|
Name |
Accession |
Description |
Interval |
E-value |
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
37-285 |
1.51e-91 |
|
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: 297.73 E-value: 1.51e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 37 RGLFPAVLNLASNALITTNATCGEKGPEMYCKLVEHVpgqpVRNPQCRICNQNssNPNQRHPITNAIDGKN----TWWQS 112
Cdd:smart00136 5 RSCYPPFVNLAFGREVTATSTCGEPGPERYCKLVGHT----EQGKKCDYCDAR--NPRRSHPAENLTDGNNpnnpTWWQS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 113 PSIKNGIeyHYVTITLDLQQVFQIAYVIVKAAnSPRPGNWILERSLDDVEYKPWQYHAvtdTECLTLYNIyPRTGPPSYA 192
Cdd:smart00136 79 EPLSNGP--QNVNLTLDLGKEFHVTYVILKFC-SPRPSLWILERSDFGKTWQPWQYFS---SDCRRTFGR-PPRGPITKG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 193 KDDEVICTSFYSKIHPLENGEIHISLINGRPSADDP--SPELLEFTSARYIRLRFQRIRTLNADLMMfahkdpreIDPIV 270
Cdd:smart00136 152 NEDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDFdnSPVLQEWVTATNIRVRLTRLRTLGDELMD--------DRPEV 223
|
250
....*....|....*
gi 1677500969 271 TRRYYYSVKDISVGG 285
Cdd:smart00136 224 TRRYYYAISDIAVGG 238
|
|
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
39-285 |
3.89e-88 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 287.56 E-value: 3.89e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 39 LFPAVLNLASNALITTNATCGEKGPEMYCKLVEHVPGQpvrnpQCRICNqnSSNPNQRHPITNAIDGKN----TWWQSPS 114
Cdd:pfam00055 1 CYPAFGNLAFGREVSATSTCGLNGPERYCILSGLEGGK-----KCFICD--SRDPHNSHPPSNLTDSNNgtneTWWQSET 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 115 IKngIEYHYVTITLDLQQVFQIAYVIVKAAnSPRPGNWILERSLD-DVEYKPWQYHAvtdTECLTLYNIypRTGPPSYAK 193
Cdd:pfam00055 74 GV--IQYENVNLTLDLGKEFHFTYLILKFK-SPRPAAMVLERSTDfGKTWQPYQYFA---SDCRRTFGR--PSGPSRGIK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 194 DDEVICTSFYSKIHPLENGEIHISLINGRPSA--DDPSPELLEFTSARYIRLRFQRIRTLNadlmmfahkDPREIDPIVT 271
Cdd:pfam00055 146 DDEVICTSEYSDISPLTGGEVIFSTLEGRPSAniFDYSPELQDWLTATNIRIRLLRLHTLG---------DELLDDPSVL 216
|
250
....*....|....
gi 1677500969 272 RRYYYSVKDISVGG 285
Cdd:pfam00055 217 RKYYYAISDISVGG 230
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1593-1852 |
5.03e-87 |
|
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: 285.46 E-value: 5.03e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1593 VMSIN-LTGPLPAPYKMLYGLENMTQELKHLLSPQRAPERLIQLAEGNLNTLVTEMNELLTRATKVTADGEQTGQDAERT 1671
Cdd:pfam06008 1 LLSLNsLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1672 NTRAKSLGEFIKELARDAEAVNEKAIKLNETLgtrDEAFERNLEGLQKEIDQMIKELRRKNLETQKEIAEDELVAAEALL 1751
Cdd:pfam06008 81 LGHAKELAEAIKNLIDNIKEINEKVATLGEND---FALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQDLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1752 KKVKKLFGESRGENEEMEKDLREKLADYKNKVDDAWDLLREATDKIREANRLFAVNQKNMTALEKKKEAVESGKRQIENT 1831
Cdd:pfam06008 158 SRIQTWFQSPQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEET 237
|
250 260
....*....|....*....|.
gi 1677500969 1832 LKEGNDILDEANRLADEINSI 1852
Cdd:pfam06008 238 LKTARDSLDAANLLLQEIDDA 258
|
|
| LamB |
smart00281 |
Laminin B domain; |
1229-1364 |
4.33e-50 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 174.37 E-value: 4.33e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1229 HLEPFYWKLPEQFEGKKLMAYGGKLKYAIYFEAREEtGFSTYNPQVIIRGGtptHARIIVRHMAAPLIGQLTRHEIEMTE 1308
Cdd:smart00281 1 DNEPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRRG-GTHVSAPDVILEGN---GLRISHPAEGPPLPDELTTVEVRFRE 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1677500969 1309 KEWKYYGddprvHRTVTREDFLDILYDIHYILIKATYGNFMRQSRISEISMEVAEQ 1364
Cdd:smart00281 77 ENWQYYG-----GRPVTREDLMMVLANLTAILIRATYSQQMAGSRLSDVSLEVAVP 127
|
|
| Laminin_II |
pfam06009 |
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 ... |
2037-2173 |
6.69e-50 |
|
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 368703 [Multi-domain] Cd Length: 138 Bit Score: 174.21 E-value: 6.69e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2037 VKDKARQANDTAKDVLAQITELHQNLDGLKKNYNKLADSVAKTNAVVKDpsKNKIIADADATVKNLEQEADRLIDKLKPI 2116
Cdd:pfam06009 1 SKELAREANETAKEVLEQLAPLSQNLENTSEKLSGINRSLEETNELVND--ANKALDDAGRSVKKLEELAPDLLDKLKPL 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2117 KELEDN---LKKNISEIKELINQARKQANSIKVSVSSGGDCIRTYKPEIKKGSYNNIVVN 2173
Cdd:pfam06009 79 KQLEVNsssLSDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTSL 138
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2789-2917 |
3.36e-47 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 165.95 E-value: 3.36e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2789 VRTEAESGLLFYMARINHADFATVQLRNGLPYFSYDLGSGDTHTMIPTKINDGQWHKIKIMRSKQEGILYVDG-ASNRTI 2867
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGeARPTGE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1677500969 2868 SPKKADI-LDVVGMLYVGGLPINYTTRRIGPVTYSIDGCVRNLHMAEAPAD 2917
Cdd:pfam00054 81 SPLGATTdLDVDGPLYVGGLPSLGVKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
1234-1378 |
6.09e-44 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 157.05 E-value: 6.09e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1234 YWKLPEQFEGKKLMAYGGKLKYAIYFEAREETGFSTYNPQVIIRGGtptHARIIVRHMA--APLIGQLTRHEIEMTEKEW 1311
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGGGSLNSEPDVILEGN---GLRLSYSSPDqpPPDPGQEQTYSVRLHEENW 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1677500969 1312 KYygddpRVHRTVTREDFLDILYDIHYILIKATYGNFMRQSRISEISMEVAEQGRgttMTPPADLIE 1378
Cdd:pfam00052 78 RD-----SDGAPVSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSAVPGG---SGPPASWVE 136
|
|
| LamB |
smart00281 |
Laminin B domain; |
578-710 |
7.26e-43 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 153.57 E-value: 7.26e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 578 LPHSYYWSAPAPYLGNKLPAVGGQLTFTISYDLeeeEEDTERVLQLMIILEGNDLSISTAQdEVYLHPSEEHTNVLLLKE 657
Cdd:smart00281 1 DNEPVYWVAPEQFLGDKVTSYGGKLRYTLSFDG---RRGGTHVSAPDVILEGNGLRISHPA-EGPPLPDELTTVEVRFRE 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1677500969 658 ESFTIHGtHFPVRRKEFMTVLANLKRVLLQITYSFGMDAIfRLSSVNLESAVS 710
Cdd:smart00281 77 ENWQYYG-GRPVTREDLMMVLANLTAILIRATYSQQMAGS-RLSDVSLEVAVP 127
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
583-722 |
8.28e-40 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 145.11 E-value: 8.28e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 583 YWSAPAPYLGNKLPAVGGQLTFTISYDLeeEEEDTERVLQLMIILEGNDLSISTAQDE-VYLHPSEEHTNVLLLKEESFT 661
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEP--LPGGGSLNSEPDVILEGNGLRLSYSSPDqPPPDPGQEQTYSVRLHEENWR 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1677500969 662 iHGTHFPVRRKEFMTVLANLKRVLLQITYSFGMDAIfRLSSVNLESAVSYPTdGSIAAAVE 722
Cdd:pfam00052 79 -DSDGAPVSREDFMMVLANLTAILIRATYSTGSGQV-SLSNVSLDSAVPGGS-GPPASWVE 136
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2368-2503 |
5.26e-38 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 139.76 E-value: 5.26e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2368 FRTFSSSALLMYLATRDLRDFMSVELTDGHIKVSYDLGSGMASVVSNQNHNDGKWKSFTLSRIQKQANISivdIDTNQEE 2447
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLS---VDGEARP 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1677500969 2448 NIATSSSGNNfglDLKADDKIYFGGLPTLR-NLRPEVNLKKYSGCLKDIEISRTPYN 2503
Cdd:pfam00054 78 TGESPLGATT---DLDVDGPLYVGGLPSLGvKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2762-2911 |
1.87e-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: 139.09 E-value: 1.87e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2762 FGLSRNSHIAIAFDDTKvKNRLTIELEVRTEAESGLLFYMARINHADFATVQLRNGLPYFSYDLGSGDTHTMIPTKINDG 2841
Cdd:cd00110 2 VSFSGSSYVRLPTLPAP-RTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1677500969 2842 QWHKIKIMRSKQEGILYVDG-ASNRTISPKKADILDVVGMLYVGGLPINYTTRRIgPVTYSIDGCVRNLHM 2911
Cdd:cd00110 81 QWHSVSVERNGRSVTLSVDGeRVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGL-PVSPGFVGCIRDLKV 150
|
|
| LamG |
smart00282 |
Laminin G domain; |
2784-2911 |
2.08e-35 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 132.46 E-value: 2.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2784 TIELEVRTEAESGLLFYMARINHADFATVQLRNGLPYFSYDLGSGDTHTMI-PTKINDGQWHKIKIMRSKQEGILYVDG- 2861
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSdPTPLNDGQWHRVAVERNGRSVTLSVDGg 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2862 ASNRTISPKKADILDVVGMLYVGGLPINYtTRRIGPVTYSIDGCVRNLHM 2911
Cdd:smart00282 81 NRVSGESPGGLTILNLDGPLYLGGLPEDL-KLPPLPVTPGFRGCIRNLKV 129
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2174-2314 |
2.21e-35 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 132.44 E-value: 2.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2174 VKTAVADNLLFYLGSAKFIDFLAIEMRKGKVSFLWDVGSGVGRVEYPDlTIDDSYWYRIVASRTGRNGTISVRALDgpka 2253
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGD-KLNDGKWHSVELERNGRSGTLSVDGEA---- 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1677500969 2254 sivpsTHHSTSPPGYTIlDVDANAMLFVGGLTG-KLKKADAVRVITFTGCMGETYFDNKPIG 2314
Cdd:pfam00054 76 -----RPTGESPLGATT-DLDVDGPLYVGGLPSlGVKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2340-2497 |
5.81e-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: 126.38 E-value: 5.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2340 TIQFDGEGYALVSRPIRWYPNiSTVMFKFRTFSSSALLMYLATRDLRDFMSVELTDGHIKVSYDLGSGMASVVSNQNHND 2419
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRTR-LSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLND 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1677500969 2420 GKWKSFTLSRIQKQANISIvdidtNQEENIATSSSGNNFGLDLkaDDKIYFGGLPTLRNLRPEVNLKKYSGCLKDIEI 2497
Cdd:cd00110 80 GQWHSVSVERNGRSVTLSV-----DGERVVESGSPGGSALLNL--DGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKV 150
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2937-3089 |
2.11e-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: 2.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2937 GTYFDGTGFAKAVGGFKVGLDLLVEFEFRTTTTTGVLLGISSQ-KMDGMGIEMIDEKLMFHVDNGAGRFTAvydaGVPGH 3015
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQnGGDFLALELEDGRLVLRYDLGSGSLVL----SSKTP 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1677500969 3016 LCDGQWHKVTANKIKHRIELTVDGNQVEAQSPNPASTSADTNDPVFVGGFPDDLKQFGLTTSIPFRGCIRSLKL 3089
Cdd:cd00110 77 LNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKV 150
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2550-2691 |
4.11e-31 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 120.11 E-value: 4.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2550 FSTKNESGIILlgSGGTpapprrkrrQTGQAYYAILLNRGRLEVHLSTGARtmrKIVIRPEPNLfHDGREHSVHVERTRG 2629
Cdd:pfam00054 1 FRTTEPSGLLL--YNGT---------QTERDFLALELRDGRLEVSYDLGSG---AAVVRSGDKL-NDGKWHSVELERNGR 65
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1677500969 2630 IFTVQVDENRR--YMQNLTVEQ-PIEVKKLFVGGAPPE-FQPSPLRNIPPFEGCIWNLVINSVPMD 2691
Cdd:pfam00054 66 SGTLSVDGEARptGESPLGATTdLDVDGPLYVGGLPSLgVKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| LamG |
smart00282 |
Laminin G domain; |
2363-2499 |
4.42e-31 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 120.14 E-value: 4.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2363 TVMFKFRTFSSSALLMYLATRDLRDFMSVELTDGHIKVSYDLGSGMASVVSNQNH-NDGKWKSFTLSRIQKQANISIvdi 2441
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPlNDGQWHRVAVERNGRSVTLSV--- 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1677500969 2442 dtNQEENIATSSSGNNFGLDLkaDDKIYFGGLPTLRNLRPEVNLKKYSGCLKDIEISR 2499
Cdd:smart00282 78 --DGGNRVSGESPGGLTILNL--DGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNG 131
|
|
| LamG |
smart00282 |
Laminin G domain; |
2960-3089 |
4.62e-30 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 117.06 E-value: 4.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2960 VEFEFRTTTTTGVLLGISS-QKMDGMGIEMIDEKLMFHVDNGAGRFTAVYDagvPGHLCDGQWHKVTANKIKHRIELTVD 3038
Cdd:smart00282 2 ISFSFRTTSPNGLLLYAGSkGGGDYLALELRDGRLVLRYDLGSGPARLTSD---PTPLNDGQWHRVAVERNGRSVTLSVD 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1677500969 3039 G-NQVEAQSPnPASTSADTNDPVFVGGFPDDLKQFGLTTSIPFRGCIRSLKL 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 |
2.73e-28 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 112.90 E-value: 2.73e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2524 TVSFPKPGFVELSPVPID-VGTEINLSFSTKNESGIILLGSGgtpapprrkrrQTGQAYYAILLNRGRLEVHLSTGARTm 2602
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPrTRLSISFSFRTTSPNGLLLYAGS-----------QNGGDFLALELEDGRLVLRYDLGSGS- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2603 rkIVIRPePNLFHDGREHSVHVERTRGIFTVQVDENR--RYMQNLTVEQPIEVKKLFVGGAPPEFQPSPLRNIPPFEGCI 2680
Cdd:cd00110 69 --LVLSS-KTPLNDGQWHSVSVERNGRSVTLSVDGERvvESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCI 145
|
....*.
gi 1677500969 2681 WNLVIN 2686
Cdd:cd00110 146 RDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
2169-2311 |
3.28e-27 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 108.97 E-value: 3.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2169 NIVVNVKTAVADNLLFYLGSAKFIDFLAIEMRKGKVSFLWDVGSGVGRVEYPDLTIDDSYWYRIVASRTGRNGTISVral 2248
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLNDGQWHRVAVERNGRSVTLSV--- 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1677500969 2249 DGPKASIVpsthhsTSPPGYTILDVDANamLFVGGLTGKLKKADAVRVITFTGCMGETYFDNK 2311
Cdd:smart00282 78 DGGNRVSG------ESPGGLTILNLDGP--LYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2150-2309 |
4.41e-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: 103.65 E-value: 4.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2150 SGGDCIRtYKPEIKKGSYNNIVVNVKTAVADNLLFYLGSAKFIDFLAIEMRKGKVSFLWDVGSGVGRVEYPDlTIDDSYW 2229
Cdd:cd00110 5 SGSSYVR-LPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKT-PLNDGQW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2230 YRIVASRTGRNGTISVralDGpkASIVpsthHSTSPPGYTILDVDANamLFVGGLTGKLKKADAVRVITFTGCMGETYFD 2309
Cdd:cd00110 83 HSVSVERNGRSVTLSV---DG--ERVV----ESGSPGGSALLNLDGP--LYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
2545-2688 |
2.11e-24 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 100.88 E-value: 2.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2545 EINLSFSTKNESGIILLGSGGTpapprrkrrqtGQAYYAILLNRGRLEVHLSTGARTmrkIVIRPEPNLFHDGREHSVHV 2624
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKG-----------GGDYLALELRDGRLVLRYDLGSGP---ARLTSDPTPLNDGQWHRVAV 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1677500969 2625 ERTRGIFTVQVD-ENRRYMQNLTVEQPIEVK-KLFVGGAPPEFQPSPLRNIPPFEGCIWNLVINSV 2688
Cdd:smart00282 67 ERNGRSVTLSVDgGNRVSGESPGGLTILNLDgPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2964-3089 |
1.95e-22 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 95.18 E-value: 1.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2964 FRTTTTTGVLLGISSQKMDGMGIEMIDEKLMFHVDNGAGRFTAVYdagVPGHLCDGQWHKVTANKIKHRIELTVDGNQVE 3043
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDFLALELVNGRLVLRYDLGSGPESLLS---SGKNLNDGQWHSVRVERNGNTLTLSVDGQTVV 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1677500969 3044 AQSPNPASTSADTNDPVFVGGFPDDLKQFGLTTSIPFRGCIRSLKL 3089
Cdd:pfam02210 78 SSLPPGESLLLNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRV 123
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1675-2164 |
9.21e-21 |
|
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: 100.48 E-value: 9.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1675 AKSLGEfIKELARDAEAVNEKA---IKLNETLGTRDEAFERNLEGLQKEIDQMIKELRRKNLEtqkeiaedeLVAAEALL 1751
Cdd:TIGR04523 141 DKFLTE-IKKKEKELEKLNNKYndlKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELL---------LSNLKKKI 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1752 KKVKKL---FGESRGENEEMEKDLREKladyKNKVDDAWDLLREATDKIreaNRLFAVNQKNMTALEKKKEAVESGKRQI 1828
Cdd:TIGR04523 211 QKNKSLesqISELKKQNNQLKDNIEKK----QQEINEKTTEISNTQTQL---NQLKDEQNKIKKQLSEKQKELEQNNKKI 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1829 ENTLKEGNDILDE------------ANRLADEINSIIDYVEDIQTKLPPMSE---ELNDKIDDLSQEI---------KDR 1884
Cdd:TIGR04523 284 KELEKQLNQLKSEisdlnnqkeqdwNKELKSELKNQEKKLEEIQNQISQNNKiisQLNEQISQLKKELtnsesenseKQR 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1885 KLAEKVSQAESHAAQlNDSSavldgiLDEAKNISfnataafkaySNIKDYIDEAEKVAKEAKDLAHEATKLATGPRGLLK 1964
Cdd:TIGR04523 364 ELEEKQNEIEKLKKE-NQSY------KQEIKNLE----------SQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEK 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1965 EdakgclQKsfRILNEAKKLANDVKENEDHLNGLKTRIENADARNGDLLRTLNDTLGKLSAIPNDTAAKLQAVKDKARQA 2044
Cdd:TIGR04523 427 E------IE--RLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKEL 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2045 ---NDTAKDVLAQITELHQNLDGLKKNYNKLADSVAKTNAVVKDPSKNKIIADADATVKNLEQEADRLIDKLKPIKELED 2121
Cdd:TIGR04523 499 kklNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQK 578
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1677500969 2122 NLKKNISEIKELINQARKQANSIKVSVSSGGDCIRTYKPEIKK 2164
Cdd:TIGR04523 579 SLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEK 621
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1636-2145 |
1.60e-19 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 96.67 E-value: 1.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1636 AEGNLNTLVTEMNELLTRATKVTAdgeQTGQDAERTNTRAKSLGEFIKElardaeaVNEKAIKLNETlgtrdeafERNLE 1715
Cdd:PRK03918 163 AYKNLGEVIKEIKRRIERLEKFIK---RTENIEELIKEKEKELEEVLRE-------INEISSELPEL--------REELE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1716 GLQKEIDQMiKELRRK--NLETQKEIAEDELVAAEALLKKVKKLFGESRGENEEMEKDLRE--KLADYKNKVDDAWDLLR 1791
Cdd:PRK03918 225 KLEKEVKEL-EELKEEieELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKElkELKEKAEEYIKLSEFYE 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1792 EATDKIREA-------NRLFAVNQKNMTALEKKKEAVESGKRQIENTLKEGNDI------LDEANRLADEINSI------ 1852
Cdd:PRK03918 304 EYLDELREIekrlsrlEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELeerhelYEEAKAKKEELERLkkrltg 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1853 ---------IDYVEDIQTKLPPMSEELNDKIDDLSQEIKDRKLA-EKVSQA--------------------ESHAAQLND 1902
Cdd:PRK03918 384 ltpeklekeLEELEKAKEEIEEEISKITARIGELKKEIKELKKAiEELKKAkgkcpvcgrelteehrkellEEYTAELKR 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1903 SS---AVLDGILDEAKN---------------ISFNATAAF--KAYSNIKDY-IDEAEKVAKEAKDLAHEATKLATGPRG 1961
Cdd:PRK03918 464 IEkelKEIEEKERKLRKelrelekvlkkeselIKLKELAEQlkELEEKLKKYnLEELEKKAEEYEKLKEKLIKLKGEIKS 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1962 LLKEdakgcLQKSFRILNEAKKLANDVKENEDHLNGLKTRIENA--------DARNGDLLRTLNDTLgKLSAIPNDTAAK 2033
Cdd:PRK03918 544 LKKE-----LEKLEELKKKLAELEKKLDELEEELAELLKELEELgfesveelEERLKELEPFYNEYL-ELKDAEKELERE 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2034 LQAVKDKARQANDTAKD---VLAQITELHQNLDGLKKNYNKladsvaKTNAVVKDP--SKNKIIADADATVKNLE---QE 2105
Cdd:PRK03918 618 EKELKKLEEELDKAFEElaeTEKRLEELRKELEELEKKYSE------EEYEELREEylELSRELAGLRAELEELEkrrEE 691
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 1677500969 2106 ADRLIDKLKP--------IKELEdNLKKNISEIKELINQARKQANSIK 2145
Cdd:PRK03918 692 IKKTLEKLKEeleerekaKKELE-KLEKALERVEELREKVKKYKALLK 738
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1705-1990 |
1.53e-14 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 77.26 E-value: 1.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1705 TRDEAFERNLEGLQKEIDQM---IKELRRKNLETQKEIAEdelVAAE--ALLKKVKKLFGESRGENEEMeKDLREKLADY 1779
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELreeIEELKEKRDELNEELKE---LAEKrdELNAQVKELREEAQELREKR-DELNEKVKEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1780 KNKVDDAWDLLREATDKIREANRLFAVNQKNMTALEKKKEAVESGKRQIEN---TLKEGNDILDEANRLADEInsiidyv 1856
Cdd:COG1340 77 KEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTevlSPEEEKELVEKIKELEKEL------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1857 EDIQtklppMSEELNDKIDDLSQEIKD---------RKLAEKVSQAESHAAQLNDSSAVLDGILDEAKnisfnatAAFKA 1927
Cdd:COG1340 150 EKAK-----KALEKNEKLKELRAELKElrkeaeeihKKIKELAEEAQELHEEMIELYKEADELRKEAD-------ELHKE 217
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1677500969 1928 YSNIKDYIDEAEK----VAKEAKDLAHEATKLATGPRGLLKEDAKgclqksfrilNEAKKLANDVKE 1990
Cdd:COG1340 218 IVEAQEKADELHEeiieLQKELRELRKELKKLRKKQRALKREKEK----------EELEEKAEEIFE 274
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1703-2105 |
2.84e-14 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 77.63 E-value: 2.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1703 LGTRDEAFERNLEGLQKEIDQMIKELrrknletqKEIAEDELVAAEALLKKVKKLFGESRGENEEMEKdLREKLADYKNK 1782
Cdd:COG4372 4 LGEKVGKARLSLFGLRPKTGILIAAL--------SEQLRKALFELDKLQEELEQLREELEQAREELEQ-LEEELEQARSE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1783 VDDAWDLLREATDKIREANRLFAVNQKNMTALEKKKEAVEsgkRQIENTLKEGNDILDEANRLADEINSIIDYVEDIQTK 1862
Cdd:COG4372 75 LEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQ---EELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1863 LppmsEELNDKIDDLSQEIKdrKLAEKVSQAESHAAQlndssAVLDGILDEAKNISFNATAAFKAYSNIKDYIDEAEKVA 1942
Cdd:COG4372 152 L----KELEEQLESLQEELA--ALEQELQALSEAEAE-----QALDELLKEANRNAEKEEELAEAEKLIESLPRELAEEL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1943 KEAKDLAHEATKLATgprgllkedakgclqksFRILNEAKKLANDVKENEDHLNGLKTRIENADARNGDLLRTLNDTLGK 2022
Cdd:COG4372 221 LEAKDSLEAKLGLAL-----------------SALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAAL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2023 LSAIPNDTAAKLQAVKDKARQANDTAKDVLAQitelhQNLDGLKKNYNKLADSVAKTNAVVKDPSKNKIIADADATVKNL 2102
Cdd:COG4372 284 ELEALEEAALELKLLALLLNLAALSLIGALED-----ALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLEL 358
|
...
