIKDRRLAEKVFQAESHAA 1894
Cdd:pfam02463 441 LKQGKLTEEKEELEKQELKLLKDELELKKSEDLlketqLVKLQEQLELLLSRQKleeRSQKESKARSGLKVLLALIKDGV 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1895 QLNDSSAVLDGILDE---AKNISFNATAAFRAYSNIKDYIDEAEKVAREAKELAQGATKLATSPQGLLKEDAKGSLQKSF 1971
Cdd:pfam02463 521 GGRIISAHGRLGDLGvavENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEID 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1972 RILNEAKKLANDVKGNHNDLNDLKTRLETADLRNSGLLGALNDTMDKLSAITNDTAAKLQAVKEKAREANDTAKAVLAQV 2051
Cdd:pfam02463 601 PILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQE 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2052 K--DLHQNLDGLK----QNYNKLADSVAKTNAVVKDPSKNKIIAD--------AGTSVRNLEQEADRLIDKLKPIKELED 2117
Cdd:pfam02463 681 LqeKAESELAKEEilrrQLEIKKKEQREKEELKKLKLEAEELLADrvqeaqdkINEELKLLKQKIDEEEEEEEKSRLKKE 760
|
570 580
....*....|....*....|....
gi 117647249 2118 NLKKNISEIKELINQARKQANSIK 2141
Cdd:pfam02463 761 EKEEEKSELSLKEKELAEEREKTE 784
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1646-2132 |
2.60e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 76.23 E-value: 2.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1646 LLTRATKVTADGEQTGQ----DAERTNSRAESLEEFIKGLVQ-DAEA-INEKAVQLNETlgnqDKTAERNLEELQKEIDR 1719
Cdd:PRK02224 82 HIERRVRLSGDRATTAKcvleTPEGTIDGARDVREEVTELLRmDAEAfVNCAYVRQGEV----NKLINATPSDRQDMIDD 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1720 MLKELRskdLQTQKEVAEDELVAAEGLLKRVNKLFGEPRAQNEDME-KDLQQKLAEYKNKLDDAWDLL------REATDK 1792
Cdd:PRK02224 158 LLQLGK---LEEYRERASDARLGVERVLSDQRGSLDQLKAQIEEKEeKDLHERLNGLESELAELDEEIeryeeqREQARE 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1793 TRDA--NRLSAANQK--------------NMTILETKKE------AIEGSKRQIENTLKEGNDILDEANRLLGEINSVID 1850
Cdd:PRK02224 235 TRDEadEVLEEHEERreeletleaeiedlRETIAETEREreelaeEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEA 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1851 YVDDIKTKLppmsEELSDKIDDLAQEIKD-----RRLAEKVFQAESHAAQLNDSSAVLDGILDEAKN------------- 1912
Cdd:PRK02224 315 RREELEDRD----EELRDRLEECRVAAQAhneeaESLREDADDLEERAEELREEAAELESELEEAREavedrreeieele 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1913 --------------ISFNATAAF---------RAYSNIKDY---IDEAEKVAREAKELaQGATK-------LATSPQGLL 1959
Cdd:PRK02224 391 eeieelrerfgdapVDLGNAEDFleelreerdELREREAELeatLRTARERVEEAEAL-LEAGKcpecgqpVEGSPHVET 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1960 KEDAKGSLQKSFRILNEAKKLANDVKGNHNDLNDLK---TRLETADLRNSGL----------LGALNDTMDKLSAITNDT 2026
Cdd:PRK02224 470 IEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVeaeDRIERLEERREDLeeliaerretIEEKRERAEELRERAAEL 549
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2027 AAKLQAVKEKAREANDTAKAVLAQVKDLHQNLDGLK---QNYNKLADSVAKtnavvkdpsknkiiadagtsVRNLEQEAD 2103
Cdd:PRK02224 550 EAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKeriESLERIRTLLAA--------------------IADAEDEIE 609
|
570 580
....*....|....*....|....*....
gi 117647249 2104 RLIDKLKPIKELEDNLKKNISEIKELINQ 2132
Cdd:PRK02224 610 RLREKREALAELNDERRERLAEKRERKRE 638
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1694-2054 |
3.43e-13 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 74.17 E-value: 3.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1694 QLNETLGNQDKTAERNLEELQKEIDRMLKELRskDLQTQKEVAEDELvaaegllkrvnklfgepraqnedmeKDLQQKLA 1773
Cdd:COG4372 17 GLRPKTGILIAALSEQLRKALFELDKLQEELE--QLREELEQAREEL-------------------------EQLEEELE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1774 EYKNKLDDAWDLLREATDKTRDANRLSAANQKNMTILETKKEAIEgskRQIENTLKEGNDILDEANRLLGEINSVIDYVD 1853
Cdd:COG4372 70 QARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQ---EELEELQKERQDLEQQRKQLEAQIAELQSEIA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1854 DIKTKLppmsEELSDKIDDLAQEIKDrrlaekvFQAESHAAQLNDSSAVLDGILDEAKNISFNATAAFRAYSNIKDYIDE 1933
Cdd:COG4372 147 EREEEL----KELEEQLESLQEELAA-------LEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1934 AEKVAREAK---ELAQGATKLATSPQGLLKEDAKGSLQKSFRILNEAKKLANDVKGNHNDLNDLKTRLETADLRNSGLLG 2010
Cdd:COG4372 216 LAEELLEAKdslEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALEL 295
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 117647249 2011 ALNDTMDKLSAITNDTAAKLQAVKEKAREANDTAKAVLAQVKDL 2054
Cdd:COG4372 296 KLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAEL 339
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
914-960 |
5.47e-13 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 65.45 E-value: 5.47e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 117647249 914 CRCNINGSFSEICHTRTGQCECRPNVQGRHCDECKPETFGLQ--LGRGC 960
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPsdPPQGC 49
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1642-2129 |
6.76e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 75.08 E-value: 6.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1642 ETNELLTRATKVTADgeQTGQDAERTNSRAESLEEFIKGLVQD-AEAINEKavqlnETLGNQDKTAERNLEELQKEIDRM 1720
Cdd:PRK02224 226 EEQREQARETRDEAD--EVLEEHEERREELETLEAEIEDLRETiAETERER-----EELAEEVRDLRERLEELEEERDDL 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1721 LKE------------LRSKDLQTQKEVAEDELV-----------AAEGLLKRVNKLfgEPRAQN-----EDMEKDLQ--- 1769
Cdd:PRK02224 299 LAEaglddadaeaveARREELEDRDEELRDRLEecrvaaqahneEAESLREDADDL--EERAEElreeaAELESELEear 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1770 QKLAEYKNKLDDAWDLLREATDKTRDAN-RLSAANQKNMTILETKkEAIEGSKRQIENTLKEGNDILDEANRLLGEIN-- 1846
Cdd:PRK02224 377 EAVEDRREEIEELEEEIEELRERFGDAPvDLGNAEDFLEELREER-DELREREAELEATLRTARERVEEAEALLEAGKcp 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1847 ---------SVIDYVDDIKTKLppmsEELSDKIDDLAQEIKDrrLAEKVFQAEShaaqLNDSSAVLDGILDEAKNISfna 1917
Cdd:PRK02224 456 ecgqpvegsPHVETIEEDRERV----EELEAELEDLEEEVEE--VEERLERAED----LVEAEDRIERLEERREDLE--- 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1918 taafraySNIKDYIDEAEKVAREAKELAQGATKLATSPQGllKEDAKGSLQKsfrilnEAKKLANDVKGNHNDLNDLKTR 1997
Cdd:PRK02224 523 -------ELIAERRETIEEKRERAEELRERAAELEAEAEE--KREAAAEAEE------EAEEAREEVAELNSKLAELKER 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1998 LEtadlrnsgllgALNDTMDKLSAITN--DTAAKLQAVKEKAREANDTAKAVLAQVKDLHQNLDGlkqnynKLadsvakt 2075
Cdd:PRK02224 588 IE-----------SLERIRTLLAAIADaeDEIERLREKREALAELNDERRERLAEKRERKRELEA------EF------- 643
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 117647249 2076 navvkDPSKnkiIADAGTSVRNLEQEADRLIDKLKPIKELEDNLKKNI----SEIKEL 2129
Cdd:PRK02224 644 -----DEAR---IEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIgaveNELEEL 693
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
914-960 |
9.87e-13 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 64.64 E-value: 9.87e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 117647249 914 CRCNINGSFSEICHTRTGQCECRPNVQGRHCDECKPETFGLQlGRGC 960
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG-PPGC 46
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1644-2146 |
1.17e-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: 73.90 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1644 NELLTRATKVTADGEQTGQDAERTNSraesLEEFIKGLVQDAEAINEKAV-------QLNETL---GNQDKTAERNLEEL 1713
Cdd:TIGR04523 47 NELKNKEKELKNLDKNLNKDEEKINN----SNNKIKILEQQIKDLNDKLKknkdkinKLNSDLskiNSEIKNDKEQKNKL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1714 QKEIDRMLKELRSKDlQTQKEVAeDELVAAEGLLKRVNKLFGEPRAQNEDMEKdlqqklaeYKNKLDDAWDLLREATDKT 1793
Cdd:TIGR04523 123 EVELNKLEKQKKENK-KNIDKFL-TEIKKKEKELEKLNNKYNDLKKQKEELEN--------ELNLLEKEKLNIQKNIDKI 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1794 RdaNRLSAANQKnMTILETKKEAIEGSKRQIENtLKEGNDIL-DEANRLLGEINsvidyvdDIKTKLPPMSEELSDKIDD 1872
Cdd:TIGR04523 193 K--NKLLKLELL-LSNLKKKIQKNKSLESQISE-LKKQNNQLkDNIEKKQQEIN-------EKTTEISNTQTQLNQLKDE 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1873 LaQEIKDRrLAEKVFQAESHAAQLNDSSAVLdgildeaknisfnataafraySNIKDYIDEAEKVareaKElaQGATKLa 1952
Cdd:TIGR04523 262 Q-NKIKKQ-LSEKQKELEQNNKKIKELEKQL---------------------NQLKSEISDLNNQ----KE--QDWNKE- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1953 tspqglLKEDAKgSLQKSFRI----LNEAKKLANDVKgnhNDLNDLKTRLETADLRNSGLLGALNDTMDKLSAITNDTAA 2028
Cdd:TIGR04523 312 ------LKSELK-NQEKKLEEiqnqISQNNKIISQLN---EQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQS 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2029 KLQAVKEKAREANDTaKAVLAQVKDLHQNLD----GLKQNYNK-------LADSVAKTNAVVKD-----PSKNKIIADAG 2092
Cdd:TIGR04523 382 YKQEIKNLESQINDL-ESKIQNQEKLNQQKDeqikKLQQEKELlekeierLKETIIKNNSEIKDltnqdSVKELIIKNLD 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2093 TSVRNLEQEADRLIDKLKPIK-ELEDN---------------------------LKKNISEIKELINQARKQANSIKVSV 2144
Cdd:TIGR04523 461 NTRESLETQLKVLSRSINKIKqNLEQKqkelkskekelkklneekkeleekvkdLTKKISSLKEKIEKLESEKKEKESKI 540
|
..
gi 117647249 2145 SS 2146
Cdd:TIGR04523 541 SD 542
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1678-2141 |
3.16e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 72.79 E-value: 3.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1678 IKGLVQDAEAiNEKAVQlnETLGNQD-KTAERNLEELQKEIDRMLKEL-----RSKDLQTQKEVAEDELvaaEGLLKRVN 1751
Cdd:PRK03918 137 IDAILESDES-REKVVR--QILGLDDyENAYKNLGEVIKEIKRRIERLekfikRTENIEELIKEKEKEL---EEVLREIN 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1752 KLfgepraqnEDMEKDLQQKLAEYKNKLddawdllrEATDKTRdaNRLSAanqknmtiLETKKEAIEGSKRQIENTLKEg 1831
Cdd:PRK03918 211 EI--------SSELPELREELEKLEKEV--------KELEELK--EEIEE--------LEKELESLEGSKRKLEEKIRE- 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1832 ndildeanrllgeinsvidyvddiktkLPPMSEELSDKIDDLaqEIKDRRLAEKVFQAESHAAQlndsSAVLDGILDEAK 1911
Cdd:PRK03918 264 ---------------------------LEERIEELKKEIEEL--EEKVKELKELKEKAEEYIKL----SEFYEEYLDELR 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1912 NISFNATAAFRAYSNIKDYIDEAEKVAREAKELaqgatklatspQGLLKEdakgsLQKSFRILNEAKKLANDVKGNHNDL 1991
Cdd:PRK03918 311 EIEKRLSRLEEEINGIEERIKELEEKEERLEEL-----------KKKLKE-----LEKRLEELEERHELYEEAKAKKEEL 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1992 NDLKTRLEtadlrnsgllgalNDTMDKLsaitndtAAKLQAVKEKAREANDTAKAVLAQVKDLHQNLDGLKQNYNKLADS 2071
Cdd:PRK03918 375 ERLKKRLT-------------GLTPEKL-------EKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKA 434
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 117647249 2072 VAK---TNAVVKDPSKNKIIADAGTSVRNLEQEADRLIDKLKPIKELEDNLKKNISEIKELINQaRKQANSIK 2141
Cdd:PRK03918 435 KGKcpvCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKL-KELAEQLK 506
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
963-1007 |
3.73e-12 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 63.10 E-value: 3.73e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 117647249 963 CNCNSFGSKSFDCEA-SGQCWCQPGVAGKKCDRCAHGYFNFQEGGC 1007
Cdd:smart00180 1 CDCDPGGSASGTCDPdTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1610-1943 |
3.93e-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: 72.78 E-value: 3.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1610 NTTQELKHLLSPQRAPERLIQLAEGNVNTLVMETNELLTRATKVTADGEQTGQDAERTNSRAESLEEFIKGLVQD----- 1684
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERiaqls 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1685 ---AEAINEKAVQLNETLGNQD--KTAERNLEELQKEID----------RMLKELRsKDLQTQKEVAEDELVAAEGLLKR 1749
Cdd:TIGR02168 754 kelTELEAEIEELEERLEEAEEelAEAEAEIEELEAQIEqlkeelkalrEALDELR-AELTLLNEEAANLRERLESLERR 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1750 VnklfGEPRAQNEDME---KDLQQKLAEYKNKLDDAWDLLREATDKTRDANRLSAANQKNMTILETKKEAIEGSKRQIEN 1826
Cdd:TIGR02168 833 I----AATERRLEDLEeqiEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1827 TLKEGNDILDEANRLLGEINSVIDyvdDIKTKLPPMSEELSDKIDDLAQEIkdrrlAEKVFQAESHAAQLNDSSAVLDGI 1906
Cdd:TIGR02168 909 KRSELRRELEELREKLAQLELRLE---GLEVRIDNLQERLSEEYSLTLEEA-----EALENKIEDDEEEARRRLKRLENK 980
|
330 340 350
....*....|....*....|....*....|....*..
gi 117647249 1907 LDEAKNISFNATAAFRAYSNIKDYIDEAEKVAREAKE 1943
Cdd:TIGR02168 981 IKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKE 1017
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1608-1879 |
9.38e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 71.24 E-value: 9.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1608 LENTTQELKHLLSPQRAPERLIQLAEGNVNTLVMETNELLTRATK-------VTADGEQTGQDAERTNSRAESLEEFIKG 1680
Cdd:TIGR02168 728 ISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEaeeelaeAEAEIEELEAQIEQLKEELKALREALDE 807
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1681 LVQDAEAINEKAVQLNETLG---NQDKTAERNLEELQKEIDRMLKELRS-----KDLQTQKEVAEDELvaaEGLLKRVNK 1752
Cdd:TIGR02168 808 LRAELTLLNEEAANLRERLEsleRRIAATERRLEDLEEQIEELSEDIESlaaeiEELEELIEELESEL---EALLNERAS 884
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1753 LFGEPRAQNEDMEkDLQQKLAEYKNKLDDAWDLLREATDKTRDAN-RLSAANQKNMTILE--------------TKKEAI 1817
Cdd:TIGR02168 885 LEEALALLRSELE-ELSEELRELESKRSELRRELEELREKLAQLElRLEGLEVRIDNLQErlseeysltleeaeALENKI 963
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 117647249 1818 EGSKRQIENTLKEGNDILDEanrlLGEIN-SVIDYVDDIKTKLppmsEELSDKIDDLAQEIKD 1879
Cdd:TIGR02168 964 EDDEEEARRRLKRLENKIKE----LGPVNlAAIEEYEELKERY----DFLTAQKEDLTEAKET 1018
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1056-1104 |
1.74e-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: 1.74e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 117647249 1056 CNCSTVGSLASQCNVNTGQCSCHPKFSGMKCSECSRGHWNYPLCTLCDC 1104
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1658-2073 |
2.56e-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: 70.09 E-value: 2.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1658 EQtGQDAERTNSRAESLEEFIkglvQDAEAINEKAVQLNETLGNQDKTAErNLEELQ---KEIDRMLKEL--------RS 1726
Cdd:TIGR02168 142 EQ-GKISEIIEAKPEERRAIF----EEAAGISKYKERRKETERKLERTRE-NLDRLEdilNELERQLKSLerqaekaeRY 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1727 KDLQTQKEVAE-----DELVAAEGLLKRVNKLFgeprAQNEDMEKDLQQKLAEYKNKLDDAWDLLREATDKTRDANR--L 1799
Cdd:TIGR02168 216 KELKAELRELElallvLRLEELREELEELQEEL----KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKelY 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1800 SAANQKNmtILETKKEAIEGSKRQIENTLKEGNDILDEANRLLGEINsvidyvdDIKTKLPPMSEELSDKIDDLAQEIKd 1879
Cdd:TIGR02168 292 ALANEIS--RLEQQKQILRERLANLERQLEELEAQLEELESKLDELA-------EELAELEEKLEELKEELESLEAELE- 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1880 rRLAEKVFQAESHAAQLNDSsavldgiLDEAKNisfnataafraysnikDYIDEAEKVAREAKELAQGATKLatspqgll 1959
Cdd:TIGR02168 362 -ELEAELEELESRLEELEEQ-------LETLRS----------------KVAQLELQIASLNNEIERLEARL-------- 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1960 kEDAKGSLQKSFRILNEAKKlandvKGNHNDLNDLKTRLETADLRNSGLLGALNDTMDKLSaitndtaaKLQAVKEKARE 2039
Cdd:TIGR02168 410 -ERLEDRRERLQQEIEELLK-----KLEEAELKELQAELEELEEELEELQEELERLEEALE--------ELREELEEAEQ 475
|
410 420 430
....*....|....*....|....*....|....
gi 117647249 2040 ANDTAKAVLAQVKDLHQNLDGLKQNYNKLADSVA 2073
Cdd:TIGR02168 476 ALDAAERELAQLQARLDSLERLQENLEGFSEGVK 509
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1673-2136 |
3.42e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 69.03 E-value: 3.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1673 SLEEFIKGLVqdAEAINEKAVQLNETLGNQDKTAERNLEELQKEIDRMLKELRS--------KDLQTQKEVAEDELVAAE 1744
Cdd:COG4717 38 TLLAFIRAML--LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEyaelqeelEELEEELEELEAELEELR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1745 GLLKRVNKLFGEPRAQNEdmEKDLQQKLAEYKNKLDDawdLLREATDKTRDANRLSAANQKnmtiLETKKEAIEGSKRQI 1824
Cdd:COG4717 116 EELEKLEKLLQLLPLYQE--LEALEAELAELPERLEE---LEERLEELRELEEELEELEAE----LAELQEELEELLEQL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1825 EN-TLKEGNDILDEANRLLGEINSVIDYVDDIKTKLppmsEELSDKIDDLAQEIKDRRLAEKVFQAESHAAQLNdSSAVL 1903
Cdd:COG4717 187 SLaTEEELQDLAEELEELQQRLAELEEELEEAQEEL----EELEEELEQLENELEAAALEERLKEARLLLLIAA-ALLAL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1904 DGILDEAKNISFNATAAF---------------RAYSNIKDYIDEAEKVAREaKELAQGATKLATSPQGLLKEDAKGSLQ 1968
Cdd:COG4717 262 LGLGGSLLSLILTIAGVLflvlgllallflllaREKASLGKEAEELQALPAL-EELEEEELEELLAALGLPPDLSPEELL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1969 KSFRILNEAKKLandvkgnHNDLNDLKTRLETADLRNsgllgALNDTMDKLSAITNDTAAKLQAVKEKAREAndtakavL 2048
Cdd:COG4717 341 ELLDRIEELQEL-------LREAEELEEELQLEELEQ-----EIAALLAEAGVEDEEELRAALEQAEEYQEL-------K 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2049 AQVKDLHQNLDGLKQNYNKLADSVAKTNavvkdpsknkiiadagtsvrnLEQEADRLIDKLKPIKELEDNLKKNISEIKE 2128
Cdd:COG4717 402 EELEELEEQLEELLGELEELLEALDEEE---------------------LEEELEELEEELEELEEELEELREELAELEA 460
|
....*...
gi 117647249 2129 LINQARKQ 2136
Cdd:COG4717 461 ELEQLEED 468
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
962-1007 |
4.55e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 60.06 E-value: 4.55e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 117647249 962 PCNCNSFGSKSFDCEA-SGQCWCQPGVAGKKCDRCAHGYFNF--QEGGC 1007
Cdd:cd00055 1 PCDCNGHGSLSGQCDPgTGQCECKPNTTGRRCDRCAPGYYGLpsQGGGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1416-1462 |
4.80e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 60.06 E-value: 4.80e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 117647249 1416 CQCNGHSS---QCDPETSVCQnCQHHTAGDFCERCALGYYGIVRGLPNDC 1462
Cdd:pfam00053 1 CDCNPHGSlsdTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
860-912 |
4.97e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 60.06 E-value: 4.97e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 117647249 860 PCQCNDNldYSIPGSCDSLSGSCLiCKPGTTGRYCELCADGYFGDAVNAKNCQ 912
Cdd:cd00055 1 PCDCNGH--GSLSGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1660-2137 |
5.20e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 68.64 E-value: 5.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1660 TGQDAERTNSRAESLEEFIKGLVQDAEAINEKAVQLNEtlgnqdktAERNLEELQKEIDRMLKELRSKDLQTQKEVAEDE 1739
Cdd:COG4717 62 QGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEE--------LEEELEELEAELEELREELEKLEKLLQLLPLYQE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1740 LVAAEGLLK----RVNKLFG--EPRAQNEDMEKDLQQKLAEYKNKLDDAWDLLREAT-----DKTRDANRLSAANQKNMT 1808
Cdd:COG4717 134 LEALEAELAelpeRLEELEErlEELRELEEELEELEAELAELQEELEELLEQLSLATeeelqDLAEELEELQQRLAELEE 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1809 ILETKKEAIEGSKRQIENTLKEGNDI-----LDEANRLLGEINSVI-------DYVDDIKTKLPPMSEELSDKIDDLAQE 1876
Cdd:COG4717 214 ELEEAQEELEELEEELEQLENELEAAaleerLKEARLLLLIAAALLallglggSLLSLILTIAGVLFLVLGLLALLFLLL 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1877 IKDRRLAEKVFQAESHAAQLND-SSAVLDGILDEAK-NISFNATAAFRAYSNIKDYIDEAEKVAREAKELAQGAtkLATS 1954
Cdd:COG4717 294 AREKASLGKEAEELQALPALEElEEEELEELLAALGlPPDLSPEELLELLDRIEELQELLREAEELEEELQLEE--LEQE 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1955 PQGLLKEDAKGSLQKSFRILNEAKKlandvkgnhndLNDLKTRLETADLRnsglLGALNDTMDKLSAITNDTaaklqAVK 2034
Cdd:COG4717 372 IAALLAEAGVEDEEELRAALEQAEE-----------YQELKEELEELEEQ----LEELLGELEELLEALDEE-----ELE 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2035 EKAREANDTAKAVLAQVKDLHQNLDGLKQNYNKLADSvaktnavvkdpsknkiiadagTSVRNLEQEADRLIDKLKpiKE 2114
Cdd:COG4717 432 EELEELEEELEELEEELEELREELAELEAELEQLEED---------------------GELAELLQELEELKAELR--EL 488
|
490 500
....*....|....*....|...