gi 1677500969 2103 EQE 2105
Cdd:COG4372 359 LSK 361
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1718-2077 |
1.43e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 77.40 E-value: 1.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1718 QKEIDQMIK---ELRRKNLE---------TQKEIAEDELVAAEALLKKVKKLFGESRG--ENEEMEKDLREKLADYKNKV 1783
Cdd:TIGR02168 143 QGKISEIIEakpEERRAIFEeaagiskykERRKETERKLERTRENLDRLEDILNELERqlKSLERQAEKAERYKELKAEL 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1784 DDA-WDLLreaTDKIREANrlfavnqKNMTALEKKKEAVESGKRQIENTLKEgndiLDEA-NRLADEINSIIDYVEDIQT 1861
Cdd:TIGR02168 223 RELeLALL---VLRLEELR-------EELEELQEELKEAEEELEELTAELQE----LEEKlEELRLEVSELEEEIEELQK 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1862 KLppmsEELNDKIDDLSQEIkdRKLAEKVSQAESHAAQLNDSSAVLDGILDEAKnisFNATAAFKAYSNIKDYIDEAEKV 1941
Cdd:TIGR02168 289 EL----YALANEISRLEQQK--QILRERLANLERQLEELEAQLEELESKLDELA---EELAELEEKLEELKEELESLEAE 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1942 AKEAKDLAHEATKLATGPRGLLKEDAKgclqKSFRILNEAKKLANDVKENEDHLNGLKTRIENADARNGDLLRTLND--- 2018
Cdd:TIGR02168 360 LEELEAELEELESRLEELEEQLETLRS----KVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEael 435
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1677500969 2019 -----TLGKLSAIPNDTAAKLQAV----------KDKARQANDTAKDVLAQITELHQNLDGLKKNYNKLADSVA 2077
Cdd:TIGR02168 436 kelqaELEELEEELEELQEELERLeealeelreeLEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVK 509
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
917-965 |
2.83e-13 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 66.22 E-value: 2.83e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1677500969 917 PCRCNAGGSFSEVCHSQTGQCECRANVQGQRCDKCKAGTFGLQS-ARGCV 965
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSqGGGCQ 50
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1640-2133 |
5.85e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 75.08 E-value: 5.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1640 LNTLVTEMNELLT------------RATKVTADG-----EQTGQDAERTNTRAKSLGEFIKELARDAEAVNEKAIKLNET 1702
Cdd:PRK02224 208 LNGLESELAELDEeieryeeqreqaRETRDEADEvleehEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRER 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1703 LGTRDEAFERNLEGLQ-KEIDQMIKELRRKNLETQKEIAEDELV-----------AAEALLKKVKKLFGES---RGENEE 1767
Cdd:PRK02224 288 LEELEEERDDLLAEAGlDDADAEAVEARREELEDRDEELRDRLEecrvaaqahneEAESLREDADDLEERAeelREEAAE 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1768 MEKDL---REKLADYKNKVDDawdlLREATDKIREANRLFAVNQKNMTA----LEKKKEAVESGKRQIENTLKEGNDILD 1840
Cdd:PRK02224 368 LESELeeaREAVEDRREEIEE----LEEEIEELRERFGDAPVDLGNAEDfleeLREERDELREREAELEATLRTARERVE 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1841 EANRLADEIN-----------SIIDYVEDIQTKLPPMSEELND---KIDDLSQEIkDRklAEKVSQAESHAAQLNDSSAV 1906
Cdd:PRK02224 444 EAEALLEAGKcpecgqpvegsPHVETIEEDRERVEELEAELEDleeEVEEVEERL-ER--AEDLVEAEDRIERLEERRED 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1907 LDGILDEAKNIsfnataafkaysnIKDYIDEAEKVAKEAKDLAHEATKlatgprgllKEDAKGCLQKsfrilnEAKKLAN 1986
Cdd:PRK02224 521 LEELIAERRET-------------IEEKRERAEELRERAAELEAEAEE---------KREAAAEAEE------EAEEARE 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1987 DVKENEDHLNGLKTRIENadarngdlLRTLNDTLGKLSaipnDTAAKLQAVKDKaRQA----NDTAKDVLAQITELHQNL 2062
Cdd:PRK02224 573 EVAELNSKLAELKERIES--------LERIRTLLAAIA----DAEDEIERLREK-REAlaelNDERRERLAEKRERKREL 639
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1677500969 2063 DGlkknynKLadsvaktnavvkDPSKnkiIADADATVKNLEQEADRLIDKLKPIKELEDNLKKNI----SEIKEL 2133
Cdd:PRK02224 640 EA------EF------------DEAR---IEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIgaveNELEEL 693
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
967-1011 |
6.55e-13 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 65.03 E-value: 6.55e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1677500969 967 CNCNSFGSKSFDCE-ESGQCWCQPGVTGKKCDRCAHGYFNFQEGGC 1011
Cdd:smart00180 1 CDCDPGGSASGTCDpDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1613-2179 |
6.92e-13 |
|
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: 74.76 E-value: 6.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1613 ENMTQELKHLLSPQRAPERLIQLAEGNLNTLVTEmnelltratkvtadGEQTGQDAERTNTRAKSLGEFIKEL-ARDAEA 1691
Cdd:pfam05483 105 ENKLQENRKIIEAQRKAIQELQFENEKVSLKLEE--------------EIQENKDLIKENNATRHLCNLLKETcARSAEK 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1692 VNEKAIKLNETlgtrdeafERNLEGLQKEIDQMI---KELR----RKNLETQKEIAEDElvaaeallKKVKKLFGESRGE 1764
Cdd:pfam05483 171 TKKYEYEREET--------RQVYMDLNNNIEKMIlafEELRvqaeNARLEMHFKLKEDH--------EKIQHLEEEYKKE 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1765 NEEMEKD---LREKLADYKNKVDDAWDLLREATDKIREANRLFAVNQKNMTALEKKKEAVESGKRQIENTLKEG---NDI 1838
Cdd:pfam05483 235 INDKEKQvslLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSmstQKA 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1839 LDEANRLADEinSIIDYVEDIQTKLppmsEELNDKIDDLSQEIKDRKLA----EKVSQAESHAAQLNDSSAVLDGILDEA 1914
Cdd:pfam05483 315 LEEDLQIATK--TICQLTEEKEAQM----EELNKAKAAHSFVVTEFEATtcslEELLRTEQQRLEKNEDQLKIITMELQK 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1915 KNISFNATAAFKaySNIKDYIDEAEKVAKEAKDLAHEATKLATgprglLKEDAKGCLQKSFRILNEAKKLAND------- 1987
Cdd:pfam05483 389 KSSELEEMTKFK--NNKEVELEELKKILAEDEKLLDEKKQFEK-----IAEELKGKEQELIFLLQAREKEIHDleiqlta 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1988 VKENEDH----LNGLKTRIENADARNGDLLRTLNDTLGKLSAIPNDTAAKLQAVKDKARQANDTAKD---VLAQI----- 2055
Cdd:pfam05483 462 IKTSEEHylkeVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQeerMLKQIenlee 541
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2056 --TELHQNLDGLKKNYNKLADSV------AKTNAVVKDPS---KNKIIADADATVKNLEQEADrliDKLKPIKELEDN-- 2122
Cdd:pfam05483 542 keMNLRDELESVREEFIQKGDEVkckldkSEENARSIEYEvlkKEKQMKILENKCNNLKKQIE---NKNKNIEELHQEnk 618
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1677500969 2123 -LKKNISEIKELINQARKQANSIKVSVSSG----GDCIRTYKPEI--KKGSYNNIVVNVKTAVA 2179
Cdd:pfam05483 619 aLKKKGSAENKQLNAYEIKVNKLELELASAkqkfEEIIDNYQKEIedKKISEEKLLEEVEKAKA 682
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1649-2142 |
1.33e-12 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 74.09 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1649 ELLTRAtKVTADGEQTG--QDAERTNTRAkslGEFIKELARDAEAVNEKAIKLNETLgtRDEAFERnLEGLQKEIDQMIK 1726
Cdd:NF041483 484 ELLTKA-KADADELRSTatAESERVRTEA---IERATTLRRQAEETLERTRAEAERL--RAEAEEQ-AEEVRAAAERAAR 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1727 ELRRKN---LETQKEIAEDEL----VAAEALLKKVKKLFGESRGENEEMEKDLREKLadyknkvddawDLLR-EATDKIR 1798
Cdd:NF041483 557 ELREETeraIAARQAEAAEELtrlhTEAEERLTAAEEALADARAEAERIRREAAEET-----------ERLRtEAAERIR 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1799 --------EANRL-----------------FAVNQKNMTALEK---KKEAVESGKR-------QIENTLKEGNDIL---- 1839
Cdd:NF041483 626 tlqaqaeqEAERLrteaaadasaaraegenVAVRLRSEAAAEAerlKSEAQESADRvraeaaaAAERVGTEAAEALaaaq 705
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1840 DEANRL---ADEI-NSIIDYVEDIQTKLPPMSEEL----NDKIDDLSQEIK------DRKLAEKVSQAESHAAQLNDSSA 1905
Cdd:NF041483 706 EEAARRrreAEETlGSARAEADQERERAREQSEELlasaRKRVEEAQAEAQrlveeaDRRATELVSAAEQTAQQVRDSVA 785
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1906 vldGILDEAKN-ISFNATAAFKAYSNIK-DYIDEAEKVAKEAKDLAHEATKLATGPRGLLKEDAKGCLQKSFRILN---- 1979
Cdd:NF041483 786 ---GLQEQAEEeIAGLRSAAEHAAERTRtEAQEEADRVRSDAYAERERASEDANRLRREAQEETEAAKALAERTVSeaia 862
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1980 EAKKLANDVKENEDhlnglKTRIENADAR---NGDLLRTLNDTLGKLSAIPNDTAAklQAVKDKARQANDTAKDVLAQIT 2056
Cdd:NF041483 863 EAERLRSDASEYAQ-----RVRTEASDTLasaEQDAARTRADAREDANRIRSDAAA--QADRLIGEATSEAERLTAEARA 935
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2057 ELHQNLDGLKKNYNKL-ADSVAKTNAVVKDPSKN--KIIADADATVKNLEQEADRLIDKLKPIK-----ELEDNLKKNIS 2128
Cdd:NF041483 936 EAERLRDEARAEAERVrADAAAQAEQLIAEATGEaeRLRAEAAETVGSAQQHAERIRTEAERVKaeaaaEAERLRTEARE 1015
|
570
....*....|....
gi 1677500969 2129 EIKELINQARKQAN 2142
Cdd:NF041483 1016 EADRTLDEARKDAN 1029
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1702-2118 |
1.42e-12 |
|
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: 73.45 E-value: 1.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1702 TLGTRDEAFERNLEGLQKEiDQMIKELRRKNLE-TQKEIAEDELVAA-----EALLKKVKKLFGESRGENEEMEKDLREK 1775
Cdd:COG5185 205 NSIKESETGNLGSESTLLE-KAKEIINIEEALKgFQDPESELEDLAQtsdklEKLVEQNTDLRLEKLGENAESSKRLNEN 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1776 LADYKNKVDDAWDLLREATDKI------REANRLFAVNQKNmTALEKKKEAVESG-KRQIENTLKEGNDILDEANRLADE 1848
Cdd:COG5185 284 ANNLIKQFENTKEKIAEYTKSIdikkatESLEEQLAAAEAE-QELEESKRETETGiQNLTAEIEQGQESLTENLEAIKEE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1849 INSIIDyvEDIQTKLPPMSEELNDKIDDLSQEIkDRKLAEKVSQAESHAAQLNDSSAVLDGILDEAKNISFNATAAFKAY 1928
Cdd:COG5185 363 IENIVG--EVELSKSSEELDSFKDTIESTKESL-DEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEV 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1929 SNIKD-YIDEAEKVAKEAKDLAHEatklatgprgllkedakgclqksfRILNEAKKLANDVKENEDHLNGLKTRIENAda 2007
Cdd:COG5185 440 SKLLNeLISELNKVMREADEESQS------------------------RLEEAYDEINRSVRSKKEDLNEELTQIESR-- 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2008 rngdlLRTLNDTLGKLSAipnDTAAKLQAVKDKARQANDTAKDvlaqiTELHQNLDGLKKNYNKLADSVAKTNavvkDPS 2087
Cdd:COG5185 494 -----VSTLKATLEKLRA---KLERQLEGVRSKLDQVAESLKD-----FMRARGYAHILALENLIPASELIQA----SNA 556
|
410 420 430
....*....|....*....|....*....|.
gi 1677500969 2088 KNKIIADADATVKNLEQEADRLIDKLKPIKE 2118
Cdd:COG5185 557 KTDGQAANLRTAVIDELTQYLSTIESQQARE 587
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
918-964 |
1.55e-12 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 64.25 E-value: 1.55e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1677500969 918 CRCNAGGSFSEVCHSQTGQCECRANVQGQRCDKCKAGTFGlQSARGC 964
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. |
918-964 |
4.60e-12 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 62.76 E-value: 4.60e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1677500969 918 CRCNAGGSFSEVCHSQTGQCECRANVQGQRCDKCKAGTFGLQ--SARGC 964
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPsdPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
966-1012 |
9.25e-12 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 61.99 E-value: 9.25e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1677500969 966 PCNCNSFGSKSFDCE-ESGQCWCQPGVTGKKCDRCAHGYFNF--QEGGCT 1012
Cdd:cd00055 1 PCDCNGHGSLSGQCDpGTGQCECKPNTTGRRCDRCAPGYYGLpsQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
864-916 |
6.10e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 59.68 E-value: 6.10e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1677500969 864 PCQCNDNldFSIPGSCDSLSGSCLiCKPGTTGRYCELCADGYFGDAVDAKNCQ 916
Cdd:cd00055 1 PCDCNGH--GSLSGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
967-1014 |
9.06e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 59.29 E-value: 9.06e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1677500969 967 CNCNSFGSKSFDCE-ESGQCWCQPGVTGKKCDRCAHGYFNFQEGGCTAC 1014
Cdd:pfam00053 1 CDCNPHGSLSDTCDpETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1420-1466 |
1.68e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 58.52 E-value: 1.68e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1420 CQCNGHSSL---CDPETSICQnCQHHTAGDFCERCALGYYGIVKGLPNDC 1466
Cdd:pfam00053 1 CDCNPHGSLsdtCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
756-805 |
1.81e-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: 1.81e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1677500969 756 PCQCFGHA---ESCDDVTGECLnCKDHTGGPYCDKCLPGFYGEPTKGtsEDCQ 805
Cdd:cd00055 1 PCDCNGHGslsGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQG--GGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1060-1108 |
2.00e-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: 2.00e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1677500969 1060 CNCSTVGSLDFQCNVNTGQCNCHPKFSGAKCTECSRGHWNYPRCNLCDC 1108
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1527-1574 |
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 1677500969 1527 CECDPYGSLPVPCDPVTGFCTCRPGATGRKCDGCKHWHAREGWECVFC 1574
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGC 49
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1612-1883 |
4.73e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.85 E-value: 4.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1612 LENMTQELKHLLSPQRAPERLIQLAEGNLNTLVTEMNELLTRATK-------VTADGEQTGQDAERTNTRAKSLGEFIKE 1684
Cdd:TIGR02168 728 ISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEaeeelaeAEAEIEELEAQIEQLKEELKALREALDE 807
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1685 LARDAEAVNEKAIKLNETLG---TRDEAFERNLEGLQKEIDQMIKEL-----RRKNLETQKEIAEDELVAAEALLKKVKK 1756
Cdd:TIGR02168 808 LRAELTLLNEEAANLRERLEsleRRIAATERRLEDLEEQIEELSEDIeslaaEIEELEELIEELESELEALLNERASLEE 887
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1757 LFGESRGENEEMEKDLREkladYKNKVDDAWDLLREATDKIREANRlfAVNQKNMTALEKKKEAVESGKRQIENTLKEGN 1836
Cdd:TIGR02168 888 ALALLRSELEELSEELRE----LESKRSELRRELEELREKLAQLEL--RLEGLEVRIDNLQERLSEEYSLTLEEAEALEN 961
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1677500969 1837 DILDEANRLADEINSI---IDYVEDIQtklpPMS----EELNDKIDDLSQEIKD 1883
Cdd:TIGR02168 962 KIEDDEEEARRRLKRLenkIKELGPVN----LAAieeyEELKERYDFLTAQKED 1011
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1527-1570 |
5.09e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.94 E-value: 5.09e-10
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1677500969 1527 CECDPYGSLPVPCDPVTGFCTCRPGATGRKCDGCKHWHAREGWE 1570
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPP 44
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1419-1467 |
6.96e-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: 6.96e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1677500969 1419 PCQCNGHSSL---CDPETSICQnCQHHTAGDFCERCALGYYGIVKGlPNDCQ 1467
Cdd:cd00055 1 PCDCNGHGSLsgqCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQ-GGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1059-1101 |
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
....*....|....*....|....*....|....*....|...
gi 1677500969 1059 ACNCSTVGSLDFQCNVNTGQCNCHPKFSGAKCTECSRGHWNYP 1101
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1106-1163 |
8.76e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 56.59 E-value: 8.76e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1677500969 1106 CDCFLPGTDATTCDSETkkcscsdqtGQCTCKVNVEGIHCDRCRPGKFGLDAKNPLGC 1163
Cdd:pfam00053 1 CDCNPHGSLSDTCDPET---------GQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1106-1163 |
2.19e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 55.40 E-value: 2.19e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1677500969 1106 CDCFLPGTDATTCDSETkkcscsdqtGQCTCKVNVEGIHCDRCRPGKFGldaKNPLGC 1163
Cdd:smart00180 1 CDCDPGGSASGTCDPDT---------GQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1014-1057 |
2.36e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 55.01 E-value: 2.36e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1677500969 1014 CECS---HLGNNCDPKTGRCICPPNTIGEKCSKCAPNTWGHSiTTGC 1057
Cdd:smart00180 1 CDCDpggSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG-PPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1106-1163 |
2.66e-09 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 55.05 E-value: 2.66e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1677500969 1106 CDCFLPGTDATTCDSETkkcscsdqtGQCTCKVNVEGIHCDRCRPGKFGlDAKNPLGC 1163
Cdd:cd00055 2 CDCNGHGSLSGQCDPGT---------GQCECKPNTTGRRCDRCAPGYYG-LPSQGGGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1013-1058 |
2.69e-09 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 55.05 E-value: 2.69e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1013 ACECSHLG---NNCDPKTGRCICPPNTIGEKCSKCAPNTWGH-SITTGCK 1058
Cdd:cd00055 1 PCDCNGHGslsGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLpSQGGGCQ 50
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1612-1888 |
2.69e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.16 E-value: 2.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1612 LENMTQELKHLLSPQRAPERLIQLAEgnlntlvtEMNELLTRATKVTA-DGEQTGQDAERTNTRAKSLGEFIKELARDAE 1690
Cdd:PRK03918 478 LRKELRELEKVLKKESELIKLKELAE--------QLKELEEKLKKYNLeELEKKAEEYEKLKEKLIKLKGEIKSLKKELE 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1691 AVNE---KAIKLNETLGTRDE---AFERNLEGL----QKEIDQMIKELR------------RKNLETQKE---IAEDELV 1745
Cdd:PRK03918 550 KLEElkkKLAELEKKLDELEEelaELLKELEELgfesVEELEERLKELEpfyneylelkdaEKELEREEKelkKLEEELD 629
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1746 AAEALLKKVKKLFGESRGENEEMEKDLREKlaDYKNKvddawdllreaTDKIREANRLFAvnqknmtALEKKKEAVESGK 1825
Cdd:PRK03918 630 KAFEELAETEKRLEELRKELEELEKKYSEE--EYEEL-----------REEYLELSRELA-------GLRAELEELEKRR 689
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1677500969 1826 RQIENTLKEGNDILDEANRLADEInsiidyvEDIQTKLPPMsEELNDKIDDLSQEIKDRKLAE 1888
Cdd:PRK03918 690 EEIKKTLEKLKEELEEREKAKKEL-------EKLEKALERV-EELREKVKKYKALLKERALSK 744
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1014-1057 |
6.32e-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: 6.32e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1677500969 1014 CECSHLG---NNCDPKTGRCICPPNTIGEKCSKCAPNTWGHSITTGC 1057
Cdd:pfam00053 1 CDCNPHGslsDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQ 47
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
865-908 |
9.21e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 53.47 E-value: 9.21e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1677500969 865 CQCNdnLDFSIPGSCDSLSGSCLiCKPGTTGRYCELCADGYFGD 908
Cdd:smart00180 1 CDCD--PGGSASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD 41
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1527-1562 |
9.26e-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: 53.51 E-value: 9.26e-09
10 20 30
....*....|....*....|....*....|....*.
gi 1677500969 1527 CECDPYGSLPVPCDPVTGFCTCRPGATGRKCDGCKH 1562
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKP 36
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1857-2146 |
1.34e-08 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 59.31 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1857 EDIQTKLPpmseELNDKIDDLSQEIKDRKLAEKVSQaeSHAAQLNDSsaVLDGILDEAKNIS-FNATAAFKA---YSNIK 1932
Cdd:cd22656 26 EEYRKRLG----ISSDIDDKLSSDFDPLLDAYKSIK--DHCTDFKDD--TYPSIVSLAGDIYnYAQNAGGTIdsyYAEIL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1933 DYIDEA-----EKVAKEAKDLAHEATKLatgprglLKEDAKGCLQKSFRILNEAKKLANDVKENEDHLNGLKTRienada 2007
Cdd:cd22656 98 ELIDDLadatdDEELEEAKKTIKALLDD-------LLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKA------ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2008 rngdllrtLNDTLGK-LSAIPNDTAAKLQAVKDKARQAndtakdvlaQITELHQNLDGLKKNYNKLADSVAKTNAVVKDp 2086
Cdd:cd22656 165 --------LKDLLTDeGGAIARKEIKDLQKELEKLNEE---------YAAKLKAKIDELKALIADDEAKLAAALRLIAD- 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2087 sknkiIADADATVKNLEQEADRLIDKLKPIKELEDNLKKNISEIKELINQARKQANSIKV 2146
Cdd:cd22656 227 -----LTAADTDLDNLLALIGPAIPALEKLQGAWQAIATDLDSLKDLLEDDISKIPAAIL 281
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
414-471 |
1.36e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 53.13 E-value: 1.36e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1677500969 414 CHCDPIGSLNEVCVkdekharrgLAPGSCHCKTGFGGVSCDRCARGYTGYPDCKACNC 471
Cdd:pfam00053 1 CDCNPHGSLSDTCD---------PETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1060-1101 |
1.69e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 52.70 E-value: 1.69e-08
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1677500969 1060 CNCSTVGSLDFQCNVNTGQCNCHPKFSGAKCTECSRGHWNYP 1101
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
757-797 |
3.00e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 51.97 E-value: 3.00e-08
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1677500969 757 CQCFGHA---ESCDDVTGECLnCKDHTGGPYCDKCLPGFYGEPT 797
Cdd:pfam00053 1 CDCNPHGslsDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPS 43
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
469-515 |
3.24e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 51.97 E-value: 3.24e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1677500969 469 CNCSGLGSKNE--DPCFGPCICKENVEGGDCSRCKSGFFNLQEDNWKGC 515
Cdd:pfam00053 1 CDCNPHGSLSDtcDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
865-911 |
3.28e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 51.97 E-value: 3.28e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1677500969 865 CQCNDNLdfSIPGSCDSLSGSCLiCKPGTTGRYCELCADGYFGDAVD 911
Cdd:pfam00053 1 CDCNPHG--SLSDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSD 44
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
413-465 |
7.07e-08 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 51.20 E-value: 7.07e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1677500969 413 PCHCDPIGSLNEVCVKDEkharrglapGSCHCKTGFGGVSCDRCARGYTGYPD 465
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGT---------GQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1630-1847 |
9.48e-08 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 58.30 E-value: 9.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1630 ERLIQLAEGNLNTLVTEMNElltRATKVTADGEQTG--------QDAERTNTRAKSLGEFIKELAR------------DA 1689
Cdd:NF041483 1040 DTLITEAAAEADQLTAKAQE---EALRTTTEAEAQAdtmvgaarKEAERIVAEATVEGNSLVEKARtdadellvgarrDA 1116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1690 EAVNEKAiklnETLGTRDEAfernleglqkEIDQMIKELRRKNLETQKEIAE--DELV-AAEallkkvkklfgESRGENE 1766
Cdd:NF041483 1117 TAIRERA----EELRDRITG----------EIEELHERARRESAEQMKSAGErcDALVkAAE-----------EQLAEAE 1171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1767 EMEKDLREKLADYKNK-----VDDAWDLLREATDK----IREANRLFAvnqknmTALEKKKEAVESGKRQIENTLKEGND 1837
Cdd:NF041483 1172 AKAKELVSDANSEASKvriaaVKKAEGLLKEAEQKkaelVREAEKIKA------EAEAEAKRTVEEGKRELDVLVRRRED 1245
|
250
....*....|
gi 1677500969 1838 ILDEANRLAD 1847
Cdd:NF041483 1246 INAEISRVQD 1255
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
757-799 |
1.39e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 50.00 E-value: 1.39e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1677500969 757 CQC--FGHA-ESCDDVTGECLnCKDHTGGPYCDKCLPGFYGEPTKG 799
Cdd:smart00180 1 CDCdpGGSAsGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
414-466 |
2.10e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 49.62 E-value: 2.10e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1677500969 414 CHCDPIGSLNEVCVKDEkharrglapGSCHCKTGFGGVSCDRCARGYTG--YPDC 466
Cdd:smart00180 1 CDCDPGGSASGTCDPDT---------GQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1684-1885 |
3.21e-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: 3.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1684 ELARDAEAV----NEKAIKLNETLGTRD-----------EAFERNLEGLQKEIDQMIkelrrknlETQKEIAEDELVAAE 1748
Cdd:cd00176 4 QFLRDADELeawlSEKEELLSSTDYGDDlesveallkkhEALEAELAAHEERVEALN--------ELGEQLIEEGHPDAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1749 ALLKKVKKLfgesrgenEEMEKDLREKLADYKNKVDDAWDLLRE----------ATDKIREANRLFAVN-----QKNMTA 1813
Cdd:cd00176 76 EIQERLEEL--------NQRWEELRELAEERRQRLEEALDLQQFfrdaddleqwLEEKEAALASEDLGKdlesvEELLKK 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1677500969 1814 LEKKKEAVESGKRQIENTLKEGNDILDEANRLADeinsiidyvEDIQTKLppmsEELNDKIDDLSQEIKDRK 1885
Cdd:cd00176 148 HKELEEELEAHEPRLKSLNELAEELLEEGHPDAD---------EEIEEKL----EELNERWEELLELAEERQ 206
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1420-1466 |
1.06e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 47.69 E-value: 1.06e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1420 CQCN--GHSSL-CDPETSICQnCQHHTAGDFCERCALGYYGIVkglPNDC 1466
Cdd:smart00180 1 CDCDpgGSASGtCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDG---PPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
287-334 |
1.94e-06 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 46.96 E-value: 1.94e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1677500969 287 CICYGHA---RACplDPATnkSRCECEHNTCGDSCDQCCPGFHQKPWRAGT 334
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. |
807-862 |
2.09e-06 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 46.96 E-value: 2.09e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1677500969 807 CACPLNIPSnnfSPTCHldrSLGLICDgCPVGYTGPRCERCAEGYFGQPSVPGGSC 862
Cdd:pfam00053 1 CDCNPHGSL---SDTCD---PETGQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
1826-2078 |
2.24e-06 |
|
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: 51.90 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1826 RQIENTLKEGNDILDEANRLADEINSIIDYVEDIQTKLPPM---SEELNDKIDDLSQEIKD-----RKLAEKVSQAESHA 1897
Cdd:smart00283 4 EAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIaatAQSAAEAAEEGREAVEDaitamDQIREVVEEAVSAV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1898 AQLNDSSAVLDGILDEAKNISF-------NAT--AAfKAysnikdyiDEAEK----VAKEAKDLAHEATKLATGPRGLLK 1964
Cdd:smart00283 84 EELEESSDEIGEIVSVIDDIADqtnllalNAAieAA-RA--------GEAGRgfavVADEVRKLAERSAESAKEIESLIK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1965 E------DAKGCLQKSFRILNEAKKLANDVKENedhLNGLKTRIENAdarngdllrtlNDTLGKLSAIPNDTAAKLQAVK 2038
Cdd:smart00283 155 EiqeetnEAVAAMEESSSEVEEGVELVEETGDA---LEEIVDSVEEI-----------ADLVQEIAAATDEQAAGSEEVN 220
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1677500969 2039 DKARQANDTAKDVLAQITELHQNLDGLKKNYNKLADSVAK 2078
Cdd:smart00283 221 AAIDEIAQVTQETAAMSEEISAAAEELSGLAEELDELVER 260
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
806-863 |
4.30e-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: 46.19 E-value: 4.30e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1677500969 806 PCACPLNIpsnNFSPTCHLDrslGLICDgCPVGYTGPRCERCAEGYFGQPSVPGGsCQ 863
Cdd:cd00055 1 PCDCNGHG---SLSGQCDPG---TGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGG-CQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
468-515 |
6.56e-06 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 45.42 E-value: 6.56e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1677500969 468 ACNCSGLGSKNE--DPCFGPCICKENVEGGDCSRCKSGFFNLQEdNWKGC 515
Cdd:cd00055 1 PCDCNGHGSLSGqcDPGTGQCECKPNTTGRRCDRCAPGYYGLPS-QGGGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1469-1524 |
9.20e-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: 45.04 E-value: 9.20e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1677500969 1469 CACPLISSSnnfSPSCVAEGlddYRCTaCPRGYEGQYCERCAPGYTGSPGNPGGSC 1524
Cdd:pfam00053 1 CDCNPHGSL---SDTCDPET---GQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
469-515 |
1.06e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 44.61 E-value: 1.06e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1677500969 469 CNCSGLGSKNE--DPCFGPCICKENVEGGDCSRCKSGFFNlqeDNWKGC 515
Cdd:smart00180 1 CDCDPGGSASGtcDPDTGQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1917-2169 |
1.94e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.76 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1917 ISFNATAAFKAYSNIKDYIDEAEKVAKEAKDLAHEATKLATGPRGLLK--EDAKGCLQKSFRILN-EAKKLANDVKENED 1993
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAalERRIAALARRIRALEqELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1994 HLNGLKTRIENADARNGDLLRTLnDTLGKLSAI--------PNDTAAKLQAVKDKARQANDTAKDVLAQITELHQNLDGL 2065
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRAL-YRLGRQPPLalllspedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2066 KKNYNKLADSVAKTNAVVKDPSKNKiiADADATVKNLEQEADRLIDKLKPIKELEDNLKKNISEIKELINQARKQANSIK 2145
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALK--AERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
250 260 270
....*....|....*....|....*....|.
gi 1677500969 2146 VSVSSG-------GDCIRTYKPEIKKGSYNN 2169
Cdd:COG4942 248 FAALKGklpwpvsGRVVRRFGERDGGGGRNK 278
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
807-855 |
2.23e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 43.84 E-value: 2.23e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1677500969 807 CACPlniPSNNFSPTCHLDrslGLICDgCPVGYTGPRCERCAEGYFGQP 855
Cdd:smart00180 1 CDCD---PGGSASGTCDPD---TGQCE-CKPNVTGRRCDRCAPGYYGDG 42
|
|
| auto_Ata |
NF033481 |
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an ... |
1665-2204 |
3.17e-05 |
|
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an architecture that consists of a long signal peptide, a repetitive passenger domain that varies in length from strain to strain, and a C-terminal domain of four transmembrane beta stands that forms one third of the pore for autotransporter activity and anchoring in the outer membrane.
Pssm-ID: 411124 [Multi-domain] Cd Length: 1862 Bit Score: 49.86 E-value: 3.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1665 GQDAERTNTRAKSLGEFIKELARDAEAVNEKAIKLNET-----------------LGTRDEAFERNLEGLQKeiDQMIKE 1727
Cdd:NF033481 642 GKGAEATNENAAAVGGGAKATGKNAAAIGGGAIADQENavavgqgaqslveggvaLGARSKVEAKNSVALGQ--DAVATE 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1728 LRRKNLETQKEIAEDELVAAEALLKKVKKLFGESRGENEEMEKDLREkladyknkvddawdlLREATDKIREANRLFAVN 1807
Cdd:NF033481 720 ATGTSFLTNRDASQSNGVISVGSAGKERRITNVEDGSADSDAVTVRQ---------------LKNVDSRVNQNTSNIGKN 784
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1808 QKNMTALEKKKEAVESG-KRQIENTLKE--------GNDILDEANRLADEINSIIDYVEDIQTKLPPM----SEELNDKI 1874
Cdd:NF033481 785 TQNITNLNQKLDDTKTNlGNQITDTNKNlndakkdlGNQITDTNTKLNTTKDQLTTQINDTKTELNNTigntKTELNTKI 864
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1875 DDLSQEIKD--------------RKLAEKV-----SQAESHAAQLNDSSAVL----DGI----LDEAK---------NIS 1918
Cdd:NF033481 865 DNTKTELENkglnfagnsgadvhRKLGDKLnivggAAASTPAAKTSGENVITrttqDGIqielLKDSKfdsvttgntTLN 944
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1919 FNATAAFKAYSNIKDYIDEAEKVAKEAKDLAHEATKLATGPRGLLKEDAKGCLQKSFRILNEAKK-LANDVKENEDHLNG 1997
Cdd:NF033481 945 TNGLTIKEGPSITKQGINAGSKQITNVADGINAKDAVNVDQLTKVKENLNGRITDTNNQLNDAKKdLGNQIADTNKNLND 1024
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1998 LKTRIENadaRNGDLLRTLNDTLGKLSAIPNDTAAKLQAV--KDKARQANDTAKDVLAQITELHQNLdGLKKNYNKLADS 2075
Cdd:NF033481 1025 AKKDLGD---QITDTNTKLNNTKDQLTTQINDTKTELNNTigNTKTELENKGLNFAGNSGADVHRKL-GDKLNIVGGAAA 1100
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2076 VAKTNAVVKDPSKNKIIADADATVKNLEQEADRLIDKLKPIKELEDNLKKNISEIKELINQARKQANSIKVSVSSggdci 2155
Cdd:NF033481 1101 STPAAKTSGENVITRTTKDGIQIELLKDSKFDSVTTGNTTLNTNGLTIKEGPSITKDGINAGGKQITNVADGINA----- 1175
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 1677500969 2156 rtyKPEIKKGSYNNIVvnVKTAVADNLLFYLGSAKFIDFLAIEMRKGKV 2204
Cdd:NF033481 1176 ---KDAVNKGQLDNLA--AKQNATDDAAVKYDDAKTKDKVTLKGKDGTV 1219
|
|
| alph_xenorhab_A |
NF033928 |
alpha-xenorhabdolysin family binary toxin subunit A; Alpha-xenorhabdolysin was the founding ... |
1904-2145 |
5.91e-05 |
|
alpha-xenorhabdolysin family binary toxin subunit A; Alpha-xenorhabdolysin was the founding member of a family of alpha-helical pore-forming binary toxins. YaxAB from Yersinia enterocolitica has been studied structurally. This HMM represents subunit A proteins such as XaxA and YaxA, capable of binding to the membrane even in the absence of the B subunit. This family is related to the Bacillus haemolytic enterotoxin family (see PF05791.9), although thresholds for this HMM are set to exclude that family.
Pssm-ID: 468250 [Multi-domain] Cd Length: 340 Bit Score: 48.06 E-value: 5.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1904 SAVLDGILDEAKNISfNATAAFKAYSN-IKDYIDEAeKVAKEAKDLAHEATKLATGPRGLLKEDAKGCLQKsfrILneaK 1982
Cdd:NF033928 62 SNLEPKIKQLANDLA-NYARNIVVTGNpIIDLINEM-PIIKRGDLTEEELSELPPIPLSSDDKEIVKELKE---IL---E 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1983 KLANDVKENEDHLNGLKTRIenadarnGDLLRTLNDTLgklsaipndtAAKLQAVKDKAR--QANDTAKDVLAQITELHQ 2060
Cdd:NF033928 134 DLKNDIKDYQQKADDVKKEL-------DDFENDLREEL----------LPQLKLKKKLYDdnLGSDSIEELREKIDQLEK 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2061 NLDGLKKNYNKLADSVAKT----NAVVkdpsknkII---------ADADATVKNLEQEADRLIDKLK---PIKELEDNLK 2124
Cdd:NF033928 197 EIEQLNKEYDDYVKLSFTGlaggPIGL-------AItggifgskaEKIRKEKNALIQEIDELQEQLKkknALLGSLERLQ 269
|
250 260
....*....|....*....|.
gi 1677500969 2125 KNISEIKELINQARKQANSIK 2145
Cdd:NF033928 270 TSLDDILTRMEDALPALKKLK 290
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1727-1883 |
2.83e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 45.78 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1727 ELRRKNLETQKEIAE---DELVAAEALLKKvkklfgesrgeNEEMEKDLREKLADYKNKVDDAWDLLREATDKIreanrl 1803
Cdd:smart00787 136 EWRMKLLEGLKEGLDenlEGLKEDYKLLMK-----------ELELLNSIKPKLRDRKDALEEELRQLKQLEDEL------ 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1804 favNQKNMTALEKKKEAVESGKRQIENTLKEGNDILDEANRLADEInsiidyvediqtklppmsEELNDKIDDLSQEIKD 1883
Cdd:smart00787 199 ---EDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKI------------------EDLTNKKSELNTEIAE 257
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1469-1520 |
2.85e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 40.76 E-value: 2.85e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1677500969 1469 CACPLissSNNFSPSCVaegLDDYRCTaCPRGYEGQYCERCAPGYTGSPGNP 1520
Cdd:smart00180 1 CDCDP---GGSASGTCD---PDTGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| V_Alix_like |
cd08915 |
Protein-interacting V-domain of mammalian Alix and related domains; This superfamily contains ... |
1971-2133 |
3.01e-04 |
|
Protein-interacting V-domain of mammalian Alix and related domains; This superfamily contains the V-shaped (V) domain of mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, and related domains. Alix, HD-PTP, Bro1, and Rim20 all interact with the ESCRT (Endosomal Sorting Complexes Required for Transport) system. Alix, also known as apoptosis-linked gene-2 interacting protein 1 (AIP1), participates in membrane remodeling processes during the budding of enveloped viruses, vesicle budding inside late endosomal multivesicular bodies (MVBs), and the abscission reactions of mammalian cell division. It also functions in apoptosis. HD-PTP functions in cell migration and endosomal trafficking, Bro1 in endosomal trafficking, and Rim20 in the response to the external pH via the Rim101 pathway. The Alix V-domain contains a binding site, partially conserved in this superfamily, for the retroviral late assembly (L) domain YPXnL motif. The Alix V-domain is also a dimerization domain. Members of this superfamily have an N-terminal Bro1-like domain, which binds components of the ESCRT-III complex. The Bro1-like domains of Alix and HD-PTP can also bind human immunodeficiency virus type 1 (HIV-1) nucleocapsid. Many members, including Alix, HD-PTP, and Bro1, also have a proline-rich region (PRR), which binds multiple partners in Alix, including Tsg101 (tumor susceptibility gene 101, a component of ESCRT-1) and the apoptotic protein ALG-2. The C-terminal portion (V-domain and PRR) of Bro1 interacts with Doa4, a ubiquitin thiolesterase needed to remove ubiquitin from MVB cargoes; it interacts with a YPxL motif in Doa4s catalytic domain to stimulate its deubiquitination activity. Rim20 may bind the ESCRT-III subunit Snf7, bringing the protease Rim13 (a YPxL-containing transcription factor) into proximity with Rim101, and promoting the proteolytic activation of Rim101. HD-PTP is encoded by the PTPN23 gene, a tumor suppressor gene candidate often absent in human kidney, breast, lung, and cervical tumors. HD-PTP has a C-terminal catalytically inactive tyrosine phosphatase domain.
Pssm-ID: 185746 [Multi-domain] Cd Length: 342 Bit Score: 45.80 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1971 LQKSFrilNEAKKLAndvKENEDHLNGLKTRIEnADARNGDLLR----TLNDTLGKLSAIPNDTAAKLQAVKDKARQAND 2046
Cdd:cd08915 75 IEQSF---KELSKLR---QNVEELLQECEELLE-EEAAEDDQLRakfgTLRWRRPSSDEAAKELYEKVTKLRGYLEQASN 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2047 TAKDVLAQITELHQNLDGLKKNYNKLADSVAKTNaVVKDPSKNKIIADADAT---VKNLEQEADRLIDKLKpIKELEDN- 2122
Cdd:cd08915 148 SDNEVLQCYESIDPNLVLLCGGYKELKAFIPSPY-PALDPEVSEVVSSLRPLlneVSELEKERERFISELE-IKSRNNDi 225
|
170
....*....|.
gi 1677500969 2123 LKKNISEIKEL 2133
Cdd:cd08915 226 LPKLITEYKKN 236
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
306-330 |
3.64e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 40.37 E-value: 3.64e-04
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1469-1525 |
4.19e-04 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 40.42 E-value: 4.19e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1677500969 1469 CACPLISSSNnfsPSCVAEGLddyRCTaCPRGYEGQYCERCAPGYTGSPGNPGGsCQ 1525
Cdd:cd00055 2 CDCNGHGSLS---GQCDPGTG---QCE-CKPNTTGRRCDRCAPGYYGLPSQGGG-CQ 50
|
|
| TNFRSF16 |
cd13416 |
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 ... |
785-919 |
1.68e-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: 41.52 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 785 CDKCLPGFYGEPTKGTSEDCQPCA-CPLNIPsnnfsPTCHLDRSLGLICdgcpvgytgprceRCAEGYFgqPSVPGGSCQ 863
Cdd:cd13416 35 CEPCLDGVTFSDVVSHTEPCQPCTrCPGLMS-----MRAPCTATHDTVC-------------ECAYGYY--LDEDSGTCE 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1677500969 864 PCQcndnldfsipgSCDSLSGSCLICKPGTTGRyCELCADGYFGDAV-DAKNCQPCR 919
Cdd:cd13416 95 PCT-----------VCPPGQGVVQSCGPNQDTV-CEACPEGTYSDEDsSTDPCLPCT 139
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
37-285 |
1.51e-91 |
|
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: 297.73 E-value: 1.51e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 37 RGLFPAVLNLASNALITTNATCGEKGPEMYCKLVEHVpgqpVRNPQCRICNQNssNPNQRHPITNAIDGKN----TWWQS 112
Cdd:smart00136 5 RSCYPPFVNLAFGREVTATSTCGEPGPERYCKLVGHT----EQGKKCDYCDAR--NPRRSHPAENLTDGNNpnnpTWWQS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 113 PSIKNGIeyHYVTITLDLQQVFQIAYVIVKAAnSPRPGNWILERSLDDVEYKPWQYHAvtdTECLTLYNIyPRTGPPSYA 192
Cdd:smart00136 79 EPLSNGP--QNVNLTLDLGKEFHVTYVILKFC-SPRPSLWILERSDFGKTWQPWQYFS---SDCRRTFGR-PPRGPITKG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 193 KDDEVICTSFYSKIHPLENGEIHISLINGRPSADDP--SPELLEFTSARYIRLRFQRIRTLNADLMMfahkdpreIDPIV 270
Cdd:smart00136 152 NEDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDFdnSPVLQEWVTATNIRVRLTRLRTLGDELMD--------DRPEV 223
|
250
....*....|....*
gi 1677500969 271 TRRYYYSVKDISVGG 285
Cdd:smart00136 224 TRRYYYAISDIAVGG 238
|
|
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
39-285 |
3.89e-88 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 287.56 E-value: 3.89e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 39 LFPAVLNLASNALITTNATCGEKGPEMYCKLVEHVPGQpvrnpQCRICNqnSSNPNQRHPITNAIDGKN----TWWQSPS 114
Cdd:pfam00055 1 CYPAFGNLAFGREVSATSTCGLNGPERYCILSGLEGGK-----KCFICD--SRDPHNSHPPSNLTDSNNgtneTWWQSET 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 115 IKngIEYHYVTITLDLQQVFQIAYVIVKAAnSPRPGNWILERSLD-DVEYKPWQYHAvtdTECLTLYNIypRTGPPSYAK 193
Cdd:pfam00055 74 GV--IQYENVNLTLDLGKEFHFTYLILKFK-SPRPAAMVLERSTDfGKTWQPYQYFA---SDCRRTFGR--PSGPSRGIK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 194 DDEVICTSFYSKIHPLENGEIHISLINGRPSA--DDPSPELLEFTSARYIRLRFQRIRTLNadlmmfahkDPREIDPIVT 271
Cdd:pfam00055 146 DDEVICTSEYSDISPLTGGEVIFSTLEGRPSAniFDYSPELQDWLTATNIRIRLLRLHTLG---------DELLDDPSVL 216
|
250
....*....|....
gi 1677500969 272 RRYYYSVKDISVGG 285
Cdd:pfam00055 217 RKYYYAISDISVGG 230
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1593-1852 |
5.03e-87 |
|
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: 285.46 E-value: 5.03e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1593 VMSIN-LTGPLPAPYKMLYGLENMTQELKHLLSPQRAPERLIQLAEGNLNTLVTEMNELLTRATKVTADGEQTGQDAERT 1671
Cdd:pfam06008 1 LLSLNsLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1672 NTRAKSLGEFIKELARDAEAVNEKAIKLNETLgtrDEAFERNLEGLQKEIDQMIKELRRKNLETQKEIAEDELVAAEALL 1751
Cdd:pfam06008 81 LGHAKELAEAIKNLIDNIKEINEKVATLGEND---FALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQDLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1752 KKVKKLFGESRGENEEMEKDLREKLADYKNKVDDAWDLLREATDKIREANRLFAVNQKNMTALEKKKEAVESGKRQIENT 1831
Cdd:pfam06008 158 SRIQTWFQSPQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEET 237
|
250 260
....*....|....*....|.
gi 1677500969 1832 LKEGNDILDEANRLADEINSI 1852
Cdd:pfam06008 238 LKTARDSLDAANLLLQEIDDA 258
|
|
| LamB |
smart00281 |
Laminin B domain; |
1229-1364 |
4.33e-50 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 174.37 E-value: 4.33e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1229 HLEPFYWKLPEQFEGKKLMAYGGKLKYAIYFEAREEtGFSTYNPQVIIRGGtptHARIIVRHMAAPLIGQLTRHEIEMTE 1308
Cdd:smart00281 1 DNEPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRRG-GTHVSAPDVILEGN---GLRISHPAEGPPLPDELTTVEVRFRE 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1677500969 1309 KEWKYYGddprvHRTVTREDFLDILYDIHYILIKATYGNFMRQSRISEISMEVAEQ 1364
Cdd:smart00281 77 ENWQYYG-----GRPVTREDLMMVLANLTAILIRATYSQQMAGSRLSDVSLEVAVP 127
|
|
| Laminin_II |
pfam06009 |
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 ... |
2037-2173 |
6.69e-50 |
|
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 368703 [Multi-domain] Cd Length: 138 Bit Score: 174.21 E-value: 6.69e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2037 VKDKARQANDTAKDVLAQITELHQNLDGLKKNYNKLADSVAKTNAVVKDpsKNKIIADADATVKNLEQEADRLIDKLKPI 2116
Cdd:pfam06009 1 SKELAREANETAKEVLEQLAPLSQNLENTSEKLSGINRSLEETNELVND--ANKALDDAGRSVKKLEELAPDLLDKLKPL 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2117 KELEDN---LKKNISEIKELINQARKQANSIKVSVSSGGDCIRTYKPEIKKGSYNNIVVN 2173
Cdd:pfam06009 79 KQLEVNsssLSDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTSL 138
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2789-2917 |
3.36e-47 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 165.95 E-value: 3.36e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2789 VRTEAESGLLFYMARINHADFATVQLRNGLPYFSYDLGSGDTHTMIPTKINDGQWHKIKIMRSKQEGILYVDG-ASNRTI 2867
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGeARPTGE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1677500969 2868 SPKKADI-LDVVGMLYVGGLPINYTTRRIGPVTYSIDGCVRNLHMAEAPAD 2917
Cdd:pfam00054 81 SPLGATTdLDVDGPLYVGGLPSLGVKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
1234-1378 |
6.09e-44 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 157.05 E-value: 6.09e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1234 YWKLPEQFEGKKLMAYGGKLKYAIYFEAREETGFSTYNPQVIIRGGtptHARIIVRHMA--APLIGQLTRHEIEMTEKEW 1311
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGGGSLNSEPDVILEGN---GLRLSYSSPDqpPPDPGQEQTYSVRLHEENW 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1677500969 1312 KYygddpRVHRTVTREDFLDILYDIHYILIKATYGNFMRQSRISEISMEVAEQGRgttMTPPADLIE 1378
Cdd:pfam00052 78 RD-----SDGAPVSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSAVPGG---SGPPASWVE 136
|
|
| LamB |
smart00281 |
Laminin B domain; |
578-710 |
7.26e-43 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 153.57 E-value: 7.26e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 578 LPHSYYWSAPAPYLGNKLPAVGGQLTFTISYDLeeeEEDTERVLQLMIILEGNDLSISTAQdEVYLHPSEEHTNVLLLKE 657
Cdd:smart00281 1 DNEPVYWVAPEQFLGDKVTSYGGKLRYTLSFDG---RRGGTHVSAPDVILEGNGLRISHPA-EGPPLPDELTTVEVRFRE 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1677500969 658 ESFTIHGtHFPVRRKEFMTVLANLKRVLLQITYSFGMDAIfRLSSVNLESAVS 710
Cdd:smart00281 77 ENWQYYG-GRPVTREDLMMVLANLTAILIRATYSQQMAGS-RLSDVSLEVAVP 127
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
583-722 |
8.28e-40 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 145.11 E-value: 8.28e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 583 YWSAPAPYLGNKLPAVGGQLTFTISYDLeeEEEDTERVLQLMIILEGNDLSISTAQDE-VYLHPSEEHTNVLLLKEESFT 661
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEP--LPGGGSLNSEPDVILEGNGLRLSYSSPDqPPPDPGQEQTYSVRLHEENWR 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1677500969 662 iHGTHFPVRRKEFMTVLANLKRVLLQITYSFGMDAIfRLSSVNLESAVSYPTdGSIAAAVE 722
Cdd:pfam00052 79 -DSDGAPVSREDFMMVLANLTAILIRATYSTGSGQV-SLSNVSLDSAVPGGS-GPPASWVE 136
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2368-2503 |
5.26e-38 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 139.76 E-value: 5.26e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2368 FRTFSSSALLMYLATRDLRDFMSVELTDGHIKVSYDLGSGMASVVSNQNHNDGKWKSFTLSRIQKQANISivdIDTNQEE 2447
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLS---VDGEARP 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1677500969 2448 NIATSSSGNNfglDLKADDKIYFGGLPTLR-NLRPEVNLKKYSGCLKDIEISRTPYN 2503
Cdd:pfam00054 78 TGESPLGATT---DLDVDGPLYVGGLPSLGvKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2762-2911 |
1.87e-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: 139.09 E-value: 1.87e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2762 FGLSRNSHIAIAFDDTKvKNRLTIELEVRTEAESGLLFYMARINHADFATVQLRNGLPYFSYDLGSGDTHTMIPTKINDG 2841
Cdd:cd00110 2 VSFSGSSYVRLPTLPAP-RTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1677500969 2842 QWHKIKIMRSKQEGILYVDG-ASNRTISPKKADILDVVGMLYVGGLPINYTTRRIgPVTYSIDGCVRNLHM 2911
Cdd:cd00110 81 QWHSVSVERNGRSVTLSVDGeRVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGL-PVSPGFVGCIRDLKV 150
|
|
| LamG |
smart00282 |
Laminin G domain; |
2784-2911 |
2.08e-35 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 132.46 E-value: 2.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2784 TIELEVRTEAESGLLFYMARINHADFATVQLRNGLPYFSYDLGSGDTHTMI-PTKINDGQWHKIKIMRSKQEGILYVDG- 2861
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSdPTPLNDGQWHRVAVERNGRSVTLSVDGg 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2862 ASNRTISPKKADILDVVGMLYVGGLPINYtTRRIGPVTYSIDGCVRNLHM 2911
Cdd:smart00282 81 NRVSGESPGGLTILNLDGPLYLGGLPEDL-KLPPLPVTPGFRGCIRNLKV 129
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2174-2314 |
2.21e-35 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 132.44 E-value: 2.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2174 VKTAVADNLLFYLGSAKFIDFLAIEMRKGKVSFLWDVGSGVGRVEYPDlTIDDSYWYRIVASRTGRNGTISVRALDgpka 2253
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGD-KLNDGKWHSVELERNGRSGTLSVDGEA---- 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1677500969 2254 sivpsTHHSTSPPGYTIlDVDANAMLFVGGLTG-KLKKADAVRVITFTGCMGETYFDNKPIG 2314
Cdd:pfam00054 76 -----RPTGESPLGATT-DLDVDGPLYVGGLPSlGVKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2340-2497 |
5.81e-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: 126.38 E-value: 5.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2340 TIQFDGEGYALVSRPIRWYPNiSTVMFKFRTFSSSALLMYLATRDLRDFMSVELTDGHIKVSYDLGSGMASVVSNQNHND 2419
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRTR-LSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLND 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1677500969 2420 GKWKSFTLSRIQKQANISIvdidtNQEENIATSSSGNNFGLDLkaDDKIYFGGLPTLRNLRPEVNLKKYSGCLKDIEI 2497
Cdd:cd00110 80 GQWHSVSVERNGRSVTLSV-----DGERVVESGSPGGSALLNL--DGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKV 150
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2937-3089 |
2.11e-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: 2.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2937 GTYFDGTGFAKAVGGFKVGLDLLVEFEFRTTTTTGVLLGISSQ-KMDGMGIEMIDEKLMFHVDNGAGRFTAvydaGVPGH 3015
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQnGGDFLALELEDGRLVLRYDLGSGSLVL----SSKTP 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1677500969 3016 LCDGQWHKVTANKIKHRIELTVDGNQVEAQSPNPASTSADTNDPVFVGGFPDDLKQFGLTTSIPFRGCIRSLKL 3089
Cdd:cd00110 77 LNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKV 150
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2550-2691 |
4.11e-31 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 120.11 E-value: 4.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2550 FSTKNESGIILlgSGGTpapprrkrrQTGQAYYAILLNRGRLEVHLSTGARtmrKIVIRPEPNLfHDGREHSVHVERTRG 2629
Cdd:pfam00054 1 FRTTEPSGLLL--YNGT---------QTERDFLALELRDGRLEVSYDLGSG---AAVVRSGDKL-NDGKWHSVELERNGR 65
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1677500969 2630 IFTVQVDENRR--YMQNLTVEQ-PIEVKKLFVGGAPPE-FQPSPLRNIPPFEGCIWNLVINSVPMD 2691
Cdd:pfam00054 66 SGTLSVDGEARptGESPLGATTdLDVDGPLYVGGLPSLgVKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| LamG |
smart00282 |
Laminin G domain; |
2363-2499 |
4.42e-31 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 120.14 E-value: 4.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2363 TVMFKFRTFSSSALLMYLATRDLRDFMSVELTDGHIKVSYDLGSGMASVVSNQNH-NDGKWKSFTLSRIQKQANISIvdi 2441
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPlNDGQWHRVAVERNGRSVTLSV--- 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1677500969 2442 dtNQEENIATSSSGNNFGLDLkaDDKIYFGGLPTLRNLRPEVNLKKYSGCLKDIEISR 2499
Cdd:smart00282 78 --DGGNRVSGESPGGLTILNL--DGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNG 131
|
|
| LamG |
smart00282 |
Laminin G domain; |
2960-3089 |
4.62e-30 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 117.06 E-value: 4.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2960 VEFEFRTTTTTGVLLGISS-QKMDGMGIEMIDEKLMFHVDNGAGRFTAVYDagvPGHLCDGQWHKVTANKIKHRIELTVD 3038
Cdd:smart00282 2 ISFSFRTTSPNGLLLYAGSkGGGDYLALELRDGRLVLRYDLGSGPARLTSD---PTPLNDGQWHRVAVERNGRSVTLSVD 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1677500969 3039 G-NQVEAQSPnPASTSADTNDPVFVGGFPDDLKQFGLTTSIPFRGCIRSLKL 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 |
2.73e-28 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 112.90 E-value: 2.73e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2524 TVSFPKPGFVELSPVPID-VGTEINLSFSTKNESGIILLGSGgtpapprrkrrQTGQAYYAILLNRGRLEVHLSTGARTm 2602
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPrTRLSISFSFRTTSPNGLLLYAGS-----------QNGGDFLALELEDGRLVLRYDLGSGS- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2603 rkIVIRPePNLFHDGREHSVHVERTRGIFTVQVDENR--RYMQNLTVEQPIEVKKLFVGGAPPEFQPSPLRNIPPFEGCI 2680
Cdd:cd00110 69 --LVLSS-KTPLNDGQWHSVSVERNGRSVTLSVDGERvvESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCI 145
|
....*.