gi 117647249 2115 LEDNLKKNIseIKELINQARKQA 2137
Cdd:COG4717 489 AEEWAALKL--ALELLEEAREEY 509
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1707-2114 |
5.85e-11 |
|
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: 68.45 E-value: 5.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1707 ERNLEELQKEIDRMLKELRSKDLQTQKEVAEDELVAA-EGLLKRVNKLFGEPRAQNEDMEKDLQQKLAEYKNKLDDAWDL 1785
Cdd:COG5185 218 ESTLLEKAKEIINIEEALKGFQDPESELEDLAQTSDKlEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEK 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1786 LREATDK------TRDANRLSAANQKNMTILETKKEAIEGSKRQIENTLKEGNDILDEANRLLGEINSVIDYVDdiktkl 1859
Cdd:COG5185 298 IAEYTKSidikkaTESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVE------ 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1860 ppmSEELSDKIDDLAQEIkdRRLAEKVFQAesHAAQLNDSSAVLDGILDEAKNISfnataafraySNIKDYIDEAEKVAR 1939
Cdd:COG5185 372 ---LSKSSEELDSFKDTI--ESTKESLDEI--PQNQRGYAQEILATLEDTLKAAD----------RQIEELQRQIEQATS 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1940 EAKELAQGATKLATSpqgLLKEDAKGSLQKSFRILNEAKKLANDVKGNHNDLNDLKTRLETAdlrnsglLGALNDTMDKL 2019
Cdd:COG5185 435 SNEEVSKLLNELISE---LNKVMREADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESR-------VSTLKATLEKL 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2020 SAITNdtaAKLQAVKEKAREANDTAKAVLAQVKDLHqnldgLKQNYNKLADSVAKTNavvkDPSKNKIIADAGTSVRNLE 2099
Cdd:COG5185 505 RAKLE---RQLEGVRSKLDQVAESLKDFMRARGYAH-----ILALENLIPASELIQA----SNAKTDGQAANLRTAVIDE 572
|
410
....*....|....*
gi 117647249 2100 QEADRLIDKLKPIKE 2114
Cdd:COG5185 573 LTQYLSTIESQQARE 587
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1635-1912 |
6.44e-11 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 66.09 E-value: 6.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1635 NVNTLVMETNELLTRATKVTadgEQTGQDAERTNSRAESLEEF----------IKGLVQDAEAINEKAVQLNETLgnQDK 1704
Cdd:COG1340 2 KTDELSSSLEELEEKIEELR---EEIEELKEKRDELNEELKELaekrdelnaqVKELREEAQELREKRDELNEKV--KEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1705 TAERNleELQKEIDRMLKELRSKDLQTQKEVAEDELVAAegLLKRVNKLfgEPRAQNEDM----EKDLQQKLAEYKNKLD 1780
Cdd:COG1340 77 KEERD--ELNEKLNELREELDELRKELAELNKAGGSIDK--LRKEIERL--EWRQQTEVLspeeEKELVEKIKELEKELE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1781 DAwdllREATDKTRDANRLSAAnqknmtiLETKKEAIEGSKRQIENTLKEGNDILDEANRLLGEINSVIDYVDDIKTKLP 1860
Cdd:COG1340 151 KA----KKALEKNEKLKELRAE-------LKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIV 219
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 117647249 1861 PMSE---ELSDKIDDLAQEIKDRRLAEKVFQAESHAAQLNDSSAVLDGILDEAKN 1912
Cdd:COG1340 220 EAQEkadELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAEEIFE 274
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1657-2030 |
8.42e-11 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 66.85 E-value: 8.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1657 GEQTGQDAERTNSRAESLEEFIKGLVQDAEAINEKAVQlnetlgnQDKTAERNLEELQKEIDRMLKELRSkdLQTQKEVA 1736
Cdd:COG4372 1 GDRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALF-------ELDKLQEELEQLREELEQAREELEQ--LEEELEQA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1737 EDELVAAEGLLKRVNKLFGEPRAQNEDMEKDLQQKLAEYKNKLDDAWDLLREATDKTRDANRLSAANQKNMTILETKKEA 1816
Cdd:COG4372 72 RSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1817 IEGSKRQIENT------LKEGNDILDEA------NRLLGEINSVIDYVdDIKTKLPPMSEELSDKIDDLAQEIKDRRLAE 1884
Cdd:COG4372 152 LKELEEQLESLqeelaaLEQELQALSEAeaeqalDELLKEANRNAEKE-EELAEAEKLIESLPRELAEELLEAKDSLEAK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1885 KVFQaesHAAQLNDSSAVLDGILDEAKNISFNATAAFRAYSNIKDYIDEAEKVAREAKELAQGATKLATSPQGLLKEDAk 1964
Cdd:COG4372 231 LGLA---LSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAA- 306
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 117647249 1965 gslQKSFRILNEAKKLANDVKGNHNDLNDLKTRLETADLRNSGLLGALNDTMDKLSAITNDTAAKL 2030
Cdd:COG4372 307 ---LSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVAD 369
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1670-2146 |
1.06e-10 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 68.32 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1670 RAESLEEFIKglvQDAEAINE---KAVQ-LNETLGNQDKTAE------RNLEELQKEIDRMLKELRSKDLQ--TQKEVAE 1737
Cdd:PTZ00440 1085 KVEALLKKID---ENKNKLIEiknKSHEhVVNADKEKNKQTEhynkkkKSLEKIYKQMEKTLKELENMNLEdiTLNEVNE 1161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1738 DELVAAEGLLKRVNKLFGEPRAQNE------------------DMEKDLQQKLA--EYKNKLDDAWDLLREATDKTRDAN 1797
Cdd:PTZ00440 1162 IEIEYERILIDHIVEQINNEAKKSKtimeeiesykkdidqvkkNMSKERNDHLTtfEYNAYYDKATASYENIEELTTEAK 1241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1798 RL--SAANQKNMTILETKKEAIEGSKRQ-------IENTLKEGND-----ILDEANRLLGEI----NSVIDYVDDIKTKL 1859
Cdd:PTZ00440 1242 GLkgEANRSTNVDELKEIKLQVFSYLQQvikennkMENALHEIKNmyeflISIDSEKILKEIlnstKKAEEFSNDAKKEL 1321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1860 ppmseelsDKIDDLAQEIKdrrlaEKVFQAESHAAQlNDSSAVLDGILDEAKNISFNATAAFRAYSNIKDYIDEAEkvar 1939
Cdd:PTZ00440 1322 --------EKTDNLIKQVE-----AKIEQAKEHKNK-IYGSLEDKQIDDEIKKIEQIKEEISNKRKEINKYLSNIK---- 1383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1940 EAKElaQGATKLATSPQGLLKED--------------------AKGSLQKSFRILNEAKKLANDVKGNHNDLNDLKTRLE 1999
Cdd:PTZ00440 1384 SNKE--KCDLHVRNASRGKDKIDflnkheaiepsnskevniikITDNINKCKQYSNEAMETENKADENNDSIIKYEKEIT 1461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2000 TAdLRNSGLLG----------ALNDTMDKLSAITNDTAAKLQAVKEKARE--------------ANDTAKAV-------L 2048
Cdd:PTZ00440 1462 NI-LNNSSILGkktklekkkkEATNIMDDINGEHSIIKTKLTKSSEKLNQlneqpnikregdvlNNDKSTIAyetiqynL 1540
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2049 AQVKDLHQNLDGLKQN----YNKLADSVAKTNAVVK-DPSKN--KIIADAGTSVRNLEQ----------EADRLIDKLKP 2111
Cdd:PTZ00440 1541 GRVKHNLLNILNIKDEietiLNKAQDLMRDISKISKiVENKNleNLNDKEADYVKYLDNilkekqlmeaEYKKLNEIYSD 1620
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 117647249 2112 IKELEDNLKK--------NISEIKELINQARKQANSIKVSVSS 2146
Cdd:PTZ00440 1621 VDNIEKELKKhkknyeigLLEKVIEINKNIKLYMDSTKESLNS 1663
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1102-1159 |
1.09e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 58.90 E-value: 1.09e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 117647249 1102 CDCFLPGTDATTCDLETrkcscsdqtGQCSCKVNVEGVHCDRCRPGKFGLDAKNPLGC 1159
Cdd:pfam00053 1 CDCNPHGSLSDTCDPET---------GQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1674-2122 |
1.36e-10 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 67.77 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1674 LEEFIKGLVQDAEAInEKAVQLNETLGNQD-------KTAERNLEELQKEIDRMLKELRSKdlqtQKEVAEDELvaaEGL 1746
Cdd:TIGR01612 605 LKEKIKNISDKNEYI-KKAIDLKKIIENNNayidelaKISPYQVPEHLKNKDKIYSTIKSE----LSKIYEDDI---DAL 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1747 LKRVNKLFGEPRAQN-EDmekdlQQKLAEYKNKLDDAWDLLREATDKTRDANRLSAANQKNM---TILETKKEaiegskr 1822
Cdd:TIGR01612 677 YNELSSIVKENAIDNtED-----KAKLDDLKSKIDKEYDKIQNMETATVELHLSNIENKKNElldIIVEIKKH------- 744
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1823 qientlkegndILDEANRLLGEInsvidyVDDIKTKlppmSEELSDKIDDLAQEiKDR--RLAEKVFQAESHaaqLNDSS 1900
Cdd:TIGR01612 745 -----------IHGEINKDLNKI------LEDFKNK----EKELSNKINDYAKE-KDElnKYKSKISEIKNH---YNDQI 799
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1901 AVlDGILDEAKNISFNATAAFRAYSNIKDyiDEAEKVAREAKelaqgatklatspqgLLKEDAKGSLQKSFRILNEAKKl 1980
Cdd:TIGR01612 800 NI-DNIKDEDAKQNYDKSKEYIKTISIKE--DEIFKIINEMK---------------FMKDDFLNKVDKFINFENNCKE- 860
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1981 anDVKGNHNDLNDL--KTRLETADLRNSGLLGALNDTMDKLSAITNDTAAKLQAVK--EKAREANDTAKAVLAQVKDLHQ 2056
Cdd:TIGR01612 861 --KIDSEHEQFAELtnKIKAEISDDKLNDYEKKFNDSKSLINEINKSIEEEYQNINtlKKVDEYIKICENTKESIEKFHN 938
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 117647249 2057 NLDGLKQNYNKLADSVAKTNAVVK---DPSKN----------KIIADAgtSVRNLEQEADRLIdklKPIKELEDNLKKN 2122
Cdd:TIGR01612 939 KQNILKEILNKNIDTIKESNLIEKsykDKFDNtlidkineldKAFKDA--SLNDYEAKNNELI---KYFNDLKANLGKN 1012
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1634-2141 |
1.41e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 67.63 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1634 GNVNTLV---M-ETNELLTRATKVTA---DGEQTGQDAERTNSRAESLEEfikgLVQDAEAINEKAVQLN--ETLGN--Q 1702
Cdd:COG4913 207 GDLDDFVreyMlEEPDTFEAADALVEhfdDLERAHEALEDAREQIELLEP----IRELAERYAAARERLAelEYLRAalR 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1703 DKTAERNLEELQKEIDRMLKELRS-----KDLQTQKEVAEDELVAAEGLL-----KRVNKLfgepRAQNEDMEKDL---Q 1769
Cdd:COG4913 283 LWFAQRRLELLEAELEELRAELARleaelERLEARLDALREELDELEAQIrgnggDRLEQL----EREIERLERELeerE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1770 QKLAEYKNKLDDA-----------WDLLREATDKTRDANRLSAANQKNMTILETKKEAIEGSKRQIENTLKE----GNDI 1834
Cdd:COG4913 359 RRRARLEALLAALglplpasaeefAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASlerrKSNI 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1835 ----------------LDE----------------------ANRLLG-----------EINSVIDYVDDIKTKL------ 1859
Cdd:COG4913 439 parllalrdalaealgLDEaelpfvgelievrpeeerwrgaIERVLGgfaltllvppeHYAAALRWVNRLHLRGrlvyer 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1860 ------PPMSEELSDK--------------------------------IDDLAQ------------------EIKDRRL- 1882
Cdd:COG4913 519 vrtglpDPERPRLDPDslagkldfkphpfrawleaelgrrfdyvcvdsPEELRRhpraitragqvkgngtrhEKDDRRRi 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1883 ----------AEKVFQAESHAAQLNDSSAVLDGILDEAKNISFNATAAFRAYSNIKDYIDEAEKVAREAKELAQgatkla 1952
Cdd:COG4913 599 rsryvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAE------ 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1953 tspqgllKEDAKGSLQKSFRILNEAKKLANDVKGNHNDL----NDLKTRLETADLRNSGLLGALNDTMDKLSAITNDTAA 2028
Cdd:COG4913 673 -------LEAELERLDASSDDLAALEEQLEELEAELEELeeelDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL 745
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2029 KLQAVKEKAREANDTAKAVLAQVKDLHQNLDGLKQNYNKLADSVAKT----NAVVKDPSknkiiADAGTSVRNLEQ---- 2100
Cdd:COG4913 746 ELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAmrafNREWPAET-----ADLDADLESLPEylal 820
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 117647249 2101 ----EADRLIDKLKPIKELednLKKN-ISEIKELINQARKQANSIK 2141
Cdd:COG4913 821 ldrlEEDGLPEYEERFKEL---LNENsIEFVADLLSKLRRAIREIK 863
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1415-1463 |
1.51e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 58.52 E-value: 1.51e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 117647249 1415 PCQCNGHSS---QCDPETSVCQnCQHHTAGDFCERCALGYYGIvRGLPNDCQ 1463
Cdd:cd00055 1 PCDCNGHGSlsgQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGL-PSQGGGCQ 50
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1638-1909 |
1.57e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 67.40 E-value: 1.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1638 TLVMETNE----LLTRATKVTADGE-------QTG----------------QDAERTNSRAESLEEFIKGLVQDAEAINE 1690
Cdd:TIGR02169 623 TLVVEDIEaarrLMGKYRMVTLEGElfeksgaMTGgsraprggilfsrsepAELQRLRERLEGLKRELSSLQSELRRIEN 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1691 KAVQLNETLgnqdKTAERNLEELQKEIDRMLKEL-----RSKDLQTQKEVAEDELVAAEGLLKRVNKLFGEP-------R 1758
Cdd:TIGR02169 703 RLDELSQEL----SDASRKIGEIEKEIEQLEQEEeklkeRLEELEEDLSSLEQEIENVKSELKELEARIEELeedlhklE 778
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1759 AQNEDMEKDL-QQKLAEYKNKLDDAWDLLREATDKTRDANRLSAANQKNMTILETKKEAIEGSKRQIENTLKEGNDILDE 1837
Cdd:TIGR02169 779 EALNDLEARLsHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEN 858
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1838 ANRLLGEINSVIdyvDDIKTKLPPMSEELSD---KIDDL-----AQEIKDRRLAEKVFQAESHAAQLNDSSAVLDGILDE 1909
Cdd:TIGR02169 859 LNGKKEELEEEL---EELEAALRDLESRLGDlkkERDELeaqlrELERKIEELEAQIEKKRKRLSELKAKLEALEEELSE 935
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
963-1010 |
2.41e-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: 2.41e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 117647249 963 CNCNSFGSKSFDCEAS-GQCWCQPGVAGKKCDRCAHGYFNFQEGGCIAC 1010
Cdd:pfam00053 1 CDCNPHGSLSDTCDPEtGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1009-1054 |
2.94e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 57.75 E-value: 2.94e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 117647249 1009 ACDCSHLG---NNCDPKTGQCICPPNTTGEKCSECLPNTWGH-SIVTGCK 1054
Cdd:cd00055 1 PCDCNGHGslsGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLpSQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1056-1098 |
3.51e-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: 3.51e-10
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 117647249 1056 CNCSTVGSLASQCNVNTGQCSCHPKFSGMKCSECSRGHWNYPL 1098
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1628-1978 |
4.42e-10 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 64.54 E-value: 4.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1628 LIQLAEGNVNTLVMETNELLTRATKVTADGEQTGQDAERT-------NSRAESLEEFIKGLVQDAEAINEKAVQLNETLg 1700
Cdd:COG4372 25 LIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLeeeleqaRSELEQLEEELEELNEQLQAAQAELAQAQEEL- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1701 nqdKTAERNLEELQKEIDRMLKELrsKDLQTQKEVAEDElvaaeglLKRVNKLFGEPRAQNEDMEKDLQQKLAEYKnKLD 1780
Cdd:COG4372 104 ---ESLQEEAEELQEELEELQKER--QDLEQQRKQLEAQ-------IAELQSEIAEREEELKELEEQLESLQEELA-ALE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1781 DAWDLLREATDKTRDANRLSAANQKNMTILETKK--EAIEGSKRQIENTLKEGNDILDEANRLLGEINSVIDYVDDIKTK 1858
Cdd:COG4372 171 QELQALSEAEAEQALDELLKEANRNAEKEEELAEaeKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1859 LPPMSEELSDKIDDLAQEIKDRRLAEKV---FQAESHAAQLNDSSAVLDGILDEAKNISFNATAAFRAYSNIKDYIDEAE 1935
Cdd:COG4372 251 LLEEVILKEIEELELAILVEKDTEEEELeiaALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLEL 330
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 117647249 1936 KVAREAKELAQGATKLAtspQGLLKEDAKGSLQKSFRILNEAK 1978
Cdd:COG4372 331 ALAILLAELADLLQLLL---VGLLDNDVLELLSKGAEAGVADG 370
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1010-1048 |
5.56e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.94 E-value: 5.56e-10
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 117647249 1010 CDCS---HLGNNCDPKTGQCICPPNTTGEKCSECLPNTWGHS 1048
Cdd:smart00180 1 CDCDpggSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1646-1839 |
6.22e-10 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 64.08 E-value: 6.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1646 LLTRATKVTADGEQTGQDAE--RTNSRAESLEEFIKGLVQDAEAINEKAVQLN---ETLGNQDKTAERNLEELQKEIDRM 1720
Cdd:COG3883 5 ALAAPTPAFADPQIQAKQKElsELQAELEAAQAELDALQAELEELNEEYNELQaelEALQAEIDKLQAEIAEAEAEIEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1721 LKEL--RSKDLQTQKEVAE--DELVAAEG---LLKRVNKLFGEPRAQNEDME--KDLQQKLAEYKNKLDDAWDLLR---- 1787
Cdd:COG3883 85 REELgeRARALYRSGGSVSylDVLLGSESfsdFLDRLSALSKIADADADLLEelKADKAELEAKKAELEAKLAELEalka 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 117647249 1788 EATDKTRDANRLSAANQKNMTILETKKEAIEGSKRQIENTLKEGNDILDEAN 1839
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1603-2177 |
7.19e-10 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 65.62 E-value: 7.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1603 KILYGLENTTQeLKHLLSPQRAPERLIQLAEGNVNTLVMETNELLTRATKVtadgeQTGQDAERTNSRAESLEEFI---- 1678
Cdd:PTZ00440 572 KIKYIEENVDH-IKDIISLNDEIDNIIQQIEELINEALFNKEKFINEKNDL-----QEKVKYILNKFYKGDLQELLdels 645
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1679 ------KGLVQDAEAINEKAVQLNETLGNQDKtaernLEELQKE-IDRMLKELR--SKDLQTQKEVAEDELVaaegllkr 1749
Cdd:PTZ00440 646 hflddhKYLYHEAKSKEDLQTLLNTSKNEYEK-----LEFMKSDnIDNIIKNLKkeLQNLLSLKENIIKKQL-------- 712
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1750 vNKLfgepraqNEDMEKDLQQKLAEYKnklddawdllreatDKTRDANRLSAANQKnmtiLETKKEAIEGSKRQIENTLK 1829
Cdd:PTZ00440 713 -NNI-------EQDISNSLNQYTIKYN--------------DLKSSIEEYKEEEEK----LEVYKHQIINRKNEFILHLY 766
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1830 EGNDILDEANRLLGEINSVIDYVDDIKTKLPPMSEELSDKIDDLAQEIKDRRLAEKVFQA--ESHAAQLNDSsavLDGIL 1907
Cdd:PTZ00440 767 ENDKDLPDGKNTYEEFLQYKDTILNKENKISNDINILKENKKNNQDLLNSYNILIQKLEAhtEKNDEELKQL---LQKFP 843
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1908 DEAKNIS-------FNatAAFRAYSNIKDYIDEAEKVAREAKELAQGATKLATSPQGLL-----KEDAKGSLQKSFRILN 1975
Cdd:PTZ00440 844 TEDENLNlkelekeFN--ENNQIVDNIIKDIENMNKNINIIKTLNIAINRSNSNKQLVEhllnnKIDLKNKLEQHMKIIN 921
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1976 EAKKLANDVKGN-HNDLNDLKTRLETadlrnsgllgALNDT-MDKLSAITNDTAAKLQAVKEKAREANDTAKAVLAQVKD 2053
Cdd:PTZ00440 922 TDNIIQKNEKLNlLNNLNKEKEKIEK----------QLSDTkINNLKMQIEKTLEYYDKSKENINGNDGTHLEKLDKEKD 991
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2054 ----LHQNLDGLKQNYNKLAdsvAKTNAVVKDPsKNKIIADAGTSVRNLEQEADRLIDKLkpIKELEDnLKKNISEIKEL 2129
Cdd:PTZ00440 992 ewehFKSEIDKLNVNYNILN---KKIDDLIKKQ-HDDIIELIDKLIKEKGKEIEEKVDQY--ISLLEK-MKTKLSSFHFN 1064
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 117647249 2130 INQARKQANSIKVSVSSGGDCVRTYRPEIKKGsyNNIVVHVKTAVADN 2177
Cdd:PTZ00440 1065 IDIKKYKNPKIKEEIKLLEEKVEALLKKIDEN--KNKLIEIKNKSHEH 1110
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
752-801 |
8.22e-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: 8.22e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 117647249 752 PCQCFAHA---EACDDITGECLnCKDHTGGPYCNECLPGFYGDPTRgsPEDCQ 801
Cdd:cd00055 1 PCDCNGHGslsGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQ--GGGCQ 50
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1688-2136 |
8.43e-10 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 65.07 E-value: 8.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1688 INEKAVQLNETLGNQD---KTAERNL-EELQKEIDRMLKELRSKDLQTQK-------EVAE-------DELVAAEGL--L 1747
Cdd:TIGR01612 1031 IEQKIEDANKNIPNIEiaiHTSIYNIiDEIEKEIGKNIELLNKEILEEAEinitnfnEIKEklkhynfDDFGKEENIkyA 1110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1748 KRVNKLFGEPRAQNEDMEKDLQQkLAEYKNKLDDAWDLLREATDKTRDANrlsaanqkNMTILETKKEAIEGSKRQIENT 1827
Cdd:TIGR01612 1111 DEINKIKDDIKNLDQKIDHHIKA-LEEIKKKSENYIDEIKAQINDLEDVA--------DKAISNDDPEEIEKKIENIVTK 1181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1828 LKEGNDILDEANRLLGEINSV-------------------------IDYVDDIKTKLPPMSEELSDKIDDL------AQE 1876
Cdd:TIGR01612 1182 IDKKKNIYDEIKKLLNEIAEIekdktsleevkginlsygknlgklfLEKIDEEKKKSEHMIKAMEAYIEDLdeikekSPE 1261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1877 IKDRRLAEKVFQAESHAAQLNDS--------SAVLDGILDEAKNISFNATAAFRAYSNIKDYIDEAEKVAREAK----EL 1944
Cdd:TIGR01612 1262 IENEMGIEMDIKAEMETFNISHDddkdhhiiSKKHDENISDIREKSLKIIEDFSEESDINDIKKELQKNLLDAQkhnsDI 1341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1945 AQGATKLaTSPQGLLKedakgsLQKSFRILNEAKKLANDVKGNHNDLND--------LKTRLETADLRN--SGLLGALND 2014
Cdd:TIGR01612 1342 NLYLNEI-ANIYNILK------LNKIKKIIDEVKEYTKEIEENNKNIKDeldkseklIKKIKDDINLEEckSKIESTLDD 1414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2015 TmDKLSAITNDTAAKLQAVKEKAReaNDTakavlaQVKDLHQNLDGLKQNYNKLADSVAKTNAVVKDpSKNKIIADAGTS 2094
Cdd:TIGR01612 1415 K-DIDECIKKIKELKNHILSEESN--IDT------YFKNADENNENVLLLFKNIEMADNKSQHILKI-KKDNATNDHDFN 1484
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 117647249 2095 VRNLEQEadrlIDKLKPIKELEDNLKKNISEIKELINQARKQ 2136
Cdd:TIGR01612 1485 INELKEH----IDKSKGCKDEADKNAKAIEKNKELFEQYKKD 1522
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1699-1946 |
9.81e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 64.70 E-value: 9.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1699 LGNQDKTAERNLEELQKEIDRMLKELrsKDLQTQKEVAEDELVAAEGLLKRVNKlfgEPRAQNEDMEKDLQQKLAEYKNK 1778
Cdd:TIGR02169 228 LLKEKEALERQKEAIERQLASLEEEL--EKLTEEISELEKRLEEIEQLLEELNK---KIKDLGEEEQLRVKEKIGELEAE 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1779 LDDAWDLLREATDKTRDANRLSAANQKNMTILETKKEAIEGS-------KRQIENTLKEGNDILDEANRLLGEINS---- 1847
Cdd:TIGR02169 303 IASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREieeerkrRDKLTEEYAELKEELEDLRAELEEVDKefae 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1848 VIDYVDDIKTKLppmsEELSDKIDDLAQEIkdRRLAEKVFQAESHAAQLNDSSAVLdgildEAKNISFNATAafraysni 1927
Cdd:TIGR02169 383 TRDELKDYREKL----EKLKREINELKREL--DRLQEELQRLSEELADLNAAIAGI-----EAKINELEEEK-------- 443
|
250
....*....|....*....