gi 1677500969 2681 WNLVIN 2686
Cdd:cd00110 146 RDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
2169-2311 |
3.28e-27 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 108.97 E-value: 3.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2169 NIVVNVKTAVADNLLFYLGSAKFIDFLAIEMRKGKVSFLWDVGSGVGRVEYPDLTIDDSYWYRIVASRTGRNGTISVral 2248
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLNDGQWHRVAVERNGRSVTLSV--- 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1677500969 2249 DGPKASIVpsthhsTSPPGYTILDVDANamLFVGGLTGKLKKADAVRVITFTGCMGETYFDNK 2311
Cdd:smart00282 78 DGGNRVSG------ESPGGLTILNLDGP--LYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2789-2911 |
8.44e-27 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 107.51 E-value: 8.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2789 VRTEAESGLLFYMARINHaDFATVQLRNGLPYFSYDLGSGDTHTM-IPTKINDGQWHKIKIMRSKQEGILYVDGASNRTI 2867
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGS-DFLALELVNGRLVLRYDLGSGPESLLsSGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSS 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1677500969 2868 S-PKKADILDVVGMLYVGGLPINYTTRRIgPVTYSIDGCVRNLHM 2911
Cdd:pfam02210 80 LpPGESLLLNLNGPLYLGGLPPLLLLPAL-PVRAGFVGCIRDVRV 123
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2150-2309 |
4.41e-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: 103.65 E-value: 4.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2150 SGGDCIRtYKPEIKKGSYNNIVVNVKTAVADNLLFYLGSAKFIDFLAIEMRKGKVSFLWDVGSGVGRVEYPDlTIDDSYW 2229
Cdd:cd00110 5 SGSSYVR-LPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKT-PLNDGQW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2230 YRIVASRTGRNGTISVralDGpkASIVpsthHSTSPPGYTILDVDANamLFVGGLTGKLKKADAVRVITFTGCMGETYFD 2309
Cdd:cd00110 83 HSVSVERNGRSVTLSV---DG--ERVV----ESGSPGGSALLNLDGP--LYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
2545-2688 |
2.11e-24 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 100.88 E-value: 2.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2545 EINLSFSTKNESGIILLGSGGTpapprrkrrqtGQAYYAILLNRGRLEVHLSTGARTmrkIVIRPEPNLFHDGREHSVHV 2624
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKG-----------GGDYLALELRDGRLVLRYDLGSGP---ARLTSDPTPLNDGQWHRVAV 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1677500969 2625 ERTRGIFTVQVD-ENRRYMQNLTVEQPIEVK-KLFVGGAPPEFQPSPLRNIPPFEGCIWNLVINSV 2688
Cdd:smart00282 67 ERNGRSVTLSVDgGNRVSGESPGGLTILNLDgPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2368-2497 |
2.95e-23 |
|
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: 97.49 E-value: 2.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2368 FRTFSSSALLMYlATRDLRDFMSVELTDGHIKVSYDLGSG-MASVVSNQNHNDGKWKSFTLSRIQKQANISIvdidtNQE 2446
Cdd:pfam02210 1 FRTRQPNGLLLY-AGGGGSDFLALELVNGRLVLRYDLGSGpESLLSSGKNLNDGQWHSVRVERNGNTLTLSV-----DGQ 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1677500969 2447 ENIATSSSGNNFGLDLKADdkIYFGGLPTLRNLRPEVNLKKYSGCLKDIEI 2497
Cdd:pfam02210 75 TVVSSLPPGESLLLNLNGP--LYLGGLPPLLLLPALPVRAGFVGCIRDVRV 123
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2964-3089 |
1.95e-22 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 95.18 E-value: 1.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2964 FRTTTTTGVLLGISSQKMDGMGIEMIDEKLMFHVDNGAGRFTAVYdagVPGHLCDGQWHKVTANKIKHRIELTVDGNQVE 3043
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDFLALELVNGRLVLRYDLGSGPESLLS---SGKNLNDGQWHSVRVERNGNTLTLSVDGQTVV 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1677500969 3044 AQSPNPASTSADTNDPVFVGGFPDDLKQFGLTTSIPFRGCIRSLKL 3089
Cdd:pfam02210 78 SSLPPGESLLLNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRV 123
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2964-3098 |
7.20e-22 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 93.54 E-value: 7.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2964 FRTTTTTGVLLGISSQ-KMDGMGIEMIDEKLMFHVDNGAGRFTAVYdagvPGHLCDGQWHKVTANKIKHRIELTVDGNQV 3042
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQtERDFLALELRDGRLEVSYDLGSGAAVVRS----GDKLNDGKWHSVELERNGRSGTLSVDGEAR 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1677500969 3043 E-AQSPNPASTSADTNDPVFVGGFPDD-LKQFGLTTSIPFRGCIRSLKLtkgTGKPLE 3098
Cdd:pfam00054 77 PtGESPLGATTDLDVDGPLYVGGLPSLgVKKRRLAISPSFDGCIRDVIV---NGKPLD 131
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1675-2164 |
9.21e-21 |
|
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: 100.48 E-value: 9.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1675 AKSLGEfIKELARDAEAVNEKA---IKLNETLGTRDEAFERNLEGLQKEIDQMIKELRRKNLEtqkeiaedeLVAAEALL 1751
Cdd:TIGR04523 141 DKFLTE-IKKKEKELEKLNNKYndlKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELL---------LSNLKKKI 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1752 KKVKKL---FGESRGENEEMEKDLREKladyKNKVDDAWDLLREATDKIreaNRLFAVNQKNMTALEKKKEAVESGKRQI 1828
Cdd:TIGR04523 211 QKNKSLesqISELKKQNNQLKDNIEKK----QQEINEKTTEISNTQTQL---NQLKDEQNKIKKQLSEKQKELEQNNKKI 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1829 ENTLKEGNDILDE------------ANRLADEINSIIDYVEDIQTKLPPMSE---ELNDKIDDLSQEI---------KDR 1884
Cdd:TIGR04523 284 KELEKQLNQLKSEisdlnnqkeqdwNKELKSELKNQEKKLEEIQNQISQNNKiisQLNEQISQLKKELtnsesenseKQR 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1885 KLAEKVSQAESHAAQlNDSSavldgiLDEAKNISfnataafkaySNIKDYIDEAEKVAKEAKDLAHEATKLATGPRGLLK 1964
Cdd:TIGR04523 364 ELEEKQNEIEKLKKE-NQSY------KQEIKNLE----------SQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEK 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1965 EdakgclQKsfRILNEAKKLANDVKENEDHLNGLKTRIENADARNGDLLRTLNDTLGKLSAIPNDTAAKLQAVKDKARQA 2044
Cdd:TIGR04523 427 E------IE--RLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKEL 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2045 ---NDTAKDVLAQITELHQNLDGLKKNYNKLADSVAKTNAVVKDPSKNKIIADADATVKNLEQEADRLIDKLKPIKELED 2121
Cdd:TIGR04523 499 kklNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQK 578
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1677500969 2122 NLKKNISEIKELINQARKQANSIKVSVSSGGDCIRTYKPEIKK 2164
Cdd:TIGR04523 579 SLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEK 621
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1669-2164 |
2.97e-20 |
|
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: 98.55 E-value: 2.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1669 ERTNTRAKSLGEFIKELARDAEAVNEKAIKLNETLGTRDEAFERnLEGLQKEIDQMIKELrrKNLETQ-KEIaEDELVAa 1747
Cdd:TIGR04523 225 KQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQ-LSEKQKELEQNNKKI--KELEKQlNQL-KSEISD- 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1748 ealLKKVKklfgesrgeNEEMEKDLREKLADYKNKVDDAWDLLREATDKIREANRLFA-----VNQKNMTALEKKKEaVE 1822
Cdd:TIGR04523 300 ---LNNQK---------EQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISqlkkeLTNSESENSEKQRE-LE 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1823 SGKRQIENTLKEGNDILDEANRLADEINSIIDYVEDiQTKLppmSEELNDKI-------DDLSQEIKDrkLAEKVSQAES 1895
Cdd:TIGR04523 367 EKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQN-QEKL---NQQKDEQIkklqqekELLEKEIER--LKETIIKNNS 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1896 HAAQLNDSSAVLDGILDEAKNIsfnaTAAFKaySNIKDYIDEAEKVAKEAKDLAHEatklatgprglLKEDAKGCLQksf 1975
Cdd:TIGR04523 441 EIKDLTNQDSVKELIIKNLDNT----RESLE--TQLKVLSRSINKIKQNLEQKQKE-----------LKSKEKELKK--- 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1976 rILNEAKKLANDVK----------ENEDHLNGLKTRIENAdarngdlLRTLNDTLGKLSAipNDTAAKLQAVKDKARQan 2045
Cdd:TIGR04523 501 -LNEEKKELEEKVKdltkkisslkEKIEKLESEKKEKESK-------ISDLEDELNKDDF--ELKKENLEKEIDEKNK-- 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2046 dtakdvlaQITELHQNLDGLKKNYNKLADSVAKTNAVVKDpsKNKIIADADATVKNLEQEAD-------RLIDKLKPIKE 2118
Cdd:TIGR04523 569 --------EIEELKQTQKSLKKKQEEKQELIDQKEKEKKD--LIKEIEEKEKKISSLEKELEkakkeneKLSSIIKNIKS 638
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1677500969 2119 LEDNLKKNISEIKELINQAR-KQAN---SIKVSVSSGGDCIRT-----------YKPEIKK 2164
Cdd:TIGR04523 639 KKNKLKQEVKQIKETIKEIRnKWPEiikKIKESKTKIDDIIELmkdwlkelslhYKKYITR 699
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1636-2145 |
1.60e-19 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 96.67 E-value: 1.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1636 AEGNLNTLVTEMNELLTRATKVTAdgeQTGQDAERTNTRAKSLGEFIKElardaeaVNEKAIKLNETlgtrdeafERNLE 1715
Cdd:PRK03918 163 AYKNLGEVIKEIKRRIERLEKFIK---RTENIEELIKEKEKELEEVLRE-------INEISSELPEL--------REELE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1716 GLQKEIDQMiKELRRK--NLETQKEIAEDELVAAEALLKKVKKLFGESRGENEEMEKDLRE--KLADYKNKVDDAWDLLR 1791
Cdd:PRK03918 225 KLEKEVKEL-EELKEEieELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKElkELKEKAEEYIKLSEFYE 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1792 EATDKIREA-------NRLFAVNQKNMTALEKKKEAVESGKRQIENTLKEGNDI------LDEANRLADEINSI------ 1852
Cdd:PRK03918 304 EYLDELREIekrlsrlEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELeerhelYEEAKAKKEELERLkkrltg 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1853 ---------IDYVEDIQTKLPPMSEELNDKIDDLSQEIKDRKLA-EKVSQA--------------------ESHAAQLND 1902
Cdd:PRK03918 384 ltpeklekeLEELEKAKEEIEEEISKITARIGELKKEIKELKKAiEELKKAkgkcpvcgrelteehrkellEEYTAELKR 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1903 SS---AVLDGILDEAKN---------------ISFNATAAF--KAYSNIKDY-IDEAEKVAKEAKDLAHEATKLATGPRG 1961
Cdd:PRK03918 464 IEkelKEIEEKERKLRKelrelekvlkkeselIKLKELAEQlkELEEKLKKYnLEELEKKAEEYEKLKEKLIKLKGEIKS 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1962 LLKEdakgcLQKSFRILNEAKKLANDVKENEDHLNGLKTRIENA--------DARNGDLLRTLNDTLgKLSAIPNDTAAK 2033
Cdd:PRK03918 544 LKKE-----LEKLEELKKKLAELEKKLDELEEELAELLKELEELgfesveelEERLKELEPFYNEYL-ELKDAEKELERE 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2034 LQAVKDKARQANDTAKD---VLAQITELHQNLDGLKKNYNKladsvaKTNAVVKDP--SKNKIIADADATVKNLE---QE 2105
Cdd:PRK03918 618 EKELKKLEEELDKAFEElaeTEKRLEELRKELEELEKKYSE------EEYEELREEylELSRELAGLRAELEELEkrrEE 691
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 1677500969 2106 ADRLIDKLKP--------IKELEdNLKKNISEIKELINQARKQANSIK 2145
Cdd:PRK03918 692 IKKTLEKLKEeleerekaKKELE-KLEKALERVEELREKVKKYKALLK 738
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1668-2145 |
1.93e-18 |
|
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: 92.78 E-value: 1.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1668 AERTNTRAKSLGEFIKELARDAEAvNEKAIKLNETLGTRDEAFERNL----EGLQKE--------------IDQMIKELR 1729
Cdd:TIGR04523 28 ANKQDTEEKQLEKKLKTIKNELKN-KEKELKNLDKNLNKDEEKINNSnnkiKILEQQikdlndklkknkdkINKLNSDLS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1730 RKNLET-----QKEIAEDELVAAEALLKKVKKLFGESRGENEEMEKDL-------------REKLADYKNKVDDAWDLLR 1791
Cdd:TIGR04523 107 KINSEIkndkeQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELeklnnkyndlkkqKEELENELNLLEKEKLNIQ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1792 EATDKIReaNRLFAVNQKnMTALEKKKEAVESGKRQIENtLKEGNDIL-DEANRLADEINsiidyveDIQTKLPPMSEEL 1870
Cdd:TIGR04523 187 KNIDKIK--NKLLKLELL-LSNLKKKIQKNKSLESQISE-LKKQNNQLkDNIEKKQQEIN-------EKTTEISNTQTQL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1871 NDKIdDLSQEIKDRkLAEKVSQAESHAAQLNDSSAVLdgildeaknisfnataafkaySNIKDYIDEAEKVAKE--AKDL 1948
Cdd:TIGR04523 256 NQLK-DEQNKIKKQ-LSEKQKELEQNNKKIKELEKQL---------------------NQLKSEISDLNNQKEQdwNKEL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1949 AHEATKlatgprgllKEDAKGCLQKSfriLNEAKKLANDVKENedhLNGLKTRIENADARNGDLLRTLNDTLGKLSAIPN 2028
Cdd:TIGR04523 313 KSELKN---------QEKKLEEIQNQ---ISQNNKIISQLNEQ---ISQLKKELTNSESENSEKQRELEEKQNEIEKLKK 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2029 DTAAKLQAVKDKARQAND----------TAKDVLAQITELHQNLDGLKKNYNKLADSVAKTNAVVKD-----PSKNKIIA 2093
Cdd:TIGR04523 378 ENQSYKQEIKNLESQINDleskiqnqekLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDltnqdSVKELIIK 457
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1677500969 2094 DADATVKNLEQEADRLIDKLKPIK-ELEDN---LKKNISEIKELINQARKQANSIK 2145
Cdd:TIGR04523 458 NLDNTRESLETQLKVLSRSINKIKqNLEQKqkeLKSKEKELKKLNEEKKELEEKVK 513
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2550-2688 |
2.31e-17 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 80.54 E-value: 2.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2550 FSTKNESGIILLGSGGtpapprrkrrqtGQAYYAILLNRGRLEVHLSTGARTmrkIVIRPEPNLFHDGREHSVHVERTRG 2629
Cdd:pfam02210 1 FRTRQPNGLLLYAGGG------------GSDFLALELVNGRLVLRYDLGSGP---ESLLSSGKNLNDGQWHSVRVERNGN 65
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1677500969 2630 IFTVQVD--ENRRYMQNLTVEQPIEVKKLFVGGAPPEFQPSPLRNIPPFEGCIWNLVINSV 2688
Cdd:pfam02210 66 TLTLSVDgqTVVSSLPPGESLLLNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2174-2311 |
2.38e-17 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 80.54 E-value: 2.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2174 VKTAVADNLLFYLGSAKfIDFLAIEMRKGKVSFLWDVGSGVGRVEYPDLTIDDSYWYRIVASRTGRNGTISVralDGpka 2253
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGG-SDFLALELVNGRLVLRYDLGSGPESLLSSGKNLNDGQWHSVRVERNGNTLTLSV---DG--- 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1677500969 2254 sivpSTHHSTSPPGYTiLDVDANAMLFVGGLTGKLKKADAVRVITFTGCMGETYFDNK 2311
Cdd:pfam02210 74 ----QTVVSSLPPGES-LLLNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1650-2141 |
1.20e-16 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 87.40 E-value: 1.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1650 LLTRATKVTADGEQTGQ----DAERTNTRAKSLGEFIKELAR-DAEA-VN---------EKAIklNETLGTRdeafernl 1714
Cdd:PRK02224 82 HIERRVRLSGDRATTAKcvleTPEGTIDGARDVREEVTELLRmDAEAfVNcayvrqgevNKLI--NATPSDR-------- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1715 eglQKEIDQMikeLRRKNLETQKEIAEDELVAAEALLKKVKKLFGESRGENEEME-KDLREKLADYKNKVDDawdlLREA 1793
Cdd:PRK02224 152 ---QDMIDDL---LQLGKLEEYRERASDARLGVERVLSDQRGSLDQLKAQIEEKEeKDLHERLNGLESELAE----LDEE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1794 TDKIrEANRLFAVNQKN-----MTALEKKKEAVESGKRQIENTLKEGNDILDEANRLADEINSIIDYVEDIQTKLPPMSE 1868
Cdd:PRK02224 222 IERY-EEQREQARETRDeadevLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLA 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1869 ELNdkIDDLSQEIkdrkLAEKVSQAESHAAQLNDSsavldgiLDEAKnisfnaTAAFKAYSNIKDYIDEAEKVAKEAKDL 1948
Cdd:PRK02224 301 EAG--LDDADAEA----VEARREELEDRDEELRDR-------LEECR------VAAQAHNEEAESLREDADDLEERAEEL 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1949 AHEATKLATGprgllKEDAKGCLQKSFRILNEakkLANDVKENEDHLNGLKTRIENADARNGDLLRTLNDTLGKLsaipN 2028
Cdd:PRK02224 362 REEAAELESE-----LEEAREAVEDRREEIEE---LEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRERE----A 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2029 DTAAKLQAVKDKARQAN---------------------DTAKDVLAQITELHQNLDGLKKNYNKLADSVAKTNAVVKdps 2087
Cdd:PRK02224 430 ELEATLRTARERVEEAEalleagkcpecgqpvegsphvETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVE--- 506
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1677500969 2088 knkiiadadatvknLEQEADRLIDKLKPIKELEDNLKKNISEIKELINQARKQA 2141
Cdd:PRK02224 507 --------------AEDRIERLEERREDLEELIAERRETIEEKRERAEELRERA 546
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1670-2228 |
2.89e-15 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 82.64 E-value: 2.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1670 RTNTRAKSLGEFIKELARDAEAVNEKAIklnetLGTRDEAFERNLEGLQKEIDQMIKELRRKNLETQKEIAEDELVAAEA 1749
Cdd:PRK01156 94 RREAYIKKDGSIIAEGFDDTTKYIEKNI-----LGISKDVFLNSIFVGQGEMDSLISGDPAQRKKILDEILEINSLERNY 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1750 LLKKvkklfgesrgeneEMEKDLREKLADYknkvDDAWDLLREATDKIREANRLFAVNQKNMTALEKKKEAVESGKRQIE 1829
Cdd:PRK01156 169 DKLK-------------DVIDMLRAEISNI----DYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAM 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1830 NTLKEGNDILDEANRLADEINSIIDYVEDIQTKLpPMSEELNDKIDDLSQEIKdrklaekvsQAESHAAQLNdSSAVLDG 1909
Cdd:PRK01156 232 DDYNNLKSALNELSSLEDMKNRYESEIKTAESDL-SMELEKNNYYKELEERHM---------KIINDPVYKN-RNYINDY 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1910 ILDEAKNISFNataafKAYSNIKDYIDEAEKVAKEAKDlaheatklatgprglLKEDAKGCLQKSFRiLNEAKKLANDVK 1989
Cdd:PRK01156 301 FKYKNDIENKK-----QILSNIDAEINKYHAIIKKLSV---------------LQKDYNDYIKKKSR-YDDLNNQILELE 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1990 ENEDHLNG-------LKTRIENADARNGDLLRTLNDTLGKLSAIPNDTAAKLQAVKDKARQANDTAKDVLAQITELHQNL 2062
Cdd:PRK01156 360 GYEMDYNSylksiesLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENL 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2063 DGLKKNYNKL-ADSVA----------KTNAVVKDPSKNKIIADADatVKNLEQEADRLIDKLKPIKELEDNLKKniSEIK 2131
Cdd:PRK01156 440 DELSRNMEMLnGQSVCpvcgttlgeeKSNHIINHYNEKKSRLEEK--IREIEIEVKDIDEKIVDLKKRKEYLES--EEIN 515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2132 ELINQ------ARKQANSIKVSVSSGGDciRTYKPEIKKGSYNNIVVNVKTAVADNLLFYLGSAKFIDFLAIEMRKGKVS 2205
Cdd:PRK01156 516 KSINEynkiesARADLEDIKIKINELKD--KHDKYEEIKNRYKSLKLEDLDSKRTSWLNALAVISLIDIETNRSRSNEIK 593
|
570 580
....*....|....*....|....*.
gi 1677500969 2206 F-LWDVGSGVGRVE--YPDltiDDSY 2228
Cdd:PRK01156 594 KqLNDLESRLQEIEigFPD---DKSY 616
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1630-2150 |
9.14e-15 |
|
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: 81.26 E-value: 9.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1630 ERLIQLAEGNLNTLVTEMNEL--------------LTRATKVTADGEQTGQDAERTNTRAKSLGEFIKELARDAEAVNEK 1695
Cdd:TIGR02168 280 EEEIEELQKELYALANEISRLeqqkqilrerlanlERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1696 AIKLNETLgtrdeafeRNLEGLQKEIDQMIKELRRK----------------NLETQKEIAEDEL--------VAAEALL 1751
Cdd:TIGR02168 360 LEELEAEL--------EELESRLEELEEQLETLRSKvaqlelqiaslnneieRLEARLERLEDRRerlqqeieELLKKLE 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1752 KKVKKLFGESRGENEEMEKDLREKLADYKNKVDDAWDLLREATDKIREANRLFAVNQKNMTALEKKKEAVESGKRQIENT 1831
Cdd:TIGR02168 432 EAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKAL 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1832 LKEGNDILDEANRLADEIN------SIIDYV--EDIQTKLPPMSEELNDKIDDLSQEIKDRK--LAEKVSQAESHAAQLN 1901
Cdd:TIGR02168 512 LKNQSGLSGILGVLSELISvdegyeAAIEAAlgGRLQAVVVENLNAAKKAIAFLKQNELGRVtfLPLDSIKGTEIQGNDR 591
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1902 DSSAVLDGILDEAKNISFNATAAFKAYSN------IKDYIDEAEKVAKEakdLAHEATkLAT------GPRGLL-KEDAK 1968
Cdd:TIGR02168 592 EILKNIEGFLGVAKDLVKFDPKLRKALSYllggvlVVDDLDNALELAKK---LRPGYR-IVTldgdlvRPGGVItGGSAK 667
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1969 ---GCLQKSFRILN---EAKKLANDVKENEDHLNGLKTRIENADARNGDLLRTLNDTLGKLSAIPNDTA---AKLQAVKD 2039
Cdd:TIGR02168 668 tnsSILERRREIEEleeKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLArleAEVEQLEE 747
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2040 KARQANDTAKDVLAQITELHQNLDGLKKNYNKLADSVAKTNAVVKDPSKNkiIADADATVKNLEQEADRLIDKLKPIKEL 2119
Cdd:TIGR02168 748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEE--LKALREALDELRAELTLLNEEAANLRER 825
|
570 580 590
....*....|....*....|....*....|.
gi 1677500969 2120 EDNLKKNISEIKELINQARKQANSIKVSVSS 2150
Cdd:TIGR02168 826 LESLERRIAATERRLEDLEEQIEELSEDIES 856
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1705-1990 |
1.53e-14 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 77.26 E-value: 1.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1705 TRDEAFERNLEGLQKEIDQM---IKELRRKNLETQKEIAEdelVAAE--ALLKKVKKLFGESRGENEEMeKDLREKLADY 1779
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELreeIEELKEKRDELNEELKE---LAEKrdELNAQVKELREEAQELREKR-DELNEKVKEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1780 KNKVDDAWDLLREATDKIREANRLFAVNQKNMTALEKKKEAVESGKRQIEN---TLKEGNDILDEANRLADEInsiidyv 1856
Cdd:COG1340 77 KEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTevlSPEEEKELVEKIKELEKEL------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1857 EDIQtklppMSEELNDKIDDLSQEIKD---------RKLAEKVSQAESHAAQLNDSSAVLDGILDEAKnisfnatAAFKA 1927
Cdd:COG1340 150 EKAK-----KALEKNEKLKELRAELKElrkeaeeihKKIKELAEEAQELHEEMIELYKEADELRKEAD-------ELHKE 217
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1677500969 1928 YSNIKDYIDEAEK----VAKEAKDLAHEATKLATGPRGLLKEDAKgclqksfrilNEAKKLANDVKE 1990
Cdd:COG1340 218 IVEAQEKADELHEeiieLQKELRELRKELKKLRKKQRALKREKEK----------EELEEKAEEIFE 274
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1703-2105 |
2.84e-14 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 77.63 E-value: 2.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1703 LGTRDEAFERNLEGLQKEIDQMIKELrrknletqKEIAEDELVAAEALLKKVKKLFGESRGENEEMEKdLREKLADYKNK 1782
Cdd:COG4372 4 LGEKVGKARLSLFGLRPKTGILIAAL--------SEQLRKALFELDKLQEELEQLREELEQAREELEQ-LEEELEQARSE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1783 VDDAWDLLREATDKIREANRLFAVNQKNMTALEKKKEAVEsgkRQIENTLKEGNDILDEANRLADEINSIIDYVEDIQTK 1862
Cdd:COG4372 75 LEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQ---EELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1863 LppmsEELNDKIDDLSQEIKdrKLAEKVSQAESHAAQlndssAVLDGILDEAKNISFNATAAFKAYSNIKDYIDEAEKVA 1942
Cdd:COG4372 152 L----KELEEQLESLQEELA--ALEQELQALSEAEAE-----QALDELLKEANRNAEKEEELAEAEKLIESLPRELAEEL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1943 KEAKDLAHEATKLATgprgllkedakgclqksFRILNEAKKLANDVKENEDHLNGLKTRIENADARNGDLLRTLNDTLGK 2022
Cdd:COG4372 221 LEAKDSLEAKLGLAL-----------------SALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAAL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2023 LSAIPNDTAAKLQAVKDKARQANDTAKDVLAQitelhQNLDGLKKNYNKLADSVAKTNAVVKDPSKNKIIADADATVKNL 2102
Cdd:COG4372 284 ELEALEEAALELKLLALLLNLAALSLIGALED-----ALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLEL 358
|
...
gi 1677500969 2103 EQE 2105
Cdd:COG4372 359 LSK 361
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1612-2145 |
7.70e-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: 78.09 E-value: 7.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1612 LENMTQELKHLLSPQRAPERLIQLAEGNLNTLVTEMNELLTRATKVtadgeqtgqdaertNTRAKSLGEF-IKELARDAE 1690
Cdd:pfam02463 231 YLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKE--------------EEKEKKLQEEeLKLLAKEEE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1691 AVNEKAIKLnetlGTRDEAFERNLEGLQKEIDQMIKELrrknLETQKEIAEDElvaaeallkKVKKLFGESRGENEEMEK 1770
Cdd:pfam02463 297 ELKSELLKL----ERRKVDDEEKLKESEKEKKKAEKEL----KKEKEEIEELE---------KELKELEIKREAEEEEEE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1771 DLREKLADYKNKVDDAWDLLREATDKIREANRLFavNQKNMTALEKKKEAvesgKRQIENTLKEGNDILDEANRLADEIN 1850
Cdd:pfam02463 360 ELEKLQEKLEQLEEELLAKKKLESERLSSAAKLK--EEELELKSEEEKEA----QLLLELARQLEDLLKEEKKEELEILE 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1851 SIIDYVEDIQTKLPPMSEELND-------KIDDLSQEIKDRKLAEKVSQAESHAAQLNDSSAVLDGILDEAKNISFN--- 1920
Cdd:pfam02463 434 EEEESIELKQGKLTEEKEELEKqelkllkDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKvll 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1921 -----------------------ATAAFKAY---------SNIKDYIDEAEKVAKEAKDLAHEATKLATGPRGLLKEDAK 1968
Cdd:pfam02463 514 alikdgvggriisahgrlgdlgvAVENYKVAistavivevSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKS 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1969 GCLQKSFRILNEAKKLANDVKENEDHLNGLKTRIENADARNGDLLRTLNDTLGKLSAIPNDTAAKLQAVKDKARQANDTA 2048
Cdd:pfam02463 594 IAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTK 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2049 KDVLAQITE--LHQNLDGLKK----NYNKLADSVAKTNAVVKDPSKNKIIAD--------ADATVKNLEQEADRLIDKLK 2114
Cdd:pfam02463 674 ELLEIQELQekAESELAKEEIlrrqLEIKKKEQREKEELKKLKLEAEELLADrvqeaqdkINEELKLLKQKIDEEEEEEE 753
|
570 580 590
....*....|....*....|....*....|.
gi 1677500969 2115 PIKELEDNLKKNISEIKELINQARKQANSIK 2145
Cdd:pfam02463 754 KSRLKKEEKEEEKSELSLKEKELAEEREKTE 784
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1656-2184 |
9.16e-14 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 78.33 E-value: 9.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1656 KVTADGEQTGQdAERTNTRAKSLG---EFIKELARDAEAVNEKAIKLNETLGTRDEaFERNLeglqkeIDQMIKELRRKN 1732
Cdd:PTZ00440 1111 VVNADKEKNKQ-TEHYNKKKKSLEkiyKQMEKTLKELENMNLEDITLNEVNEIEIE-YERIL------IDHIVEQINNEA 1182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1733 LETQKEIAEDELVAAEALLKKvKKLFGESRGENEEME-KDLREKLADYKNKVDDawdLLREATDKIREANRlfavnQKNM 1811
Cdd:PTZ00440 1183 KKSKTIMEEIESYKKDIDQVK-KNMSKERNDHLTTFEyNAYYDKATASYENIEE---LTTEAKGLKGEANR-----STNV 1253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1812 TALEKKKEAVESGKRQ-------IENTLKEGND-----ILDEANRLADEI-------------------------NSIID 1854
Cdd:PTZ00440 1254 DELKEIKLQVFSYLQQvikennkMENALHEIKNmyeflISIDSEKILKEIlnstkkaeefsndakkelektdnliKQVEA 1333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1855 YVEDIQTKLPPMSEELNDK-IDD-------LSQEIKDRKLA---------EKVSQAESHAAQLNDSSAVLDgILDEAKNI 1917
Cdd:PTZ00440 1334 KIEQAKEHKNKIYGSLEDKqIDDeikkieqIKEEISNKRKEinkylsnikSNKEKCDLHVRNASRGKDKID-FLNKHEAI 1412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1918 SFNATAAFKAySNIKDYIDEAEKVAKEAKDLA-------------------------------------HEATKLATGPR 1960
Cdd:PTZ00440 1413 EPSNSKEVNI-IKITDNINKCKQYSNEAMETEnkadenndsiikyekeitnilnnssilgkktklekkkKEATNIMDDIN 1491
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1961 G---LLKEDAKGcLQKSFRILNEAKklanDVKENEDHLNGLKTRIENAdarngdllrTLNDTLGKL-SAIPNdtaakLQA 2036
Cdd:PTZ00440 1492 GehsIIKTKLTK-SSEKLNQLNEQP----NIKREGDVLNNDKSTIAYE---------TIQYNLGRVkHNLLN-----ILN 1552
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2037 VKDKAR----QANDTAKDVL--AQITElHQNLDGLKK---NYNKLADSVAKTNAVVKDpSKNKIIaDADATVKNLEQEAD 2107
Cdd:PTZ00440 1553 IKDEIEtilnKAQDLMRDISkiSKIVE-NKNLENLNDkeaDYVKYLDNILKEKQLMEA-EYKKLN-EIYSDVDNIEKELK 1629
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2108 RL-----IDKLKPIKELEDNLKKNISEIKELINQARKQANSIKVSVSsggdcIRTYKPE------IKK---------GSY 2167
Cdd:PTZ00440 1630 KHkknyeIGLLEKVIEINKNIKLYMDSTKESLNSLVNNFSSLFNNFY-----LNKYNINenlekyKKKlneiynefmESY 1704
|
650
....*....|....*..
gi 1677500969 2168 NNIVVNVKTAVADNLLF 2184
Cdd:PTZ00440 1705 NIIQEKMKEVSNDDVDY 1721
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1635-2133 |
1.09e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 77.39 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1635 LAEGNLNTLVTEMNELLTRATKVTADGEQTGQDAERTNTRAKSLGEFIKELARDAEAVNEKAIKLNETL-GTRDEAFERn 1713
Cdd:PRK02224 304 LDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELeEAREAVEDR- 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1714 lEGLQKEIDQMIKELRRK--NLETQKEIAEDELvaaEALLkkvkklfgESRGENEEMEKDLReklADyknkvddawdlLR 1791
Cdd:PRK02224 383 -REEIEELEEEIEELRERfgDAPVDLGNAEDFL---EELR--------EERDELREREAELE---AT-----------LR 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1792 EATDKIREANRLFAVNQ-----------KNMTALEKKKEAVESGKRQIEntlkegnDILDEANRLADEINSIIDYVEdiq 1860
Cdd:PRK02224 437 TARERVEEAEALLEAGKcpecgqpvegsPHVETIEEDRERVEELEAELE-------DLEEEVEEVEERLERAEDLVE--- 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1861 tkLPPMSEELNDKIDDLSQEIKDRK--LAEKVSQAEShaaqLNDSSAVLDGILDEAKNisfnatAAFKAYsnikdyiDEA 1938
Cdd:PRK02224 507 --AEDRIERLEERREDLEELIAERRetIEEKRERAEE----LRERAAELEAEAEEKRE------AAAEAE-------EEA 567
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1939 EKVAKEAKDLaheatklatgprgllkEDAKGCLQKSFRILNEAKKLANDVKENEDHLNGLKTRIENADARNgDLLRtlnD 2018
Cdd:PRK02224 568 EEAREEVAEL----------------NSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREALAELN-DERR---E 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2019 TLGKLSAIPNDTAAKLQAVK-DKARQANDTAKDVLAQITElhqnldglkknynKLADSVAKtnavvKDPSKNKIIAdada 2097
Cdd:PRK02224 628 RLAEKRERKRELEAEFDEARiEEAREDKERAEEYLEQVEE-------------KLDELREE-----RDDLQAEIGA---- 685
|
490 500 510
....*....|....*....|....*....|....*.
gi 1677500969 2098 tVKNLEQEADRLIDKLKPIKELEDNLKKNISEIKEL 2133
Cdd:PRK02224 686 -VENELEELEELRERREALENRVEALEALYDEAEEL 720
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1718-2077 |
1.43e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 77.40 E-value: 1.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1718 QKEIDQMIK---ELRRKNLE---------TQKEIAEDELVAAEALLKKVKKLFGESRG--ENEEMEKDLREKLADYKNKV 1783
Cdd:TIGR02168 143 QGKISEIIEakpEERRAIFEeaagiskykERRKETERKLERTRENLDRLEDILNELERqlKSLERQAEKAERYKELKAEL 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1784 DDA-WDLLreaTDKIREANrlfavnqKNMTALEKKKEAVESGKRQIENTLKEgndiLDEA-NRLADEINSIIDYVEDIQT 1861
Cdd:TIGR02168 223 RELeLALL---VLRLEELR-------EELEELQEELKEAEEELEELTAELQE----LEEKlEELRLEVSELEEEIEELQK 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1862 KLppmsEELNDKIDDLSQEIkdRKLAEKVSQAESHAAQLNDSSAVLDGILDEAKnisFNATAAFKAYSNIKDYIDEAEKV 1941
Cdd:TIGR02168 289 EL----YALANEISRLEQQK--QILRERLANLERQLEELEAQLEELESKLDELA---EELAELEEKLEELKEELESLEAE 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1942 AKEAKDLAHEATKLATGPRGLLKEDAKgclqKSFRILNEAKKLANDVKENEDHLNGLKTRIENADARNGDLLRTLND--- 2018
Cdd:TIGR02168 360 LEELEAELEELESRLEELEEQLETLRS----KVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEael 435
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1677500969 2019 -----TLGKLSAIPNDTAAKLQAV----------KDKARQANDTAKDVLAQITELHQNLDGLKKNYNKLADSVA 2077
Cdd:TIGR02168 436 kelqaELEELEEELEELQEELERLeealeelreeLEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVK 509
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
917-965 |
2.83e-13 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 66.22 E-value: 2.83e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1677500969 917 PCRCNAGGSFSEVCHSQTGQCECRANVQGQRCDKCKAGTFGLQS-ARGCV 965
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSqGGGCQ 50
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1640-2133 |
5.85e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 75.08 E-value: 5.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1640 LNTLVTEMNELLT------------RATKVTADG-----EQTGQDAERTNTRAKSLGEFIKELARDAEAVNEKAIKLNET 1702
Cdd:PRK02224 208 LNGLESELAELDEeieryeeqreqaRETRDEADEvleehEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRER 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1703 LGTRDEAFERNLEGLQ-KEIDQMIKELRRKNLETQKEIAEDELV-----------AAEALLKKVKKLFGES---RGENEE 1767
Cdd:PRK02224 288 LEELEEERDDLLAEAGlDDADAEAVEARREELEDRDEELRDRLEecrvaaqahneEAESLREDADDLEERAeelREEAAE 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1768 MEKDL---REKLADYKNKVDDawdlLREATDKIREANRLFAVNQKNMTA----LEKKKEAVESGKRQIENTLKEGNDILD 1840
Cdd:PRK02224 368 LESELeeaREAVEDRREEIEE----LEEEIEELRERFGDAPVDLGNAEDfleeLREERDELREREAELEATLRTARERVE 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1841 EANRLADEIN-----------SIIDYVEDIQTKLPPMSEELND---KIDDLSQEIkDRklAEKVSQAESHAAQLNDSSAV 1906
Cdd:PRK02224 444 EAEALLEAGKcpecgqpvegsPHVETIEEDRERVEELEAELEDleeEVEEVEERL-ER--AEDLVEAEDRIERLEERRED 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1907 LDGILDEAKNIsfnataafkaysnIKDYIDEAEKVAKEAKDLAHEATKlatgprgllKEDAKGCLQKsfrilnEAKKLAN 1986
Cdd:PRK02224 521 LEELIAERRET-------------IEEKRERAEELRERAAELEAEAEE---------KREAAAEAEE------EAEEARE 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1987 DVKENEDHLNGLKTRIENadarngdlLRTLNDTLGKLSaipnDTAAKLQAVKDKaRQA----NDTAKDVLAQITELHQNL 2062
Cdd:PRK02224 573 EVAELNSKLAELKERIES--------LERIRTLLAAIA----DAEDEIERLREK-REAlaelNDERRERLAEKRERKREL 639
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1677500969 2063 DGlkknynKLadsvaktnavvkDPSKnkiIADADATVKNLEQEADRLIDKLKPIKELEDNLKKNI----SEIKEL 2133
Cdd:PRK02224 640 EA------EF------------DEAR---IEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIgaveNELEEL 693
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
967-1011 |
6.55e-13 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 65.03 E-value: 6.55e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1677500969 967 CNCNSFGSKSFDCE-ESGQCWCQPGVTGKKCDRCAHGYFNFQEGGC 1011
Cdd:smart00180 1 CDCDPGGSASGTCDpDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1613-2179 |
6.92e-13 |
|
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: 74.76 E-value: 6.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1613 ENMTQELKHLLSPQRAPERLIQLAEGNLNTLVTEmnelltratkvtadGEQTGQDAERTNTRAKSLGEFIKEL-ARDAEA 1691
Cdd:pfam05483 105 ENKLQENRKIIEAQRKAIQELQFENEKVSLKLEE--------------EIQENKDLIKENNATRHLCNLLKETcARSAEK 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1692 VNEKAIKLNETlgtrdeafERNLEGLQKEIDQMI---KELR----RKNLETQKEIAEDElvaaeallKKVKKLFGESRGE 1764
Cdd:pfam05483 171 TKKYEYEREET--------RQVYMDLNNNIEKMIlafEELRvqaeNARLEMHFKLKEDH--------EKIQHLEEEYKKE 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1765 NEEMEKD---LREKLADYKNKVDDAWDLLREATDKIREANRLFAVNQKNMTALEKKKEAVESGKRQIENTLKEG---NDI 1838
Cdd:pfam05483 235 INDKEKQvslLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSmstQKA 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1839 LDEANRLADEinSIIDYVEDIQTKLppmsEELNDKIDDLSQEIKDRKLA----EKVSQAESHAAQLNDSSAVLDGILDEA 1914
Cdd:pfam05483 315 LEEDLQIATK--TICQLTEEKEAQM----EELNKAKAAHSFVVTEFEATtcslEELLRTEQQRLEKNEDQLKIITMELQK 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1915 KNISFNATAAFKaySNIKDYIDEAEKVAKEAKDLAHEATKLATgprglLKEDAKGCLQKSFRILNEAKKLAND------- 1987
Cdd:pfam05483 389 KSSELEEMTKFK--NNKEVELEELKKILAEDEKLLDEKKQFEK-----IAEELKGKEQELIFLLQAREKEIHDleiqlta 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1988 VKENEDH----LNGLKTRIENADARNGDLLRTLNDTLGKLSAIPNDTAAKLQAVKDKARQANDTAKD---VLAQI----- 2055
Cdd:pfam05483 462 IKTSEEHylkeVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQeerMLKQIenlee 541
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2056 --TELHQNLDGLKKNYNKLADSV------AKTNAVVKDPS---KNKIIADADATVKNLEQEADrliDKLKPIKELEDN-- 2122
Cdd:pfam05483 542 keMNLRDELESVREEFIQKGDEVkckldkSEENARSIEYEvlkKEKQMKILENKCNNLKKQIE---NKNKNIEELHQEnk 618
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1677500969 2123 -LKKNISEIKELINQARKQANSIKVSVSSG----GDCIRTYKPEI--KKGSYNNIVVNVKTAVA 2179
Cdd:pfam05483 619 aLKKKGSAENKQLNAYEIKVNKLELELASAkqkfEEIIDNYQKEIedKKISEEKLLEEVEKAKA 682
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1717-2141 |
8.16e-13 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 74.72 E-value: 8.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1717 LQKEIDQMIK----ElRRKNLE---------TQKEIAEDELVAAEALLKKVKKLFGESRGENEEMEKDlREKLADYKnkv 1783
Cdd:TIGR02169 140 LQGDVTDFISmspvE-RRKIIDeiagvaefdRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRE-REKAERYQ--- 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1784 ddawDLLREatdkIREANRLFAVNQKNmtALEKKKEAVEsgkRQIENTLKEGNDILDEANRLADEINSIIDYVEDIQTKL 1863
Cdd:TIGR02169 215 ----ALLKE----KREYEGYELLKEKE--ALERQKEAIE---RQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKI 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1864 PPMSEE----LNDKIDDLSQEIK--DRKLAEKVSQAESHAAQLNDSSAVLDGILDEAKNISfnataafkaySNIKDYIDE 1937
Cdd:TIGR02169 282 KDLGEEeqlrVKEKIGELEAEIAslERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELE----------REIEEERKR 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1938 AEKVAKEAKDLAHEATKLatgprgllkedakgclqksfriLNEAKKLANDVKENEDHLNGLKTRIENADARNGDLLRT-- 2015
Cdd:TIGR02169 352 RDKLTEEYAELKEELEDL----------------------RAELEEVDKEFAETRDELKDYREKLEKLKREINELKREld 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2016 -LNDTLGKLSAIPNDTAAKLQAVKDKARQANDTAKDVLAQITELHQNLDGLKKnynkladsvaktnavvkdpsknkIIAD 2094
Cdd:TIGR02169 410 rLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAA-----------------------DLSK 466
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1677500969 2095 ADATVKNLEQEADRLidklkpikelEDNLKKNISEIKELinQARKQA 2141
Cdd:TIGR02169 467 YEQELYDLKEEYDRV----------EKELSKLQRELAEA--EAQARA 501
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1649-2142 |
1.33e-12 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 74.09 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1649 ELLTRAtKVTADGEQTG--QDAERTNTRAkslGEFIKELARDAEAVNEKAIKLNETLgtRDEAFERnLEGLQKEIDQMIK 1726
Cdd:NF041483 484 ELLTKA-KADADELRSTatAESERVRTEA---IERATTLRRQAEETLERTRAEAERL--RAEAEEQ-AEEVRAAAERAAR 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1727 ELRRKN---LETQKEIAEDEL----VAAEALLKKVKKLFGESRGENEEMEKDLREKLadyknkvddawDLLR-EATDKIR 1798
Cdd:NF041483 557 ELREETeraIAARQAEAAEELtrlhTEAEERLTAAEEALADARAEAERIRREAAEET-----------ERLRtEAAERIR 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1799 --------EANRL-----------------FAVNQKNMTALEK---KKEAVESGKR-------QIENTLKEGNDIL---- 1839
Cdd:NF041483 626 tlqaqaeqEAERLrteaaadasaaraegenVAVRLRSEAAAEAerlKSEAQESADRvraeaaaAAERVGTEAAEALaaaq 705
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1840 DEANRL---ADEI-NSIIDYVEDIQTKLPPMSEEL----NDKIDDLSQEIK------DRKLAEKVSQAESHAAQLNDSSA 1905
Cdd:NF041483 706 EEAARRrreAEETlGSARAEADQERERAREQSEELlasaRKRVEEAQAEAQrlveeaDRRATELVSAAEQTAQQVRDSVA 785
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1906 vldGILDEAKN-ISFNATAAFKAYSNIK-DYIDEAEKVAKEAKDLAHEATKLATGPRGLLKEDAKGCLQKSFRILN---- 1979
Cdd:NF041483 786 ---GLQEQAEEeIAGLRSAAEHAAERTRtEAQEEADRVRSDAYAERERASEDANRLRREAQEETEAAKALAERTVSeaia 862
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1980 EAKKLANDVKENEDhlnglKTRIENADAR---NGDLLRTLNDTLGKLSAIPNDTAAklQAVKDKARQANDTAKDVLAQIT 2056
Cdd:NF041483 863 EAERLRSDASEYAQ-----RVRTEASDTLasaEQDAARTRADAREDANRIRSDAAA--QADRLIGEATSEAERLTAEARA 935
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2057 ELHQNLDGLKKNYNKL-ADSVAKTNAVVKDPSKN--KIIADADATVKNLEQEADRLIDKLKPIK-----ELEDNLKKNIS 2128
Cdd:NF041483 936 EAERLRDEARAEAERVrADAAAQAEQLIAEATGEaeRLRAEAAETVGSAQQHAERIRTEAERVKaeaaaEAERLRTEARE 1015
|
570
....*....|....
gi 1677500969 2129 EIKELINQARKQAN 2142
Cdd:NF041483 1016 EADRTLDEARKDAN 1029
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1661-2012 |
1.38e-12 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 72.24 E-value: 1.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1661 GEQTGQDAERTNTRAKSLGEFIKELARDAEAVNEKAIKLNETLgtrdEAFERNLEGLQKEIDQMIKELRRKN-----LET 1735
Cdd:COG4372 5 GEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEEL----EQLREELEQAREELEQLEEELEQARseleqLEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1736 QKEIAEDELVAAEALLKKVKKLFGESRGENEEMEKDL------REKLADYKNKVDDAWDLLREA-TDKIREANRLfavnQ 1808
Cdd:COG4372 81 ELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELeelqkeRQDLEQQRKQLEAQIAELQSEiAEREEELKEL----E 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1809 KNMTALEKKKEAVESGKRQIENTLKEG--NDILDEANRLAdeinsiidYVEDIQTKLPPMSEELNDKIDDLSQEIKDRKL 1886
Cdd:COG4372 157 EQLESLQEELAALEQELQALSEAEAEQalDELLKEANRNA--------EKEEELAEAEKLIESLPRELAEELLEAKDSLE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1887 AEKVSQAESHAAQLNDSSAVLDGILDEAKNISFNATAAFKAYSNIKDYIDEAEKVAKEAKDLAHEATKLATGPRGLLKED 1966
Cdd:COG4372 229 AKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALS 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1677500969 1967 AKGCLQKSFRILNE--AKKLANDVKENEDHLNGLKTRIENADARNGDL 2012
Cdd:COG4372 309 LIGALEDALLAALLelAKKLELALAILLAELADLLQLLLVGLLDNDVL 356
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1702-2118 |
1.42e-12 |
|
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: 73.45 E-value: 1.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1702 TLGTRDEAFERNLEGLQKEiDQMIKELRRKNLE-TQKEIAEDELVAA-----EALLKKVKKLFGESRGENEEMEKDLREK 1775
Cdd:COG5185 205 NSIKESETGNLGSESTLLE-KAKEIINIEEALKgFQDPESELEDLAQtsdklEKLVEQNTDLRLEKLGENAESSKRLNEN 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1776 LADYKNKVDDAWDLLREATDKI------REANRLFAVNQKNmTALEKKKEAVESG-KRQIENTLKEGNDILDEANRLADE 1848
Cdd:COG5185 284 ANNLIKQFENTKEKIAEYTKSIdikkatESLEEQLAAAEAE-QELEESKRETETGiQNLTAEIEQGQESLTENLEAIKEE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1849 INSIIDyvEDIQTKLPPMSEELNDKIDDLSQEIkDRKLAEKVSQAESHAAQLNDSSAVLDGILDEAKNISFNATAAFKAY 1928
Cdd:COG5185 363 IENIVG--EVELSKSSEELDSFKDTIESTKESL-DEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEV 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1929 SNIKD-YIDEAEKVAKEAKDLAHEatklatgprgllkedakgclqksfRILNEAKKLANDVKENEDHLNGLKTRIENAda 2007
Cdd:COG5185 440 SKLLNeLISELNKVMREADEESQS------------------------RLEEAYDEINRSVRSKKEDLNEELTQIESR-- 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2008 rngdlLRTLNDTLGKLSAipnDTAAKLQAVKDKARQANDTAKDvlaqiTELHQNLDGLKKNYNKLADSVAKTNavvkDPS 2087
Cdd:COG5185 494 -----VSTLKATLEKLRA---KLERQLEGVRSKLDQVAESLKD-----FMRARGYAHILALENLIPASELIQA----SNA 556
|
410 420 430
....*....|....*....|....*....|.
gi 1677500969 2088 KNKIIADADATVKNLEQEADRLIDKLKPIKE 2118
Cdd:COG5185 557 KTDGQAANLRTAVIDELTQYLSTIESQQARE 587
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
918-964 |
1.55e-12 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 64.25 E-value: 1.55e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1677500969 918 CRCNAGGSFSEVCHSQTGQCECRANVQGQRCDKCKAGTFGlQSARGC 964
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. |
918-964 |
4.60e-12 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 62.76 E-value: 4.60e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1677500969 918 CRCNAGGSFSEVCHSQTGQCECRANVQGQRCDKCKAGTFGLQ--SARGC 964
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPsdPPQGC 49
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1676-2140 |
5.24e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 71.72 E-value: 5.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1676 KS-LGEFIKELARDAeaVNEKAIKLNETLGTRDEAFERNLEGLQKEIDQMIKEL--------RRKNLETQKEIAEDELVA 1746
Cdd:COG4717 36 KStLLAFIRAMLLER--LEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEeeyaelqeELEELEEELEELEAELEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1747 AEALLKKVKKLfgESRGENEEMEKDLREKLADYknkvDDAWDLLREATDKIREAnrlfavnqknMTALEKKKEAVESGKR 1826
Cdd:COG4717 114 LREELEKLEKL--LQLLPLYQELEALEAELAEL----PERLEELEERLEELREL----------EEELEELEAELAELQE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1827 QIEN--------TLKEGNDILDEANRLADEINSIIDYVEDIQTKLppmsEELNDKIDDLSQEIKDRKLAEKVSQAESHAA 1898
Cdd:COG4717 178 ELEElleqlslaTEEELQDLAEELEELQQRLAELEEELEEAQEEL----EELEEELEQLENELEAAALEERLKEARLLLL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1899 QLNdSSAVLDGILDEAKNISFNATAAF---------------KAYSNIKDYIDEAEKVAKEaKDLAHEATKLATGPRGLL 1963
Cdd:COG4717 254 IAA-ALLALLGLGGSLLSLILTIAGVLflvlgllallflllaREKASLGKEAEELQALPAL-EELEEEELEELLAALGLP 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1964 KEDAKGCLQKSFRILNEAKKLANDVKENEDHLnglktRIENADARNGDLLRTLNdtlgklsaipndtAAKLQAVKDKARQ 2043
Cdd:COG4717 332 PDLSPEELLELLDRIEELQELLREAEELEEEL-----QLEELEQEIAALLAEAG-------------VEDEEELRAALEQ 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2044 ANDtAKDVLAQITELHQNLDGLKKNYNKLADsvaktnavvkdpsknkiiadaDATVKNLEQEADRLIDKLKPIKELEDNL 2123
Cdd:COG4717 394 AEE-YQELKEELEELEEQLEELLGELEELLE---------------------ALDEEELEEELEELEEELEELEEELEEL 451
|
490
....*....|....*..
gi 1677500969 2124 KKNISEIKELINQARKQ 2140
Cdd:COG4717 452 REELAELEAELEQLEED 468
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
966-1012 |
9.25e-12 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 61.99 E-value: 9.25e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1677500969 966 PCNCNSFGSKSFDCE-ESGQCWCQPGVTGKKCDRCAHGYFNF--QEGGCT 1012
Cdd:cd00055 1 PCDCNGHGSLSGQCDpGTGQCECKPNTTGRRCDRCAPGYYGLpsQGGGCQ 50
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1711-2207 |
1.15e-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: 71.24 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1711 ERNLEGL--QKEIDQMIKELRRKNLETQKEIAEDELVAAEALLKKVKklfgESRGENEEMEKDLREKLADYKNKVDDAWD 1788
Cdd:TIGR02168 199 ERQLKSLerQAEKAERYKELKAELRELELALLVLRLEELREELEELQ----EELKEAEEELEELTAELQELEEKLEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1789 LLREATDKIREAN-RLFAVNQKnMTALEKKKEAVESGKRQIENTLKEGNDILDEANRLADEinsiidyvedIQTKLppms 1867
Cdd:TIGR02168 275 EVSELEEEIEELQkELYALANE-ISRLEQQKQILRERLANLERQLEELEAQLEELESKLDE----------LAEEL---- 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1868 EELNDKIDDLSQEIKDrkLAEKVsqaeshaaqlndssavldgildeaknisfnataafkaysnikdyiDEAEKVAKEAKD 1947
Cdd:TIGR02168 340 AELEEKLEELKEELES--LEAEL---------------------------------------------EELEAELEELES 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1948 LAHEATKLATGPRgllkedakgclQKSFRILNEAKKLANDVKENEDHLNGLKTRIENADARNGDLLRTLndtlgklsaip 2027
Cdd:TIGR02168 373 RLEELEEQLETLR-----------SKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL----------- 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2028 ndtaaklqavkdkarqandtakdVLAQITELHQNLDGLKKNYNKLADSVAKTNAVVKdpSKNKIIADADATVKNLEQEAD 2107
Cdd:TIGR02168 431 -----------------------EEAELKELQAELEELEEELEELQEELERLEEALE--ELREELEEAEQALDAAERELA 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2108 RLIDKLKPIKELEDNLKKNISEIKELINQARKQANSI-----KVSVSSGgdcirtYKPEIKK---GSYNNIVVNVKTAVA 2179
Cdd:TIGR02168 486 QLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILgvlseLISVDEG------YEAAIEAalgGRLQAVVVENLNAAK 559
|
490 500
....*....|....*....|....*...
gi 1677500969 2180 DNllfylgsakfIDFLAiEMRKGKVSFL 2207
Cdd:TIGR02168 560 KA----------IAFLK-QNELGRVTFL 576
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1813-2148 |
1.21e-11 |
|
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: 70.87 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1813 ALEKKKEAVESGKRQIENTLKEGNDILDEANRLADEINSIIDYVEDIQTKLPPMSEELNDKIDDLSQEIKDRK-----LA 1887
Cdd:TIGR02169 685 GLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKselkeLE 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1888 EKVSQAESHAAQLNDSSAVLDGILDEaknisfnataafkaySNIKDYIDEAEKVAKEAKDL--AHEATKLATGPRGLLKE 1965
Cdd:TIGR02169 765 ARIEELEEDLHKLEEALNDLEARLSH---------------SRIPEIQAELSKLEEEVSRIeaRLREIEQKLNRLTLEKE 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1966 DAKGCLQKSFRILNEAKKLANDVKENEDHLNG----LKTRIENADARngdlLRTLNDTLGKLSAIPNDTAAKLQAVKDKA 2041
Cdd:TIGR02169 830 YLEKEIQELQEQRIDLKEQIKSIEKEIENLNGkkeeLEEELEELEAA----LRDLESRLGDLKKERDELEAQLRELERKI 905
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2042 RQAN---DTAKDVLAQITELHQNLDGLKKNYNKLadsvakTNAVVKDPSKNKIIADADATVKNLE--------------Q 2104
Cdd:TIGR02169 906 EELEaqiEKKRKRLSELKAKLEALEEELSEIEDP------KGEDEEIPEEELSLEDVQAELQRVEeeiralepvnmlaiQ 979
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1677500969 2105 EADRLIDKLKPIKELEDNLKKNISEIKELINQARKQANSIKVSV 2148
Cdd:TIGR02169 980 EYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREVFMEA 1023
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1639-2143 |
1.52e-11 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 71.02 E-value: 1.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1639 NLNTLVTEMNELLTRATKVTADGEQTGQ-----DAERTNTRAKSLGEFIKELARDAEAVNEKAIKLNETLGTRDEafern 1713
Cdd:PTZ00440 1549 NILNIKDEIETILNKAQDLMRDISKISKivenkNLENLNDKEADYVKYLDNILKEKQLMEAEYKKLNEIYSDVDN----- 1623
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1714 legLQKEIDQMIKELRRKNLETQKEIAEDelvaaeallkkvKKLFGESRGE--------------NEEMEK-DLREKLAD 1778
Cdd:PTZ00440 1624 ---IEKELKKHKKNYEIGLLEKVIEINKN------------IKLYMDSTKEslnslvnnfsslfnNFYLNKyNINENLEK 1688
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1779 YKNKVDDAWDLLREATDKIREANRLFAVNQKNMTALEKKKEAVESGKRQIENTLKEGNDILDEANRlaDEINSIIDYVED 1858
Cdd:PTZ00440 1689 YKKKLNEIYNEFMESYNIIQEKMKEVSNDDVDYNEAKTLREEAQKEEVNLNNKEEEAKKYLNDIKK--QESFRFILYMKE 1766
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1859 IQTKLPPMSEELNDKIDD-------LSQEIK----DRKLAEKVSQAE---------SHAAQLNDSSAVLDGILDEAKNIS 1918
Cdd:PTZ00440 1767 KLDELSKMCKQQYNIVDEgynyikkKIEYIKtlndENNLSDSLNQAEdknkevanlTHYTNKNEAKNLLGHVVKSANFIG 1846
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1919 FNATAAFkAYSNIKDyiDEAEKVAKEAKDLAHEATKLATGPRGLLK------EDAKGCLQKSFRIL-------------N 1979
Cdd:PTZ00440 1847 IKIMTGL-QPTELTP--DASLETAPELTFESENNSDLELDHLSSNKneldvyKNIQDAYKSSLQILkysddidkkqrdcN 1923
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1980 EAKKLANDVKENEDHLNGLKTRIENADARNGDLLRTLNDTLGKLSAI--------------PNDTAAKLQAVKDKARQAN 2045
Cdd:PTZ00440 1924 KLVEDGNEIYLKSTAINELKNMINSVKNKESAISNKIDNVSNKLSELnkitcndesydeilEKEEYEELKDLRNSFNQEK 2003
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2046 D-TAKDVlaQITELHQNLDGLKKNYNKLADSVAKTNA------VVKDpsKNKIIADADATVKNLEQEA-------DRLID 2111
Cdd:PTZ00440 2004 AeTLNNL--KLNKIKEDFNSYKNLLDELEKSVKTLKAsenikkIVEN--KKTSIDAINTNIEDIEKEIesinpslDELLK 2079
|
570 580 590
....*....|....*....|....*....|....*..