gi 117647249 1928 KDYIDEAEKVAREAKELAQ 1946
Cdd:TIGR02169 444 EDKALEIKKQEWKLEQLAA 462
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1653-2119 |
1.04e-09 |
|
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: 63.94 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1653 VTADGEQTGQDAERTNSRAESLEEFIKGLVQDAEAINEKAVQLnETLGNQDKTAERNLEELQKEIDRMLKELrskdlqTQ 1732
Cdd:pfam05622 5 AQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQL-ESGDDSGTPGGKKYLLLQKQLEQLQEEN------FR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1733 KEVAEDEL-VAAEGLLKRVnklfGEPRAQNEDMekdlqQKLAEYKNKLDDAWDLLREATDKtrdANRLSAAnqknmtiLE 1811
Cdd:pfam05622 78 LETARDDYrIKCEELEKEV----LELQHRNEEL-----TSLAEEAQALKDEMDILRESSDK---VKKLEAT-------VE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1812 TKKEAIEGS---KRQIEnTLKEGN-----------DILDEANRLLGEINSVIDYVDDIKTKLppmSEE------------ 1865
Cdd:pfam05622 139 TYKKKLEDLgdlRRQVK-LLEERNaeymqrtlqleEELKKANALRGQLETYKRQVQELHGKL---SEEskkadklefeyk 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1866 -LSDKIDDLAQEiKDRRLAE----KVFQAESHAAQLNDSSAVLDGILDEAKNISFNATAAFRAYSNIKDYID--EAE-KV 1937
Cdd:pfam05622 215 kLEEKLEALQKE-KERLIIErdtlRETNEELRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIrlQHEnKM 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1938 AREAKElAQGATKLATSpQGLLkEDAKGSLQKsfriLNEAKKLAND-VKGNHNDLNDLKTRLETADLRN--SGLLGA-LN 2013
Cdd:pfam05622 294 LRLGQE-GSYRERLTEL-QQLL-EDANRRKNE----LETQNRLANQrILELQQQVEELQKALQEQGSKAedSSLLKQkLE 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2014 DTMDKLSaitndtaaKLQAVKEKAREA-NDTAKAVLAQvkdLHQNLDGLKQNYNKLADS-----------VAKTNAVVK- 2080
Cdd:pfam05622 367 EHLEKLH--------EAQSELQKKKEQiEELEPKQDSN---LAQKIDELQEALRKKDEDmkameerykkyVEKAKSVIKt 435
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 117647249 2081 -DPSKNKIIADAGTSVRNLEQEADRLID-------KLKPIKELEDNL 2119
Cdd:pfam05622 436 lDPKQNPASPPEIQALKNQLLEKDKKIEhlerdfeKSKLQREQEEKL 482
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
465-511 |
1.07e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 56.21 E-value: 1.07e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 117647249 465 CNCSGLGSTNE--DPCVGPCSCKENVEGEDCSRCKSGFFNLQEDNQKGC 511
Cdd:pfam00053 1 CDCNPHGSLSDtcDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1010-1053 |
1.23e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 56.21 E-value: 1.23e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 117647249 1010 CDCSHLG---NNCDPKTGQCICPPNTTGEKCSECLPNTWGHSIVTGC 1053
Cdd:pfam00053 1 CDCNPHGslsDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQ 47
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
410-467 |
1.26e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 55.82 E-value: 1.26e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 117647249 410 CHCDPTGSLSEVCVKDekyaqrglkPGSCHCKTGFGGVNCDRCVRGYHGYPDCQPCNC 467
Cdd:pfam00053 1 CDCNPHGSLSDTCDPE---------TGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1645-2136 |
1.34e-09 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 64.30 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1645 ELLTRATKVTADGEQTGQDAERTNSRAESLEefIKGLVQDAEAINekavQLNETLGNQDKTAERNLEELQKEIDRMLKEL 1724
Cdd:TIGR00606 369 LIQSLATRLELDGFERGPFSERQIKNFHTLV--IERQEDEAKTAA----QLCADLQSKERLKQEQADEIRDEKKGLGRTI 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1725 RSKDLQTQKEVAE-----DELVAAEGLLKRVNKLFGEPRAQNEDMEK-----DLQQKLAEYKNKLDDAWDL---LREATD 1791
Cdd:TIGR00606 443 ELKKEILEKKQEElkfviKELQQLEGSSDRILELDQELRKAERELSKaeknsLTETLKKEVKSLQNEKADLdrkLRKLDQ 522
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1792 KTRDANRLSAANQKNMTILETKKEAIE--------GS------------KRQIENTL----KEGNDILDEANRLLGEINS 1847
Cdd:TIGR00606 523 EMEQLNHHTTTRTQMEMLTKDKMDKDEqirkiksrHSdeltsllgyfpnKKQLEDWLhsksKEINQTRDRLAKLNKELAS 602
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1848 VIDYVDDIKTKLPPMSEELS---DKIDDL----AQEIKDRRLAEKVFQAESHAAQLNDSSAVLDGILDEAKNISFNATAA 1920
Cdd:TIGR00606 603 LEQNKNHINNELESKEEQLSsyeDKLFDVcgsqDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPV 682
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1921 ----FRAYSNIKDYIDEAEKVAR----EAKELAQGATKLATSPQGLLkedAKGSLQKSF--RILNEAKKLANDVKGNHND 1990
Cdd:TIGR00606 683 cqrvFQTEAELQEFISDLQSKLRlapdKLKSTESELKKKEKRRDEML---GLAPGRQSIidLKEKEIPELRNKLQKVNRD 759
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1991 LNDLKTRLEtadlRNSGLLGALNDTMDKLSAITNDTAAkLQAVKEKAREANDTAKAVLAQ---------VKDLHQNLDGL 2061
Cdd:TIGR00606 760 IQRLKNDIE----EQETLLGTIMPEEESAKVCLTDVTI-MERFQMELKDVERKIAQQAAKlqgsdldrtVQQVNQEKQEK 834
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 117647249 2062 KQNYNKLADSVAKTNAVVKDpsKNKIIADAGTSVRNLEQEADRLIDKLKPIKELEDNLKKNISEIKEL---INQARKQ 2136
Cdd:TIGR00606 835 QHELDTVVSKIELNRKLIQD--QQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLireIKDAKEQ 910
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1701-1901 |
1.72e-09 |
|
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: 62.86 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1701 NQDKTAERNLEELQKEIDRMLKELRS-----KDLQTQKEVAEDELVAAEGLLKRVNKLFGEPR---AQNEDMEKDLQQKL 1772
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAAlkkeeKALLKQLAALERRIAALARRIRALEQELAALEaelAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1773 AE------------YKNKLDDAWDLL---REATDKTRDA---NRLSAANQKNMTILETKKEAIEGSKRQIENTLKEGNDI 1834
Cdd:COG4942 100 EAqkeelaellralYRLGRQPPLALLlspEDFLDAVRRLqylKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 117647249 1835 LDEANRLLGEINSVIDYVDDIKTKLPPMSEELSDKIDDLAQEIKD-RRLAEKVFQAESHAAQLNDSSA 1901
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEElEALIARLEAEAAAAAERTPAAG 247
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1674-2175 |
2.03e-09 |
|
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: 63.59 E-value: 2.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1674 LEEFI---KGLVQDAEAINEKAVQLNETLG-NQDKTAERNLE---------ELQKEIDRMLkeLRSKDLQTQKEVAEDEL 1740
Cdd:pfam05483 136 LEEEIqenKDLIKENNATRHLCNLLKETCArSAEKTKKYEYEreetrqvymDLNNNIEKMI--LAFEELRVQAENARLEM 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1741 -VAAEGLLKRVNKLFGEPRAQNEDMEKD---LQQKLAEYKNKLDDAWDLLREATDKtrdanrlsaANQknmtiLETKkea 1816
Cdd:pfam05483 214 hFKLKEDHEKIQHLEEEYKKEINDKEKQvslLLIQITEKENKMKDLTFLLEESRDK---------ANQ-----LEEK--- 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1817 iegSKRQIENtLKEGNDildEANRLLGEInsvidyvDDIKTKLP-PMSEELSDKiDDLaqEIKDRRLAEKVFQAESHAAQ 1895
Cdd:pfam05483 277 ---TKLQDEN-LKELIE---KKDHLTKEL-------EDIKMSLQrSMSTQKALE-EDL--QIATKTICQLTEEKEAQMEE 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1896 LNDSSAVLDGILDEAKNISFNATAAFRA----YSNIKDYID----EAEKVAREAKELaqgaTKLATSPQGLLkEDAKGSL 1967
Cdd:pfam05483 340 LNKAKAAHSFVVTEFEATTCSLEELLRTeqqrLEKNEDQLKiitmELQKKSSELEEM----TKFKNNKEVEL-EELKKIL 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1968 QKSFRILNEAK---KLANDVKGNHNDL--------------------------------NDLKTRLETADLRNSGLLGAL 2012
Cdd:pfam05483 415 AEDEKLLDEKKqfeKIAEELKGKEQELifllqarekeihdleiqltaiktseehylkevEDLKTELEKEKLKNIELTAHC 494
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2013 NDTM---DKLSAITNDTAAKLQAVKEKAREANDTAKAVLAQVKDLHQN-------LDGLKQNYNKLADSV------AKTN 2076
Cdd:pfam05483 495 DKLLlenKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKemnlrdeLESVREEFIQKGDEVkckldkSEEN 574
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2077 AVVKDPS---KNKIIADAGTSVRNLEQEADrliDKLKPIKELEDN---LKKNISEIKELINQARKQANSIKVSVSSG--- 2147
Cdd:pfam05483 575 ARSIEYEvlkKEKQMKILENKCNNLKKQIE---NKNKNIEELHQEnkaLKKKGSAENKQLNAYEIKVNKLELELASAkqk 651
|
570 580 590
....*....|....*....|....*....|.
gi 117647249 2148 -GDCVRTYRPEI--KKGSYNNIVVHVKTAVA 2175
Cdd:pfam05483 652 fEEIIDNYQKEIedKKISEEKLLEEVEKAKA 682
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
753-800 |
2.33e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 55.05 E-value: 2.33e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 117647249 753 CQCFAHA---EACDDITGECLnCKDHTGGPYCNECLPGFYGDPTrGSPEDC 800
Cdd:pfam00053 1 CDCNPHGslsDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPS-DPPQGC 49
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1701-1979 |
2.37e-09 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 61.47 E-value: 2.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1701 NQDKTAERNLEELQKEIDRMLKELRS-KDLQTQ-----KEVAE--DELVAaegllkRVNKLFGEPRAQNEDMeKDLQQKL 1772
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEElKEKRDElneelKELAEkrDELNA------QVKELREEAQELREKR-DELNEKV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1773 AEYKNKLDDAWDLLREATDKTRDANRLSAANQKNMTILETKKEAIEGSKRQIEN---TLKEGNDILDEANRL---LGEIN 1846
Cdd:COG1340 74 KELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTevlSPEEEKELVEKIKELekeLEKAK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1847 SVIDYVDDIKTKLpPMSEELSDKIDDLAQEIKDrrLAEkvfQAESHAAQLNDSSAVLDGILDEAKnisfnataafRAYSN 1926
Cdd:COG1340 154 KALEKNEKLKELR-AELKELRKEAEEIHKKIKE--LAE---EAQELHEEMIELYKEADELRKEAD----------ELHKE 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 117647249 1927 IKDYIDEAEKVAREAKELAQGATKLATSPQGLLKEDAKGSLQKSFRILNEAKK 1979
Cdd:COG1340 218 IVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAE 270
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1102-1159 |
2.99e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 55.01 E-value: 2.99e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 117647249 1102 CDCFLPGTDATTCDLETrkcscsdqtGQCSCKVNVEGVHCDRCRPGKFGldaKNPLGC 1159
Cdd:smart00180 1 CDCDPGGSASGTCDPDT---------GQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1626-2137 |
3.17e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.03 E-value: 3.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1626 ERLIQLAEGNVNTLVMETNELLTRATKVTADGEQTGQDAERTNSRAESLEEFIKGLVQDAEAINEKAVQLNETLGNqdkt 1705
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE---- 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1706 AERNLEELQKEIDRMLKELRskDLQTQKEVAEDELVAAEGLLKRVNKLfgepRAQNEDMEKDLQQKLAEYKNKLDDAWDL 1785
Cdd:COG1196 314 LEERLEELEEELAELEEELE--ELEEELEELEEELEEAEEELEEAEAE----LAEAEEALLEAEAELAEAEEELEELAEE 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1786 LREATDKTRDANRLSAANQKNMTILETKKEAIEGSKRQIENTLKEGNDILDEANRLLGEINSVIDYVDDIKTKLPPMSEE 1865
Cdd:COG1196 388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1866 LSDKIDDLAQEIKDRR--LAEKVFQAESHAAQLNDSSAVLDGILDEAKNISFNATAAFRAYSNIKDYIDEAEKVAREAKE 1943
Cdd:COG1196 468 LLEEAALLEAALAELLeeLAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAA 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1944 LAQGATKLATSPQ---GLLKEDAKGSLqkSFRILNEAKKLANDVKGNHNDLNDLKTRLETADLRNsgLLGALNDTMDKLS 2020
Cdd:COG1196 548 LQNIVVEDDEVAAaaiEYLKAAKAGRA--TFLPLDKIRARAALAAALARGAIGAAVDLVASDLRE--ADARYYVLGDTLL 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2021 AITNDTAAKLQAVKEkAREANDTAKAVLAQVKDLHQNLDGLKQNYNKLADSVAKTNAVVKDPSKNKIIADAGTSVRNLEQ 2100
Cdd:COG1196 624 GRTLVAARLEAALRR-AVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAE 702
|
490 500 510
....*....|....*....|....*....|....*..
gi 117647249 2101 EADRLIDKLKPIKELEDNLKKNISEIKELINQARKQA 2137
Cdd:COG1196 703 EEEERELAEAEEERLEEELEEEALEEQLEAEREELLE 739
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1523-1566 |
3.36e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 54.62 E-value: 3.36e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 117647249 1523 CECDPYGSLPVPCDRVTGLCTCRPGATGRKCDGCEHWHAREGAE 1566
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPP 44
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1523-1560 |
3.43e-09 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 54.67 E-value: 3.43e-09
10 20 30
....*....|....*....|....*....|....*...
gi 117647249 1523 CECDPYGSLPVPCDRVTGLCTCRPGATGRKCDGCEHWH 1560
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGY 39
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1056-1097 |
3.64e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 54.62 E-value: 3.64e-09
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 117647249 1056 CNCSTVGSLASQCNVNTGQCSCHPKFSGMKCSECSRGHWNYP 1097
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1673-2229 |
4.09e-09 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 62.61 E-value: 4.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1673 SLEEFIKGLVQDAEaINEKAVQLNETLGNQDKTAERNLEELQKEI--------DRMLKELRSKDLQTQKEVAeDELVAAE 1744
Cdd:PRK01156 85 SIERRGKGSRREAY-IKKDGSIIAEGFDDTTKYIEKNILGISKDVflnsifvgQGEMDSLISGDPAQRKKIL-DEILEIN 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1745 GLLKRVNKLfgepraqnEDMEKDLQQKLAEYknklDDAWDLLREATDKTRDANRLSAANQKNMTILETKKEAIEGSKRQI 1824
Cdd:PRK01156 163 SLERNYDKL--------KDVIDMLRAEISNI----DYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNA 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1825 EN-------TLKEGNDILDEANRL---LGEINSVIDYVDDIKTKLPPMSEELSDKIDDLAqeIKDRrlaEKVFQAESHAA 1894
Cdd:PRK01156 231 MDdynnlksALNELSSLEDMKNRYeseIKTAESDLSMELEKNNYYKELEERHMKIINDPV--YKNR---NYINDYFKYKN 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1895 QLNDSSAVLDGILDEAKNISfnatAAFRAYSNIKDYIDEAEKVAREAKELAQGATKLATSpqgllkEDAKGSLQKSFRIL 1974
Cdd:PRK01156 306 DIENKKQILSNIDAEINKYH----AIIKKLSVLQKDYNDYIKKKSRYDDLNNQILELEGY------EMDYNSYLKSIESL 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1975 NeaKKLANDVKgNHNDLNDLKTRletadlrnsgLLGALNDTMDKLSAITNDTAAKLQAVKEKAREANdtakavlAQVKDL 2054
Cdd:PRK01156 376 K--KKIEEYSK-NIERMSAFISE----------ILKIQEIDPDAIKKELNEINVKLQDISSKVSSLN-------QRIRAL 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2055 HQNLDGLKQNYNKL-ADSVA----------KTNAVVKDPS--KNKIIADagtsVRNLEQEADRLIDKLKPIKELEDNLKK 2121
Cdd:PRK01156 436 RENLDELSRNMEMLnGQSVCpvcgttlgeeKSNHIINHYNekKSRLEEK----IREIEIEVKDIDEKIVDLKKRKEYLES 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2122 niSEIKELINQ------ARKQANSIKVSVSSGGDCVRTYrpEIKKGSYNNIVVHVKTAVADNLLFYLGSAKFIDFLAIEM 2195
Cdd:PRK01156 512 --EEINKSINEynkiesARADLEDIKIKINELKDKHDKY--EEIKNRYKSLKLEDLDSKRTSWLNALAVISLIDIETNRS 587
|
570 580 590
....*....|....*....|....*....|....*...
gi 117647249 2196 RKGKVSF-LWDVGSGVGRVE--YPDL-TIDDSYWYRIE 2229
Cdd:PRK01156 588 RSNEIKKqLNDLESRLQEIEigFPDDkSYIDKSIREIE 625
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
1684-1830 |
5.19e-09 |
|
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.
Pssm-ID: 403808 [Multi-domain] Cd Length: 142 Bit Score: 57.31 E-value: 5.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1684 DAEAINEKAVQLNEtlgnQDKTAERNLEELQKEIdrmlkelrsKDLQTQKEVAEDELVAAEGLLKRVNKLFGEP---RAQ 1760
Cdd:pfam12718 8 EAENAQERAEELEE----KVKELEQENLEKEQEI---------KSLTHKNQQLEEEVEKLEEQLKEAKEKAEESeklKTN 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1761 NEDMEKDLQQkLAEyknKLDDAWDLLREATDKTRDANRLSAANQKNMTILETKKEAIEGSKRQIENTLKE 1830
Cdd:pfam12718 75 NENLTRKIQL-LEE---ELEESDKRLKETTEKLRETDVKAEHLERKVQALEQERDEWEKKYEELEEKYKE 140
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1665-2146 |
5.33e-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: 62.76 E-value: 5.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1665 ERTNSRAESLEEFIKGLVQDAEAINEKAVQlNETLGNQDKTAERNLEELQK------EIDRMLKELR--SKDLQTQKEVA 1736
Cdd:TIGR01612 1135 EEIKKKSENYIDEIKAQINDLEDVADKAIS-NDDPEEIEKKIENIVTKIDKkkniydEIKKLLNEIAeiEKDKTSLEEVK 1213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1737 EDELVAAEGLlkrvNKLF----GEPRAQNEDMEK----------DLQQKLAEYKNKLDDAWDLLRE------ATDKTRDA 1796
Cdd:TIGR01612 1214 GINLSYGKNL----GKLFlekiDEEKKKSEHMIKameayiedldEIKEKSPEIENEMGIEMDIKAEmetfniSHDDDKDH 1289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1797 NRLSAANQKNMTILETK----------KEAIEGSKRQIENTLKEGNDILDEANRLLGEINSV--IDYVDDIKtKLPPMSE 1864
Cdd:TIGR01612 1290 HIISKKHDENISDIREKslkiiedfseESDINDIKKELQKNLLDAQKHNSDINLYLNEIANIynILKLNKIK-KIIDEVK 1368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1865 ELSDKIDDLAQEIKDR-RLAEKVFQAESHAAQLNDSSAVLDGILDEA------KNISFNATAAFRAYSNIKDYIDEAEKV 1937
Cdd:TIGR01612 1369 EYTKEIEENNKNIKDElDKSEKLIKKIKDDINLEECKSKIESTLDDKdideciKKIKELKNHILSEESNIDTYFKNADEN 1448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1938 AREAKELAQGATKLATSPQGLLKEDAKGSLQKSFRILNEAKKLANDVKGNHNDLNDLKTRLETADLRNSGLLGALNDTMD 2017
Cdd:TIGR01612 1449 NENVLLLFKNIEMADNKSQHILKIKKDNATNDHDFNINELKEHIDKSKGCKDEADKNAKAIEKNKELFEQYKKDVTELLN 1528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2018 KLSAItndtaaklqAVKEKAREANDTAKAVLAQVKDLH-----------QNLDGLKQNYNKLADSVAKTNavvkdpSKNK 2086
Cdd:TIGR01612 1529 KYSAL---------AIKNKFAKTKKDSEIIIKEIKDAHkkfileaekseQKIKEIKKEKFRIEDDAAKND------KSNK 1593
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2087 IIADAGTSVRNLEqeadrliDKLkpikelednLKknISEIKELINQARKQANSIKVSVSS 2146
Cdd:TIGR01612 1594 AAIDIQLSLENFE-------NKF---------LK--ISDIKKKINDCLKETESIEKKISS 1635
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1630-2172 |
5.85e-09 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 62.54 E-value: 5.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1630 QLAEGNVNTLVMETNELLTRATKVTADGEqtgqDAERTNsrAESLEEFIKGLVQDAEAINEKAVQLNETLGNQDKTAERN 1709
Cdd:PTZ00440 948 QLSDTKINNLKMQIEKTLEYYDKSKENIN----GNDGTH--LEKLDKEKDEWEHFKSEIDKLNVNYNILNKKIDDLIKKQ 1021
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1710 LEELQKEIDRMLKELRSK-DLQTQKEVAEDELVAAEGLLKRVN---KLFGEPRAQN-----EDMEKDLQQKLAEYKNKLD 1780
Cdd:PTZ00440 1022 HDDIIELIDKLIKEKGKEiEEKVDQYISLLEKMKTKLSSFHFNidiKKYKNPKIKEeikllEEKVEALLKKIDENKNKLI 1101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1781 DAWDLLREatdktrdaNRLSAANQKNMT--ILETKKEAIEGSKRQIENTLKEGNDILDEANRlLGEINSV-IDY----VD 1853
Cdd:PTZ00440 1102 EIKNKSHE--------HVVNADKEKNKQteHYNKKKKSLEKIYKQMEKTLKELENMNLEDIT-LNEVNEIeIEYerilID 1172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1854 DIKTKlppMSEElSDKIDDLAQEIKDRRlaEKVFQAEshaaqlNDSSAVLDGILDEaknisFNATAAFRAYSNIKDYIDE 1933
Cdd:PTZ00440 1173 HIVEQ---INNE-AKKSKTIMEEIESYK--KDIDQVK------KNMSKERNDHLTT-----FEYNAYYDKATASYENIEE 1235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1934 AEKVAREAKELAQGATKlaTSPQGLLKEDAKGSLQKSfrilneaKKLANDVKGNHNDLNDLKTRLETADLRNsgLLGALN 2013
Cdd:PTZ00440 1236 LTTEAKGLKGEANRSTN--VDELKEIKLQVFSYLQQV-------IKENNKMENALHEIKNMYEFLISIDSEK--ILKEIL 1304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2014 DTMDKLSAITNDTAAKL-------QAVKEKAREANDTAKAVLAQVKD--LHQNLDGLKQNYNKLADSVAKTNAVVKDPSK 2084
Cdd:PTZ00440 1305 NSTKKAEEFSNDAKKELektdnliKQVEAKIEQAKEHKNKIYGSLEDkqIDDEIKKIEQIKEEISNKRKEINKYLSNIKS 1384
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2085 NKIIADagTSVRNLEQEADrLIDKLKPIKELEDNLKK--NISEIKELINQARK---QANSIKVSVSSGGDCVRTYRPEIK 2159
Cdd:PTZ00440 1385 NKEKCD--LHVRNASRGKD-KIDFLNKHEAIEPSNSKevNIIKITDNINKCKQysnEAMETENKADENNDSIIKYEKEIT 1461
|
570
....*....|...
gi 117647249 2160 KGSYNNIVVHVKT 2172
Cdd:PTZ00440 1462 NILNNSSILGKKT 1474
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1523-1558 |
6.02e-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: 6.02e-09
10 20 30
....*....|....*....|....*....|....*.
gi 117647249 1523 CECDPYGSLPVPCDRVTGLCTCRPGATGRKCDGCEH 1558
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKP 36
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1102-1159 |
6.29e-09 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 53.90 E-value: 6.29e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 117647249 1102 CDCFLPGTDATTCDLETrkcscsdqtGQCSCKVNVEGVHCDRCRPGKFGlDAKNPLGC 1159
Cdd:cd00055 2 CDCNGHGSLSGQCDPGT---------GQCECKPNTTGRRCDRCAPGYYG-LPSQGGGC 49
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1853-2142 |
6.33e-09 |
|
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: 60.46 E-value: 6.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1853 DDIKTKLPpmseELSDKIDDLAQEIKDRRLAEKVFQaeSHAAQLNDSsaVLDGILDEAKNISFNATAA----FRAYSNIK 1928
Cdd:cd22656 26 EEYRKRLG----ISSDIDDKLSSDFDPLLDAYKSIK--DHCTDFKDD--TYPSIVSLAGDIYNYAQNAggtiDSYYAEIL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1929 DYIDEA-----EKVAREAKELAQGATKLatspqglLKEDAKgslqksfRILNEAKKLANDVKGNHNDLNDLKTRLETADL 2003
Cdd:cd22656 98 ELIDDLadatdDEELEEAKKTIKALLDD-------LLKEAK-------KYQDKAAKVVDKLTDFENQTEKDQTALETLEK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2004 RNSGLLGalndtmDKLSAITNDTAAKLQAVKEKAREandtakavlAQVKDLHQNLDGLKQNYNKLADSVAKTNAVVKDps 2083
Cdd:cd22656 164 ALKDLLT------DEGGAIARKEIKDLQKELEKLNE---------EYAAKLKAKIDELKALIADDEAKLAAALRLIAD-- 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 117647249 2084 knkiIADAGTSVRNLEQEADRLIDKLKPIKELEDNLKKNISEIKELINQARKQANSIKV 2142
Cdd:cd22656 227 ----LTAADTDLDNLLALIGPAIPALEKLQGAWQAIATDLDSLKDLLEDDISKIPAAIL 281
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
861-904 |
7.36e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 53.85 E-value: 7.36e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 117647249 861 CQCNdnLDYSIPGSCDSLSGSCLiCKPGTTGRYCELCADGYFGD 904
Cdd:smart00180 1 CDCD--PGGSASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD 41
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1711-2137 |
7.55e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 62.01 E-value: 7.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1711 EELQKEIDRMLKELRskdlQTQKEVAEDELVAAEgLLKRVNKLFGEpRAQNEDMeKDLQQKLAEYKnklddAWDLLREAT 1790
Cdd:TIGR02169 166 AEFDRKKEKALEELE----EVEENIERLDLIIDE-KRQQLERLRRE-REKAERY-QALLKEKREYE-----GYELLKEKE 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1791 DKTRDANRLSAAnqknmtiLETKKEAIEGSKRQIENTLKEgndiLDEANRLLGEINSVIDYVDD-----IKTKLPPMSEE 1865
Cdd:TIGR02169 234 ALERQKEAIERQ-------LASLEEELEKLTEEISELEKR----LEEIEQLLEELNKKIKDLGEeeqlrVKEKIGELEAE 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1866 LS---DKIDDLAQEIKDrrLAEKVFQAESHaaqlndssavLDGILDEAKNISfnataafraySNIKDYIDEAEKVAREAK 1942
Cdd:TIGR02169 303 IAsleRSIAEKERELED--AEERLAKLEAE----------IDKLLAEIEELE----------REIEEERKRRDKLTEEYA 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1943 ELAQgatKLATSPQGLLKEDAKgsLQKSFRILNEAKKLANDVKGNHNDLNDLKTRLEtadlrnsgllgalnDTMDKLSAI 2022
Cdd:TIGR02169 361 ELKE---ELEDLRAELEEVDKE--FAETRDELKDYREKLEKLKREINELKRELDRLQ--------------EELQRLSEE 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2023 TNDTAAKLQAVKEKAREANDTAKAVLAQVKDLHQNLDGLKqnynkladsvaktnavvkdpsknKIIADAGTSVRNLEQEA 2102
Cdd:TIGR02169 422 LADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLA-----------------------ADLSKYEQELYDLKEEY 478
|
410 420 430
....*....|....*....|....*....|....*
gi 117647249 2103 DRLidklkpikelEDNLKKNISEIKELinQARKQA 2137
Cdd:TIGR02169 479 DRV----------EKELSKLQRELAEA--EAQARA 501
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1658-2131 |
8.98e-09 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 61.77 E-value: 8.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1658 EQTGQDAERTNSRAESLEEFIKGLVQ-DAEAINEKAVQLNE----TLGNQDKTAERNLEELQKEIDRMLKEL-RSKDLQT 1731
Cdd:PTZ00440 1176 EQINNEAKKSKTIMEEIESYKKDIDQvKKNMSKERNDHLTTfeynAYYDKATASYENIEELTTEAKGLKGEAnRSTNVDE 1255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1732 QKEVAEDelvaaegllkrVNKLFGEPRAQNEDMEKDLQQK---------------LAEYKNKLDDAWDLLREATDKTRDA 1796
Cdd:PTZ00440 1256 LKEIKLQ-----------VFSYLQQVIKENNKMENALHEIknmyeflisidsekiLKEILNSTKKAEEFSNDAKKELEKT 1324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1797 NRLSAANQKNMTILETKKEAIEGS--KRQIENTLKEGNDILDEANRLLGEINSVIDYVDDIKTKLppMSEELS-----DK 1869
Cdd:PTZ00440 1325 DNLIKQVEAKIEQAKEHKNKIYGSleDKQIDDEIKKIEQIKEEISNKRKEINKYLSNIKSNKEKC--DLHVRNasrgkDK 1402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1870 IDDL----------AQEIKDRRLAEKVFQAESHAAQLNDS----SAVLDGILDEAKNIS--FNataafraYSNIKDYIDE 1933
Cdd:PTZ00440 1403 IDFLnkheaiepsnSKEVNIIKITDNINKCKQYSNEAMETenkaDENNDSIIKYEKEITniLN-------NSSILGKKTK 1475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1934 AEKVAREAKELAQGATKLATSPQGLLKedakgSLQKSFRILNEAKK-------LAND---------------VKGNHNDL 1991
Cdd:PTZ00440 1476 LEKKKKEATNIMDDINGEHSIIKTKLT-----KSSEKLNQLNEQPNikregdvLNNDkstiayetiqynlgrVKHNLLNI 1550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1992 NDLKTRLETadlrnsgLLGALNDTMDKLSAITNDTAAK-LQAVKEKarEANDTAKavLAQVKDLHQNLdglKQNYNKLAD 2070
Cdd:PTZ00440 1551 LNIKDEIET-------ILNKAQDLMRDISKISKIVENKnLENLNDK--EADYVKY--LDNILKEKQLM---EAEYKKLNE 1616
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 117647249 2071 SVAKTNAVVKDPSKNKIIADagtsVRNLEQeadrlidklkpIKELEDNLKKNISEIKELIN 2131
Cdd:PTZ00440 1617 IYSDVDNIEKELKKHKKNYE----IGLLEK-----------VIEINKNIKLYMDSTKESLN 1662
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1665-2160 |
9.93e-09 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 61.46 E-value: 9.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1665 ERTNSRAESLEEFIKGL---VQDAEAINEKAVQLNETLGNQDKtaerNLEELQKEIDRMLKELrsKDLQTQKEVAEDELV 1741
Cdd:PRK01156 162 NSLERNYDKLKDVIDMLraeISNIDYLEEKLKSSNLELENIKK----QIADDEKSHSITLKEI--ERLSIEYNNAMDDYN 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1742 AAEGLLKRVNKLfgepraqnEDMEKDLQQKLAEYKNKLDDAWDLLREATDKTRDANRL--SAANQKNMTI---------L 1810
Cdd:PRK01156 236 NLKSALNELSSL--------EDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIinDPVYKNRNYIndyfkykndI 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1811 ETKKEAIEGSKRQI---ENTLKEGNDI-------------LDEANRLLGEI-------NSVIDYVDDIKTKLppmsEELS 1867
Cdd:PRK01156 308 ENKKQILSNIDAEInkyHAIIKKLSVLqkdyndyikkksrYDDLNNQILELegyemdyNSYLKSIESLKKKI----EEYS 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1868 DKIDDLAQEIKdRRLAEKVFQAESHAAQLNDSSAVLDGIldEAKNISFNATaafraysnIKDYIDEAEKVAREAKEL-AQ 1946
Cdd:PRK01156 384 KNIERMSAFIS-EILKIQEIDPDAIKKELNEINVKLQDI--SSKVSSLNQR--------IRALRENLDELSRNMEMLnGQ 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1947 G-----ATKLATSPQGLLKEDAKgslQKSFRILNEAKKLANDVKGNHNDLNDLKTRLETADLRNSGLLGALNDTMDKLSA 2021
Cdd:PRK01156 453 SvcpvcGTTLGEEKSNHIINHYN---EKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARA 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2022 ITNDTAAKLQAVKEKareaNDTAKAVLAQVKDLH-QNLDGLKQNYNKLA---DSVAKTNAVVKDPSKNKIIADA------ 2091
Cdd:PRK01156 530 DLEDIKIKINELKDK----HDKYEEIKNRYKSLKlEDLDSKRTSWLNALaviSLIDIETNRSRSNEIKKQLNDLesrlqe 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2092 ------------GTSVRNLEQEADRLIDKLKPIKELE----------DNLKKNISEIKELI-----------------NQ 2132
Cdd:PRK01156 606 ieigfpddksyiDKSIREIENEANNLNNKYNEIQENKilieklrgkiDNYKKQIAEIDSIIpdlkeitsrindiednlKK 685
|
570 580
....*....|....*....|....*...