gi 1677500969 2112 KLKPIK-----ELEDNLKKNISEIKELINQARKQANS 2143
Cdd:PTZ00440 2080 KGHKIEisrytSIIDNVQTKISNDSKNINDIEKKAQI 2116
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1680-2168 |
2.55e-11 |
|
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: 70.00 E-value: 2.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1680 EFIKElardaEAVNEKAIKLNETLGTRDEAFERNLEGLQKEIDQMIKELRRKNLETQKEIAEDELvaaeaLLKKVKKLFG 1759
Cdd:pfam02463 167 LKRKK-----KEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYL-----LYLDYLKLNE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1760 ESRGENEEMEKDLREKLADYKNKVDDAWDLLREATDKIREANRLFAVNQKNMTALEKKKEAVESGKRQIENTLKEGNDIL 1839
Cdd:pfam02463 237 ERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1840 DEAN----RLADEINSIIDYVEDIQTKLppmseelndkiddLSQEIKDRKLAEKVSQAEshaAQLNDSSAVLDGILDEAK 1915
Cdd:pfam02463 317 KESEkekkKAEKELKKEKEEIEELEKEL-------------KELEIKREAEEEEEEELE---KLQEKLEQLEEELLAKKK 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1916 NISFNATAAFKAYSNIKDYIDEAEKVAKEAKDLAHEatklatgprglLKEDAKGCLQKSFRILNEAKKL-------ANDV 1988
Cdd:pfam02463 381 LESERLSSAAKLKEEELELKSEEEKEAQLLLELARQ-----------LEDLLKEEKKEELEILEEEEESielkqgkLTEE 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1989 KENEDHLNGLKTRIENADARNGDLLRTLNDTLGKLSAIPNDTAAKLQAVKDKARQANDTAKDVLAQITEL----HQNLDG 2064
Cdd:pfam02463 450 KEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGvggrIISAHG 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2065 LKKNYN--KLADSVAKTNAVVKDPSKNKIIADADATVKNLEQEADRLIDKLKPIKELEDNLKKNIS--EIKELINQARKQ 2140
Cdd:pfam02463 530 RLGDLGvaVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAvlEIDPILNLAQLD 609
|
490 500
....*....|....*....|....*...
gi 1677500969 2141 ANSIKVSVSSGGDCIRTYKPEIKKGSYN 2168
Cdd:pfam02463 610 KATLEADEDDKRAKVVEGILKDTELTKL 637
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1630-2181 |
4.22e-11 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 69.48 E-value: 4.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1630 ERLIQLAEGNLNTLVTEMNELLTRaTKVTADGEQTGQDAERTNtrakSLGEFIKE---LARDAEAVNEKAIKLNETLGTR 1706
Cdd:PTZ00440 601 EELINEALFNKEKFINEKNDLQEK-VKYILNKFYKGDLQELLD----ELSHFLDDhkyLYHEAKSKEDLQTLLNTSKNEY 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1707 DEAFERNLEglqkEIDQMIKELRR--KNLETQKEiaedelvaaeallKKVKKLFgesrgenEEMEKDLREKLADYKNKVD 1784
Cdd:PTZ00440 676 EKLEFMKSD----NIDNIIKNLKKelQNLLSLKE-------------NIIKKQL-------NNIEQDISNSLNQYTIKYN 731
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1785 DawdlLREATDKIREANRLFAVNQKNMtalEKKKEAVESGKRQIENTLKEGNDILDE-----------ANRLADEINSII 1853
Cdd:PTZ00440 732 D----LKSSIEEYKEEEEKLEVYKHQI---INRKNEFILHLYENDKDLPDGKNTYEEflqykdtilnkENKISNDINILK 804
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1854 DYVEDIQT----------KLPPMSEELNDKIDDLSQEIKDRKLAEKVSQAEShaaQLNDSSAVLDGILDEAKNISFNaTA 1923
Cdd:PTZ00440 805 ENKKNNQDllnsyniliqKLEAHTEKNDEELKQLLQKFPTEDENLNLKELEK---EFNENNQIVDNIIKDIENMNKN-IN 880
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1924 AFKAYSNIKDYIDEAEKVakeakdLAHEATKlatgprgllKEDAKGCLQKSFRILNEAKKLANDVKEN-EDHLNGLKTRI 2002
Cdd:PTZ00440 881 IIKTLNIAINRSNSNKQL------VEHLLNN---------KIDLKNKLEQHMKIINTDNIIQKNEKLNlLNNLNKEKEKI 945
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2003 EN--ADARNGDLLRTLNDTLGKLSAIPNDTAAKLQAVKDKARQANDTAKDVlaqitelHQNLDGLKKNYNKLAdsvAKTN 2080
Cdd:PTZ00440 946 EKqlSDTKINNLKMQIEKTLEYYDKSKENINGNDGTHLEKLDKEKDEWEHF-------KSEIDKLNVNYNILN---KKID 1015
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2081 AVVKDPsKNKIIADADATVKNLEQEADRLIDKLkpIKELEDnLKKNISEIKELINQARKQANSIKVSVSSGGDCIRTYKP 2160
Cdd:PTZ00440 1016 DLIKKQ-HDDIIELIDKLIKEKGKEIEEKVDQY--ISLLEK-MKTKLSSFHFNIDIKKYKNPKIKEEIKLLEEKVEALLK 1091
|
570 580
....*....|....*....|.
gi 1677500969 2161 EIKKGsyNNIVVNVKTAVADN 2181
Cdd:PTZ00440 1092 KIDEN--KNKLIEIKNKSHEH 1110
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1713-2168 |
4.82e-11 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 69.31 E-value: 4.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1713 NLEGLQKEIDQMIKELrrKNLETQKEIAEDELVAAEALLKKV--KKLFGESRGENEEMEKDLREKLADYKNKVDDAWDLL 1790
Cdd:TIGR01612 1119 DIKNLDQKIDHHIKAL--EEIKKKSENYIDEIKAQINDLEDVadKAISNDDPEEIEKKIENIVTKIDKKKNIYDEIKKLL 1196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1791 REATdKIreanrlfavnQKNMTALEKKK---------------EAVESGKRQIENTLKEGN---DILDEANRLADEINSI 1852
Cdd:TIGR01612 1197 NEIA-EI----------EKDKTSLEEVKginlsygknlgklflEKIDEEKKKSEHMIKAMEayiEDLDEIKEKSPEIENE 1265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1853 IDYVEDIQTKLPPM-------------SEELNDKIDDLSQE-------------IKDRK--LAEKVSQAESHAAQLNDSS 1904
Cdd:TIGR01612 1266 MGIEMDIKAEMETFnishdddkdhhiiSKKHDENISDIREKslkiiedfseesdINDIKkeLQKNLLDAQKHNSDINLYL 1345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1905 AVLDGI-----LDEAKNIsFNATAAF-----KAYSNIKDYIDEAEKVAKEAKDLAHEATKLATGPRGLLKEDAKGCLQK- 1973
Cdd:TIGR01612 1346 NEIANIynilkLNKIKKI-IDEVKEYtkeieENNKNIKDELDKSEKLIKKIKDDINLEECKSKIESTLDDKDIDECIKKi 1424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1974 ---SFRILNEAKKLAN---DVKENEDHLNGLKTRIENADARNGDLLRT-----LNDTLGKLSAIPN--DTAAKLQAVKDK 2040
Cdd:TIGR01612 1425 kelKNHILSEESNIDTyfkNADENNENVLLLFKNIEMADNKSQHILKIkkdnaTNDHDFNINELKEhiDKSKGCKDEADK 1504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2041 ARQANDTAKDVLAQ----ITELhqnldgLKKNY-----NKLADSVAKTNAVVKD--PSKNKIIADADAT------VKN-- 2101
Cdd:TIGR01612 1505 NAKAIEKNKELFEQykkdVTEL------LNKYSalaikNKFAKTKKDSEIIIKEikDAHKKFILEAEKSeqkikeIKKek 1578
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1677500969 2102 --LEQEADR-------LIDKLKPIKELEDNLKKnISEIKELINQARKQANSIKVSVSSGGdcIRTYKPEIKKGSYN 2168
Cdd:TIGR01612 1579 frIEDDAAKndksnkaAIDIQLSLENFENKFLK-ISDIKKKINDCLKETESIEKKISSFS--IDSQDTELKENGDN 1651
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1669-2145 |
6.00e-11 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 68.92 E-value: 6.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1669 ERTNTRAKSLGEFIKELARDAEAVNEKAIKL--------NETLGTRDEAFERNleGLQKEIDQMIKELRRKNLETQKEIa 1740
Cdd:TIGR01612 547 KESYELAKNWKKLIHEIKKELEEENEDSIHLekeikdlfDKYLEIDDEIIYIN--KLKLELKEKIKNISDKNEYIKKAI- 623
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1741 edelvaaeallkKVKKLFGESRGENEEMEKDLREKLADYKNKVDDAWDLLREATDKIREA------NRLFAVNQKN---- 1810
Cdd:TIGR01612 624 ------------DLKKIIENNNAYIDELAKISPYQVPEHLKNKDKIYSTIKSELSKIYEDdidalyNELSSIVKENaidn 691
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1811 ---MTALEKKK---------------EAVESGKRQIENTLKEGNDILDEANR-----LADEINSIidyVEDIQTKlppmS 1867
Cdd:TIGR01612 692 tedKAKLDDLKskidkeydkiqnmetATVELHLSNIENKKNELLDIIVEIKKhihgeINKDLNKI---LEDFKNK----E 764
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1868 EELNDKIDDLSQEiKDR--KLAEKVSQAESHaaqLNDSSAVlDGILDE------------AKNISFNATAAFKAYSNIKD 1933
Cdd:TIGR01612 765 KELSNKINDYAKE-KDElnKYKSKISEIKNH---YNDQINI-DNIKDEdakqnydkskeyIKTISIKEDEIFKIINEMKF 839
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1934 YIDEA----------EKVAKEAKDLAHEA-TKLATGPRGLLKEDAKGCLQKSFrilNEAKKLAND----VKENEDHLNGL 1998
Cdd:TIGR01612 840 MKDDFlnkvdkfinfENNCKEKIDSEHEQfAELTNKIKAEISDDKLNDYEKKF---NDSKSLINEinksIEEEYQNINTL 916
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1999 KT-------------RIENADARNGDLLRTLN---DTLGKLSAIPNDTAAKLQ-AVKDKARQANDTAKDVL-----AQIT 2056
Cdd:TIGR01612 917 KKvdeyikicentkeSIEKFHNKQNILKEILNkniDTIKESNLIEKSYKDKFDnTLIDKINELDKAFKDASlndyeAKNN 996
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2057 ELHQNLDGLKKNYNKLADSVAKTNAVVKDPSKNKI---IADADATVKNLEQEADRLIDKLkpIKELEDNLKKNI----SE 2129
Cdd:TIGR01612 997 ELIKYFNDLKANLGKNKENMLYHQFDEKEKATNDIeqkIEDANKNIPNIEIAIHTSIYNI--IDEIEKEIGKNIellnKE 1074
|
570
....*....|....*.
gi 1677500969 2130 IKELINQARKQANSIK 2145
Cdd:TIGR01612 1075 ILEEAEINITNFNEIK 1090
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1614-1806 |
6.00e-11 |
|
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: 65.33 E-value: 6.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1614 NMTQELKHLLSPQRAPERLIQLAEgNLNTLVTEMNELLTRATKVTADgeqtgqdAERTNTRAKSLGEFIKELARDAEAVN 1693
Cdd:COG1579 1 AMPEDLRALLDLQELDSELDRLEH-RLKELPAELAELEDELAALEAR-------LEAAKTELEDLEKEIKRLELEIEEVE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1694 EKAIKLNETLGT----RD-EAFERNLEGLQKEIDQM---IKEL--RRKNLETQKEIAEDELVAAEALLKKVKKLFGESRG 1763
Cdd:COG1579 73 ARIKKYEEQLGNvrnnKEyEALQKEIESLKRRISDLedeILELmeRIEELEEELAELEAELAELEAELEEKKAELDEELA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1677500969 1764 ENEEMEKDLREKLADYKNKVDDawDLLReATDKIREANRLFAV 1806
Cdd:COG1579 153 ELEAELEELEAEREELAAKIPP--ELLA-LYERIRKRKNGLAV 192
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
864-916 |
6.10e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 59.68 E-value: 6.10e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1677500969 864 PCQCNDNldFSIPGSCDSLSGSCLiCKPGTTGRYCELCADGYFGDAVDAKNCQ 916
Cdd:cd00055 1 PCDCNGH--GSLSGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
967-1014 |
9.06e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 59.29 E-value: 9.06e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1677500969 967 CNCNSFGSKSFDCE-ESGQCWCQPGVTGKKCDRCAHGYFNFQEGGCTAC 1014
Cdd:pfam00053 1 CDCNPHGSLSDTCDpETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1684-2140 |
1.16e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 67.86 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1684 ELARDAEAVNE-KAIKLNETLGTRDEAFERNLEGLQKEIDQMIKELRRknletQKEIAEDELVAAEALLKKVKKLFGESR 1762
Cdd:PTZ00121 1221 EDAKKAEAVKKaEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARR-----QAAIKAEEARKADELKKAEEKKKADEA 1295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1763 GENEEMEK-DLREKLADYKNKVDDAWDLLREA-------TDKIREANRLFAVNQKNMTALEKKKEAVESGKRQIENTLKE 1834
Cdd:PTZ00121 1296 KKAEEKKKaDEAKKKAEEAKKADEAKKKAEEAkkkadaaKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEE 1375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1835 GNDILDEANRLADEINSiidyVEDIQTKlppmSEELNDKIDDLSQEIKDRKLAEkvsQAESHAAQLNDSsavldgilDEA 1914
Cdd:PTZ00121 1376 AKKKADAAKKKAEEKKK----ADEAKKK----AEEDKKKADELKKAAAAKKKAD---EAKKKAEEKKKA--------DEA 1436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1915 KNisfNATAAFKAysnikdyiDEAEKVAKEAKDlAHEATKLAtgprgllkEDAKGClqksfrilNEAKKLANDVKENEDh 1994
Cdd:PTZ00121 1437 KK---KAEEAKKA--------DEAKKKAEEAKK-AEEAKKKA--------EEAKKA--------DEAKKKAEEAKKADE- 1487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1995 lngLKTRIENADaRNGDLLRTLNDTLGKLsaipnDTAAKLQAVK--DKARQANDTAKDVLAQITELHQNLDGLKKnynkl 2072
Cdd:PTZ00121 1488 ---AKKKAEEAK-KKADEAKKAAEAKKKA-----DEAKKAEEAKkaDEAKKAEEAKKADEAKKAEEKKKADELKK----- 1553
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1677500969 2073 ADSVAKTNAVVKDPSKNKiiADADATVKNLEQEADRLIDKlkpiKELEDNLKKNISEIKELINQARKQ 2140
Cdd:PTZ00121 1554 AEELKKAEEKKKAEEAKK--AEEDKNMALRKAEEAKKAEE----ARIEEVMKLYEEEKKMKAEEAKKA 1615
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1712-1902 |
1.30e-10 |
|
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: 64.18 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1712 RNLEGLQkEIDQMIKELRRKNLETQKEIA--EDELVAAEALLKKVKKLFgesrgeneemeKDLREKLADYKNKVDDAWDL 1789
Cdd:COG1579 7 RALLDLQ-ELDSELDRLEHRLKELPAELAelEDELAALEARLEAAKTEL-----------EDLEKEIKRLELEIEEVEAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1790 LREATDKIREANrlfavNQKNMTALEKKKEAVESGKRQIENTLKEGNDILDEANRLADEINSIIDYVEdiqtklppmsEE 1869
Cdd:COG1579 75 IKKYEEQLGNVR-----NNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELE----------AE 139
|
170 180 190
....*....|....*....|....*....|....*
gi 1677500969 1870 LNDKIDDLSQEIK--DRKLAEKVSQAESHAAQLND 1902
Cdd:COG1579 140 LEEKKAELDEELAelEAELEELEAEREELAAKIPP 174
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1420-1466 |
1.68e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 58.52 E-value: 1.68e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1420 CQCNGHSSL---CDPETSICQnCQHHTAGDFCERCALGYYGIVKGLPNDC 1466
Cdd:pfam00053 1 CDCNPHGSLsdtCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
756-805 |
1.81e-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: 1.81e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1677500969 756 PCQCFGHA---ESCDDVTGECLnCKDHTGGPYCDKCLPGFYGEPTKGtsEDCQ 805
Cdd:cd00055 1 PCDCNGHGslsGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQG--GGCQ 50
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1682-2149 |
1.98e-10 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 66.85 E-value: 1.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1682 IKELARDAEAVNEKAIKLNETLgtrdeafeRNLEGLQKEIDQMIKELRRknLETQKEIAEDELVAAEALLKKVKKLfges 1761
Cdd:PRK01156 220 IERLSIEYNNAMDDYNNLKSAL--------NELSSLEDMKNRYESEIKT--AESDLSMELEKNNYYKELEERHMKI---- 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1762 rgENEEMEKDlREKLADYKNKVDDAWDL------LREATDKIREANRLFAVNQKNMTALEKKKE---------------- 1819
Cdd:PRK01156 286 --INDPVYKN-RNYINDYFKYKNDIENKkqilsnIDAEINKYHAIIKKLSVLQKDYNDYIKKKSryddlnnqilelegye 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1820 --------AVESGKRQIENTLKEGNDILDEANRL-------ADEINSIIdyvEDIQTKLppmsEELNDKIDDLSQEIkdR 1884
Cdd:PRK01156 363 mdynsylkSIESLKKKIEEYSKNIERMSAFISEIlkiqeidPDAIKKEL---NEINVKL----QDISSKVSSLNQRI--R 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1885 KLAEKVSQAESHAAQLNDSSA--VLDGILDEAKnisfnataafkaySN--IKDYIDEAEKVAKEAKDLAHEATKLATGPR 1960
Cdd:PRK01156 434 ALRENLDELSRNMEMLNGQSVcpVCGTTLGEEK-------------SNhiINHYNEKKSRLEEKIREIEIEVKDIDEKIV 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1961 GLLKED---AKGCLQKSFRILNEAKKLANDVKENEDHLNGLK---TRIENADARN-----GDLLRTLNDTLGKLSAIPND 2029
Cdd:PRK01156 501 DLKKRKeylESEEINKSINEYNKIESARADLEDIKIKINELKdkhDKYEEIKNRYkslklEDLDSKRTSWLNALAVISLI 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2030 TAAKLQAVKD-KARQANDTAKDVLAQITELHQNLDGLKKNYNKLADSVAKTNAVVKDPSKNKIIADA-DATVKNLEQEad 2107
Cdd:PRK01156 581 DIETNRSRSNeIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKlRGKIDNYKKQ-- 658
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1677500969 2108 rlIDKLKPIKELEDNLKKNISEIKELINQARKQANSIKVSVS 2149
Cdd:PRK01156 659 --IAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRA 698
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1060-1108 |
2.00e-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: 2.00e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1677500969 1060 CNCSTVGSLDFQCNVNTGQCNCHPKFSGAKCTECSRGHWNYPRCNLCDC 1108
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1782-2145 |
2.03e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 67.01 E-value: 2.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1782 KVDDAWDLLREATDKIRE-ANRLFAVN---------QKNMTALEKKKEAVESGKRQI------ENTLKEGNDILDEANRL 1845
Cdd:PRK03918 98 KYLDGSEVLEEGDSSVREwVERLIPYHvflnaiyirQGEIDAILESDESREKVVRQIlglddyENAYKNLGEVIKEIKRR 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1846 ADEINSIIDYVEDIQTKLPPMSEELNDKIDDLSQ-EIKDRKLAEKVSQAESHAAQLNDSSAVLDGILDEAKNISFNATAA 1924
Cdd:PRK03918 178 IERLEKFIKRTENIEELIKEKEKELEEVLREINEiSSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKL 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1925 FKAYSNIKDYIDEAEKVAKEAKDLAHEATKlatgprglLKEDAkgclqKSFRILNEAKKLANDVKEN--------EDHLN 1996
Cdd:PRK03918 258 EEKIRELEERIEELKKEIEELEEKVKELKE--------LKEKA-----EEYIKLSEFYEEYLDELREiekrlsrlEEEIN 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1997 GLKTRI---ENADARNGDLLRTLNDTLGKLSAI----------------------------PNDTAAKLQAVKDKARQAN 2045
Cdd:PRK03918 325 GIEERIkelEEKEERLEELKKKLKELEKRLEELeerhelyeeakakkeelerlkkrltgltPEKLEKELEELEKAKEEIE 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2046 DTAKDVLAQITELHQNLDGLKKNYNKLADSVAK---TNAVVKDPSKNKIIADADATVKNLEQEADRLIDKLKPIKELEDN 2122
Cdd:PRK03918 405 EEISKITARIGELKKEIKELKKAIEELKKAKGKcpvCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRE 484
|
410 420
....*....|....*....|...
gi 1677500969 2123 LKKNISEIKELINQaRKQANSIK 2145
Cdd:PRK03918 485 LEKVLKKESELIKL-KELAEQLK 506
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1740-2112 |
3.25e-10 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 65.63 E-value: 3.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1740 AEDELVAAEALLKKVKKLFGESRgenEEMeKDLREKLADYKNKVDDAWDLLREATDKIREANRLFAVNQKnmtALEKKKE 1819
Cdd:PRK04778 103 AKHEINEIESLLDLIEEDIEQIL---EEL-QELLESEEKNREEVEQLKDLYRELRKSLLANRFSFGPALD---ELEKQLE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1820 AVESGKRQIENTLKEGN-----DILDEANRLADEINSIID----YVEDIQTKLPPMSEELNDKIDDLSQE---IKDRKLA 1887
Cdd:PRK04778 176 NLEEEFSQFVELTESGDyvearEILDQLEEELAALEQIMEeipeLLKELQTELPDQLQELKAGYRELVEEgyhLDHLDIE 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1888 EKVSQAESHAAQLNDSSAVLDgiLDEAKNIsfNAtaafkaysNIKDYID------EAE-----KVAKEAKDLAHEATKLA 1956
Cdd:PRK04778 256 KEIQDLKEQIDENLALLEELD--LDEAEEK--NE--------EIQERIDqlydilEREvkarkYVEKNSDTLPDFLEHAK 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1957 TGPRGLLKEDAKgcLQKSFRI----LNEAKKLANDVKENEDHLNGLKTRIENADARNGDLLRTLNDTLGKLSAIPN---D 2029
Cdd:PRK04778 324 EQNKELKEEIDR--VKQSYTLneseLESVRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKeqeK 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2030 TAAKLQAVKDKARQANDTAKDVLAQITELH-----QNLDGLKKNY-NKLADSVAKTNAVVKDPSKNKI--------IADA 2095
Cdd:PRK04778 402 LSEMLQGLRKDELEAREKLERYRNKLHEIKrylekSNLPGLPEDYlEMFFEVSDEIEALAEELEEKPInmeavnrlLEEA 481
|
410
....*....|....*..
gi 1677500969 2096 DATVKNLEQEADRLIDK 2112
Cdd:PRK04778 482 TEDVETLEEETEELVEN 498
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1527-1574 |
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 1677500969 1527 CECDPYGSLPVPCDPVTGFCTCRPGATGRKCDGCKHWHAREGWECVFC 1574
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGC 49
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1680-2064 |
3.72e-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: 66.24 E-value: 3.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1680 EFIKELARDAEAVNEKAIKLNEtLGTRDEAFER----------NLEGLQKEIDQMIK--ELRRK--------------NL 1733
Cdd:TIGR02169 157 KIIDEIAGVAEFDRKKEKALEE-LEEVEENIERldliidekrqQLERLRREREKAERyqALLKEkreyegyellkekeAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1734 ETQKEIAEDELVAAEALLKKVKKLFGESRGENEEMEKDLREkladyknkvddawdllreatdkirEANRLFAVNQKNMTA 1813
Cdd:TIGR02169 236 ERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEE------------------------LNKKIKDLGEEEQLR 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1814 LEKKKEAVESGKRQIENTLKEGNDILDEA-NRLAD---EINSIIDYVEDIQTKLppmsEELNDKIDDLSQEIKDRK--LA 1887
Cdd:TIGR02169 292 VKEKIGELEAEIASLERSIAEKERELEDAeERLAKleaEIDKLLAEIEELEREI----EEERKRRDKLTEEYAELKeeLE 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1888 EKVSQAEShaaqlndssavldgiLDEAKNISFNATAAFKaySNIKDYIDEAEKVAKEAKDLAHEATKLaTGPRGLLKEDA 1967
Cdd:TIGR02169 368 DLRAELEE---------------VDKEFAETRDELKDYR--EKLEKLKREINELKRELDRLQEELQRL-SEELADLNAAI 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1968 KGCLQKSFRILNEAKKLANDVKENEDHLNGLKTRIENADARNGDLLRTLNDTLGKLSaipnDTAAKLQAVKDKARQANDT 2047
Cdd:TIGR02169 430 AGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELS----KLQRELAEAEAQARASEER 505
|
410
....*....|....*..