gi 117647249 2133 ARKQANSIKVSVSSGGDCVRTYRPEIKK 2160
Cdd:PRK01156 686 SRKALDDAKANRARLESTIEILRTRINE 713
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1665-1909 |
1.08e-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: 61.24 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1665 ERTNSRAESLEEFIKGLVQDAEAINEKAVQLNETLgnqdktaernlEELQKEIDRM-----------LKELRSK--DLQT 1731
Cdd:TIGR02169 240 EAIERQLASLEEELEKLTEEISELEKRLEEIEQLL-----------EELNKKIKDLgeeeqlrvkekIGELEAEiaSLER 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1732 QKEVAEDELVAAEGLLKRVNKLFGEPRAQNEDMEKDLQQKLAEyKNKLDDAWDLLREATDKTR-DANRLSAANQKNMTIL 1810
Cdd:TIGR02169 309 SIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKR-RDKLTEEYAELKEELEDLRaELEEVDKEFAETRDEL 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1811 ETKKEAIEGSKRQIENTLKEGNDILDEANRLLGEINSVIDYVDDIKTKLPPMSEELSDKIDDL-AQEIKDRRLAEKVFQA 1889
Cdd:TIGR02169 388 KDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIkKQEWKLEQLAADLSKY 467
|
250 260
....*....|....*....|
gi 117647249 1890 EShaaQLNDSSAVLDGILDE 1909
Cdd:TIGR02169 468 EQ---ELYDLKEEYDRVEKE 484
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1633-2166 |
1.46e-08 |
|
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: 61.22 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1633 EGNVNTLVMETNELLTRATKVtadgeQTGQDAERTNSRAESLEEFIKGLVQDAEAINEKAVQLNETLGNQDKTAE-RNLE 1711
Cdd:TIGR01612 721 ELHLSNIENKKNELLDIIVEI-----KKHIHGEINKDLNKILEDFKNKEKELSNKINDYAKEKDELNKYKSKISEiKNHY 795
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1712 ELQKEIDRMLKELRSKDLQTQKE------VAEDELVAA--------EGLLKRVNKLFGEPRAQNEDMEKDLQQ------- 1770
Cdd:TIGR01612 796 NDQINIDNIKDEDAKQNYDKSKEyiktisIKEDEIFKIinemkfmkDDFLNKVDKFINFENNCKEKIDSEHEQfaeltnk 875
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1771 --------KLAEYKNKLDDAWDLLREAT----DKTRDANRLSAANQKnMTILETKKEAIEgSKRQIENTLKEgndILDEA 1838
Cdd:TIGR01612 876 ikaeisddKLNDYEKKFNDSKSLINEINksieEEYQNINTLKKVDEY-IKICENTKESIE-KFHNKQNILKE---ILNKN 950
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1839 NRLLGEINSV-IDYVDDIKTKLppmseelSDKIDDLaqeikdrrlaEKVFQAEShaaqLNDSsavldgildEAKNisfna 1917
Cdd:TIGR01612 951 IDTIKESNLIeKSYKDKFDNTL-------IDKINEL----------DKAFKDAS----LNDY---------EAKN----- 995
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1918 TAAFRAYSNIKDYI------------DEAEKVAREAKELAQGATK--------LATSPQGLLKEDAKgSLQKSFRILNea 1977
Cdd:TIGR01612 996 NELIKYFNDLKANLgknkenmlyhqfDEKEKATNDIEQKIEDANKnipnieiaIHTSIYNIIDEIEK-EIGKNIELLN-- 1072
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1978 KKLANDVKGNHNDLNDLKTRLETADLRNSGLLGALNDTmDKLSAITNDTAAKLQAVKEKAREandtakavLAQVKDLHQN 2057
Cdd:TIGR01612 1073 KEILEEAEINITNFNEIKEKLKHYNFDDFGKEENIKYA-DEINKIKDDIKNLDQKIDHHIKA--------LEEIKKKSEN 1143
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2058 -LDGLKQNYNKLADsVAKTNAVVKDPsknkiiadagtsvRNLEQEADRLIDKLKPIKELEDNLKKNISEIKElINQARKQ 2136
Cdd:TIGR01612 1144 yIDEIKAQINDLED-VADKAISNDDP-------------EEIEKKIENIVTKIDKKKNIYDEIKKLLNEIAE-IEKDKTS 1208
|
570 580 590
....*....|....*....|....*....|....
gi 117647249 2137 ANSIK-VSVSSGGDCVRTYRPEI---KKGSYNNI 2166
Cdd:TIGR01612 1209 LEEVKgINLSYGKNLGKLFLEKIdeeKKKSEHMI 1242
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1708-1884 |
1.57e-08 |
|
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: 58.01 E-value: 1.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1708 RNLEELQkEIDRMLKELRS--KDLQTQKEVAEDELVAAEGLLKRVNKLFGEPRAQNEDME---KDLQQKLAEYKNKLDDA 1782
Cdd:COG1579 7 RALLDLQ-ELDSELDRLEHrlKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLEleiEEVEARIKKYEEQLGNV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1783 WD------LLREATDKTRDANRLSAANQKNMTILETKKEAIEGSKRQIENTLKEGNDILDEANRLLGEINSVIdyvddik 1856
Cdd:COG1579 86 RNnkeyeaLQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAEL------- 158
|
170 180
....*....|....*....|....*...
gi 117647249 1857 tklppmsEELSDKIDDLAQEIKDRRLAE 1884
Cdd:COG1579 159 -------EELEAEREELAAKIPPELLAL 179
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1857-2141 |
1.96e-08 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 58.77 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1857 TKLPPMSEELSDKIDDLAQEIKD--RRLAEKVFQAESHAAQLNDSSAVLDGILDEAKNI-----SFNAtaafraysNIKD 1929
Cdd:COG1340 4 DELSSSLEELEEKIEELREEIEElkEKRDELNEELKELAEKRDELNAQVKELREEAQELrekrdELNE--------KVKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1930 YIDEAEKVAREAKELAQGATKLatspqgllKEDAKgSLQKSFRILNEAKKlandvkgnhnDLNDLKTRLETADLRnsglL 2009
Cdd:COG1340 76 LKEERDELNEKLNELREELDEL--------RKELA-ELNKAGGSIDKLRK----------EIERLEWRQQTEVLS----P 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2010 GALNDTMDKLSAITN--DTAAKLQAVKEKAREANDTAKAVLAQVKDLHQNLDGLKQNYNKLADSVAKTnavvkdpsKNKi 2087
Cdd:COG1340 133 EEEKELVEKIKELEKelEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIEL--------YKE- 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 117647249 2088 iADAgtsvrnLEQEADRLIDKLKPIKELEDNLKKNISEIKELINQARKQANSIK 2141
Cdd:COG1340 204 -ADE------LRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLR 250
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
409-461 |
2.76e-08 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 52.36 E-value: 2.76e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 117647249 409 PCHCDPTGSLSEVCVKDEkyaqrglkpGSCHCKTGFGGVNCDRCVRGYHGYPD 461
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. |
861-907 |
3.95e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 51.59 E-value: 3.95e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 117647249 861 CQCNDNLDYSipGSCDSLSGSCLiCKPGTTGRYCELCADGYFGDAVN 907
Cdd:pfam00053 1 CDCNPHGSLS--DTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSD 44
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1622-2158 |
4.65e-08 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 59.42 E-value: 4.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1622 QRAPERLIQLA------EGNVNTLVMETNEL---LTRATKVTADGEQTgqdAERTNSRAESLEEfikgLVQDAEAINEKA 1692
Cdd:pfam01576 15 QKVKERQQKAEselkelEKKHQQLCEEKNALqeqLQAETELCAEAEEM---RARLAARKQELEE----ILHELESRLEEE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1693 VQLNETLGNQDKTAERNLEELQKEIDRmlKELRSKDLQTQKevaedelVAAEGLLKRVNKLFGEPRAQNEDMEKdlQQKL 1772
Cdd:pfam01576 88 EERSQQLQNEKKKMQQHIQDLEEQLDE--EEAARQKLQLEK-------VTTEAKIKKLEEDILLLEDQNSKLSK--ERKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1773 AEykNKLDDAWDLLREATDKTRDANRLSAANQKNMTILET--KKEA-----IEGSKRQIEntlKEGNDILDEANRLLGEI 1845
Cdd:pfam01576 157 LE--ERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEErlKKEEkgrqeLEKAKRKLE---GESTDLQEQIAELQAQI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1846 nsvidyvDDIKTKLPPMSEELSDKIDDLAQEIKDRRLAEK-VFQAESHAAQLN------------------DSSAVLDGI 1906
Cdd:pfam01576 232 -------AELRAQLAKKEEELQAALARLEEETAQKNNALKkIRELEAQISELQedleseraarnkaekqrrDLGEELEAL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1907 LDEAKNiSFNATAA---FRA-----YSNIKDYIDEaEKVAREAK--ELAQGATKLATSPQGLLKE--DAKGSLQKSFRIL 1974
Cdd:pfam01576 305 KTELED-TLDTTAAqqeLRSkreqeVTELKKALEE-ETRSHEAQlqEMRQKHTQALEELTEQLEQakRNKANLEKAKQAL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1975 -NEAKKLANDVKgnhnDLNDLKTRLETadlRNSGLLGALNDTMDKLSaitnDTaaklqavkEKAR-EANDTAKAVLAQVK 2052
Cdd:pfam01576 383 eSENAELQAELR----TLQQAKQDSEH---KRKKLEGQLQELQARLS----ES--------ERQRaELAEKLSKLQSELE 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2053 DLHQNLDGLKQNYNKLADSVAKTNAVVKD-------PSKNKIiaDAGTSVRNLEQEADRLIDKLKPIKELEDNLKKNISE 2125
Cdd:pfam01576 444 SVSSLLNEAEGKNIKLSKDVSSLESQLQDtqellqeETRQKL--NLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLST 521
|
570 580 590
....*....|....*....|....*....|...
gi 117647249 2126 IKELINQARKQANSIKVSVSSGGDCVRTYRPEI 2158
Cdd:pfam01576 522 LQAQLSDMKKKLEEDAGTLEALEEGKKRLQREL 554
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1607-1962 |
6.08e-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: 58.43 E-value: 6.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1607 GLENTTQELKHLLSPQRAPERLIQLAEgNVNTLVMETNELLTratkvtadgEQTGQDAERTNSRAESLEEFIKGLVQDAE 1686
Cdd:COG5185 227 EIINIEEALKGFQDPESELEDLAQTSD-KLEKLVEQNTDLRL---------EKLGENAESSKRLNENANNLIKQFENTKE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1687 AINEK-----AVQLNETLGNQDKTAERN--LEELQKEIDRMLKELRSKDLQTQKEVAEDElvaaEGLLKRVNKLFGEPR- 1758
Cdd:COG5185 297 KIAEYtksidIKKATESLEEQLAAAEAEqeLEESKRETETGIQNLTAEIEQGQESLTENL----EAIKEEIENIVGEVEl 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1759 AQNEDMEKDLQQKLAEYKNKLDDAwdlLREATDKTRDANrlsAANQKNMTILETKKEAIEGSKRQIENTlkegndiLDEA 1838
Cdd:COG5185 373 SKSSEELDSFKDTIESTKESLDEI---PQNQRGYAQEIL---ATLEDTLKAADRQIEELQRQIEQATSS-------NEEV 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1839 NRLLGEINSVIDYVDDiktklpPMSEELSDKIDDLAQEIKdRRLAEKVFQAESHAAQLNDSsavLDGILDEAKNISFNAT 1918
Cdd:COG5185 440 SKLLNELISELNKVMR------EADEESQSRLEEAYDEIN-RSVRSKKEDLNEELTQIESR---VSTLKATLEKLRAKLE 509
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 117647249 1919 aafRAYSNIKDYIDEAEKVAREAKELAQGATKLATSPQGLLKED 1962
Cdd:COG5185 510 ---RQLEGVRSKLDQVAESLKDFMRARGYAHILALENLIPASEL 550
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1688-1957 |
6.13e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 57.92 E-value: 6.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1688 INEKAVQLNEtLGNQDKTAERNLEELQKEIDRMLKELrsKDLQTQKEVAEDELVAAEGLLKRVNKLFgepRAQNEDMEKD 1767
Cdd:COG3883 18 IQAKQKELSE-LQAELEAAQAELDALQAELEELNEEY--NELQAELEALQAEIDKLQAEIAEAEAEI---EERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1768 LQqklAEYKNKLD-DAWDLLREATDKTRDANRLSAANQknmtiletkkeaiegskrqientlkegndILDEANRLLGEIN 1846
Cdd:COG3883 92 AR---ALYRSGGSvSYLDVLLGSESFSDFLDRLSALSK-----------------------------IADADADLLEELK 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1847 SVIDYVDDIKTKLPPMSEELSDKIDDLAQEIKDrrLAEKVFQAESHAAQLNDSSAVLDGILDEAKNISFNATAAFRAYSN 1926
Cdd:COG3883 140 ADKAELEAKKAELEAKLAELEALKAELEAAKAE--LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
250 260 270
....*....|....*....|....*....|.
gi 117647249 1927 IKDYIDEAEKVAREAKELAQGATKLATSPQG 1957
Cdd:COG3883 218 AAAAAAAAAAAAAAAAAAAAAAAAAAASAAG 248
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1416-1462 |
6.47e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 51.16 E-value: 6.47e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 117647249 1416 CQCN--GH-SSQCDPETSVCQnCQHHTAGDFCERCALGYYGIVrglPNDC 1462
Cdd:smart00180 1 CDCDpgGSaSGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDG---PPGC 46
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1658-2144 |
8.22e-08 |
|
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: 58.52 E-value: 8.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1658 EQTGQDAERTNSRAESLEEFIKglvqDAEAINEKAVQL-NETLGNQDKTAERNLEELQ-----------KEIDRMLKELR 1725
Cdd:TIGR01612 1229 EKIDEEKKKSEHMIKAMEAYIE----DLDEIKEKSPEIeNEMGIEMDIKAEMETFNIShdddkdhhiisKKHDENISDIR 1304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1726 SKDLQTQKEVAEDELVaaEGLLKRVNKLFGEPRAQNEDMEKDLQQKLAEYK----NKLDDAWDLLREATDKTRDANR-LS 1800
Cdd:TIGR01612 1305 EKSLKIIEDFSEESDI--NDIKKELQKNLLDAQKHNSDINLYLNEIANIYNilklNKIKKIIDEVKEYTKEIEENNKnIK 1382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1801 AANQKNMTILETKKEAI--EGSKRQIENTLkEGNDIldeanrllgeiNSVIDYVDDIKTKLppMSEElsDKIDDLAQEIK 1878
Cdd:TIGR01612 1383 DELDKSEKLIKKIKDDInlEECKSKIESTL-DDKDI-----------DECIKKIKELKNHI--LSEE--SNIDTYFKNAD 1446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1879 DRRlaEKVFQAESHAAQLNDSSAVldgILDEAKNisfNATAAFRAYSN-IKDYIDEAEKVAREAKElaqgaTKLATSPQG 1957
Cdd:TIGR01612 1447 ENN--ENVLLLFKNIEMADNKSQH---ILKIKKD---NATNDHDFNINeLKEHIDKSKGCKDEADK-----NAKAIEKNK 1513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1958 LLKEDAKgslQKSFRILNEAKKLA--NDVKGNHNDLNDLKTrlETADLRNSGLLGAlNDTMDKLSAITNDTAAklqaVKE 2035
Cdd:TIGR01612 1514 ELFEQYK---KDVTELLNKYSALAikNKFAKTKKDSEIIIK--EIKDAHKKFILEA-EKSEQKIKEIKKEKFR----IED 1583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2036 KAREANDTAKAVLaqvkDLHQNLDGLKQNYNKLADSVAKTNAVVKDP-SKNKIIADagTSVRNLEQEADRLIDKLKPIKE 2114
Cdd:TIGR01612 1584 DAAKNDKSNKAAI----DIQLSLENFENKFLKISDIKKKINDCLKETeSIEKKISS--FSIDSQDTELKENGDNLNSLQE 1657
|
490 500 510
....*....|....*....|....*....|...
gi 117647249 2115 LEDNLK---KNISEIKELINQARKQANSIKVSV 2144
Cdd:TIGR01612 1658 FLESLKdqkKNIEDKKKELDELDSEIEKIEIDV 1690
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1622-2131 |
9.49e-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: 58.14 E-value: 9.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1622 QRAPERLIQLAEgNVNTLVMETNELLTRATKVTADGEQTGQDAERTNSRAESLEEFIKGLVQDAEAINEKAVQLNETLGN 1701
Cdd:TIGR02168 326 EELESKLDELAE-ELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1702 QDKTAER---NLEELQKEI---DRMLKELRSKDLQTQKEVAEDELVAAEGLLKRVN---KLFGEPRAQNEDMEKDLQQKL 1772
Cdd:TIGR02168 405 LEARLERledRRERLQQEIeelLKKLEEAELKELQAELEELEEELEELQEELERLEealEELREELEEAEQALDAAEREL 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1773 AEYKNKLDDAWDLLREATDKTRDA-----NR-----------------------LSAANQKNMTILETK-----KEAIEG 1819
Cdd:TIGR02168 485 AQLQARLDSLERLQENLEGFSEGVkallkNQsglsgilgvlselisvdegyeaaIEAALGGRLQAVVVEnlnaaKKAIAF 564
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1820 SK-----------------RQIE----NTLKEGNDILDEANRLLG---EINSVIDY-------VDDIKTKLppmseELSD 1868
Cdd:TIGR02168 565 LKqnelgrvtflpldsikgTEIQgndrEILKNIEGFLGVAKDLVKfdpKLRKALSYllggvlvVDDLDNAL-----ELAK 639
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1869 KID-----------------------------DLAQEIKDRRLAEKVFQAESHAAQLndsSAVLDGILDEAKNISFNATA 1919
Cdd:TIGR02168 640 KLRpgyrivtldgdlvrpggvitggsaktnssILERRREIEELEEKIEELEEKIAEL---EKALAELRKELEELEEELEQ 716
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1920 AFRAYSNIKDYIDEAEKVAREAKELAQGATKLATSPQGLLKE------DAKGSLQKSFRILNEAKKLANDVKGnhnDLND 1993
Cdd:TIGR02168 717 LRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEleaeieELEERLEEAEEELAEAEAEIEELEA---QIEQ 793
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1994 LKTRLETADLRNSGLLGALNDT----------MDKLSAITNDTAAKLQAVKEKAREANDTAKAVLAQVKDLHQNLDGLKQ 2063
Cdd:TIGR02168 794 LKEELKALREALDELRAELTLLneeaanlrerLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELES 873
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 117647249 2064 NYNKLADSVAKTNAVVKDPSKNKI-----IADAGTSVRNLEQEADRLIDKLKPIKELEDNLKKNISEIKELIN 2131
Cdd:TIGR02168 874 ELEALLNERASLEEALALLRSELEelseeLRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLS 946
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1665-2141 |
1.01e-07 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 58.26 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1665 ERTNSRAESLEEFIKGLVQDAEAIN----EKAVQ--------------LNETLGNQDKTAE--RNLEELQKEIDRMLKEL 1724
Cdd:pfam01576 534 EEDAGTLEALEEGKKRLQRELEALTqqleEKAAAydklektknrlqqeLDDLLVDLDHQRQlvSNLEKKQKKFDQMLAEE 613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1725 R--SKDLQTQKEVAE-----------------DELVAAEGLLKRVNKLFgepRAQNEDM--EKD---------------L 1768
Cdd:pfam01576 614 KaiSARYAEERDRAEaeareketralslaralEEALEAKEELERTNKQL---RAEMEDLvsSKDdvgknvhelerskraL 690
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1769 QQKLAEYKNKLDDAWDLLREATD-KTRDANRLSAANQKNMTILETKKEAIEGSKRQIENTLKEGNDILDEANRLLGEINS 1847
Cdd:pfam01576 691 EQQVEEMKTQLEELEDELQATEDaKLRLEVNMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVA 770
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1848 VidyvddiKTKLPPMSEELSDKIDDlAQEIKDRRLAE-KVFQAE--SHAAQLNDSSAVLDGILDEAKnisfnataafray 1924
Cdd:pfam01576 771 A-------KKKLELDLKELEAQIDA-ANKGREEAVKQlKKLQAQmkDLQRELEEARASRDEILAQSK------------- 829
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1925 snikdyidEAEKVAR--EAkELAQGATKLATSpqgllkEDAKGSLQKSFRILneAKKLANDVKGNhNDLNDLKTRLET-- 2000
Cdd:pfam01576 830 --------ESEKKLKnlEA-ELLQLQEDLAAS------ERARRQAQQERDEL--ADEIASGASGK-SALQDEKRRLEAri 891
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2001 ADLRN-----SGLLGALNDTMDKLSAITNDTAAKLQAVKEKAREaNDTAKAVLA-QVKDLH---QNLDG-----LKQNYN 2066
Cdd:pfam01576 892 AQLEEeleeeQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQK-SESARQQLErQNKELKaklQEMEGtvkskFKSSIA 970
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 117647249 2067 KLADSVAKTNAVVKDPSKNKIIadAGTSVRNLEQeadrlidKLKPIKELEDNLKKNISEIKElinQARKQANSIK 2141
Cdd:pfam01576 971 ALEAKIAQLEEQLEQESRERQA--ANKLVRRTEK-------KLKEVLLQVEDERRHADQYKD---QAEKGNSRMK 1033
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1645-2141 |
1.41e-07 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 57.27 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1645 ELLTRATKVTADGEQTgQDAERTNSRAESLEEFIKGLVQDAEAINEKAVQLNETLGNQDKTAERNLEELQKEIDRMLKEL 1724
Cdd:COG5185 17 EGNANKELIEILLESS-KSEGKTLVFITILFFPLGISRDSLRVTLRSVINVLDGLNYQNDVKKSESSVKARKFLKEKKLD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1725 RSKDLQTQKEVA-----EDELVAAEGLLKRVNKLfgeprAQNEDMEKDLQQKLAEYKNklDDAwDLLREATDKTRDANRL 1799
Cdd:COG5185 96 TKILQEYVNSLIklpnyEWSADILISLLYLYKSE-----IVALKDELIKVEKLDEIAD--IEA-SYGEVETGIIKDIFGK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1800 SAANQKNMTILETKKEAIEGSKRQIENTLKEGNDILDEANRLLGEINSVIDY------------------VDDIKTKLPP 1861
Cdd:COG5185 168 LTQELNQNLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGSEStllekakeiinieealkgFQDPESELED 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1862 MsEELSDKIDDLAQEIKDRRLAEKVFQAEShaaqlndssavldgildeAKNISFNATAAFRAYSNIKDYIDEAEKVAREA 1941
Cdd:COG5185 248 L-AQTSDKLEKLVEQNTDLRLEKLGENAES------------------SKRLNENANNLIKQFENTKEKIAEYTKSIDIK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1942 KELAQGAtklatspqgllKEDAKGSLQKSF--RILNEAKKLANDVKGNHNDLNDLKTRLETADLRNSGLLGA-------- 2011
Cdd:COG5185 309 KATESLE-----------EQLAAAEAEQELeeSKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEvelsksse 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2012 -LNDTMDKLSAITNDTAAKLQAVKEKAREA----NDTAKAVLAQVKDLHQNLDGLKQNY-------NKLADSVAKTNAVV 2079
Cdd:COG5185 378 eLDSFKDTIESTKESLDEIPQNQRGYAQEIlatlEDTLKAADRQIEELQRQIEQATSSNeevskllNELISELNKVMREA 457
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 117647249 2080 KDPSKNKIIADAGTSVRNLEQEADRLIDKLKPIK-----------ELEDNLKKNISEIKELINQarkQANSIK 2141
Cdd:COG5185 458 DEESQSRLEEAYDEINRSVRSKKEDLNEELTQIEsrvstlkatleKLRAKLERQLEGVRSKLDQ---VAESLK 527
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1688-2166 |
2.00e-07 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 57.53 E-value: 2.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1688 INEKAVQLNETLGNQDKTAERNLEELQKEIDR------------MLKELRSKDLQTQKEVAEDELVAAEGLLKRVNKL-- 1753
Cdd:PTZ00440 1764 MKEKLDELSKMCKQQYNIVDEGYNYIKKKIEYiktlndennlsdSLNQAEDKNKEVANLTHYTNKNEAKNLLGHVVKSan 1843
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1754 ---------FGEPRAQNEDMEKDLQQKLAEYKNKLDDAWDLLREATDKTRDANRLSAANQKNMTILETKKEaIEGSKRQI 1824
Cdd:PTZ00440 1844 figikimtgLQPTELTPDASLETAPELTFESENNSDLELDHLSSNKNELDVYKNIQDAYKSSLQILKYSDD-IDKKQRDC 1922
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1825 ENTLKEGNDI---LDEANRLLGEINSVIDYVDDIktklppmseelSDKIDDLAQEIKdrrlaekvfqaESHAAQLNDSSa 1901
Cdd:PTZ00440 1923 NKLVEDGNEIylkSTAINELKNMINSVKNKESAI-----------SNKIDNVSNKLS-----------ELNKITCNDES- 1979
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1902 vLDGILDEAKNISFNataafRAYSNikdYIDEAEKVAREAKelAQGATKLATSPQGLLKEdakgsLQKSFRILNEAKKLA 1981
Cdd:PTZ00440 1980 -YDEILEKEEYEELK-----DLRNS---FNQEKAETLNNLK--LNKIKEDFNSYKNLLDE-----LEKSVKTLKASENIK 2043
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1982 NDVKGNHNDLNDLKTRLETADLRNSGLLGALNDTMDKLSAITNdtaAKLQAVKEK-AREANDTAKAVLAQVKDLHQNLDG 2060
Cdd:PTZ00440 2044 KIVENKKTSIDAINTNIEDIEKEIESINPSLDELLKKGHKIEI---SRYTSIIDNvQTKISNDSKNINDIEKKAQIYLAY 2120
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2061 LKQNYNKLADSVAKTNAVVK-------DPSK----NKIIAD---AGTSVRNL-------------EQEADRLIDKLKPIK 2113
Cdd:PTZ00440 2121 IKNNYNSIKKDISTLNEYFDekqvsnyILTNidkaNKLSSElseAVTNSEEIienikkeiieineNTEMNTLENTADKLK 2200
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 117647249 2114 ELEDNLKKNiseiKELINQARKQANSIKVSvssggdcvrtyrpEIKKGS--YNNI 2166
Cdd:PTZ00440 2201 ELYENLKKK----KNIINNIYKKINFIKLQ-------------EIENSSekYNDI 2238
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1672-2108 |
2.02e-07 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 56.77 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1672 ESLEEFikglvqdaEAINEKAVQL-NETLGNqdktAERNLEELQKEIDRMlkelRSKDLQTQKEVAEDELVAAEGLLKRV 1750
Cdd:PRK04778 61 QSEEKF--------EEWRQKWDEIvTNSLPD----IEEQLFEAEELNDKF----RFRKAKHEINEIESLLDLIEEDIEQI 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1751 NKLFGEPRAQNEDMEKDLQQKLAEYKNklddawdlLReatdKTRDANRLS--AANQKnmtiLETKKEAIEGSKRQIENTL 1828
Cdd:PRK04778 125 LEELQELLESEEKNREEVEQLKDLYRE--------LR----KSLLANRFSfgPALDE----LEKQLENLEEEFSQFVELT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1829 KEGN-----DILDEANRLLGEINsviDYVDDIktklPPMSEELSDKIDDLAQEIKD--RRLAEK-----VFQAESHAAQL 1896
Cdd:PRK04778 189 ESGDyvearEILDQLEEELAALE---QIMEEI----PELLKELQTELPDQLQELKAgyRELVEEgyhldHLDIEKEIQDL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1897 NDS-SAVLDGI----LDEAKNIsfNAtaafraysNIKDYID------EAE-----KVAREAKELAQGATKLATSPQGLLK 1960
Cdd:PRK04778 262 KEQiDENLALLeeldLDEAEEK--NE--------EIQERIDqlydilEREvkarkYVEKNSDTLPDFLEHAKEQNKELKE 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1961 EDAkgSLQKSFRI----LNEAKKLANDVKGNHNDLNDLKTRLETADLRNSGLLGALNDTMDKLSAITN---DTAAKLQAV 2033
Cdd:PRK04778 332 EID--RVKQSYTLneseLESVRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKeqeKLSEMLQGL 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2034 KEKAREANDTAKAVlaqVKDLH--------QNLDGLKQNY-NKLADSVAKTNAVVKDPSKNKI--------IADAGTSVR 2096
Cdd:PRK04778 410 RKDELEAREKLERY---RNKLHeikrylekSNLPGLPEDYlEMFFEVSDEIEALAEELEEKPInmeavnrlLEEATEDVE 486
|
490
....*....|..
gi 117647249 2097 NLEQEADRLIDK 2108
Cdd:PRK04778 487 TLEEETEELVEN 498
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1659-2110 |
2.04e-07 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 57.14 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1659 QTGQDAERTnsRAESLEEFI-KGLVQDAEAINEKAVQLNETLGNQD--KTAERNLEELQKEIDRMLKELRSKD------- 1728
Cdd:pfam10174 344 QTEVDALRL--RLEEKESFLnKKTKQLQDLTEEKSTLAGEIRDLKDmlDVKERKINVLQKKIENLQEQLRDKDkqlaglk 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1729 -----LQTQKEVAEDELVAAEGLLKRVNKLFGEPRAQNEDMEKDLQQKLAEYKNKLDDAWD----LLREATDKTRDANRL 1799
Cdd:pfam10174 422 ervksLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERLEELESLKKENKDLKEkvsaLQPELTEKESSLIDL 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1800 --SAANQ-----------KNMTI-LETKKEaiEGSKrqIENTLKEGNDILDEANrllgeinsvidyvddiktklppMSEE 1865
Cdd:pfam10174 502 keHASSLassglkkdsklKSLEIaVEQKKE--ECSK--LENQLKKAHNAEEAVR----------------------TNPE 555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1866 LSDKIDDLAQEIKdrRLAEkvfqaESHAAQlndsSAV--LDGILDEAKNisfnataafraYSNIKD-YIDEAEKVA-REA 1941
Cdd:pfam10174 556 INDRIRLLEQEVA--RYKE-----ESGKAQ----AEVerLLGILREVEN-----------EKNDKDkKIAELESLTlRQM 613
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1942 KELAQGATKLATSPQGLLKEDAKgslqksfrILNEAKKLANDVKGNHndlndLKTRLETadlrnsgLLGALNDTMDKLSA 2021
Cdd:pfam10174 614 KEQNKKVANIKHGQQEMKKKGAQ--------LLEEARRREDNLADNS-----QQLQLEE-------LMGALEKTRQELDA 673
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2022 ITNDTAAKLQAVKEKAREANdtaKAVLAQVKDLHQNLDgLKQNYNKLADSVAKTN-AVVK-DPSKNKIIADagtSVRNLE 2099
Cdd:pfam10174 674 TKARLSSTQQSLAEKDGHLT---NLRAERRKQLEEILE-MKQEALLAAISEKDANiALLElSSSKKKKTQE---EVMALK 746
|
490
....*....|.
gi 117647249 2100 QEADRLIDKLK 2110
Cdd:pfam10174 747 REKDRLVHQLK 757
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
410-462 |
2.24e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 49.62 E-value: 2.24e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 117647249 410 CHCDPTGSLSEVCVKDEkyaqrglkpGSCHCKTGFGGVNCDRCVRGYHG--YPDC 462
Cdd:smart00180 1 CDCDPGGSASGTCDPDT---------GQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
464-512 |
2.84e-07 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 49.27 E-value: 2.84e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 117647249 464 PCNCSGLGSTNE--DPCVGPCSCKENVEGEDCSRCKSGFFNLQEDNQkGCE 512
Cdd:cd00055 1 PCDCNGHGSLSGqcDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGG-GCQ 50
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1762-2110 |
3.31e-07 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 54.92 E-value: 3.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1762 EDMEKDLQQKLAEYKNKLDDAWDLLREATDKTRD-ANRLSAANQKNMTILETKKEAIEgSKRQIENTLKEGNDILDEANR 1840
Cdd:COG1340 7 SSSLEELEEKIEELREEIEELKEKRDELNEELKElAEKRDELNAQVKELREEAQELRE-KRDELNEKVKELKEERDELNE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1841 llgEINSVIDYVDDIKTKLPPMSEELSDkIDDLAQEIkdRRLaEKVFQaeshaaqlndsSAVLDgiLDEAKNIsfnataa 1920
Cdd:COG1340 86 ---KLNELREELDELRKELAELNKAGGS-IDKLRKEI--ERL-EWRQQ-----------TEVLS--PEEEKEL------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1921 fraysnIKDyIDEAEKVAREAKELAQGATKLATspqgLLKEdakgslqksfriLNEAKKLANDVkgnHNDLNDLktrlet 2000
Cdd:COG1340 139 ------VEK-IKELEKELEKAKKALEKNEKLKE----LRAE------------LKELRKEAEEI---HKKIKEL------ 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2001 adlrnSGLLGALNDTMDKLSAitndtaaKLQAVKEKAREANDTAKAVLAQVKDLHQNLDGLKQNYNKLADSVAKTNAVVK 2080
Cdd:COG1340 187 -----AEEAQELHEEMIELYK-------EADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQR 254
|
330 340 350
....*....|....*....|....*....|
gi 117647249 2081 DPSKNKIIADagtsvrnLEQEADRLIDKLK 2110
Cdd:COG1340 255 ALKREKEKEE-------LEEKAEEIFEKLK 277
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1682-1881 |
3.36e-07 |
|
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: 53.60 E-value: 3.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1682 VQDAEA-INEKAVQLNETLGNQDktaERNLEELQKEIDRMLKEL-----RSKDLQTQ-KEVAEDELVAAEGLLKRVNKLf 1754
Cdd:cd00176 9 ADELEAwLSEKEELLSSTDYGDD---LESVEALLKKHEALEAELaaheeRVEALNELgEQLIEEGHPDAEEIQERLEEL- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1755 gepraqnEDMEKDLQQKLAEYKNKLDDAWDLLRE----------ATDKTRDANRLSAAnqKNMTILETKKEAIEGSKRQI 1824
Cdd:cd00176 85 -------NQRWEELRELAEERRQRLEEALDLQQFfrdaddleqwLEEKEAALASEDLG--KDLESVEELLKKHKELEEEL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 117647249 1825 ENTLKEGNDILDEANRLLGEINSviDYVDDIKTKLppmsEELSDKIDDLAQEIKDRR 1881
Cdd:cd00176 156 EAHEPRLKSLNELAEELLEEGHP--DADEEIEEKL----EELNERWEELLELAEERQ 206
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1929-2142 |
3.79e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 55.29 E-value: 3.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1929 DYIDEAEKVAREAKELAQGATKLATSpqgLLKEDAKGSLQKSFRILNEAKKLANDVKGNHNDLNDLKTRLETAD---LRN 2005
Cdd:COG4372 2 DRLGEKVGKARLSLFGLRPKTGILIA---ALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARselEQL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2006 SGLLGALNDTMDKLSAITNDTAAKLQAVKEKAREANDTAKAVLAQVKDLHQNLDGLKQNYNKLADSVAktnavvkdpSKN 2085
Cdd:COG4372 79 EEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIA---------ERE 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 117647249 2086 KIIADAGTSVRNLEQEADRLIDKLKPIKElednlKKNISEIKELINQARKQANSIKV 2142
Cdd:COG4372 150 EELKELEEQLESLQEELAALEQELQALSE-----AEAEQALDELLKEANRNAEKEEE 201
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
753-795 |
4.16e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 48.85 E-value: 4.16e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 117647249 753 CQCF---AHAEACDDITGECLnCKDHTGGPYCNECLPGFYGDPTRG 795
Cdd:smart00180 1 CDCDpggSASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1613-1980 |
5.70e-07 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 55.60 E-value: 5.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1613 QELKHLLSPQRaperliQLAEGNVNTLVMETNELLTRatkvtadgeqTGQDAER--TNSRAESlEEFIKGLVQDAEAINE 1690
Cdd:NF041483 130 QQLDQELAERR------QTVESHVNENVAWAEQLRAR----------TESQARRllDESRAEA-EQALAAARAEAERLAE 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1691 KAVQlneTLGNQDKTAERNLEEL----QKEIDRMLKELrskdlQTQKEVAEDElvaAEGLLKRVNKLFGEPRAQNEDMEK 1766
Cdd:NF041483 193 EARQ---RLGSEAESARAEAEAIlrraRKDAERLLNAA-----STQAQEATDH---AEQLRSSTAAESDQARRQAAELSR 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1767 DLQQKLAEYKNKLD----DAWDLLREAtdKTRDANRLSAANQKNMTILETKKEAIegsKRQIENTLKEGNDILDEANRLL 1842
Cdd:NF041483 262 AAEQRMQEAEEALRearaEAEKVVAEA--KEAAAKQLASAESANEQRTRTAKEEI---ARLVGEATKEAEALKAEAEQAL 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1843 GeinsvidyvdDIKTKLPPMSEELSDKIDDLAqeikdrrlaekvfqAESHAAQLNDSSAVLDGILDEAkniSFNATAAFR 1922
Cdd:NF041483 337 A----------DARAEAEKLVAEAAEKARTVA--------------AEDTAAQLAKAARTAEEVLTKA---SEDAKATTR 389
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 117647249 1923 AYSnikdyiDEAEKVAREAK----ELAQGATKLATSPQGLLKEDAKGSLQKSFRILNEAKKL 1980
Cdd:NF041483 390 AAA------EEAERIRREAEaeadRLRGEAADQAEQLKGAAKDDTKEYRAKTVELQEEARRL 445
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1810-2144 |
6.35e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.46 E-value: 6.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1810 LETKKEAIEGSKRQIENTLKEGNDILDEANRLLGEINSVIDYVDDIKTKLPPMSEELSDKIDDLAQEIKD---------R 1880
Cdd:TIGR02169 686 LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENvkselkeleA 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1881 RLAEKVFQAESHAAQLNDSSAVLDGilDEAKNISfnataafRAYSNIKDYIDEAEKVAREAKElaqgatklATSPQGLLK 1960
Cdd:TIGR02169 766 RIEELEEDLHKLEEALNDLEARLSH--SRIPEIQ-------AELSKLEEEVSRIEARLREIEQ--------KLNRLTLEK 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1961 EDAKGSLQKSFRILNEAKklaNDVKGNHNDLNDLKTRLETADLRNSGLLGALNDTMDKLSAITNDTA---AKLQAVKEKA 2037
Cdd:TIGR02169 829 EYLEKEIQELQEQRIDLK---EQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDeleAQLRELERKI 905
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2038 REANDTAKAVLAQVKDLHQNLDGLKQNYNKLADSVAktnAVVKDPSKNKIIADAGTSVRNLE--------------QEAD 2103
Cdd:TIGR02169 906 EELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKG---EDEEIPEEELSLEDVQAELQRVEeeiralepvnmlaiQEYE 982
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 117647249 2104 RLIDKLKPIKELEDNLKKNISEIKELINQARKQANSIKVSV 2144
Cdd:TIGR02169 983 EVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREVFMEA 1023
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1626-2181 |
6.86e-07 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 55.61 E-value: 6.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1626 ERLIQLAEGNVNTLVMETNELLTRATKVtadgeqtgQDAERTNSRAESLEEFIKGLVQDAEAInEKAVQlnetlgNQDKT 1705
Cdd:PTZ00440 149 EPLNEEIIKNIEQCLGNKNDLDNLIIVL--------ENPEKYNVRKTLYDEKFNEYKNKKEAF-YNCLK------NKKED 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1706 AERNLEELQKEIDRMLKELRSKDLQTQKEVAEDELvaaEGLLKRVNKLfgepraqnedMEKDLQQKLAEYKNKLDDAWDL 1785
Cdd:PTZ00440 214 YDKKIKKINNEIRKLLKNIKCTGNMCKTDTYVDMV---ELYLLRVNEV----------PSNNYDNYLNRAKELLESGSDL 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1786 LREATDKTRDANRLSAanqknmtiletkkeaiegskrqIENTLKEGNDILDEANRLLGEINSVIDYVDDIKT-KLPPmse 1864
Cdd:PTZ00440 281 INKIKKELGDNKTIYS----------------------INFIQEEIGDIIKRYNFHLKKIEKGKEYIKRIQNnNIPP--- 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1865 elsdkiddlaqEIKDRRLAEKVFQAESHAAQL---NDSSAVLDGILDEAKNISFNATAAFRAY--SNIKDYID------E 1933
Cdd:PTZ00440 336 -----------QVKKDELKKKYFESAKHYASFkfsLEMLSMLDSLLIKKEKILNNLFNKLFGDlkEKIETLLDseyfisK 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1934 AEKVAREAKELAQGATKLATSPQGLLKEDAKGS------LQKSF--------RILNEAKKLANDVKGNHNDLNDLKTRLE 1999
Cdd:PTZ00440 405 YTNIISLSEHTLKAAEDVLKENSQKIADYALYSnleiieIKKKYdekinelkKSINQLKTLISIMKSFYDLIISEKDSMD 484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2000 TADLRNSgllgALNDTMDKLSAITNdtaaKLQAVKEKAREANDTAKAV---LAQVKDLHQNLDGLKQNYNKLADSVakTN 2076
Cdd:PTZ00440 485 SKEKKES----SDSNYQEKVDELLQ----IINSIKEKNNIVNNNFKNIedyYITIEGLKNEIEGLIELIKYYLQSI--ET 554
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2077 AVVKDPSKNKIIADAGTSVRNLEQEadrlIDKLKPIKELEDNLKKNISEIKELINQARKQANSIKVSVSSGGDCVRTYRP 2156
Cdd:PTZ00440 555 LIKDEKLKRSMKNDIKNKIKYIEEN----VDHIKDIISLNDEIDNIIQQIEELINEALFNKEKFINEKNDLQEKVKYILN 630
|
570 580
....*....|....*....|....*
gi 117647249 2157 EIKKGSYNNIVVHVKTAVADNLLFY 2181
Cdd:PTZ00440 631 KFYKGDLQELLDELSHFLDDHKYLY 655
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1626-1913 |
9.36e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 54.64 E-value: 9.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1626 ERLIQLAEGNVNTLVMETNELLTRATKVTADGEQTGQDAERTNSRAESLEEFIKGLVQDAEAINEKAVQLNetlgNQDKT 1705
Cdd:TIGR04523 460 DNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLE----SEKKE 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1706 AERNLEELQKEIDRMLKELRSKDLQT-----QKEVaeDELVAAEGLLKRVNKLFGEPRAQNEDMEKDLQQKLAEYKNKLd 1780
Cdd:TIGR04523 536 KESKISDLEDELNKDDFELKKENLEKeidekNKEI--EELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKI- 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1781 daWDLLREATdKTRDANRLSAANQKNmtiLETKKEAIEGSKRQIENTLKEgndILDEANRLLGEINSVIDYVDDIkTKLp 1860
Cdd:TIGR04523 613 --SSLEKELE-KAKKENEKLSSIIKN---IKSKKNKLKQEVKQIKETIKE---IRNKWPEIIKKIKESKTKIDDI-IEL- 681
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 117647249 1861 pMSEELSDKIDDLAQEIKDRRLAEKVFQAESHAAQLNDSSAVLDGILDEAKNI 1913
Cdd:TIGR04523 682 -MKDWLKELSLHYKKYITRMIRIKDLPKLEEKYKEIEKELKKLDEFSKELENI 733
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1630-2130 |
1.23e-06 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 54.70 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1630 QLAEGNVNTLVMETNELLTRATKVTadgeQTGQDAERTNSraESLEEFI---KGLVQDAEAINEKAVQLNET-LGNQDKT 1705
Cdd:COG5022 888 KIDVKSISSLKLVNLELESEIIELK----KSLSSDLIENL--EFKTELIarlKKLLNNIDLEEGPSIEYVKLpELNKLHE 961
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1706 AERNLEELQKEIDRMLKELrskdlqtqkevaedelvaaegllkrvNKLFGEPRAQNEDMEKdLQQKLAEYKNKLDDawdl 1785
Cdd:COG5022 962 VESKLKETSEEYEDLLKKS--------------------------TILVREGNKANSELKN-FKKELAELSKQYGA---- 1010
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1786 LREATDKTRDANRLSAANQKNMTILETkkeaiEGSKRQIENTLKE-GNDILDEANRLLGEINSVIDYVDDIKTKLPPMSE 1864
Cdd:COG5022 1011 LQESTKQLKELPVEVAELQSASKIISS-----ESTELSILKPLQKlKGLLLLENNQLQARYKALKLRRENSLLDDKQLYQ 1085
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1865 ELSDKIDDLAQEIKDRRLAEKVFQAESHAAQLNDSSAVLDGILDEAKniSFNAtaafRAYSNIKDYideaeKVAREAKEL 1944
Cdd:COG5022 1086 LESTENLLKTINVKDLEVTNRNLVKPANVLQFIVAQMIKLNLLQEIS--KFLS----QLVNTLEPV-----FQKLSVLQL 1154
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1945 AQGATKLATSPQGLLKEDAKGSLQKSFRILNEAKKLANdvKGNHNDLNDLKTRLET-ADLRNSGLLgaLNDTMDKLSAIT 2023
Cdd:COG5022 1155 ELDGLFWEANLEALPSPPPFAALSEKRLYQSALYDEKS--KLSSSEVNDLKNELIAlFSKIFSGWP--RGDKLKKLISEG 1230
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2024 NDTAAKLQAVKE-------KAREANDTAKAVLAQVKDLHQNLDGLKQNYNKLADSVAKTNAVVKDPSKNKIIADA----G 2092
Cdd:COG5022 1231 WVPTEYSTSLKGfnnlnkkFDTPASMSNEKLLSLLNSIDNLLSSYKLEEEVLPATINSLLQYINVGLFNALRTKAsslrW 1310
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 117647249 2093 TSVRNLEQEADRLIDKLKPIK------ELEDN---------LKKNISEIKELI 2130
Cdd:COG5022 1311 KSATEVNYNSEELDDWCREFEisdvdeELEELiqavkvlqlLKDDLNKLDELL 1363
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1663-1888 |
1.80e-06 |
|
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: 52.76 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1663 DAERTNSRaESLEEFIKGLVQDAEAINEKAVQLNETLG---NQDKTAERNLEELQKEIDRMLKElrSKDLQTQKEVAEde 1739
Cdd:cd22656 109 DEELEEAK-KTIKALLDDLLKEAKKYQDKAAKVVDKLTdfeNQTEKDQTALETLEKALKDLLTD--EGGAIARKEIKD-- 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1740 lvaaegLLKRVnklfgepraqnedmeKDLQQKLA-EYKNKLDDAWDLLREATDKTRDANRLSAanqknmtiletkkeAIE 1818
Cdd:cd22656 184 ------LQKEL---------------EKLNEEYAaKLKAKIDELKALIADDEAKLAAALRLIA--------------DLT 228
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1819 GSKRQIENTLkegnDILDEAnrlLGEINSVIDYVDDIKTKLppmsEELSDKIDDLAQEIKDRRLAEKVFQ 1888
Cdd:cd22656 229 AADTDLDNLL----ALIGPA---IPALEKLQGAWQAIATDL----DSLKDLLEDDISKIPAAILAKLELE 287
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1585-2146 |
2.09e-06 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 54.07 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1585 LEQMTMNINLTGplpapYKILYGLENTtqELKHLLSPQRAPErLIQLAEGNVN----TLVMETNEL-----LTRATKVTA 1655
Cdd:PTZ00440 1835 LGHVVKSANFIG-----IKIMTGLQPT--ELTPDASLETAPE-LTFESENNSDleldHLSSNKNELdvyknIQDAYKSSL 1906
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1656 DGEQTGQDAERTNSRAESLEEFIKGLVQDAEAINEKAVQLNETLGNQDKTAER--NLEELQKEIDRMLKELRSKDLQTQK 1733
Cdd:PTZ00440 1907 QILKYSDDIDKKQRDCNKLVEDGNEIYLKSTAINELKNMINSVKNKESAISNKidNVSNKLSELNKITCNDESYDEILEK 1986
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1734 EVAEDelvaaeglLKRVNKLFGEPRAQ--NEDMEKDLQQKLAEYKNKLDD----AWDLLREATDKTRDANRLSAAN--QK 1805
Cdd:PTZ00440 1987 EEYEE--------LKDLRNSFNQEKAEtlNNLKLNKIKEDFNSYKNLLDEleksVKTLKASENIKKIVENKKTSIDaiNT 2058
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1806 NMTILETKKEAIEGSkrqIENTLKEGNDIldEANRLlgeiNSVIDyvddiktklppmseELSDKIDDLAQEIKDRrlaEK 1885
Cdd:PTZ00440 2059 NIEDIEKEIESINPS---LDELLKKGHKI--EISRY----TSIID--------------NVQTKISNDSKNINDI---EK 2112
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1886 VFQAESHAAQLNDSSAVLD------------------GILDEAKNISFNATAAFRAYSNI-------------KDYIDEA 1934
Cdd:PTZ00440 2113 KAQIYLAYIKNNYNSIKKDistlneyfdekqvsnyilTNIDKANKLSSELSEAVTNSEEIienikkeiieineNTEMNTL 2192
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1935 EKVAREAKELAQGATKLATSPQGLLK-------EDAKGSLQKSFRIlneAKKLANDVKGNHNDLNDLKTRLETADLRNSG 2007
Cdd:PTZ00440 2193 ENTADKLKELYENLKKKKNIINNIYKkinfiklQEIENSSEKYNDI---SKLFNNVVETQKKKLLDNKNKINNIKDKIND 2269
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2008 LLGALND-----TMDKLSAITNDTAAKLQAVKEkAREANDTAKAVLAQVKDLHQNLDGLKQNYNKL---------ADSVA 2073
Cdd:PTZ00440 2270 KEKELINvdssfTLESIKTFNEIYDDIKSNIGD-LYKLEDTNNDELKKVKLYIENITHLLNRINTLindldnyqdENYGK 2348
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 117647249 2074 KTNAVVKDPSKNKIIaDAGTSVRNLEQEADRLIDKLKpikelEDNLKKNISEIKELINQARKQANSIKVSVSS 2146
Cdd:PTZ00440 2349 DKNIELNNENNSYII-KTKEKINNLKEEFSKLLKNIK-----RNNTLCNNNNIKDFISNIGKSVETIKQRFSS 2415
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
802-859 |
2.19e-06 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 46.96 E-value: 2.19e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 117647249 802 PCACPLNIpsnNFSPTCHLDrslGLICdECPIGYTGPRCERCAEGYFGQPSIPGGsCQ 859
Cdd:cd00055 1 PCDCNGHG---SLSGQCDPG---TGQC-ECKPNTTGRRCDRCAPGYYGLPSQGGG-CQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
283-330 |
2.41e-06 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 46.58 E-value: 2.41e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 117647249 283 CICYGHA---RACplDPATnkSRCECEHNTCGESCDRCCPGFHQKPWRAGT 330
Cdd:cd00055 2 CDCNGHGslsGQC--DPGT--GQCECKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
803-858 |
4.63e-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: 4.63e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 117647249 803 CACPLNIPSnnfSPTCHldrSLGLICDeCPIGYTGPRCERCAEGYFGQPSIPGGSC 858
Cdd:pfam00053 1 CDCNPHGSL---SDTCD---PETGQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| alph_xenorhab_A |
NF033928 |
alpha-xenorhabdolysin family binary toxin subunit A; Alpha-xenorhabdolysin was the founding ... |
1664-1944 |
5.07e-06 |
|
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: 51.53 E-value: 5.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1664 AERTNSRAESLEEFIKGLvQDAEAINEKAVQLNE----TLGNQDKTAERN----LEELQKEIDRMLKELR--SKDLQT-Q 1732
Cdd:NF033928 79 ARNIVVTGNPIIDLINEM-PIIKRGDLTEEELSElppiPLSSDDKEIVKElkeiLEDLKNDIKDYQQKADdvKKELDDfE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1733 KEVAEDELVAAEGLLKRVNKLFGEP-----RAQNEDMEKDLQQKLAEYKNKLDDAWdllreatdktrdanrlSAANQKN- 1806
Cdd:NF033928 158 NDLREELLPQLKLKKKLYDDNLGSDsieelREKIDQLEKEIEQLNKEYDDYVKLSF----------------TGLAGGPi 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1807 -----MTILETKKEAIEGSKRQIENTLKEGNDILDEANRLLGEINSVIDYVDDIKTKlppMSEELS--DKIDDLAQEIkd 1879
Cdd:NF033928 222 glaitGGIFGSKAEKIRKEKNALIQEIDELQEQLKKKNALLGSLERLQTSLDDILTR---MEDALPalKKLKGVWQSL-- 296
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 117647249 1880 rrlaekvfqaeshAAQLNDSSAVLDGILDEAKNISFNAtaafraysNIKDYIDEAEKVAREAKEL 1944
Cdd:NF033928 297 -------------LTDIDSSINALKEIDDADSLRLFKL--------EFEQVIAPWKEIQDYAKQL 340
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1608-1779 |
5.81e-06 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 49.18 E-value: 5.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1608 LENTTQELKHLLSP--QRAPERLIQLAEGNVNTLVMETNELLTRATKVTADGEQT-GQDAERTNSRAESL-EEFIKGLVQ 1683
Cdd:pfam01442 9 LSTYAEELQEQLGPvaQELVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKlGQNVEELRQRLEPYtEELRKRLNA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1684 DAEAINEKAVQLNETLgnqDKTAERNLEELQKEIDRMLKELRSKdlqtqkeVAEdelvAAEGLLKRVNKLFGEPRAQNED 1763
Cdd:pfam01442 89 DAEELQEKLAPYGEEL---RERLEQNVDALRARLAPYAEELRQK-------LAE----RLEELKESLAPYAEEVQAQLSQ 154
|
170
....*....|....*.