gi 1677500969 2048 AKDVLAQITELHQNLDG 2064
Cdd:TIGR02169 506 VRGGRAVEEVLKASIQG 522
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1680-2176 |
3.80e-10 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 66.39 E-value: 3.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1680 EFIKELARDAEAVNEKAIKLNETLGTRDEAFERNLEG---------------------LQKEIDQMIKELRRKNL----- 1733
Cdd:PTZ00440 952 TKINNLKMQIEKTLEYYDKSKENINGNDGTHLEKLDKekdewehfkseidklnvnyniLNKKIDDLIKKQHDDIIelidk 1031
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1734 ---ETQKEIAE--DELVAA-EALLKKVKKLFGESRGEN-------EEMeKDLREKLADYKNKVDDAWDLLREATDKIREa 1800
Cdd:PTZ00440 1032 likEKGKEIEEkvDQYISLlEKMKTKLSSFHFNIDIKKyknpkikEEI-KLLEEKVEALLKKIDENKNKLIEIKNKSHE- 1109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1801 NRLFAVNQKNMTA--LEKKKEAVESGKRQIENTLKEGNDILDEANRLaDEINSI-IDY----VEDIQTKlppMSEElNDK 1873
Cdd:PTZ00440 1110 HVVNADKEKNKQTehYNKKKKSLEKIYKQMEKTLKELENMNLEDITL-NEVNEIeIEYerilIDHIVEQ---INNE-AKK 1184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1874 IDDLSQEIKDRKlaEKVSQAEshaaqlNDSSAVLDGILDEaknisFNATAAFKAYSNIKDYIDEAEKVAKEAKDLAHEAT 1953
Cdd:PTZ00440 1185 SKTIMEEIESYK--KDIDQVK------KNMSKERNDHLTT-----FEYNAYYDKATASYENIEELTTEAKGLKGEANRST 1251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1954 KLATGPRglLKEDAKGCLQKSFRILNEAKKLANDVKENEDHLNGLKTR-----IENADARNGDLLRTLNDTLGKLSAIPN 2028
Cdd:PTZ00440 1252 NVDELKE--IKLQVFSYLQQVIKENNKMENALHEIKNMYEFLISIDSEkilkeILNSTKKAEEFSNDAKKELEKTDNLIK 1329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2029 DTAAKLQAVKDKARQANDTAKDvlAQITELHQNLDGLKKNYNKLADSVaktNAVVKDPSKNKiiADADATVKNLEQEADr 2108
Cdd:PTZ00440 1330 QVEAKIEQAKEHKNKIYGSLED--KQIDDEIKKIEQIKEEISNKRKEI---NKYLSNIKSNK--EKCDLHVRNASRGKD- 1401
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1677500969 2109 LIDKLKPIKELEDNLKK--NISEIKELINQARK---QANSIKVSVSSGGDCIRTYKPEIKKGSYNNIVVNVKT 2176
Cdd:PTZ00440 1402 KIDFLNKHEAIEPSNSKevNIIKITDNINKCKQysnEAMETENKADENNDSIIKYEKEITNILNNSSILGKKT 1474
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1612-1883 |
4.73e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.85 E-value: 4.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1612 LENMTQELKHLLSPQRAPERLIQLAEGNLNTLVTEMNELLTRATK-------VTADGEQTGQDAERTNTRAKSLGEFIKE 1684
Cdd:TIGR02168 728 ISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEaeeelaeAEAEIEELEAQIEQLKEELKALREALDE 807
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1685 LARDAEAVNEKAIKLNETLG---TRDEAFERNLEGLQKEIDQMIKEL-----RRKNLETQKEIAEDELVAAEALLKKVKK 1756
Cdd:TIGR02168 808 LRAELTLLNEEAANLRERLEsleRRIAATERRLEDLEEQIEELSEDIeslaaEIEELEELIEELESELEALLNERASLEE 887
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1757 LFGESRGENEEMEKDLREkladYKNKVDDAWDLLREATDKIREANRlfAVNQKNMTALEKKKEAVESGKRQIENTLKEGN 1836
Cdd:TIGR02168 888 ALALLRSELEELSEELRE----LESKRSELRRELEELREKLAQLEL--RLEGLEVRIDNLQERLSEEYSLTLEEAEALEN 961
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1677500969 1837 DILDEANRLADEINSI---IDYVEDIQtklpPMS----EELNDKIDDLSQEIKD 1883
Cdd:TIGR02168 962 KIEDDEEEARRRLKRLenkIKELGPVN----LAAieeyEELKERYDFLTAQKED 1011
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1717-2148 |
4.88e-10 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 65.36 E-value: 4.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1717 LQKEIDQMIKELRRKNLETQKEIAEDELVAAEALLKK------VKKLFGESRGENEEMEK---DLREKLaDYKNKVDDAw 1787
Cdd:COG5185 2 VQRSKFLQVKNPLAKEGNANKELIEILLESSKSEGKTlvfitiLFFPLGISRDSLRVTLRsviNVLDGL-NYQNDVKKS- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1788 DLLREATDKIREANRLFAVNQK---------NMTALEKKKEAVESGKRQIENTLKEGNDILDEANRLADEINSIIDyVE- 1857
Cdd:COG5185 80 ESSVKARKFLKEKKLDTKILQEyvnsliklpNYEWSADILISLLYLYKSEIVALKDELIKVEKLDEIADIEASYGE-VEt 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1858 ----DIQTKLPPMSEELNDKIDDLSQEIKDRK--LAEKVSQAESHAAQLNDSSA---VLDGILDEAKNISFNATAAFKAY 1928
Cdd:COG5185 159 giikDIFGKLTQELNQNLKKLEIFGLTLGLLKgiSELKKAEPSGTVNSIKESETgnlGSESTLLEKAKEIINIEEALKGF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1929 SNIKDYIDEAEKVAKEAKDLAHEATKLATGPRGLLKEDAKGclqksfriLNEAKKlaNDVKENEDHLNGLKTRIENADAR 2008
Cdd:COG5185 239 QDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKR--------LNENAN--NLIKQFENTKEKIAEYTKSIDIK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2009 NgdLLRTLNDTLgklsaipndtaAKLQAVKDKARQANDTAKDVLAQITELHQNLDGLKKNYNKLadsVAKTNAVVKDPSK 2088
Cdd:COG5185 309 K--ATESLEEQL-----------AAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAI---KEEIENIVGEVEL 372
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1677500969 2089 NKIIADADATVKNLEQEADRLIDKLKPIKE--------LEDNLKKNISEIKELINQARKQANSIKVSV 2148
Cdd:COG5185 373 SKSSEELDSFKDTIESTKESLDEIPQNQRGyaqeilatLEDTLKAADRQIEELQRQIEQATSSNEEVS 440
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1612-1889 |
4.92e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 65.86 E-value: 4.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1612 LENMTQELKHLLSPQRAPERLiqlaegnLNTLVTEMNELLTRATKVTADGEQTGQDAERTNTRAKSLGEFIKELARDAEA 1691
Cdd:TIGR02169 683 LEGLKRELSSLQSELRRIENR-------LDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIEN 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1692 VNEKAIKLNETLGTRDE---AFERNLEGL------------QKEIDQMIKELRR------------KNLETQKEIAEDE- 1743
Cdd:TIGR02169 756 VKSELKELEARIEELEEdlhKLEEALNDLearlshsripeiQAELSKLEEEVSRiearlreieqklNRLTLEKEYLEKEi 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1744 --LVAAEALLKKVKKLFG----ESRGENEEME----------KDLREKLADYKNKVDDAWDLLREATDKIREANRLFAVN 1807
Cdd:TIGR02169 836 qeLQEQRIDLKEQIKSIEkeieNLNGKKEELEeeleeleaalRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKK 915
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1808 QKNMTALEKKKEAVESGKRQIENTLKEGNDILDEANRLAD------EINSIIDYVEDIQTKLPPMSEELNDKIDDLsQEI 1881
Cdd:TIGR02169 916 RKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDvqaelqRVEEEIRALEPVNMLAIQEYEEVLKRLDEL-KEK 994
|
....*...
gi 1677500969 1882 KDRKLAEK 1889
Cdd:TIGR02169 995 RAKLEEER 1002
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1630-1913 |
5.01e-10 |
|
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: 65.43 E-value: 5.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1630 ERLIQLAEGNLNTLVTEMNELLTRATKVTADGEQTGQDAERTNTRAKSLGEFIKELARDAEAVNEKAIKLNETLGTRdea 1709
Cdd:TIGR04523 460 DNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEK--- 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1710 fERNLEGLQKEIDQMIKELRRKNLET-----QKEIAEDELvAAEALLKKVKKLfgESRGENEEMEK-DLREKLADYKNKV 1783
Cdd:TIGR04523 537 -ESKISDLEDELNKDDFELKKENLEKeidekNKEIEELKQ-TQKSLKKKQEEK--QELIDQKEKEKkDLIKEIEEKEKKI 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1784 ddaWDLLREATdKIREANRLFAVNQKNmtaLEKKKEAVESGKRQIENTLKE----GNDILDEANRLADEINSIIDYVEDI 1859
Cdd:TIGR04523 613 ---SSLEKELE-KAKKENEKLSSIIKN---IKSKKNKLKQEVKQIKETIKEirnkWPEIIKKIKESKTKIDDIIELMKDW 685
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1677500969 1860 QTKLppmSEELNDKIDDLSQEIKDRKLAEKVSQAESHAAQLNDSSAVLDGILDE 1913
Cdd:TIGR04523 686 LKEL---SLHYKKYITRMIRIKDLPKLEEKYKEIEKELKKLDEFSKELENIIKN 736
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1527-1570 |
5.09e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.94 E-value: 5.09e-10
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1677500969 1527 CECDPYGSLPVPCDPVTGFCTCRPGATGRKCDGCKHWHAREGWE 1570
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPP 44
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1419-1467 |
6.96e-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: 6.96e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1677500969 1419 PCQCNGHSSL---CDPETSICQnCQHHTAGDFCERCALGYYGIVKGlPNDCQ 1467
Cdd:cd00055 1 PCDCNGHGSLsgqCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQ-GGGCQ 50
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1861-2164 |
7.15e-10 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 63.01 E-value: 7.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1861 TKLPPMSEELNDKIDDLSQEIKD--RKLAEKVSQAESHAAQLNDSSAVLDGILDEAKNI-----SFNAtaafkaysNIKD 1933
Cdd:COG1340 4 DELSSSLEELEEKIEELREEIEElkEKRDELNEELKELAEKRDELNAQVKELREEAQELrekrdELNE--------KVKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1934 YIDEAEKVAKEAKDLAHEATKLatgprgllkedakgclqksFRILNEAKKLANDVKENEDHLNGLKTRIENADArNGDLL 2013
Cdd:COG1340 76 LKEERDELNEKLNELREELDEL-------------------RKELAELNKAGGSIDKLRKEIERLEWRQQTEVL-SPEEE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2014 RTLNDTLGKLsaipndtAAKLQAVKdKARQANDTAKDVLAQITELHQNLDGLKKNYNKLADSVAKTnavvkdpsKNKIIa 2093
Cdd:COG1340 136 KELVEKIKEL-------EKELEKAK-KALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQEL--------HEEMI- 198
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1677500969 2094 dadatvkNLEQEADRLIDKLKPIKELEDNLKKNISEIKELINQARKQANSIKVSVSSggdcIRTYKPEIKK 2164
Cdd:COG1340 199 -------ELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKK----LRKKQRALKR 258
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1059-1101 |
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
....*....|....*....|....*....|....*....|...
gi 1677500969 1059 ACNCSTVGSLDFQCNVNTGQCNCHPKFSGAKCTECSRGHWNYP 1101
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1106-1163 |
8.76e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 56.59 E-value: 8.76e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1677500969 1106 CDCFLPGTDATTCDSETkkcscsdqtGQCTCKVNVEGIHCDRCRPGKFGLDAKNPLGC 1163
Cdd:pfam00053 1 CDCNPHGSLSDTCDPET---------GQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1637-2170 |
9.24e-10 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 65.07 E-value: 9.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1637 EGNLNTLVTEMNELLTRATKVTAD--GE---QTGQDAERTNTRAKSLGEFIKELARDAEAVNEKAIKLNETlgtrdeafe 1711
Cdd:TIGR01612 721 ELHLSNIENKKNELLDIIVEIKKHihGEinkDLNKILEDFKNKEKELSNKINDYAKEKDELNKYKSKISEI--------- 791
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1712 RNLEGLQKEIDQMIKELRRKNLETQKE------IAEDELVAA--------EALLKKVKKL--FGESRGEN--------EE 1767
Cdd:TIGR01612 792 KNHYNDQINIDNIKDEDAKQNYDKSKEyiktisIKEDEIFKIinemkfmkDDFLNKVDKFinFENNCKEKidseheqfAE 871
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1768 MEKDLR-----EKLADYKNKVDDAWDLLREATDKIREA----NRLFAVNQKnMTALEKKKEAVESGKRQiENTLKEgndI 1838
Cdd:TIGR01612 872 LTNKIKaeisdDKLNDYEKKFNDSKSLINEINKSIEEEyqniNTLKKVDEY-IKICENTKESIEKFHNK-QNILKE---I 946
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1839 LDEANRLADEINSIIDYVEDiqtklpPMSEELNDKIDDLSQEIKDRKLAEKVSQAESHAAQLNDSSAVLDGILDEAKNIS 1918
Cdd:TIGR01612 947 LNKNIDTIKESNLIEKSYKD------KFDNTLIDKINELDKAFKDASLNDYEAKNNELIKYFNDLKANLGKNKENMLYHQ 1020
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1919 FNATAafKAYSNIKDYIDEAEKVAKEAKDLAHeaTKLATgprglLKEDAKGCLQKSFRILNeaKKLANDVKENEDHLNGL 1998
Cdd:TIGR01612 1021 FDEKE--KATNDIEQKIEDANKNIPNIEIAIH--TSIYN-----IIDEIEKEIGKNIELLN--KEILEEAEINITNFNEI 1089
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1999 KTRienadarngdlLRTLN-DTLGKLSAIpnDTAAKLQAVKDKARQANDTAKDVLAQITELHQN----LDGLKKNYNKLA 2073
Cdd:TIGR01612 1090 KEK-----------LKHYNfDDFGKEENI--KYADEINKIKDDIKNLDQKIDHHIKALEEIKKKsenyIDEIKAQINDLE 1156
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2074 DSVAKTnavvkdpsknkiIADADatVKNLEQEADRLIDKLKPIKELEDNLKKNISEIKElINQARKQANSIK-VSVSSGG 2152
Cdd:TIGR01612 1157 DVADKA------------ISNDD--PEEIEKKIENIVTKIDKKKNIYDEIKKLLNEIAE-IEKDKTSLEEVKgINLSYGK 1221
|
570 580
....*....|....*....|.
gi 1677500969 2153 DCIRTYKPEI---KKGSYNNI 2170
Cdd:TIGR01612 1222 NLGKLFLEKIdeeKKKSEHMI 1242
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1682-1905 |
1.10e-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: 63.24 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1682 IKELARDAEAVNEKAIKLNETLgTRDEAFERNLEGLQKEIDQMIKELRRKNLETQKEIAEdelvaAEALLKKVKKLFGES 1761
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKEL-AALKKEEKALLKQLAALERRIAALARRIRALEQELAA-----LEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1762 RGENEEMEKDLREKL-ADYKNKVDDAWDLL---REATDKIREANRLFAVN---QKNMTALEKKKEAVESGKRQIENTLKE 1834
Cdd:COG4942 96 RAELEAQKEELAELLrALYRLGRQPPLALLlspEDFLDAVRRLQYLKYLAparREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1677500969 1835 GNDILDEANRLADEINSIIDYVEDIQTKLPPMSEELNDKIDDLSQEIKD-RKLAEKVSQAESHAAQLNDSSA 1905
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEElEALIARLEAEAAAAAERTPAAG 247
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1612-2140 |
1.24e-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: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1612 LENMTQElKHLLSpQRAPERLIQLAEGNLNTLVTEMN------ELLTRATKVTADGEQTGQDAER--------------- 1670
Cdd:TIGR00606 328 LEKLNKE-RRLLN-QEKTELLVEQGRLQLQADRHQEHirardsLIQSLATRLELDGFERGPFSERqiknfhtlvierqed 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1671 -TNTRAKSLGEFIKELARDAEAVNEKAIK---LNETLGTRDEAFERNLEGLQKEIDQM------IKELRRKNLETQKEIA 1740
Cdd:TIGR00606 406 eAKTAAQLCADLQSKERLKQEQADEIRDEkkgLGRTIELKKEILEKKQEELKFVIKELqqlegsSDRILELDQELRKAER 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1741 E----DELVAAEALLKKVKKLFGES-------RGENEEMEKDLREKLADYKnkvddawdLLREATDKIREANRLFAVNQK 1809
Cdd:TIGR00606 486 ElskaEKNSLTETLKKEVKSLQNEKadldrklRKLDQEMEQLNHHTTTRTQ--------MEMLTKDKMDKDEQIRKIKSR 557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1810 -------------NMTALEKKKEAVESGKRQIENTLKEGNDILDEANRLADEINSIIDYVEDIQTKLppmSEELNDKIDD 1876
Cdd:TIGR00606 558 hsdeltsllgyfpNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSY---EDKLFDVCGS 634
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1877 LSQEIKDRKLAEKVSQAESHAAQLNDSSAVLDGILDEAKNISFNATAA----FKAYSNIKDYI-----------DEAEKV 1941
Cdd:TIGR00606 635 QDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVcqrvFQTEAELQEFIsdlqsklrlapDKLKST 714
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1942 AKEAKDLAHEATK---LATGPRGLLKEDAKGC--LQKSFRILN-EAKKLANDVKENEDHLNGLKTRIENADARNGD--LL 2013
Cdd:TIGR00606 715 ESELKKKEKRRDEmlgLAPGRQSIIDLKEKEIpeLRNKLQKVNrDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDvtIM 794
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2014 RTLNDTLGKLSAIPNDTAAKLQAVkdkarqandtakDVLAQITELHQNLDGLKKNYNKLADSVAKTNAVVKDpsKNKIIA 2093
Cdd:TIGR00606 795 ERFQMELKDVERKIAQQAAKLQGS------------DLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQD--QQEQIQ 860
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2094 DADATVKNLEQEADRLIDKLKPIKELEDNLKKNISEIKEL---INQARKQ 2140
Cdd:TIGR00606 861 HLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLireIKDAKEQ 910
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1106-1163 |
2.19e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 55.40 E-value: 2.19e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1677500969 1106 CDCFLPGTDATTCDSETkkcscsdqtGQCTCKVNVEGIHCDRCRPGKFGldaKNPLGC 1163
Cdd:smart00180 1 CDCDPGGSASGTCDPDT---------GQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1014-1057 |
2.36e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 55.01 E-value: 2.36e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1677500969 1014 CECS---HLGNNCDPKTGRCICPPNTIGEKCSKCAPNTWGHSiTTGC 1057
Cdd:smart00180 1 CDCDpggSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG-PPGC 46
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1647-2153 |
2.49e-09 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 63.70 E-value: 2.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1647 MNELLT--RATKVTADGEQTGQDAERTNTRAKslGEFIKElARDAEAVNEKAIKLNETLGTRDEAFE--------RNLEG 1716
Cdd:PTZ00440 1287 MYEFLIsiDSEKILKEILNSTKKAEEFSNDAK--KELEKT-DNLIKQVEAKIEQAKEHKNKIYGSLEdkqiddeiKKIEQ 1363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1717 LQKEIDQMIKELRR--KNLETQKEIAEDELVAAE------ALLKKvKKLFGESRGENEEMEKdLREKLADYKNKVDDAWD 1788
Cdd:PTZ00440 1364 IKEEISNKRKEINKylSNIKSNKEKCDLHVRNASrgkdkiDFLNK-HEAIEPSNSKEVNIIK-ITDNINKCKQYSNEAME 1441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1789 LlreaTDKIREANRLFAVNQKNMTALEKKKEAVESGKRqIENTLKEGNDILDEANrladEINSIIdyvediQTKLPPMSE 1868
Cdd:PTZ00440 1442 T----ENKADENNDSIIKYEKEITNILNNSSILGKKTK-LEKKKKEATNIMDDIN----GEHSII------KTKLTKSSE 1506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1869 ELND-----KIDDLSQEIKDRKLAEKVSQAESHAAQLNDSSAVLDGILDEAKNISFNATAAFKAYSNIK----------- 1932
Cdd:PTZ00440 1507 KLNQlneqpNIKREGDVLNNDKSTIAYETIQYNLGRVKHNLLNILNIKDEIETILNKAQDLMRDISKISkivenknlenl 1586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1933 -----DYIDEAEKVAKEAKDLAHEATKL------ATGPRGLLKEDAK----GCLQKSFRILNEAKKLANDVKEN-EDHLN 1996
Cdd:PTZ00440 1587 ndkeaDYVKYLDNILKEKQLMEAEYKKLneiysdVDNIEKELKKHKKnyeiGLLEKVIEINKNIKLYMDSTKESlNSLVN 1666
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1997 GLKTRIENADARNGDLLRTLNDTLGKLSAIPNDTAAKLQAVKDKARQANDTAKDvLAQITELHQNLdglKKNYNKLADSV 2076
Cdd:PTZ00440 1667 NFSSLFNNFYLNKYNINENLEKYKKKLNEIYNEFMESYNIIQEKMKEVSNDDVD-YNEAKTLREEA---QKEEVNLNNKE 1742
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1677500969 2077 AKTNAVVKDpsknkiiadadatVKNleQEADRLIDKlkpIKELEDNLKKNISEIKELINQARKQANSIKVSVSSGGD 2153
Cdd:PTZ00440 1743 EEAKKYLND-------------IKK--QESFRFILY---MKEKLDELSKMCKQQYNIVDEGYNYIKKKIEYIKTLND 1801
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1106-1163 |
2.66e-09 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 55.05 E-value: 2.66e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1677500969 1106 CDCFLPGTDATTCDSETkkcscsdqtGQCTCKVNVEGIHCDRCRPGKFGlDAKNPLGC 1163
Cdd:cd00055 2 CDCNGHGSLSGQCDPGT---------GQCECKPNTTGRRCDRCAPGYYG-LPSQGGGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1013-1058 |
2.69e-09 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 55.05 E-value: 2.69e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1013 ACECSHLG---NNCDPKTGRCICPPNTIGEKCSKCAPNTWGH-SITTGCK 1058
Cdd:cd00055 1 PCDCNGHGslsGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLpSQGGGCQ 50
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1612-1888 |
2.69e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.16 E-value: 2.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1612 LENMTQELKHLLSPQRAPERLIQLAEgnlntlvtEMNELLTRATKVTA-DGEQTGQDAERTNTRAKSLGEFIKELARDAE 1690
Cdd:PRK03918 478 LRKELRELEKVLKKESELIKLKELAE--------QLKELEEKLKKYNLeELEKKAEEYEKLKEKLIKLKGEIKSLKKELE 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1691 AVNE---KAIKLNETLGTRDE---AFERNLEGL----QKEIDQMIKELR------------RKNLETQKE---IAEDELV 1745
Cdd:PRK03918 550 KLEElkkKLAELEKKLDELEEelaELLKELEELgfesVEELEERLKELEpfyneylelkdaEKELEREEKelkKLEEELD 629
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1746 AAEALLKKVKKLFGESRGENEEMEKDLREKlaDYKNKvddawdllreaTDKIREANRLFAvnqknmtALEKKKEAVESGK 1825
Cdd:PRK03918 630 KAFEELAETEKRLEELRKELEELEKKYSEE--EYEEL-----------REEYLELSRELA-------GLRAELEELEKRR 689
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1677500969 1826 RQIENTLKEGNDILDEANRLADEInsiidyvEDIQTKLPPMsEELNDKIDDLSQEIKDRKLAE 1888
Cdd:PRK03918 690 EEIKKTLEKLKEELEEREKAKKEL-------EKLEKALERV-EELREKVKKYKALLKERALSK 744
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1612-2135 |
3.52e-09 |
|
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: 62.89 E-value: 3.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1612 LENMTQELKhllsPQRAPERLIQLAEGNlNTLVTEMNELLTRATkvtadgEQTGQDAERTNtRAKSLGEfikeLARDAEA 1691
Cdd:pfam01576 124 LEKVTTEAK----IKKLEEDILLLEDQN-SKLSKERKLLEERIS------EFTSNLAEEEE-KAKSLSK----LKNKHEA 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1692 VN---EKAIKLNETLGTRDEAFERNLEG-----------LQKEIDQMIKELRRKNLETQKEIA--EDELVAAEALLKKVK 1755
Cdd:pfam01576 188 MIsdlEERLKKEEKGRQELEKAKRKLEGestdlqeqiaeLQAQIAELRAQLAKKEEELQAALArlEEETAQKNNALKKIR 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1756 KLFGE-------------SRGENEEMEKDLREKLADYKNKVDDAWD-----------------LLREATD---KIREAnR 1802
Cdd:pfam01576 268 ELEAQiselqedleseraARNKAEKQRRDLGEELEALKTELEDTLDttaaqqelrskreqevtELKKALEeetRSHEA-Q 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1803 LFAVNQKNMTALEKKKEAVESGKRQIENTLKEGNDILDEANRLADEINSIIDYVEDIQT---KLPPMSEELNDKIDDlsQ 1879
Cdd:pfam01576 347 LQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHkrkKLEGQLQELQARLSE--S 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1880 EIKDRKLAEKVSQAEShaaQLNDSSAVLDGIldEAKNISFNataafkaysniKDyIDEAEKVAKEAKDLAHEAT--KLAT 1957
Cdd:pfam01576 425 ERQRAELAEKLSKLQS---ELESVSSLLNEA--EGKNIKLS-----------KD-VSSLESQLQDTQELLQEETrqKLNL 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1958 GPRGLLKEDAKGCLQKSFRILNEAKK-LANDVKENEDHLNGLKTRIENaDARNGDLL-----RTLNDTLGKLSAIPNDTA 2031
Cdd:pfam01576 488 STRLRQLEDERNSLQEQLEEEEEAKRnVERQLSTLQAQLSDMKKKLEE-DAGTLEALeegkkRLQRELEALTQQLEEKAA 566
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2032 A--KLQAVKDKARQANDtakDVLAQITELHQNLDGLKKNYNKLADSVAKTNAVVKDPSKNKIIADADATVK-----NLEQ 2104
Cdd:pfam01576 567 AydKLEKTKNRLQQELD---DLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKetralSLAR 643
|
570 580 590
....*....|....*....|....*....|.