gi 117647249 1764 MEKDLQQKLAEYKNKL 1779
Cdd:pfam01442 155 RLQELREKLEPQAEDL 170
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1608-1887 |
5.89e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.44 E-value: 5.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1608 LENTTQELKHLLSPQRAPERLIQLAEGNVNTLVMETNELLTRATKVTADGEQTGQDAERTNSRAESLEEFIKGLVQDAEA 1687
Cdd:COG4372 82 LEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLES 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1688 INEKAVQLNETLGNQDKT-AERNLEELQKEIDRMLKELRSKDLQTQKEVAEDELVA----------AEGLLKRVNKLFGE 1756
Cdd:COG4372 162 LQEELAALEQELQALSEAeAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAeelleakdslEAKLGLALSALLDA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1757 PRAQNEDMEKDLQQKLAEYKNKLDDAWDLLREATDKTRDANRLSAANQKnmtILETKKEAIEGSKRQIENTLKEGNDILD 1836
Cdd:COG4372 242 LELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEE---AALELKLLALLLNLAALSLIGALEDALL 318
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 117647249 1837 EANRLLGEINSVIDYVDDIKTKLPPMSEELSDKIDDLAQEIKDRRLAEKVF 1887
Cdd:COG4372 319 AALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVAD 369
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1635-2146 |
6.08e-06 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 52.53 E-value: 6.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1635 NVNTLVMETNELLTRATKVTADGEQTGQDAERTNSraESLE-------EFIKGLVQDAEAINEKAVQLNETLGNQDKTaE 1707
Cdd:PTZ00440 1549 NILNIKDEIETILNKAQDLMRDISKISKIVENKNL--ENLNdkeadyvKYLDNILKEKQLMEAEYKKLNEIYSDVDNI-E 1625
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1708 RNLEELQK--EIDRM--LKELrSKDLQTQKEVAEDELVAaegLLKRVNKLFgepraQNEDMEK-DLQQKLAEYKNKLDDA 1782
Cdd:PTZ00440 1626 KELKKHKKnyEIGLLekVIEI-NKNIKLYMDSTKESLNS---LVNNFSSLF-----NNFYLNKyNINENLEKYKKKLNEI 1696
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1783 WDLLREATDKTRDANRLSAANQKNMTILETKKEAIEGSKRQIENTLKEGNDILDEANRLlgEINSVIDYVDDIKTKLPPM 1862
Cdd:PTZ00440 1697 YNEFMESYNIIQEKMKEVSNDDVDYNEAKTLREEAQKEEVNLNNKEEEAKKYLNDIKKQ--ESFRFILYMKEKLDELSKM 1774
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1863 SEELSDKIDD-------LAQEIK----DRRLAEKVFQAE---------SHAAQLNDSSAVLDGILDEAKNISFNATAAFr 1922
Cdd:PTZ00440 1775 CKQQYNIVDEgynyikkKIEYIKtlndENNLSDSLNQAEdknkevanlTHYTNKNEAKNLLGHVVKSANFIGIKIMTGL- 1853
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1923 AYSNIKDyiDEAEKVAREAKELAQGATKLATSPQGLLK------EDAKGSLQKSFRIL-------------NEAKKLAND 1983
Cdd:PTZ00440 1854 QPTELTP--DASLETAPELTFESENNSDLELDHLSSNKneldvyKNIQDAYKSSLQILkysddidkkqrdcNKLVEDGNE 1931
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1984 VKGNHNDLNDLKTRLETADLRNSGLLGALNDTMDKLSAItndtaaklqavkeKAREAND-TAKAVLAqvKDLHQNLDGLK 2062
Cdd:PTZ00440 1932 IYLKSTAINELKNMINSVKNKESAISNKIDNVSNKLSEL-------------NKITCNDeSYDEILE--KEEYEELKDLR 1996
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2063 QNYNKladsvaKTNAVVKDPSKNKIIADAGTSVRNLeqeaDRLIDKLKPIKElEDNLKKNISEIKELINQARKQANSIKV 2142
Cdd:PTZ00440 1997 NSFNQ------EKAETLNNLKLNKIKEDFNSYKNLL----DELEKSVKTLKA-SENIKKIVENKKTSIDAINTNIEDIEK 2065
|
....
gi 117647249 2143 SVSS 2146
Cdd:PTZ00440 2066 EIES 2069
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
1931-2141 |
6.32e-06 |
|
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: 51.23 E-value: 6.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1931 IDEAEKVAREAKELAQGATKLATSPQGLLKEdakgsLQKSFRILNEA-KKLANDVKGNHNDLNDLKTRLETADLRNSGLL 2009
Cdd:pfam04108 2 LSSAQDLCRWANELLTDARSLLEELVVLLAK-----IAFLRRGLSVQlANLEKVREGLEKVLNELKKDFKQLLKDLDAAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2010 GALNDTMDKLSAITNDTAAKLQAVK----------EKAREANDTAKAVLAQVKDLHQNLDG-LKQNYNKLADSVAKTNAV 2078
Cdd:pfam04108 77 ERLEETLDKLRNTPVEPALPPGEEKqktlldfideDSVEILRDALKELIDELQAAQESLDSdLKRFDDDLRDLQKELESL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2079 VKDPSKNKIIADAGTSVRNLEQEADRLIDKL--------------------------KPIKELED---NLKKNISEIKEL 2129
Cdd:pfam04108 157 SSPSESISLIPTLLKELESLEEEMASLLESLtnhydqcvtavklteggraemlevleNDARELDDvvpELQDRLDEMENN 236
|
250
....*....|..
gi 117647249 2130 INQARKQANSIK 2141
Cdd:pfam04108 237 YERLQKLLEQKN 248
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1652-2137 |
7.07e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 51.97 E-value: 7.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1652 KVTADGEQTGQDAERTNSRAESLEEFIKGLVQDAEAINEKAVQLNETL----GNQDKtaERNLEELQKEIDRMLKELRSK 1727
Cdd:TIGR00606 581 SKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLfdvcGSQDE--ESDLERLKEEIEKSSKQRAML 658
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1728 DLQTQ--KEVAEDELVAAEGLLKRVNKLFgEPRAQNEDMEKDLQQKLAEYKNKLDDAWDLLREaTDKTRDANRLSAANQK 1805
Cdd:TIGR00606 659 AGATAvySQFITQLTDENQSCCPVCQRVF-QTEAELQEFISDLQSKLRLAPDKLKSTESELKK-KEKRRDEMLGLAPGRQ 736
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1806 NMTILETK--KEAIEGSKRQIENTLKEGNDIlDEANRLLGEINSVIDYVDDIKTKLPPMsEELSDKIDDLaqeikDRRLA 1883
Cdd:TIGR00606 737 SIIDLKEKeiPELRNKLQKVNRDIQRLKNDI-EEQETLLGTIMPEEESAKVCLTDVTIM-ERFQMELKDV-----ERKIA 809
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1884 EKVfqAESHAAQLNDSSAVLDGILDEAKNisfnataafrAYSNIKDYIDEAEKVAREAKELAQ---------GATKLATS 1954
Cdd:TIGR00606 810 QQA--AKLQGSDLDRTVQQVNQEKQEKQH----------ELDTVVSKIELNRKLIQDQQEQIQhlksktnelKSEKLQIG 877
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1955 PQGllkEDAKGSLQKSFRILNEAKKLANDVKGNHNDLNDLKTRLETADLRNSGLLGALNDTMDKlsaitndTAAKLQAVK 2034
Cdd:TIGR00606 878 TNL---QRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKK-------AQDKVNDIK 947
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2035 EKAREANDTAKAVLAQVKDLHQnlDGLKQNYNKLADSVAKTNAVVKdpSKNKIIADAGTSVRNLEQEADR---LIDKL-- 2109
Cdd:TIGR00606 948 EKVKNIHGYMKDIENKIQDGKD--DYLKQKETELNTVNAQLEECEK--HQEKINEDMRLMRQDIDTQKIQerwLQDNLtl 1023
|
490 500 510
....*....|....*....|....*....|..
gi 117647249 2110 ----KPIKELEDNLKKNISEIKELINQARKQA 2137
Cdd:TIGR00606 1024 rkreNELKEVEEELKQHLKEMGQMQVLQMKQE 1055
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
803-851 |
8.45e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 44.99 E-value: 8.45e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 117647249 803 CACPlniPSNNFSPTCHLDrslGLICdECPIGYTGPRCERCAEGYFGQP 851
Cdd:smart00180 1 CDCD---PGGSASGTCDPD---TGQC-ECKPNVTGRRCDRCAPGYYGDG 42
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1793-2053 |
8.60e-06 |
|
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: 50.10 E-value: 8.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1793 TRDANRLSAA----NQKNMTILETKKE------AIEGSKRQIENTLKEGNDILDEANRLLGEINSVIDyvddiktklppM 1862
Cdd:pfam06008 1 LLSLNSLTGAlpapYKINYNLENLTKQlqeylsPENAHKIQIEILEKELSSLAQETEELQKKATQTLA-----------K 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1863 SEELSDKIDDLAQEIKDrrLAEKVFQAESHAAQLNDSSAVLDGILDEAKNisfnataafraySNIKDYIDEAEKV----- 1937
Cdd:pfam06008 70 AQQVNAESERTLGHAKE--LAEAIKNLIDNIKEINEKVATLGENDFALPS------------SDLSRMLAEAQRMlgeir 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1938 AREAKELAQGATKLATSPQGLLKEdakgsLQKSF-RILNEAKKLANDVK---GNHND-LNDLKTRLETA----------D 2002
Cdd:pfam06008 136 SRDFGTQLQNAEAELKAAQDLLSR-----IQTWFqSPQEENKALANALRdslAEYEAkLSDLRELLREAaaktrdanrlN 210
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 117647249 2003 LRNSGLLGALNDTMDKLSAITNDTAAKLQavkeKAREANDTAKAVLAQVKD 2053
Cdd:pfam06008 211 LANQANLREFQRKKEEVSEQKNQLEETLK----TARDSLDAANLLLQEIDD 257
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1635-2149 |
9.01e-06 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 51.76 E-value: 9.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1635 NVNTLVMET--NELLTRATKVTADGEQTGQDAERT-NSRAESLEEFIKGLVQDAEAINEKAVQLNEtlgNQDKTAERNLE 1711
Cdd:PTZ00440 1286 NMYEFLISIdsEKILKEILNSTKKAEEFSNDAKKElEKTDNLIKQVEAKIEQAKEHKNKIYGSLED---KQIDDEIKKIE 1362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1712 ELQKEIDRMLKELRS--KDLQTQKEVAEDELVAAE------GLLKRVNKLfgEPRAQNE-------DMEKDLQQKLAE-- 1774
Cdd:PTZ00440 1363 QIKEEISNKRKEINKylSNIKSNKEKCDLHVRNASrgkdkiDFLNKHEAI--EPSNSKEvniikitDNINKCKQYSNEam 1440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1775 -YKNKLDDAWDLLRE-ATDKTRDANRLSAANQKnmTILETKK-------EAIEGSKRQIE----------NTLKEGNDIL 1835
Cdd:PTZ00440 1441 eTENKADENNDSIIKyEKEITNILNNSSILGKK--TKLEKKKkeatnimDDINGEHSIIKtkltksseklNQLNEQPNIK 1518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1836 DEANRL---------------LGEINSVIDYVDDIKTKLppmsEELSDKIDDLAQEIKDRRLAEKVFQAESHAAQLNDSS 1900
Cdd:PTZ00440 1519 REGDVLnndkstiayetiqynLGRVKHNLLNILNIKDEI----ETILNKAQDLMRDISKISKIVENKNLENLNDKEADYV 1594
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1901 AVLDGILDEAKNISFNATAAfraySNIKDYIDEAEKVAREAKELAQgatklatspQGLLKedakgslqksfRILNEAKKL 1980
Cdd:PTZ00440 1595 KYLDNILKEKQLMEAEYKKL----NEIYSDVDNIEKELKKHKKNYE---------IGLLE-----------KVIEINKNI 1650
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1981 ANDVKGNHNDLNDL----KTRLETADLRNSGLLGALNDTMDKLSAITNDTAAKLQAVKEKAREANDtaKAV-LAQVKDLH 2055
Cdd:PTZ00440 1651 KLYMDSTKESLNSLvnnfSSLFNNFYLNKYNINENLEKYKKKLNEIYNEFMESYNIIQEKMKEVSN--DDVdYNEAKTLR 1728
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2056 QNLDGLKQNYNKLADSVAKTNAVVKdpsknkiiadagtsvrnlEQEADRLIDKlkpIKELEDNLKKNISEIKELINQARK 2135
Cdd:PTZ00440 1729 EEAQKEEVNLNNKEEEAKKYLNDIK------------------KQESFRFILY---MKEKLDELSKMCKQQYNIVDEGYN 1787
|
570
....*....|....
gi 117647249 2136 QANSIKVSVSSGGD 2149
Cdd:PTZ00440 1788 YIKKKIEYIKTLND 1801
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
1662-2005 |
9.07e-06 |
|
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular sites as centrioles, basal bodies, and along ciliary and flagellar doublet microtubules. Tektins form unique protofilaments, organized as longitudinal polymers of tektin heterodimers with axial periodicity matching tubulin. Tektin polypeptides consist of several alpha-helical regions that are predicted to form coiled coils. Indeed, tektins share considerable structural similarities with intermediate filament proteins. Possible functional roles for tektins are: stabilization of tubulin protofilaments; attachment of A and B-tubules in ciliary/flagellar microtubule doublets and C-tubules in centrioles; binding of axonemal components.
Pssm-ID: 460827 [Multi-domain] Cd Length: 383 Bit Score: 51.01 E-value: 9.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1662 QDAERTNSRAESLEEFIKGLVQDAEAINEKAvQL--NETLGNQDKTAERNLEELQKEIDRMLKElrSKDLQTQKEVAEDE 1739
Cdd:pfam03148 10 REAEAQRNDAERLRQESRRLRNETDAKTKWD-QYdsNRRLGERIQDITFWKSELEKELEELDEE--IELLLEEKRRLEKA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1740 L--------VAAEGLLKRvnklfgEPRaQNEDM-----EKDLQQKL-------AEYKNKLDDAWDLLREatdktrdaNRl 1799
Cdd:pfam03148 87 LealeeplhIAQECLTLR------EKR-QGIDLvhdevEKELLKEVeliegiqELLQRTLEQAWEQLRL--------LR- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1800 saANQKNMTI-LETKKEAIEgskrqientlkegndiLDEANRLLGEINSVIDYVDDIkTKLPPMSEELSDkIDDLAQEIK 1878
Cdd:pfam03148 151 --AARHKLEKdLSDKKEALE----------------IDEKCLSLNNTSPNISYKPGP-TRIPPNSSTPEE-WEKFTQDNI 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1879 DRrlAEKVFQAeshAAQLNdssAVLDGILDEAKNI---SFNAT-AAFR--------AYS-------NIKDYIDEAEK--- 1936
Cdd:pfam03148 211 ER--AEKERAA---SAQLR---ELIDSILEQTANDlraQADAVnFALRkrieetedAKNklewqlkKTLQEIAELEKnie 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1937 ---VAREAKE----LAQgaTKLAT------------SPQ-GLLKEDAKgsLQKSFRILNEakKLAnDVKGNHNDLNDLKT 1996
Cdd:pfam03148 283 aleKAIRDKEaplkLAQ--TRLENrtyrpnvelcrdEAQyGLVDEVKE--LEETIEALKQ--KLA-EAEASLQALERTRL 355
|
....*....
gi 117647249 1997 RLETaDLRN 2005
Cdd:pfam03148 356 RLEE-DIAV 363
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
465-511 |
1.03e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 44.99 E-value: 1.03e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 117647249 465 CNCSGLGSTNE--DPCVGPCSCKENVEGEDCSRCKSGFFNlqeDNQKGC 511
Cdd:smart00180 1 CDCDPGGSASGtcDPDTGQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1465-1520 |
1.49e-05 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 44.65 E-value: 1.49e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 117647249 1465 CACPLISPSnnfSPSCVLEGledYRCTaCPRGYEGQYCERCAPGYTGSPSSPGGSC 1520
Cdd:pfam00053 1 CDCNPHGSL---SDTCDPET---GQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1605-1911 |
1.77e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1605 LYGLENTTQELKHLLspQRAPERLIQLAEGnvntlVMETNELLTRATKVTADGEQTGQDAERT-NSRAESLEEFIKGLVQ 1683
Cdd:COG4717 127 LLPLYQELEALEAEL--AELPERLEELEER-----LEELRELEEELEELEAELAELQEELEELlEQLSLATEEELQDLAE 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1684 DAEAINEKAVQLNETLgnqdKTAERNLEELQKEIDRMLKELRSKDLQTQKEVAEDELVAAEGLL---------------- 1747
Cdd:COG4717 200 ELEELQQRLAELEEEL----EEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLallglggsllslilti 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1748 ------------------KRVNKLFGEP--RAQNEDMEKDLQQK-------------------LAEYKNKLDDAWDLLRE 1788
Cdd:COG4717 276 agvlflvlgllallflllAREKASLGKEaeELQALPALEELEEEeleellaalglppdlspeeLLELLDRIEELQELLRE 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1789 ATDKTRDANR----------LSAANQKNMTILETK----------KEAIEGSKRQIENTLKEGNDILDEAN--RLLGEIN 1846
Cdd:COG4717 356 AEELEEELQLeeleqeiaalLAEAGVEDEEELRAAleqaeeyqelKEELEELEEQLEELLGELEELLEALDeeELEEELE 435
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 117647249 1847 SVIDYVDDIKTKLppmsEELSDKIDDLAQEIK----DRRLAEKVFQAESHAAQLND------SSAVLDGILDEAK 1911
Cdd:COG4717 436 ELEEELEELEEEL----EELREELAELEAELEqleeDGELAELLQELEELKAELRElaeewaALKLALELLEEAR 506
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1727-1845 |
2.02e-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: 48.49 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1727 KDLQTQKEVAEDELVAAEGLLKRVNKLFGEPRAQNEDMEKDLQQKLAEyknkLDDAWDLLREATDKTRDANRLSAANQKN 1806
Cdd:pfam00261 4 QQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEE----LERTEERLAEALEKLEEAEKAADESERG 79
|
90 100 110
....*....|....*....|....*....|....*....
gi 117647249 1807 MTILETKKEAIEGSKRQIENTLKEGNDILDEANRLLGEI 1845
Cdd:pfam00261 80 RKVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEV 118
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1665-1915 |
2.02e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 50.61 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1665 ERTNSRAESLEEFIKGLVQDAEAINEKAVQLNETLGNQDKT---AERNLEELQKEIDRMLKELRSKDLQTQKEVAEDELV 1741
Cdd:pfam12128 600 EELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREetfARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDS 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1742 AAEgllkRVNKLfgepRAQNEDMEKDLQQKLAEYKNK------------------LDDAWDLLREATDKTRDAN--RLSA 1801
Cdd:pfam12128 680 ANE----RLNSL----EAQLKQLDKKHQAWLEEQKEQkreartekqaywqvvegaLDAQLALLKAAIAARRSGAkaELKA 751
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1802 ANQKNMTILETK---KEAIEGSKRQIENTLKEgndiLDEANRLLGEINSVIDYV--------DDIKTKLPPMSEELSDKI 1870
Cdd:pfam12128 752 LETWYKRDLASLgvdPDVIAKLKREIRTLERK----IERIAVRRQEVLRYFDWYqetwlqrrPRLATQLSNIERAISELQ 827
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 117647249 1871 DDLAQEIKDRRLAEKVFQAESHA--AQLNDSSAVLDGILDEAKNISF 1915
Cdd:pfam12128 828 QQLARLIADTKLRRAKLEMERKAseKQQVRLSENLRGLRCEMSKLAT 874
|
|
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
1822-2062 |
2.17e-05 |
|
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo reversible methylation in response to attractants or repellants during bacterial chemotaxis.
Pssm-ID: 214599 [Multi-domain] Cd Length: 262 Bit Score: 48.82 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1822 RQIENTLKEGNDILDEANRLLGEINSVIDYVDDIKTKLPPMSE------ELSDKIDDLAQEIKDR--RLAEKVFQAESHA 1893
Cdd:smart00283 4 EAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAAtaqsaaEAAEEGREAVEDAITAmdQIREVVEEAVSAV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1894 AQLNDSSAVLDGILDEAKNISF-------NAT--AAfRAysnikdyiDEAEK----VAREAKELAQGATKLATSPQGLLK 1960
Cdd:smart00283 84 EELEESSDEIGEIVSVIDDIADqtnllalNAAieAA-RA--------GEAGRgfavVADEVRKLAERSAESAKEIESLIK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1961 E------DAKGSLQKSFRILNEAKKLANDVKGNHNDLNDL---------KTRLETADLRNSglLGALNDTMDKLSAITND 2025
Cdd:smart00283 155 EiqeetnEAVAAMEESSSEVEEGVELVEETGDALEEIVDSveeiadlvqEIAAATDEQAAG--SEEVNAAIDEIAQVTQE 232
|
250 260 270
....*....|....*....|....*....|....*..
gi 117647249 2026 TAAKLQavkekarEANDTAKAVLAQVKDLHQNLDGLK 2062
Cdd:smart00283 233 TAAMSE-------EISAAAEELSGLAEELDELVERFK 262
|
|
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
1740-2149 |
2.19e-05 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 50.02 E-value: 2.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1740 LVAAEGLLKRVNKLFGEPRAQNEDMEKDLQQKLAEYKNKLDDAWDLLREATDKTRDANRLSAANQKNMTILETKKEAIEG 1819
Cdd:COG0840 4 LLLLLALLLALLLLALSLLALLAAALLILLALLLAALTALALLLLLSLLALLLLLLLLALALLLVLLALLLLLALVVLLA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1820 SKRQIENTLKEGNDILDEANRLLGEINSVIDYVDDIKTKLPPMSEELSD---KIDDLAQEIKDRRLAEKVFQAESHAAQL 1896
Cdd:COG0840 84 LLLALLLLLLALLALALAALALLAALAALLALLELLLAALLAALAIALLalaALLALAALALALLALALLAAAAAAAAAL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1897 NDSSAVLDGILDEAKNISFNATAAFRAYSNIKDYIDE--AEKVAREAKELAQGATKLA----TSPQGLLKEDAKGSLQKS 1970
Cdd:COG0840 164 AALLEAAALALAAAALALALLAAALLALVALAIILALllSRSITRPLRELLEVLERIAegdlTVRIDVDSKDEIGQLADA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1971 F--------RILNEAKKLANDVKGNHNDLNDLKTRLETADLRNSGLLGALNDTMDKLSAITNDTAAKLQAVKEKAREAND 2042
Cdd:COG0840 244 FnrmienlrELVGQVRESAEQVASASEELAASAEELAAGAEEQAASLEETAAAMEELSATVQEVAENAQQAAELAEEASE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2043 TAK-------AVLAQVKDLHQNLDGLKQNYNKLADSVAKTNAVVKDpsknkI--IAD---------------AGTS---- 2094
Cdd:COG0840 324 LAEeggevveEAVEGIEEIRESVEETAETIEELGESSQEIGEIVDV-----IddIAEqtnllalnaaieaarAGEAgrgf 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 117647249 2095 ------VRNLeqeADRLIDKLKPIKELEDNLKKNISEIKELINQARKQANSIKVSVSSGGD 2149
Cdd:COG0840 399 avvadeVRKL---AERSAEATKEIEELIEEIQSETEEAVEAMEEGSEEVEEGVELVEEAGE 456
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1682-2048 |
2.33e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.52 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1682 VQDAEAIN--EKAVQLNETLGNQDKTAE--RNLEELQKEIDRMLKELRSKDLQTQKEVAEDELVAAEGLLKR---VNKLF 1754
Cdd:PTZ00121 1557 LKKAEEKKkaEEAKKAEEDKNMALRKAEeaKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAeeeKKKVE 1636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1755 GEPRAQNEDMEKDLQQKLAEYKNKLDDAwDLLREATDKTRDANRLSAANQKNMTILE-TKKEAIEgsKRQIENTLKEGND 1833
Cdd:PTZ00121 1637 QLKKKEAEEKKKAEELKKAEEENKIKAA-EEAKKAEEDKKKAEEAKKAEEDEKKAAEaLKKEAEE--AKKAEELKKKEAE 1713
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1834 ILDEANRLLGEINSVIDYVDDIKTKlppmSEELSDKIDDLAQEIKDRRLAEKVFQAESHAAQ--LNDSSAVLDGIL---D 1908
Cdd:PTZ00121 1714 EKKKAEELKKAEEENKIKAEEAKKE----AEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEeiRKEKEAVIEEELdeeD 1789
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1909 EAKNISFNATA--AFRAYSNIKDYIDEAEKVAREAKELAQGATKLATSPQGLLKEDAKGSLQKSFRILNEAKKLANDvKG 1986
Cdd:PTZ00121 1790 EKRRMEVDKKIkdIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNK-EA 1868
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 117647249 1987 NHNDLNDLKTRLETADLRNSGLLGALNDTMDKLSAITN-------DTAAKLQAVKEKAREANDTAKAVL 2048
Cdd:PTZ00121 1869 DFNKEKDLKEDDEEEIEEADEIEKIDKDDIEREIPNNNmagknndIIDDKLDKDEYIKRDAEETREEII 1937
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1697-2053 |
3.37e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.94 E-value: 3.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1697 ETLGNQDKTAERNLEELQKEIDRMLKELRskDLQTQKEVAEDELVAAEGLLKRVNKLFgepRAQNEDMEKdLQQKLAEYK 1776
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELA--ELEAELEELRLELEELELELEEAQAEE---YELLAELAR-LEQDIARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1777 NKLDDAWDLLREATDKTRDANRLSAANQKNMTILETKKEAIEGSKRQIENTLKEGNDILDEANRLLGEINSVIDyvddik 1856
Cdd:COG1196 309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE------ 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1857 tklppmsEELSDKIDDLAQEIKDRRLAEKvfQAESHAAQLNDSSAVLDGILDEAKNISFNATAAFRAYSNIKDYIDEAEK 1936
Cdd:COG1196 383 -------ELAEELLEALRAAAELAAQLEE--LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1937 VAREAKELAQGATKLATSPQGLLKEDAKGSLQKSfRILNEAKKLANDVKGNHNDLNDLKTRLETADLRNSGLLGALNDTm 2016
Cdd:COG1196 454 LEEEEEALLELLAELLEEAALLEAALAELLEELA-EAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIG- 531
|
330 340 350
....*....|....*....|....*....|....*..
gi 117647249 2017 DKLSAITNDTAAKLQAVKEKAREANDTAKAVLAQVKD 2053
Cdd:COG1196 532 VEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKA 568
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1684-2176 |
3.57e-05 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 49.83 E-value: 3.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1684 DAEAINEKAVQLNETLGNQDKTaERNLEELQKEIDRMLKELRSKDLQTQKEVAEDelvaaegllkrVNKLFGEPRAQNED 1763
Cdd:PTZ00440 2042 IKKIVENKKTSIDAINTNIEDI-EKEIESINPSLDELLKKGHKIEISRYTSIIDN-----------VQTKISNDSKNIND 2109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1764 MEKDLQQKLAEYKNKLDDAW---DLLREATDKTRDANRLSAANQKNMTILETKKEAIEGSKRQIENTLKEGNDILDeanr 1840
Cdd:PTZ00440 2110 IEKKAQIYLAYIKNNYNSIKkdiSTLNEYFDEKQVSNYILTNIDKANKLSSELSEAVTNSEEIIENIKKEIIEINE---- 2185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1841 llgeiNSVIDYVDDIKTKLPPMSEELSDK---IDDLAQEIKDRRLAEkvfqAESHAAQLNDSSAVLDGILD-EAKNISFN 1916
Cdd:PTZ00440 2186 -----NTEMNTLENTADKLKELYENLKKKkniINNIYKKINFIKLQE----IENSSEKYNDISKLFNNVVEtQKKKLLDN 2256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1917 ATAafraYSNIKDYIDEAEKVareakelaqgatklatspqgLLKEDAKGSLQkSFRILNEakkLANDVKGNHNDLNDLKT 1996
Cdd:PTZ00440 2257 KNK----INNIKDKINDKEKE--------------------LINVDSSFTLE-SIKTFNE---IYDDIKSNIGDLYKLED 2308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1997 -------RLETADLRNSGLLGALNDTMDKLSAITNDTAAKLQAVKEKAREANdtakavlaQVKDLHQNLDGLKQNYNKLA 2069
Cdd:PTZ00440 2309 tnndelkKVKLYIENITHLLNRINTLINDLDNYQDENYGKDKNIELNNENNS--------YIIKTKEKINNLKEEFSKLL 2380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2070 DSVAKTNAVVKDPSKNKIIADAGTSVRNLEQEadrlIDKLKPIKELEDNLKKNISEIKELINQARKQANsIKVSVSSggd 2149
Cdd:PTZ00440 2381 KNIKRNNTLCNNNNIKDFISNIGKSVETIKQR----FSSNLPEKEKLHQIEENLNEIKNIMNETKRISN-VDAFTNK--- 2452
|
490 500
....*....|....*....|....*..
gi 117647249 2150 CVRTYRPEIKKGSYNNIVVHVKTAVAD 2176
Cdd:PTZ00440 2453 ILQDIDNEKNKENNNMNAEKIDDLIEN 2479
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1603-2150 |
5.24e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 49.27 E-value: 5.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1603 KILYGLENTTQELKhllspqrapERLIQLAE--GNVNTLVMETNELLTRATKVTADGEQTGQDAER----TNSRAESLEE 1676
Cdd:TIGR00606 238 EIVKSYENELDPLK---------NRLKEIEHnlSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKvfqgTDEQLNDLYH 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1677 FIKGLVQDAEA----INEKAVQLNET--LGNQDKTA-ERNLEELQKEIDRMLKELRSKDLQTQKEVAEDELVAAE--GLL 1747
Cdd:TIGR00606 309 NHQRTVREKERelvdCQRELEKLNKErrLLNQEKTElLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFErgPFS 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1748 KRVNKLFGE-PRAQNEDMEKDLQQKLAEYKNKLDdawdLLREATDKTRDanRLSAANQknmtILETKKEAIEGSKRQIEN 1826
Cdd:TIGR00606 389 ERQIKNFHTlVIERQEDEAKTAAQLCADLQSKER----LKQEQADEIRD--EKKGLGR----TIELKKEILEKKQEELKF 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1827 TLKEGNDILDEANRLLGEINSVIDYVDD---------IKTKLppmSEELSDKIDDLAQEIKDRRLAEKVFQAESHAAQLN 1897
Cdd:TIGR00606 459 VIKELQQLEGSSDRILELDQELRKAERElskaeknslTETLK---KEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRT 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1898 DSSAVLDGILDEAKNI-------SFNATAAFRAYSNIKDYIDEAEKVAREAKELAQGATKLATSPQGLlkEDAKGSLQKS 1970
Cdd:TIGR00606 536 QMEMLTKDKMDKDEQIrkiksrhSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASL--EQNKNHINNE 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1971 FRILNEAK-KLAN---DVKGNHN---DLNDLKTRLETAdlrnsgllgalNDTMDKLSAITNDTAAKLQAVKEKAREANDT 2043
Cdd:TIGR00606 614 LESKEEQLsSYEDklfDVCGSQDeesDLERLKEEIEKS-----------SKQRAMLAGATAVYSQFITQLTDENQSCCPV 682
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2044 AKAVLAQVKDLHQNLDGLKQNYNKLADSVAKTNAVVKDPSKNKIIADAGTSVRnlEQEADRLIDKLKPIKELEDNLKKNI 2123
Cdd:TIGR00606 683 CQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGR--QSIIDLKEKEIPELRNKLQKVNRDI 760
|
570 580
....*....|....*....|....*..
gi 117647249 2124 SEIKELINQARKQANSIKVSVSSGGDC 2150
Cdd:TIGR00606 761 QRLKNDIEEQETLLGTIMPEEESAKVC 787
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1678-1880 |
6.66e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 48.47 E-value: 6.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1678 IKGLVQDAEAINEKAVQLNETLGNQDKTAERNLEELQKEIDRMLKElrSKDLQTQKEVAEDELVAAE-------GLLKRV 1750
Cdd:PHA02562 183 IQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEE--AKTIKAEIEELTDELLNLVmdiedpsAALNKL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1751 NKLFGEPRAQNEDMEKDL-------------QQ------KLAEYKNKLDDAWDLLREATDKTRDAN-RLSAANQKNMTIL 1810
Cdd:PHA02562 261 NTAAAKIKSKIEQFQKVIkmyekggvcptctQQisegpdRITKIKDKLKELQHSLEKLDTAIDELEeIMDEFNEQSKKLL 340
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1811 ETKKEaIEGSKRQIENTLKEGNDILDEANRLLGEinsVIDYVDDIKTklppMSEELSDKIDDLAQEIKDR 1880
Cdd:PHA02562 341 ELKNK-ISTNKQSLITLVDKAKKVKAAIEELQAE---FVDNAEELAK----LQDELDKIVKTKSELVKEK 402
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1764-1961 |
7.07e-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: 46.84 E-value: 7.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1764 MEKDLQQ--KLAEYKNKLDDAWDLLREATDKTRDANRLSAANQKNMTILETKKEAIEGSKRQIENTLKEGNDILDEANRL 1841
Cdd:COG1579 2 MPEDLRAllDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1842 LGEINSVIDYvddiktklppmsEELSDKIDDLAQEIKDR--RLAEKVFQAESHAAQLNDSSAVLDGILDEAKnisfNATA 1919
Cdd:COG1579 82 LGNVRNNKEY------------EALQKEIESLKRRISDLedEILELMERIEELEEELAELEAELAELEAELE----EKKA 145
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 117647249 1920 AFRAysnikdyidEAEKVAREAKELAQGATKLATS-PQGLLKE 1961
Cdd:COG1579 146 ELDE---------ELAELEAELEELEAEREELAAKiPPELLAL 179
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1682-2140 |
8.53e-05 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 48.67 E-value: 8.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1682 VQDAEAINEKAvqLNETLGNQDKTAERNLEELQKEIDRMLKELRSKDL---QTQKEVAEDELVAAEGLLKR---VNKLFG 1755
Cdd:PTZ00440 2166 VTNSEEIIENI--KKEIIEINENTEMNTLENTADKLKELYENLKKKKNiinNIYKKINFIKLQEIENSSEKyndISKLFN 2243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1756 EpraqnedMEKDLQQKLAEYKNKLDDAWDLLREATDKTRDANrlsaanqKNMTiLETKKEAIE---------GSKRQIEN 1826
Cdd:PTZ00440 2244 N-------VVETQKKKLLDNKNKINNIKDKINDKEKELINVD-------SSFT-LESIKTFNEiyddiksniGDLYKLED 2308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1827 T----LKEGNDILDEANRLLGEINSVIDYVDDIKTKLPPMSEELSDKIDDLAQEIKdrrLAEKVfqaeshaaqlNDSSAV 1902
Cdd:PTZ00440 2309 TnndeLKKVKLYIENITHLLNRINTLINDLDNYQDENYGKDKNIELNNENNSYIIK---TKEKI----------NNLKEE 2375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1903 LDGILdeaKNISFNATaaFRAYSNIKDYIDEAEKVAREAKElaqgatKLATSpqglLKEDAKGSLQKSFriLNEAKKLAN 1982
Cdd:PTZ00440 2376 FSKLL---KNIKRNNT--LCNNNNIKDFISNIGKSVETIKQ------RFSSN----LPEKEKLHQIEEN--LNEIKNIMN 2438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1983 DVKGNHNdlNDLKTRLETADLRNsgllgalndtmDKLSAITNDTAAKLQAVKEKAREANDTAKAVLAQVKDLHQNLDGLK 2062
Cdd:PTZ00440 2439 ETKRISN--VDAFTNKILQDIDN-----------EKNKENNNMNAEKIDDLIENVTSHNEKIKSELLIINDALRRVKEKK 2505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2063 QNYNKLADSVAKTNAVVKDPSKNKIiadagTSVRNLEQEADRLIDKL--------KPIKELEDNLKKNISEIKelINQAR 2134
Cdd:PTZ00440 2506 DEMNKLFNSLTENNNNNNNSAKNIV-----DNSTYIINELESHVSKLnellsyidNEIKELENEKLKLLEKAK--IEESR 2578
|
....*.
gi 117647249 2135 KQANSI 2140
Cdd:PTZ00440 2579 KERERI 2584
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1635-1838 |
9.67e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.09 E-value: 9.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1635 NVNTLVMETNELLTRATKVTADGEQTGQDAERTNSRAESLEEFIKGLVQDAEAINEKAVQLNetLGNQDKTAERNLEELQ 1714
Cdd:COG3206 206 GLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQ--LRAQLAELEAELAELS 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1715 ----------KEIDRMLKELRSKDLQTQKEVAEDELVAAEGLLKRvnklfgepraqnedmEKDLQQKLAEYKNKLDDAWD 1784
Cdd:COG3206 284 arytpnhpdvIALRAQIAALRAQLQQEAQRILASLEAELEALQAR---------------EASLQAQLAQLEARLAELPE 348
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 117647249 1785 LLREATDKTRDANrlsaANQKNMTILETKKEAIegskrQIENTLKEGN-DILDEA 1838
Cdd:COG3206 349 LEAELRRLEREVE----VARELYESLLQRLEEA-----RLAEALTVGNvRVIDPA 394
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1686-1946 |
1.15e-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: 46.98 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1686 EAINEKAVQLNETlgNQDKTAERNLEELQKEIDRMLKElrSKDLQTQKEVAEDEL-----------VAAEGLLKRVNKLF 1754
Cdd:cd22656 94 AEILELIDDLADA--TDDEELEEAKKTIKALLDDLLKE--AKKYQDKAAKVVDKLtdfenqtekdqTALETLEKALKDLL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1755 GE--PRAQNEDMeKDLQQKLAEYKNKLddawdllreatdktrdANRLsaanqknmtiletkKEAIEGSKRQIENTlkegN 1832
Cdd:cd22656 170 TDegGAIARKEI-KDLQKELEKLNEEY----------------AAKL--------------KAKIDELKALIADD----E 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1833 DILDEANRLLGEINSVIDYVDDIKTKLPPMSEELsdkiddlaQEIKDrrlaekVFQAeshaaqLNDSsavLDGILDEAKN 1912
Cdd:cd22656 215 AKLAAALRLIADLTAADTDLDNLLALIGPAIPAL--------EKLQG------AWQA------IATD---LDSLKDLLED 271
|
250 260 270
....*....|....*....|....*....|....
gi 117647249 1913 ISFNATAAFRAYSNIKDYIDEAEKVAREAKELAQ 1946
Cdd:cd22656 272 DISKIPAAILAKLELEKAIEKWNELAEKADKFRQ 305
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1609-1815 |
1.20e-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: 48.12 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1609 ENTTQELKHLLSPQRAPERLIQLAEGNVNTLVMETNELLTRATKVTADGEQTGQDAERTNSRAESLEEFIKGLVQDAEAI 1688
Cdd:TIGR00606 832 QEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQD 911
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1689 N------EKAVQLNETLGN----QDKTAERNLEELQKEIDRMLKELRSKDLQTQkEVAEDELVAAEGLLKRVNKLFGEPR 1758
Cdd:TIGR00606 912 SpletflEKDQQEKEELISsketSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQ-DGKDDYLKQKETELNTVNAQLEECE 990
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 117647249 1759 AQNEDMEKDLQQKLAEY-KNKLDDAW---DL-LREATDKTRDANRLSAANQKNMT---ILETKKE 1815
Cdd:TIGR00606 991 KHQEKINEDMRLMRQDIdTQKIQERWlqdNLtLRKRENELKEVEEELKQHLKEMGqmqVLQMKQE 1055
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1608-1890 |
1.35e-04 |
|
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: 47.66 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1608 LENTTQE--LKHLLSPQRAPERLIQLAEgnvntlvMETNELLTRATKVTADGEQTGQdaerTNSRAESLEEFIKGLVQDA 1685
Cdd:TIGR00618 652 QLTLTQErvREHALSIRVLPKELLASRQ-------LALQKMQSEKEQLTYWKEMLAQ----CQTLLRELETHIEEYDREF 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1686 EAINEKAVQLNETLGNQDKTAERNLEELQKEIDRMLKELRSKDlqtqkEVAEDELVAAEGLLKRVNKLFGEPRAQNEDME 1765
Cdd:TIGR00618 721 NEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAH-----FNNNEEVTAALQTGAELSHLAAEIQFFNRLRE 795
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1766 KD---LQQKLAEYKNKLDDaWDLLREATDKT---RDANRLSAANQKNMTILETKKE--AIEGSKRQIENTLKEGNDILDE 1837
Cdd:TIGR00618 796 EDthlLKTLEAEIGQEIPS-DEDILNLQCETlvqEEEQFLSRLEEKSATLGEITHQllKYEECSKQLAQLTQEQAKIIQL 874
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 117647249 1838 ANRLLGeINSVIdyVDDIKTKLPPMSEELS-DKIDDLAQEIKDRRLAEKVFQAE 1890
Cdd:TIGR00618 875 SDKLNG-INQIK--IQFDGDALIKFLHEITlYANVRLANQSEGRFHGRYADSHV 925
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1808-2051 |
1.51e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1808 TILETKKEAIEGSKRQIENTLKEGNDILDEANRLLGEINSVIDYVDDIKTKLppmsEELSDKIDDLAQEIKDRR--LAEK 1885
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEI----DKLQAEIAEAEAEIEERReeLGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1886 VfqaesHAAQLNDSSAVLDGILDEAKNISfnataafraysnikDYIDEAEKVareakelaqgaTKLATSPQGLLKEdakg 1965
Cdd:COG3883 92 A-----RALYRSGGSVSYLDVLLGSESFS--------------DFLDRLSAL-----------SKIADADADLLEE---- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1966 sLQKSFRILNEAKKLANDVKgnhNDLNDLKTRLETAdlrnsglLGALNDTMDKLSAITNDTAAKLQAVKEKAREANDTAK 2045
Cdd:COG3883 138 -LKADKAELEAKKAELEAKL---AELEALKAELEAA-------KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELA 206
|
....*.
gi 117647249 2046 AVLAQV 2051
Cdd:COG3883 207 AAEAAA 212
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1872-2137 |
1.58e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.62 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1872 DLAQEIKDRRLAEKVFQAESHAAQLndssAVLDGILDEAKnisfnataafraysnikdyideaEKVAREAKELAQGATKL 1951
Cdd:COG1196 217 ELKEELKELEAELLLLKLRELEAEL----EELEAELEELE-----------------------AELEELEAELAELEAEL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1952 ATSPQGLLKEDAKGS-LQKSFRIL-NEAKKLANDVKGNHNDLNDLKTRLETADLRNSGLLGALNDTMDKLSAITNDTAAK 2029
Cdd:COG1196 270 EELRLELEELELELEeAQAEEYELlAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2030 LQAVKEKAREANDTAKAVLAQVKDLHQNLDGLKQNYNKLADSVAKTNAVVKDpsknkiIADAGTSVRNLEQEADRLIDKl 2109
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ------LEELEEAEEALLERLERLEEE- 422
|
250 260
....*....|....*....|....*...
gi 117647249 2110 kpIKELEDNLKKNISEIKELINQARKQA 2137
Cdd:COG1196 423 --LEELEEALAELEEEEEEEEEALEEAA 448
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1613-1845 |
1.97e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1613 QELKHLLSPQRAPERLIqlaegnvNTLVMETNELLTRATKVTADGEQTGQDAERTNSRAESLEEFIKGLVQDAEAINEKA 1692
Cdd:COG4717 319 EELEELLAALGLPPDLS-------PEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAAL 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1693 VQLNEtlgNQDKTAErnLEELQKEIDRMLKELRSKDLQTQKEVAEDELVAAEGLLKRVNKLF-------GEPRAQNEDME 1765
Cdd:COG4717 392 EQAEE---YQELKEE--LEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELeelreelAELEAELEQLE 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1766 KD--LQQKLAEYKnklddawDLLREATDKTRDANRLSAAnqknMTILETKKEAIEGSKRQientlkegnDILDEANRLLG 1843
Cdd:COG4717 467 EDgeLAELLQELE-------ELKAELRELAEEWAALKLA----LELLEEAREEYREERLP---------PVLERASEYFS 526
|
..
gi 117647249 1844 EI 1845
Cdd:COG4717 527 RL 528
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
1827-2130 |
2.25e-04 |
|
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.
Pssm-ID: 427715 [Multi-domain] Cd Length: 360 Bit Score: 46.23 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1827 TLKEGNDILDEANRLLgeiNSVIDYVDDIktklppmsEELSDKIDDLAQEIKD--------RRLAEKVFQ-----AESHA 1893
Cdd:pfam04108 1 SLSSAQDLCRWANELL---TDARSLLEEL--------VVLLAKIAFLRRGLSVqlanlekvREGLEKVLNelkkdFKQLL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1894 AQLNDSSAVLDGILDEAKNIS--FNATAAFRAYSNIKDYIDEaEKVareakelaqgatklatspqgllkEDAKGSLQKSF 1971
Cdd:pfam04108 70 KDLDAALERLEETLDKLRNTPvePALPPGEEKQKTLLDFIDE-DSV-----------------------EILRDALKELI 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1972 RILNEA-KKLANDVKGNHNDLNDLKTRLETADLRN--SGLLGALNDTMDKLSA--------ITNDTAAKLQAVK--EKAR 2038
Cdd:pfam04108 126 DELQAAqESLDSDLKRFDDDLRDLQKELESLSSPSesISLIPTLLKELESLEEemasllesLTNHYDQCVTAVKltEGGR 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2039 E------ANDtAKAVLAQVKDLHQNLDGLKQNYNKLADSVAKTNAVVKDPSKN-KIIADAGT---SVRNLEQEADRLIDK 2108
Cdd:pfam04108 206 AemlevlEND-ARELDDVVPELQDRLDEMENNYERLQKLLEQKNSLIDELLSAlQLIAEIQSrlpEYLAALKEFEERWEE 284
|
330 340
....*....|....*....|..
gi 117647249 2109 LKpikeleDNLKKNISEIKELI 2130
Cdd:pfam04108 285 EK------ETIEDYLSELEDLR 300
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1840-2059 |
2.26e-04 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 44.56 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1840 RLLGEINSVIDYVDDIKTKLPPMSEELSDKI----DDLAQEIkDRRLAEKVFQAESHAAQLNdssAVLDGILDEAKNIsf 1915
Cdd:pfam01442 1 LLEDSLDELSTYAEELQEQLGPVAQELVDRLeketEALRERL-QKDLEEVRAKLEPYLEELQ---AKLGQNVEELRQR-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1916 nataafraysnIKDYIDE-AEKVAREAKELAQgatKLATSPQGLLK--EDAKGSLQKSFRILNEakklandvkgnhndln 1992
Cdd:pfam01442 75 -----------LEPYTEElRKRLNADAEELQE---KLAPYGEELRErlEQNVDALRARLAPYAE---------------- 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 117647249 1993 DLKTRLETAdlrnsglLGALNDTMdklsaitndtAAKLQAVKEKAREANDTAKAVLA-QVKDLHQNLD 2059
Cdd:pfam01442 125 ELRQKLAER-------LEELKESL----------APYAEEVQAQLSQRLQELREKLEpQAEDLREKLD 175
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1650-1947 |
2.28e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1650 ATKVTADGEQTGQDAERTNSRAESLEEFIKGLVQDAEAINEKAVQLNETLGNQdKTAERNLEELQKEIDRM-LKELRSKD 1728
Cdd:COG4717 297 KASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEEL-QELLREAEELEEELQLEeLEQEIAAL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1729 LQTQKEVAEDELVAAeglLKRVNKLfgepraqnedmeKDLQQKLAEYKNKLDDAWDLLREATDKTrDANRLsaanqknmt 1808
Cdd:COG4717 376 LAEAGVEDEEELRAA---LEQAEEY------------QELKEELEELEEQLEELLGELEELLEAL-DEEEL--------- 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1809 iletkKEAIEGSKRQIENTLKEGNDILDEANRLLGEINSVI--DYVDDIKTKLppmsEELSDKIDDLAQEIKDRRLAEKV 1886
Cdd:COG4717 431 -----EEELEELEEELEELEEELEELREELAELEAELEQLEedGELAELLQEL----EELKAELRELAEEWAALKLALEL 501
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 117647249 1887 FQAESHAAQLNDSSAVLDgildeaknisfNATAAFR-----AYSNIkdYIDEAEKVA--------REAKELAQG 1947
Cdd:COG4717 502 LEEAREEYREERLPPVLE-----------RASEYFSrltdgRYRLI--RIDEDLSLKvdtedgrtRPVEELSRG 562
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1464-1521 |
2.41e-04 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 41.19 E-value: 2.41e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 117647249 1464 PCACPLISpsnNFSPSCVLEGLedyRCTaCPRGYEGQYCERCAPGYTGSPSSPGGsCQ 1521
Cdd:cd00055 1 PCDCNGHG---SLSGQCDPGTG---QCE-CKPNTTGRRCDRCAPGYYGLPSQGGG-CQ 50
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1603-1940 |
2.65e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 46.75 E-value: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1603 KILYGLENTTQELKHLLspQRAPERLIQLaegnVNTLVMETNELLTRATKVTADG--------EQTGQDAERTNSRAES- 1673
Cdd:PRK04778 198 EILDQLEEELAALEQIM--EEIPELLKEL----QTELPDQLQELKAGYRELVEEGyhldhldiEKEIQDLKEQIDENLAl 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1674 LEEF-IKGLVQDAEAINEKAVQLNETL-----------GNQDKT------AERNLEELQKEIDRmLKE---LRSKDLQTQ 1732
Cdd:PRK04778 272 LEELdLDEAEEKNEEIQERIDQLYDILerevkarkyveKNSDTLpdflehAKEQNKELKEEIDR-VKQsytLNESELESV 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1733 KEVaEDELVAAEGLLKRVNKLFGEPRA---QNEDMEKDLQQKLAEYKNKLDDAWDLLREATDKTRDAnrlsaanQKNMTI 1809
Cdd:PRK04778 351 RQL-EKQLESLEKQYDEITERIAEQEIaysELQEELEEILKQLEEIEKEQEKLSEMLQGLRKDELEA-------REKLER 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1810 LETKKEAIegsKRQIentlkegndildEANRLLGEINSVIDYVddiktklppmsEELSDKIDDLAQEIKDRRL-AEKVfq 1888
Cdd:PRK04778 423 YRNKLHEI---KRYL------------EKSNLPGLPEDYLEMF-----------FEVSDEIEALAEELEEKPInMEAV-- 474
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 117647249 1889 aeshAAQLNDSSAVLDGILDEAKNISFNATAAFRA--YSN--------IKDYIDEAEKVARE 1940
Cdd:PRK04778 475 ----NRLLEEATEDVETLEEETEELVENATLTEQLiqYANryrsdneeVAEALNEAERLFRE 532
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1375-1403 |
2.88e-04 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 40.80 E-value: 2.88e-04
10 20
....*....|....*....|....*....
gi 117647249 1375 RCDCPPGYSGLSCETCAPGFYRLRSEPGG 1403
Cdd:cd00055 20 QCECKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1465-1513 |
3.30e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 40.76 E-value: 3.30e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 117647249 1465 CACPlisPSNNFSPSCVLEGLedyRCTaCPRGYEGQYCERCAPGYTGSP 1513
Cdd:smart00180 1 CDCD---PGGSASGTCDPDTG---QCE-CKPNVTGRRCDRCAPGYYGDG 42
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
302-326 |
3.61e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 40.37 E-value: 3.61e-04
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1375-1403 |
3.93e-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: 40.41 E-value: 3.93e-04
10 20
....*....|....*....|....*....
gi 117647249 1375 RCDCPPGYSGLSCETCAPGFYRLRSEPGG 1403
Cdd:pfam00053 19 QCLCKPGVTGRHCDRCKPGYYGLPSDPPQ 47
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1653-1774 |
3.95e-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: 44.63 E-value: 3.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1653 VTADGEQTGQDAERTNSRAESLEEFIKGL---VQDAEAINEKAVQLNETLGNQDKT--------------AERNLEELQK 1715
Cdd:pfam00261 125 VEGDLERAEERAELAESKIVELEEELKVVgnnLKSLEASEEKASEREDKYEEQIRFlteklkeaetraefAERSVQKLEK 204
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 117647249 1716 EIDRMlkelrskdlqtqkevaEDELVAAegllkrvnklfgepRAQNEDMEKDLQQKLAE 1774
Cdd:pfam00261 205 EVDRL----------------EDELEAE--------------KEKYKAISEELDQTLAE 233
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1814-2089 |
4.19e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.78 E-value: 4.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1814 KEAIEGSKRQIentlkegnDILD-EANRLLGEINSVIDYVDDIKTKLPPMSEELSDKIDDLAQEIKD---------RRLA 1883
Cdd:PHA02562 173 KDKIRELNQQI--------QTLDmKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTikaeieeltDELL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1884 EKVFQAESHAAQLNDSSavlDGILDEAKNI-SFNATAAF--------RAYSNIKDYIDEAEKVAREAKELAQGATKLats 1954
Cdd:PHA02562 245 NLVMDIEDPSAALNKLN---TAAAKIKSKIeQFQKVIKMyekggvcpTCTQQISEGPDRITKIKDKLKELQHSLEKL--- 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1955 pqgllkEDAKGSLQKsfrILNEAKKLANDVKGNHNDLNDLKTRLETADLRNSgllgALNDTMDKLSAITNDTAAKLQAVK 2034
Cdd:PHA02562 319 ------DTAIDELEE---IMDEFNEQSKKLLELKNKISTNKQSLITLVDKAK----KVKAAIEELQAEFVDNAEELAKLQ 385
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 117647249 2035 EKAREANDTaKAVLAQVKDLHQNLDGLkqnynkLADSVAKTnAVVKD--PSKNKIIA 2089
Cdd:PHA02562 386 DELDKIVKT-KSELVKEKYHRGIVTDL------LKDSGIKA-SIIKKyiPYFNKQIN 434
|
|
| VSP |
pfam03302 |
Giardia variant-specific surface protein; |
771-1090 |
4.71e-04 |
|
Giardia variant-specific surface protein;
Pssm-ID: 146106 [Multi-domain] Cd Length: 397 Bit Score: 45.35 E-value: 4.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 771 NCK--DHTGGPYCNECLPGFYGDPTRGSPEDCQPCAcplnipsNNFSPTCHLDRslgLICDECPIGytgpRCERCAEgyf 848
Cdd:pfam03302 27 NCKacSNDKREVCEECNSNNYLTPTSQCIDDCAKIG-------NYYYTTNANNK---KICKECTVA----NCKTCED--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 849 gqpsipGGSCQpcQCNDNLdYSIPGSCDSLSGSCLICKPGTTGRyCELCADG---YFGDAVNAKNCqpcrcningsfSEI 925
Cdd:pfam03302 90 ------QGQCQ--ACNDGF-YKSGDACSPCHESCKTCSGGTASD-CTECLTGkalRYGNDGTKGTC-----------GEG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 926 CHTRTGQCECRP---NVQG-RHCDECKPETFGLQLGrgclPCNCNSFGSKSFdCEASgqcwcqpGVAGKKCDRCAHGYFN 1001
Cdd:pfam03302 149 CTTGTGAGACKTcglTIDGtSYCSECATETEYPQNG----VCTSTAARATAT-CKAS-------SVANGMCSSCANGYFR 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1002 fQEGGCI---------ACDCSHLGNNCDPKTGQCICPPN---TTGEKCSECLPNTWGHSIVTG-------CKVCN--CST 1060
Cdd:pfam03302 217 -MNGGCYettkfpgksVCEEANSGGTCQKEAPGYKLNNGdlvTCSPGCKTCTSNTVCTTCMDGyvktsdsCTKCDssCET 295
|
330 340 350
....*....|....*....|....*....|
gi 117647249 1061 VGSLASQCNVntgqCSCHPKFSGMKCSECS 1090
Cdd:pfam03302 296 CTGATTTCKT----CATGYYKSGTGCVSCT 321
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1713-2141 |
5.29e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 45.60 E-value: 5.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1713 LQKEIDRMLKELRSKDLQTQKEVAEDELVAAEGLlkrvnKLFGEPRAQNEDMEKDLQQ----KLAEYKNKLDDAwdllRE 1788
Cdd:PRK04778 23 LRKRNYKRIDELEERKQELENLPVNDELEKVKKL-----NLTGQSEEKFEEWRQKWDEivtnSLPDIEEQLFEA----EE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1789 ATDKTRdanrLSAAnQKNMTILETKKEAIEGskrQIENTLKEGNDIL--DEANRllGEINSVIDYVDDIKTKLPPMSEEL 1866
Cdd:PRK04778 94 LNDKFR----FRKA-KHEINEIESLLDLIEE---DIEQILEELQELLesEEKNR--EEVEQLKDLYRELRKSLLANRFSF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1867 SDKIDDLAQEIKDrrlAEKVFQaesHAAQLNDSSAVLD--GILDEAKNisfnATAAFRAYSN-IKDYIDEAEKVAREA-K 1942
Cdd:PRK04778 164 GPALDELEKQLEN---LEEEFS---QFVELTESGDYVEarEILDQLEE----ELAALEQIMEeIPELLKELQTELPDQlQ 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1943 ELAQGATKLAtspqgllkedAKGSLQKSFRILNEAKKLANDVKGNHNDLNDLKtrLETAdlrnSGLLGALNDTMDKL-SA 2021
Cdd:PRK04778 234 ELKAGYRELV----------EEGYHLDHLDIEKEIQDLKEQIDENLALLEELD--LDEA----EEKNEEIQERIDQLyDI 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2022 ITNDTAAKlQAVKEKAREANDTAKAVLAQVKDLHQNLDGLKQNY----------NKLADSVAKTNAVVKDPSKNkiIADA 2091
Cdd:PRK04778 298 LEREVKAR-KYVEKNSDTLPDFLEHAKEQNKELKEEIDRVKQSYtlneselesvRQLEKQLESLEKQYDEITER--IAEQ 374
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 117647249 2092 GTSVRNLEQEADRLIDKLKPIKELEDNLKKNISEIKELINQARKQANSIK 2141
Cdd:PRK04778 375 EIAYSELQEELEEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYR 424
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1989-2141 |
6.20e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 6.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1989 NDLNDLKTRLETADLRnsglLGALNDTMDKLSAITNDTAAKLQAVKEKAREANdtakavlAQVKDLHQNLDGLKQNYNKL 2068
Cdd:COG3883 23 KELSELQAELEAAQAE----LDALQAELEELNEEYNELQAELEALQAEIDKLQ-------AEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2069 ADSVAKTNAVV---------KDPS---------------KNKIIADAGTSVRNLEQEADRLIDKLKPIKELEDNLKKNIS 2124
Cdd:COG3883 92 ARALYRSGGSVsyldvllgsESFSdfldrlsalskiadaDADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170
....*....|....*..
gi 117647249 2125 EIKELINQARKQANSIK 2141
Cdd:COG3883 172 ELEAQQAEQEALLAQLS 188
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
1666-1833 |
6.59e-04 |
|
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance.
Pssm-ID: 463102 [Multi-domain] Cd Length: 140 Bit Score: 42.28 E-value: 6.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1666 RTNSRAESLEEFIKGLVQDAEAINEKavqlNETLGNQDKTAERNLEELQKEIDRMLKELRskDLQTqkevaedELVAAeg 1745
Cdd:pfam10473 14 ESERKADSLKDKVENLERELEMSEEN----QELAILEAENSKAEVETLKAEIEEMAQNLR--DLEL-------DLVTL-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1746 llkrvnklfgepRAQNEDMEKDLQQKlaeyKNKLDDAwDLLREATdktrdANRLSAANQKNMTILETKKEAIEgskrQIE 1825
Cdd:pfam10473 79 ------------RSEKENLTKELQKK----QERVSEL-ESLNSSL-----ENLLEEKEQEKVQMKEESKTAVE----MLQ 132
|
....*...
gi 117647249 1826 NTLKEGND 1833
Cdd:pfam10473 133 TQLKELNE 140
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
1817-2068 |
6.67e-04 |
|
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.
Pssm-ID: 427715 [Multi-domain] Cd Length: 360 Bit Score: 44.69 E-value: 6.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1817 IEGSKRQIENTLKEGNDILDEANRLLGEINSVIDYVDDIK--TKLPPMSEE---LSD-----KIDDLAQEIKD--RRLAE 1884
Cdd:pfam04108 51 REGLEKVLNELKKDFKQLLKDLDAALERLEETLDKLRNTPvePALPPGEEKqktLLDfidedSVEILRDALKEliDELQA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1885 KVFQAESHAAQLNDSSAVLDGILDEAKNISfnataafRAYSNIKDYIDEAEKVAREAKELA--------QGATKLATSPQ 1956
Cdd:pfam04108 131 AQESLDSDLKRFDDDLRDLQKELESLSSPS-------ESISLIPTLLKELESLEEEMASLLesltnhydQCVTAVKLTEG 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1957 G------LLKEDAKgSLQksfRILNEAKKLANDVKGNHNDLNDLKTRLETAdlrnsglLGALNDTMDKLSAITN---DTA 2027
Cdd:pfam04108 204 GraemleVLENDAR-ELD---DVVPELQDRLDEMENNYERLQKLLEQKNSL-------IDELLSALQLIAEIQSrlpEYL 272
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 117647249 2028 AKLQAVKEKAREANDTAKAVLAQVKDLHQNLDGLKQNYNKL 2068
Cdd:pfam04108 273 AALKEFEERWEEEKETIEDYLSELEDLREFYEGFPSAYGSL 313
|
|
| NtpE |
COG1390 |
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal ... |
1672-1849 |
1.31e-03 |
|
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: 42.62 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1672 ESLEEFIKGLVQDAEAinekavQLNETLGNQDKTAERNLEELQKEIDRMLKELRSKDLQTQKEVAEDELVAAEGLLKR-- 1749
Cdd:COG1390 2 MSLEKIIEEILEEAEA------EAEEILEEAEEEAEKILEEAEEEAEEIKEEILEKAEREAEREKRRIISSAELEARKel 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1750 -------VNKLFGEPRAQNEDMEKDlqqklAEYKNKLDdawDLLREA---------------TDKTRDANRLSAANQKNM 1807
Cdd:COG1390 76 leakeelIEEVFEEALEKLKNLPKD-----PEYKELLK---KLLKEAaeelgsgdlvvyvneKDKELLEELLKELKKKGL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 117647249 1808 TILETKKEAIEG-------SKRQIENTLKEgndILDEA-NRLLGEINSVI 1849
Cdd:COG1390 148 EVSEEDIDILGGvivesedGRIRVDNTFES---LLERLkEELLKEIAEIL 194
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1745-1949 |
2.13e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 42.12 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1745 GLLKRVNKLFgepRA-------QNEDMEKDLQQKLAEYKNKLDDAwdllREATDKTrdanrlsAANQKNMTI-LETKKEA 1816
Cdd:COG1842 1 GIFKRLSDII---RAninalldKAEDPEKMLDQAIRDMEEDLVEA----RQALAQV-------IANQKRLERqLEELEAE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1817 IEGSKRQIENTLKEGNDilDEANRLLGEINSVIDYVDDIKT---KLPPMSEELSDKIDDLAQEIKDRRLAEKVFQAESHA 1893
Cdd:COG1842 67 AEKWEEKARLALEKGRE--DLAREALERKAELEAQAEALEAqlaQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1894 A----QLNDSSAvldgildeakniSFNATAAFRAYSNIKDYIDEAEKVAREAKELAQGAT 1949
Cdd:COG1842 145 AkaqeKVNEALS------------GIDSDDATSALERMEEKIEEMEARAEAAAELAAGDS 192
|
|
| F5_F8_type_C |
pfam00754 |
F5/8 type C domain; This domain is also known as the discoidin (DS) domain family. |
86-170 |
2.78e-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: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 86 SSNPYQRHPITNAIDGK-NTWWQSpsiKNGVEYHYvtITLDLQQVFQIAYVIVKAANSPRPGN---WILERSLDDVEYKP 161
Cdd:pfam00754 5 SSSYSGEGPAAAALDGDpNTAWSA---WSGDDPQW--IQVDLGKPKKITGVVTQGRQDGSNGYvtsYKIEYSLDGENWTT 79
|
....*....
gi 117647249 162 WQYHAVTDT 170
Cdd:pfam00754 80 VKDEKIPGN 88
|
|
| TNFRSF16 |
cd13416 |
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 ... |
781-915 |
3.36e-03 |
|
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: 40.75 E-value: 3.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 781 CNECLPGFYGDPTRGSPEDCQPCA-CPLNIPsnnfsPTCHLDRSLGLICdecpigytgprceRCAEGYFgqPSIPGGSCQ 859
Cdd:cd13416 35 CEPCLDGVTFSDVVSHTEPCQPCTrCPGLMS-----MRAPCTATHDTVC-------------ECAYGYY--LDEDSGTCE 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 117647249 860 PCQcndnldysipgSCDSLSGSCLICKPGTTGRyCELCADGYFGDAVNAKN-CQPCR 915
Cdd:cd13416 95 PCT-----------VCPPGQGVVQSCGPNQDTV-CEACPEGTYSDEDSSTDpCLPCT 139
|
|
| TNFRSF4 |
cd13406 |
Tumor necrosis factor receptor superfamily member 4 (TNFRSF4), also known as CD134 or OXO40; ... |
882-969 |
4.21e-03 |
|
Tumor necrosis factor receptor superfamily member 4 (TNFRSF4), also known as CD134 or OXO40; TNFRSF4 (also known as OX40, ACT35, CD134, IMD16, TXGP1L) activates NF-kappaB through its interaction with adaptor proteins TRAF2 and TRAF5. It also promotes the expression of apoptosis inhibitors BCL2 and BCL2lL1/BCL2-XL, and thus suppresses apoptosis. It is primarily expressed on activated CD4+ and CD8+ T cells, where it is transiently expressed and upregulated on the most recently antigen-activated T cells within inflammatory lesions. This makes it an attractive target to modulate immune responses, i.e. TNFRSF4 (OX40) blocking agents to inhibit adverse inflammation or agonists to enhance immune responses. An artificially created biologic fusion protein, OX40-immunoglobulin (OX40-Ig), prevents OX40 from reaching the T-cell receptors, thus reducing the T-cell response. Some single nucleotide polymorphisms (SNPs) of its natural ligand OX40 ligand (OX40L, CD252), which is also found on activated T cells, have been associated with systemic lupus erythematosus.
Pssm-ID: 276911 [Multi-domain] Cd Length: 142 Bit Score: 40.07 E-value: 4.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 882 CLICKPG---------TTGRYCELCADGYFGDAVNAKNCQPC-RCNINGSFSEI--C-HTRTGQCECRPNVQ-------G 941
Cdd:cd13406 15 CHECPPGegmesrctgTQDTVCSPCEPGFYNEAVNYEPCKPCtQCNQRSGSEEKqkCtKTSDTVCRCRPGTQpldsykpG 94
|
90 100
....*....|....*....|....*....
gi 117647249 942 RHCDECKPETFGLQLGRGCLP-CNCNSFG 969
Cdd:cd13406 95 VDCVPCPPGHFSRGDNQACKPwTNCSLAG 123
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1375-1396 |
5.00e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 37.29 E-value: 5.00e-03
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1663-1879 |
5.02e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.62 E-value: 5.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1663 DAERTNSRAESLEEFIKGLVQDAEAINEKAVQLNETLGNQDKTAERNLEELQKEIDRMLKELRskDLQTQKEVAEDELVA 1742
Cdd:COG1196 631 RLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEEL--ELEEALLAEEEEERE 708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1743 AEGLLKRvnklfgepRAQNEDMEKDLQQKLAEYKNKLDDAWDLLREATDKTRDANRLSAANqknmtiLETKKEAIEGSKR 1822
Cdd:COG1196 709 LAEAEEE--------RLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPD------LEELERELERLER 774
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 117647249 1823 QIENtlkegndildeanrlLGEIN-SVIDYVDDIKTKLppmsEELSDKIDDLAQEIKD 1879
Cdd:COG1196 775 EIEA---------------LGPVNlLAIEEYEELEERY----DFLSEQREDLEEARET 813
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
1972-2099 |
5.09e-03 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 42.02 E-value: 5.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1972 RILNEAKKLANDVKGNHNDLNDLKTRLETADLRNSGLLGALNDTMDKLSAITNDTAAKLQAVKekareandTAKAVLAQV 2051
Cdd:TIGR04320 237 YIADGNKFDKTPIPNPPNSLAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALA--------TAQKELANA 308
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 117647249 2052 KDlhQNLDGLKQNYNKLADSVAKTNAVVKDPSKNK--IIADAGTSVRNLE 2099
Cdd:TIGR04320 309 QA--QALQTAQNNLATAQAALANAEARLAKAKEALanLNADLAKKQAALD 356
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
1694-1782 |
5.47e-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: 39.87 E-value: 5.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1694 QLNETLGNQDKTAERNLEELQKEIDRMLKELRSK--DLQTQKEVAEDELVAAEGLLKRVNklfgepRAQNEDMEKDLQQK 1771
Cdd:pfam03938 19 AAQAQLEKKFKKRQAELEAKQKELQKLYEELQKDgaLLEEEREEKEQELQKKEQELQQLQ------QKAQQELQKKQQEL 92
|
90
....*....|.
gi 117647249 1772 LAEYKNKLDDA 1782
Cdd:pfam03938 93 LQPIQDKINKA 103
|
|
| TNFRSF4 |
cd13406 |
Tumor necrosis factor receptor superfamily member 4 (TNFRSF4), also known as CD134 or OXO40; ... |
828-913 |
7.32e-03 |
|
Tumor necrosis factor receptor superfamily member 4 (TNFRSF4), also known as CD134 or OXO40; TNFRSF4 (also known as OX40, ACT35, CD134, IMD16, TXGP1L) activates NF-kappaB through its interaction with adaptor proteins TRAF2 and TRAF5. It also promotes the expression of apoptosis inhibitors BCL2 and BCL2lL1/BCL2-XL, and thus suppresses apoptosis. It is primarily expressed on activated CD4+ and CD8+ T cells, where it is transiently expressed and upregulated on the most recently antigen-activated T cells within inflammatory lesions. This makes it an attractive target to modulate immune responses, i.e. TNFRSF4 (OX40) blocking agents to inhibit adverse inflammation or agonists to enhance immune responses. An artificially created biologic fusion protein, OX40-immunoglobulin (OX40-Ig), prevents OX40 from reaching the T-cell receptors, thus reducing the T-cell response. Some single nucleotide polymorphisms (SNPs) of its natural ligand OX40 ligand (OX40L, CD252), which is also found on activated T cells, have been associated with systemic lupus erythematosus.
Pssm-ID: 276911 [Multi-domain] Cd Length: 142 Bit Score: 39.30 E-value: 7.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 828 CDECPIGY---------TGPRCERCAEGYFGQP--SIPggsCQPC-QCNDNLDYSIPGSCDSLSGSCLICKPGTT----- 890
Cdd:cd13406 15 CHECPPGEgmesrctgtQDTVCSPCEPGFYNEAvnYEP---CKPCtQCNQRSGSEEKQKCTKTSDTVCRCRPGTQpldsy 91
|
90 100
....*....|....*....|....*
gi 117647249 891 --GRYCELCADGYFGDAVNaKNCQP 913
Cdd:cd13406 92 kpGVDCVPCPPGHFSRGDN-QACKP 115
|
|
| ClyA-like |
cd21116 |
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ... |
1983-2143 |
8.55e-03 |
|
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including Bacillus cereus HblB, Aeromonas hydrophila AhlB, Bacillus thuringiensis Cry6Aa and similar proteins; This family belongs to the ClyA family of alpha-PFT bacterial toxins. PFTs form the major group of virulence factors in many pathogenic bacteria and in general are critical components of the molecular offensive and defensive machinery of cells in all kingdoms of life. Bacterial PFTs facilitate the takeover of host resources by puncturing holes in the membrane. PFTs can be classified as alpha-PFTs and beta-PFTs depending on the secondary structures of their membrane component. Alpha-PFTs use a ring of amphipathic helices while beta-PFTs use a beta-barrel to construct the pore. Members of this family include the toxins: Bacillus cereus hemolysin binding component B (HblB or HBL-B) of the diarrheal enterotoxin hemolysin BL, Aeromonas hydrophila hemolytic (Ahl) component B (AhlB) of the tripartite AhlABC toxin, Vibrio cholerae cytotoxin motility associated killing factor A (MakA) cytotoxin, Xenorhabdus nematophila alpha-xenorhabdolysin (XaxA), Bacillus thuringiensis crystal 6Aa (Cry6Aa) parasporal crystal (Cry) toxin, and Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA) of the non-hemolytic enterotoxin Nhe, which, despite its name, is hemolytic, among others. In solution, ClyA proteins have an elongated, almost entirely alpha-helical structure, except for a short hydrophobic beta-hairpin known as the beta-tongue. Pore formation by ClyA requires circular oligomerization of the toxin by a sequential mechanism. This, in turn, concentrates the amphipathic helices in the center of the ring-like structure, forming a helical barrel that inserts into the membrane by a wedge-like mechanism. Compared with ClyA, NheA is almost entirely alpha-helical with an enlarged "head" domain, and an enlarged beta-tongue; it has been proposed that NheA could even form beta-barrel pores. Alpha-PFTs with similar structures are increasingly being found in eukaryotes, in particular as components of the immune systems of animals. This family may be distantly related to Escherichia coli alpha-PFT hemolysin E (HlyE, also known as ClyA or SheA).
Pssm-ID: 439149 [Multi-domain] Cd Length: 224 Bit Score: 40.47 E-value: 8.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 1983 DVKGNHND-LNDLKTRLE---TADLRNSGLLGALNDTMDKL--SAITNDTAAK------LQAVKEKAREANDTAKAVLAQ 2050
Cdd:cd21116 41 LARAHALEwLNEIKPKLLslpNDIIGYNNTFQSYYPDLIELadNLIKGDQGAKqqllqgLEALQSQVTKKQTSVTSFINE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117647249 2051 VKDLHQNLDGLKQNYNKLADSVAKTNAVVKDPSKNkiiadagtsVRNLEQEADRLIDKLKPIKELEDNLKKNISEIKELI 2130
Cdd:cd21116 121 LTTFKNDLDDDSRNLQTDATKAQAQVAVLNALKNQ---------LNSLAEQIDAAIDALEKLSNDWQTLDSDIKELITDL 191
|
170
....*....|...
gi 117647249 2131 NQARKQANSIKVS 2143
Cdd:cd21116 192 EDAESSIDAAFLQ 204
|
|
| |