gi 1677500969 2105 EADRLIDKlkpIKELEDNLKKNISEIKELIN 2135
Cdd:pfam01576 644 ALEEALEA---KEELERTNKQLRAEMEDLVS 671
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1717-2145 |
4.19e-09 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 62.18 E-value: 4.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1717 LQKEIDQMIKELrrknlETQKEIAEDELVAAEalLKKVKKL--FGESRGENEEMEKDLRE----KLADYKNKVDDAwdll 1790
Cdd:pfam06160 4 LRKKIYKEIDEL-----EERKNELMNLPVQEE--LSKVKKLnlTGETQEKFEEWRKKWDDivtkSLPDIEELLFEA---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1791 REATDKIReanrLFAVNQKnMTALEKKKEAVESgkrQIENTLKEGNDILDEANRLADEINSIIDYVEDIQTKL------- 1863
Cdd:pfam06160 73 EELNDKYR----FKKAKKA-LDEIEELLDDIEE---DIKQILEELDELLESEEKNREEVEELKDKYRELRKTLlanrfsy 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1864 PPMSEELNDKIDDLSQEIkdrklaekvsqaeSHAAQLNDSSAVLD--GILDEAKNisfnATAAFKAY-SNIKDYIDEAEK 1940
Cdd:pfam06160 145 GPAIDELEKQLAEIEEEF-------------SQFEELTESGDYLEarEVLEKLEE----ETDALEELmEDIPPLYEELKT 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1941 VAKEAKDlaheatKLATGPRGLLKEdakGCLQKSFRILNEAKKLANDVKENEDHLNglKTRIENADARNGDL---LRTLN 2017
Cdd:pfam06160 208 ELPDQLE------ELKEGYREMEEE---GYALEHLNVDKEIQQLEEQLEENLALLE--NLELDEAEEALEEIeerIDQLY 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2018 DTLGKLSAIPNDTAAKLQAVKDKARQANDTAKDVLAQITELHQN--LD----GLKKNYNKLADSVAKTNAVVKdpsknKI 2091
Cdd:pfam06160 277 DLLEKEVDAKKYVEKNLPEIEDYLEHAEEQNKELKEELERVQQSytLNenelERVRGLEKQLEELEKRYDEIV-----ER 351
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1677500969 2092 IADADATVKNLEQEADRLIDKLKPIKELEDNLKKNISEIKELINQARKQANSIK 2145
Cdd:pfam06160 352 LEEKEVAYSELQEELEEILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFK 405
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1712-2080 |
4.63e-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: 62.39 E-value: 4.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1712 RNLEGLQKEIDQMIKELRRknletqkeiAEDELVAAEALLKKVKKLFGESRGENEEMEKD---LREKLADYKNKVDdawD 1788
Cdd:TIGR02169 681 ERLEGLKRELSSLQSELRR---------IENRLDELSQELSDASRKIGEIEKEIEQLEQEeekLKERLEELEEDLS---S 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1789 LLREATDKIREANRLFAVNQKNMTALEKKKEAVESGKRQI-ENTLKEGNDILDEANRLADEINSIIDYVEDIQTKLPPMS 1867
Cdd:TIGR02169 749 LEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLsHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEK 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1868 EELNDKIDDLSQEIKDRKLAEKVSQAESHAaqLNDSSAVLDGILDEAKNisfnataafkaysNIKDYIDEAEKVAKEAKD 1947
Cdd:TIGR02169 829 EYLEKEIQELQEQRIDLKEQIKSIEKEIEN--LNGKKEELEEELEELEA-------------ALRDLESRLGDLKKERDE 893
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1948 laheatklatgprgllkedakgcLQKSFRILNEAK-KLANDVKENEDHLNGLKTRIENADARngdlLRTLNDTLGKLSAI 2026
Cdd:TIGR02169 894 -----------------------LEAQLRELERKIeELEAQIEKKRKRLSELKAKLEALEEE----LSEIEDPKGEDEEI 946
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1677500969 2027 PNDTAA--KLQAVKDKARQA-------NDTA----KDVLAQITELHQNLDGLKKNYNKLADSVAKTN 2080
Cdd:TIGR02169 947 PEEELSleDVQAELQRVEEEiralepvNMLAiqeyEEVLKRLDELKEKRAKLEEERKAILERIEEYE 1013
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1698-2123 |
4.65e-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: 62.01 E-value: 4.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1698 KLNETLGtRDEAFE-------RNLEGLQKEIDQMIKELRRknLETQKEiaeDELVAAEALLKKVkklfGESRGENEEMEK 1770
Cdd:pfam05622 39 KLQERLD-QLESGDdsgtpggKKYLLLQKQLEQLQEENFR--LETARD---DYRIKCEELEKEV----LELQHRNEELTS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1771 dlrekLADYKNKVDDAWDLLREATDKIreanrlfavnqknmtaleKKKEA-VESGKRQIE--NTLKEGNDILDEANrlAD 1847
Cdd:pfam05622 109 -----LAEEAQALKDEMDILRESSDKV------------------KKLEAtVETYKKKLEdlGDLRRQVKLLEERN--AE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1848 EINSIIDY--------------------VEDIQTKLppmSEE-------------LNDKIDDLSQEiKDRKLAEKVSQAE 1894
Cdd:pfam05622 164 YMQRTLQLeeelkkanalrgqletykrqVQELHGKL---SEEskkadklefeykkLEEKLEALQKE-KERLIIERDTLRE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1895 S----HAAQLNDSSAVLDGILDEAKNISFNATAAFKAYSNIKDYID--EAE-KVAKEAKDlAHEATKLATGPRGLlkEDA 1967
Cdd:pfam05622 240 TneelRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIrlQHEnKMLRLGQE-GSYRERLTELQQLL--EDA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1968 kgclQKSFRILNEAKKLAND-VKENEDHLNGLKTRIENADARNGD---LLRTLNDTLGKLSAIpNDTAAKLQAVKDKARQ 2043
Cdd:pfam05622 317 ----NRRKNELETQNRLANQrILELQQQVEELQKALQEQGSKAEDsslLKQKLEEHLEKLHEA-QSELQKKKEQIEELEP 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2044 ANDTAKDVlaQITELHQNLDglKKNY-NKLADS-----VAKTNAVVK--DPSKNKIIADADATVKNLEQEADRLID---- 2111
Cdd:pfam05622 392 KQDSNLAQ--KIDELQEALR--KKDEdMKAMEErykkyVEKAKSVIKtlDPKQNPASPPEIQALKNQLLEKDKKIEhler 467
|
490
....*....|....*
gi 1677500969 2112 ---KLKPIKELEDNL 2123
Cdd:pfam05622 468 dfeKSKLQREQEEKL 482
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1014-1057 |
6.32e-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: 6.32e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1677500969 1014 CECSHLG---NNCDPKTGRCICPPNTIGEKCSKCAPNTWGHSITTGC 1057
Cdd:pfam00053 1 CDCNPHGslsDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQ 47
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1648-2148 |
6.56e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 62.08 E-value: 6.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1648 NELLTRATKVTADGEQTGQDAERTNTRAKSLGEFIKELARDAEAVNEKAiklnETLGTRDEAFERNLEGLQKEIDQMIK- 1726
Cdd:PTZ00121 1318 DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKA----EAAEKKKEEAKKKADAAKKKAEEKKKa 1393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1727 -ELRRKNLETQKEiaEDELVAAEALLKKVKklfgESRGENEEMEK-DLREKLADYKNKVDDAwdllREATDKIREANRLF 1804
Cdd:PTZ00121 1394 dEAKKKAEEDKKK--ADELKKAAAAKKKAD----EAKKKAEEKKKaDEAKKKAEEAKKADEA----KKKAEEAKKAEEAK 1463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1805 AVNQKNMTALEKKKEAVEsgKRQIENTLKEGndilDEANRLADEINSiidyvediqtklppmSEELNDKIDDLSQEIKDR 1884
Cdd:PTZ00121 1464 KKAEEAKKADEAKKKAEE--AKKADEAKKKA----EEAKKKADEAKK---------------AAEAKKKADEAKKAEEAK 1522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1885 KlAEKVSQAES--HAAQLNDSSAVLDGilDEAKNISFNATAAFKAYSNIKDYIDEAEKVAKEAKDLAHEATKLATGPRGL 1962
Cdd:PTZ00121 1523 K-ADEAKKAEEakKADEAKKAEEKKKA--DELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMK 1599
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1963 LKEDAKGCLQKSFRILNEAKKLANDVKENEDHLNGLK--TRIENADARNGDLLRTLNDTLGKLSAipnDTAAKLQAVKDK 2040
Cdd:PTZ00121 1600 LYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEqlKKKEAEEKKKAEELKKAEEENKIKAA---EEAKKAEEDKKK 1676
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2041 ARQANDTAKD------VLAQITELHQNLDGLKKnynKLADSVAKTNAVVKDPSKNKIIADadaTVKNLEQEADRLIDKLK 2114
Cdd:PTZ00121 1677 AEEAKKAEEDekkaaeALKKEAEEAKKAEELKK---KEAEEKKKAEELKKAEEENKIKAE---EAKKEAEEDKKKAEEAK 1750
|
490 500 510
....*....|....*....|....*....|....
gi 1677500969 2115 pikeLEDNLKKNISEIKELINQARKQANSIKVSV 2148
Cdd:PTZ00121 1751 ----KDEEEKKKIAHLKKEEEKKAEEIRKEKEAV 1780
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1612-1876 |
8.10e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 61.57 E-value: 8.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1612 LENMTQELKHLLSpqrAPERLIQLAEGNLNTLVTEM----NELLTrATKVTADGEQTGQDAER----TNTRAKSLGEFIK 1683
Cdd:TIGR04523 459 LDNTRESLETQLK---VLSRSINKIKQNLEQKQKELkskeKELKK-LNEEKKELEEKVKDLTKkissLKEKIEKLESEKK 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1684 ELARDAEAVNEKAIKLNETLgTRDEaFERNLEGLQKEIDQM---IKELRRKNLETQKEIAE---------DELVAAEALL 1751
Cdd:TIGR04523 535 EKESKISDLEDELNKDDFEL-KKEN-LEKEIDEKNKEIEELkqtQKSLKKKQEEKQELIDQkekekkdliKEIEEKEKKI 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1752 KKVKKLFGESRGENEEME---KDLREKladyKNKVDDAWDLLREATDKIReaNRLFAVNQKNMTALEK-----------K 1817
Cdd:TIGR04523 613 SSLEKELEKAKKENEKLSsiiKNIKSK----KNKLKQEVKQIKETIKEIR--NKWPEIIKKIKESKTKiddiielmkdwL 686
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1818 KEAVESGKRQIENTLKEGNDI-LDEANRLADEINSIIDYVEDIqtkLPPMSEELNDKIDD 1876
Cdd:TIGR04523 687 KELSLHYKKYITRMIRIKDLPkLEEKYKEIEKELKKLDEFSKE---LENIIKNFNKKFDD 743
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
865-908 |
9.21e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 53.47 E-value: 9.21e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1677500969 865 CQCNdnLDFSIPGSCDSLSGSCLiCKPGTTGRYCELCADGYFGD 908
Cdd:smart00180 1 CDCD--PGGSASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD 41
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1527-1562 |
9.26e-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: 53.51 E-value: 9.26e-09
10 20 30
....*....|....*....|....*....|....*.
gi 1677500969 1527 CECDPYGSLPVPCDPVTGFCTCRPGATGRKCDGCKH 1562
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKP 36
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1684-2052 |
1.24e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 61.31 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1684 ELARDAEAVNEKAIKLNETLGTRDEAFERNLEGLQKEIDQMIKELRRKnlETQKEIAEDELVAAEALLKKVKKLfgeSRG 1763
Cdd:PTZ00121 1567 EEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKK--AEEAKIKAEELKKAEEEKKKVEQL---KKK 1641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1764 ENEEMEKDLREKLADYKNKVDDAwDLLREATDKIREANRLFAVNQKNMTALEK-KKEAVEsgKRQIENTLKEGNDILDEA 1842
Cdd:PTZ00121 1642 EAEEKKKAEELKKAEEENKIKAA-EEAKKAEEDKKKAEEAKKAEEDEKKAAEAlKKEAEE--AKKAEELKKKEAEEKKKA 1718
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1843 NRL--ADEINSIidYVEDIQTKlppmSEELNDKIDDLSQEIKDRKLAEKVSQAESHAAQ--LNDSSAVLDGIL---DEAK 1915
Cdd:PTZ00121 1719 EELkkAEEENKI--KAEEAKKE----AEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEeiRKEKEAVIEEELdeeDEKR 1792
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1916 NISFNATA--AFKAYSNIKDYIDEAEKVAKEAKDLAHEATKLATGPRGLLKEDAKGCLQKSFRILNEAKKLAN---DVKE 1990
Cdd:PTZ00121 1793 RMEVDKKIkdIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNkeaDFNK 1872
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1677500969 1991 NEDHLNGLKTRIENADA----RNGDLLRTL--NDTLGKLSAIPNDtaaKLQAVKDKARQANDTAKDVL 2052
Cdd:PTZ00121 1873 EKDLKEDDEEEIEEADEiekiDKDDIEREIpnNNMAGKNNDIIDD---KLDKDEYIKRDAEETREEII 1937
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1612-1902 |
1.31e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 59.92 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1612 LENMTQELKHLLSPQRAPERLIQLAEGNLNTLVTEMNELLTRATKVTADGEQTGQDAERTNTRAKSLGEFIKELARDAEA 1691
Cdd:COG4372 47 LEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQD 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1692 VNEKAIKLNET-------LGTRDE---AFERNLEGLQKEIDQMIKELRR-KNLETQKEIAEDELVAAEALLKKVKKLFGE 1760
Cdd:COG4372 127 LEQQRKQLEAQiaelqseIAEREEelkELEEQLESLQEELAALEQELQAlSEAEAEQALDELLKEANRNAEKEEELAEAE 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1761 SRGENEEMEKDLREKLADYKNKVDDAWDLLREATDKIREANRLFAVNQKNMTALEKKKEAVESGKRQIENTLKEGNDILD 1840
Cdd:COG4372 207 KLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELE 286
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1677500969 1841 EANRLADEINSIIDYVEDIQTKLPPMSEE----LNDKIDDLSQEIKDRKLAEKVSQAESHAAQLND 1902
Cdd:COG4372 287 ALEEAALELKLLALLLNLAALSLIGALEDallaALLELAKKLELALAILLAELADLLQLLLVGLLD 352
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1857-2146 |
1.34e-08 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 59.31 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1857 EDIQTKLPpmseELNDKIDDLSQEIKDRKLAEKVSQaeSHAAQLNDSsaVLDGILDEAKNIS-FNATAAFKA---YSNIK 1932
Cdd:cd22656 26 EEYRKRLG----ISSDIDDKLSSDFDPLLDAYKSIK--DHCTDFKDD--TYPSIVSLAGDIYnYAQNAGGTIdsyYAEIL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1933 DYIDEA-----EKVAKEAKDLAHEATKLatgprglLKEDAKGCLQKSFRILNEAKKLANDVKENEDHLNGLKTRienada 2007
Cdd:cd22656 98 ELIDDLadatdDEELEEAKKTIKALLDD-------LLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKA------ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2008 rngdllrtLNDTLGK-LSAIPNDTAAKLQAVKDKARQAndtakdvlaQITELHQNLDGLKKNYNKLADSVAKTNAVVKDp 2086
Cdd:cd22656 165 --------LKDLLTDeGGAIARKEIKDLQKELEKLNEE---------YAAKLKAKIDELKALIADDEAKLAAALRLIAD- 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2087 sknkiIADADATVKNLEQEADRLIDKLKPIKELEDNLKKNISEIKELINQARKQANSIKV 2146
Cdd:cd22656 227 -----LTAADTDLDNLLALIGPAIPALEKLQGAWQAIATDLDSLKDLLEDDISKIPAAIL 281
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
414-471 |
1.36e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 53.13 E-value: 1.36e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1677500969 414 CHCDPIGSLNEVCVkdekharrgLAPGSCHCKTGFGGVSCDRCARGYTGYPDCKACNC 471
Cdd:pfam00053 1 CDCNPHGSLSDTCD---------PETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1694-2082 |
1.45e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.72 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1694 EKAI-KLNETlgtrdeafERNLEglqkEIDQMIKELRR--KNLETQKEIAEdelvaaeallkKVKKLfgesrgENEEMEK 1770
Cdd:COG1196 175 EEAErKLEAT--------EENLE----RLEDILGELERqlEPLERQAEKAE-----------RYREL------KEELKEL 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1771 DLREKLADYknkvddawdllREATDKIREAnrlfavnQKNMTALEKKKEAVESGKRQIENTLKEgndILDEANRLADEIN 1850
Cdd:COG1196 226 EAELLLLKL-----------RELEAELEEL-------EAELEELEAELEELEAELAELEAELEE---LRLELEELELELE 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1851 SiidyvediqtklppMSEELNDKIDDLSQEIKDRK-LAEKVSQAESHAAQLNDSSAVLDGILDEAKNisfNATAAFKAYS 1929
Cdd:COG1196 285 E--------------AQAEEYELLAELARLEQDIArLEERRRELEERLEELEEELAELEEELEELEE---ELEELEEELE 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1930 NIKDYIDEAEKVAKEAKDLAHEATKLatgpRGLLKEDAKGCLQKSFRILNEAKKLANDVKENEDHLNGLKTRIENADARn 2009
Cdd:COG1196 348 EAEEELEEAEAELAEAEEALLEAEAE----LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE- 422
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1677500969 2010 gdlLRTLNDTLGKLSAIPNDTAAKLQAVKDKARQANDTAKDVLAQITELHQNLDGLKKNYNKLADSVAKTNAV 2082
Cdd:COG1196 423 ---LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR 492
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1060-1101 |
1.69e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 52.70 E-value: 1.69e-08
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1677500969 1060 CNCSTVGSLDFQCNVNTGQCNCHPKFSGAKCTECSRGHWNYP 1101
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| DUF4795 |
pfam16043 |
Domain of unknown function (DUF4795); This family of proteins is functionally uncharacterized. ... |
1676-1842 |
1.91e-08 |
|
Domain of unknown function (DUF4795); This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 285 and 978 amino acids in length.
Pssm-ID: 464990 [Multi-domain] Cd Length: 181 Bit Score: 56.54 E-value: 1.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1676 KSLGEFIKELARDAEAVNEKAIKLNETLGTRDEaferNLEGLQKEIDQMIKElrrKNLETQKEIAEDELVAAEALLKKVk 1755
Cdd:pfam16043 10 DQLQALILDLQEELEKLSETTSELSERLQQRQK----HLEALYQQIEKLEKV---KADKEVVEEELDEKADKEALASKV- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1756 klfgeSRGENEEMEKDLREKLADYKNKVDDAWDLLREATDKIREanrlfAVNQKN-MTALEKKKEAVESGKRQIENTLKE 1834
Cdd:pfam16043 82 -----SRDQFDETLEELNQMLQELLDKLEGQEDAWKKALETLSE-----ELDTKLdRLELDPLKELLERRIKALQKLLQE 151
|
....*...
gi 1677500969 1835 GNDILDEA 1842
Cdd:pfam16043 152 GSEELDEA 159
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1612-2137 |
2.21e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.34 E-value: 2.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1612 LENMTQELKHLLSPQRAPERLIQLAEGNLNTLVTEMNELLTRATKVTADGEQTGQDAERTNTRAKSLGEFIKELARDAEA 1691
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1692 VNEKAIKLNETLGTRDEAFERnLEGLQKEIDQMIKELRRKNLETQKEIAE-----DELVAAEALLKKVKKLFGESRGENE 1766
Cdd:COG1196 328 LEEELEELEEELEELEEELEE-AEEELEEAEAELAEAEEALLEAEAELAEaeeelEELAEELLEALRAAAELAAQLEELE 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1767 EMEKDLREKLADYKNKVDDAWDLLREATDKIREANRLFAVNQKNMTALEKKKEAVESGKRQIENTLKEGNDILDEANRLA 1846
Cdd:COG1196 407 EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1847 DEINSIIDYVEDIQTKLPPMSE---------ELNDKIDDLSQEIKDRKLAEKVSQAESHAAQLN----DSSAVLDGILDE 1913
Cdd:COG1196 487 AEAAARLLLLLEAEADYEGFLEgvkaalllaGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNivveDDEVAAAAIEYL 566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1914 AKNisFNATAAFKAYSNIKDYIDEAEKVAKEAKDLAheatklatgpRGLLKEDAKGCLQKSFRILN-------EAKKLAN 1986
Cdd:COG1196 567 KAA--KAGRATFLPLDKIRARAALAAALARGAIGAA----------VDLVASDLREADARYYVLGDtllgrtlVAARLEA 634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1987 DVKENEDHLNGLKTRIENADARNGDLLRTLNDTLGKLSAIPNDTAAKLQAVKDKARQANDTAKDVLAQITELHQNLDGLK 2066
Cdd:COG1196 635 ALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEE 714
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1677500969 2067 KNYNKLADSVAKTNAVVKDpsKNKIIADADATVKNLEQEADRLIDKLKPIKELEDNLKKNISEIKEL--INQA 2137
Cdd:COG1196 715 ERLEEELEEEALEEQLEAE--REELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALgpVNLL 785
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1610-2141 |
2.41e-08 |
|
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: 60.06 E-value: 2.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1610 YGLENMTQELKHLLSPQRA---PERLIQLAEGNLNTLVTEM------NELLTRATKVTADGEQTGQDAERTNTRAKSLGE 1680
Cdd:TIGR00606 461 KELQQLEGSSDRILELDQElrkAERELSKAEKNSLTETLKKevkslqNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEML 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1681 FIKELARDAEAVNEKAIKLNETLGT-----RDEAFERNLEGLQKEIDQMIKELRRKNLETQK------EIAEDELVAAEA 1749
Cdd:TIGR00606 541 TKDKMDKDEQIRKIKSRHSDELTSLlgyfpNKKQLEDWLHSKSKEINQTRDRLAKLNKELASleqnknHINNELESKEEQ 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1750 LLKKVKKLFGESRGENEEMEKD-LREKL--------------ADYKNKVDDAWDL-----------------LREATDKI 1797
Cdd:TIGR00606 621 LSSYEDKLFDVCGSQDEESDLErLKEEIeksskqramlagatAVYSQFITQLTDEnqsccpvcqrvfqteaeLQEFISDL 700
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1798 REANRLFAVNQKNMTALEKKKEavesgkrqientlKEGNDILDEANRLADEINSIIDYVEDIQTKLPPMSEELNDKIDDL 1877
Cdd:TIGR00606 701 QSKLRLAPDKLKSTESELKKKE-------------KRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDI 767
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1878 SqeiKDRKLAEKVSQAESHAAQLNDSSAVLDGILDEAKNISfNATAAFKAYSNIKDYIDEAEKVAKEAKDLAHEATKLAT 1957
Cdd:TIGR00606 768 E---EQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVE-RKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVS 843
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1958 GPRGLLK--EDAKGCLQKSFRILNEAKKLANDVKEN-------EDHLNGLKTRIEN-----ADARNGDL--------LRT 2015
Cdd:TIGR00606 844 KIELNRKliQDQQEQIQHLKSKTNELKSEKLQIGTNlqrrqqfEEQLVELSTEVQSlireiKDAKEQDSpletflekDQQ 923
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2016 LNDTLGKLSAIPNDTAA-KLQAVKDKARQANDTAKDVLAQITELHQnlDGLKKNYNKLADSVAKTNAVVKDPSK-NKIIA 2093
Cdd:TIGR00606 924 EKEELISSKETSNKKAQdKVNDIKEKVKNIHGYMKDIENKIQDGKD--DYLKQKETELNTVNAQLEECEKHQEKiNEDMR 1001
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 1677500969 2094 DADATVKNLEQEADRLIDKL------KPIKELEDNLKKNISEIKELINQARKQA 2141
Cdd:TIGR00606 1002 LMRQDIDTQKIQERWLQDNLtlrkreNELKEVEEELKQHLKEMGQMQVLQMKQE 1055
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1676-2162 |
2.43e-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: 60.45 E-value: 2.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1676 KSLGEFIKELARDAEAVNEKaikLNETLGTRDEA----------FERNLEGLQKEIDQMIKELRRKNLETQKeiaeDELV 1745
Cdd:TIGR01612 927 ENTKESIEKFHNKQNILKEI---LNKNIDTIKESnlieksykdkFDNTLIDKINELDKAFKDASLNDYEAKN----NELI 999
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1746 AaeaLLKKVKKLFGESRG--------ENEEMEKDLREKLADYKNKVDDAWDLLREAT-DKIREANRLFAVNQKNM-TALE 1815
Cdd:TIGR01612 1000 K---YFNDLKANLGKNKEnmlyhqfdEKEKATNDIEQKIEDANKNIPNIEIAIHTSIyNIIDEIEKEIGKNIELLnKEIL 1076
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1816 KKKEAVESGKRQIENTLKEGN--DILDEAN-RLADEINSIIDyveDIQTklppmseeLNDKIDdlsQEIKDrkLAEKVSQ 1892
Cdd:TIGR01612 1077 EEAEINITNFNEIKEKLKHYNfdDFGKEENiKYADEINKIKD---DIKN--------LDQKID---HHIKA--LEEIKKK 1140
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1893 AESHA----AQLNDSSAVLDGIL--DEAKNISfnataafKAYSNIKDYIDEAEKVAKEAKDLAHEATKLATGPRGLlkED 1966
Cdd:TIGR01612 1141 SENYIdeikAQINDLEDVADKAIsnDDPEEIE-------KKIENIVTKIDKKKNIYDEIKKLLNEIAEIEKDKTSL--EE 1211
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1967 AKGC-------LQKSF--RILNEAKKLANDVKENEDHLNGLktrienadarngDLLRTLNDTLGKLSAIPNDTAAKLQAV 2037
Cdd:TIGR01612 1212 VKGInlsygknLGKLFleKIDEEKKKSEHMIKAMEAYIEDL------------DEIKEKSPEIENEMGIEMDIKAEMETF 1279
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2038 K---DKARQANDTAKDVLAQITEL-HQNLDGLKKNYNKladsvAKTNAVVKDPSKNkiIADADATVKNLEQEADRlIDKL 2113
Cdd:TIGR01612 1280 NishDDDKDHHIISKKHDENISDIrEKSLKIIEDFSEE-----SDINDIKKELQKN--LLDAQKHNSDINLYLNE-IANI 1351
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1677500969 2114 KPIKELeDNLKKNISEIKELINQARKQANSIKVSVSSGGDCIRTYKPEI 2162
Cdd:TIGR01612 1352 YNILKL-NKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDDI 1399
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1645-2175 |
2.60e-08 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 60.23 E-value: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1645 TEMNEL---LTRATKVTADGEQTGQDAERTNTRAKSLGEFIKELarDAEAVNEKAIKLNETLGTRDEAFERNLEGLQKE- 1720
Cdd:PTZ00440 1990 EELKDLrnsFNQEKAETLNNLKLNKIKEDFNSYKNLLDELEKSV--KTLKASENIKKIVENKKTSIDAINTNIEDIEKEi 2067
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1721 --IDQMIKELrrknLETQKEIaedELVAAEALLKKVKKLFGESRGENEEMEKDLREKLADYKNKVDDAW---DLLREATD 1795
Cdd:PTZ00440 2068 esINPSLDEL----LKKGHKI---EISRYTSIIDNVQTKISNDSKNINDIEKKAQIYLAYIKNNYNSIKkdiSTLNEYFD 2140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1796 KIREANRLFAVNQKNMTALEKKKEAVESGKRQIENTLKEGNDILDeanrlADEINSIidyvEDIQTKLPPMSEELNDK-- 1873
Cdd:PTZ00440 2141 EKQVSNYILTNIDKANKLSSELSEAVTNSEEIIENIKKEIIEINE-----NTEMNTL----ENTADKLKELYENLKKKkn 2211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1874 -IDDLSQEIKDRKLAEKVSQAESHaaqlNDSSAVLDGILD-EAKNISFNATAafkaYSNIKDYIDEAEKvakeakdlahe 1951
Cdd:PTZ00440 2212 iINNIYKKINFIKLQEIENSSEKY----NDISKLFNNVVEtQKKKLLDNKNK----INNIKDKINDKEK----------- 2272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1952 atKLATGPRGLLKEDAKGCLQKSFRILNEAKKLANDVKENEDHLNGLKTRIENADarngDLLRTLNDTLGKLSAIPNDta 2031
Cdd:PTZ00440 2273 --ELINVDSSFTLESIKTFNEIYDDIKSNIGDLYKLEDTNNDELKKVKLYIENIT----HLLNRINTLINDLDNYQDE-- 2344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2032 aklQAVKDKARQANdtaKDVLAQITELHQNLDGLKKNYNKLADSVAKTNAVVKDPSKNKIIADADATVKNLEQEadrlID 2111
Cdd:PTZ00440 2345 ---NYGKDKNIELN---NENNSYIIKTKEKINNLKEEFSKLLKNIKRNNTLCNNNNIKDFISNIGKSVETIKQR----FS 2414
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1677500969 2112 KLKPIKELEDNLKKNISEIKELINQARKQANsikVSVSSGgdcIRTYKPEIKKGSYNNIVVNVK 2175
Cdd:PTZ00440 2415 SNLPEKEKLHQIEENLNEIKNIMNETKRISN---VDAFTN---KILQDIDNEKNKENNNMNAEK 2472
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
757-797 |
3.00e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 51.97 E-value: 3.00e-08
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1677500969 757 CQCFGHA---ESCDDVTGECLnCKDHTGGPYCDKCLPGFYGEPT 797
Cdd:pfam00053 1 CDCNPHGslsDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPS 43
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
469-515 |
3.24e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 51.97 E-value: 3.24e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1677500969 469 CNCSGLGSKNE--DPCFGPCICKENVEGGDCSRCKSGFFNLQEDNWKGC 515
Cdd:pfam00053 1 CDCNPHGSLSDtcDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
865-911 |
3.28e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 51.97 E-value: 3.28e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1677500969 865 CQCNDNLdfSIPGSCDSLSGSCLiCKPGTTGRYCELCADGYFGDAVD 911
Cdd:pfam00053 1 CDCNPHG--SLSDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSD 44
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1612-2148 |
3.32e-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: 60.07 E-value: 3.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1612 LENMTQELKHLLspqRAPERLIQLAEGNLNTLVTEMNELLTRATKVTADGEQTGQDAERTNT-----RAKSLGEFIKELA 1686
Cdd:TIGR01612 1120 IKNLDQKIDHHI---KALEEIKKKSENYIDEIKAQINDLEDVADKAISNDDPEEIEKKIENIvtkidKKKNIYDEIKKLL 1196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1687 RDAEAVNEKAIKLNEtlgtrdeafernLEGLQKEIDQMIKELRRKNLETQKEIAEDELVAAEALLKKVKKLFGESRGENE 1766
Cdd:TIGR01612 1197 NEIAEIEKDKTSLEE------------VKGINLSYGKNLGKLFLEKIDEEKKKSEHMIKAMEAYIEDLDEIKEKSPEIEN 1264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1767 EM--EKDLREKL-------ADYKN------KVDDAWDLLREATDKIREAN-RLFAVN------QKNMTALEKKKEAVESG 1824
Cdd:TIGR01612 1265 EMgiEMDIKAEMetfnishDDDKDhhiiskKHDENISDIREKSLKIIEDFsEESDINdikkelQKNLLDAQKHNSDINLY 1344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1825 KRQIENTLkegnDILdEANRLADEINSIIDYVEDIQTKLPPMSEELnDKIDDLSQEIKDR-KLAEKVSQAEShaaQLNDS 1903
Cdd:TIGR01612 1345 LNEIANIY----NIL-KLNKIKKIIDEVKEYTKEIEENNKNIKDEL-DKSEKLIKKIKDDiNLEECKSKIES---TLDDK 1415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1904 SavLDGILdeaKNISFNATAAFKAYSNIKDYIDEAEKVAKEAKdlaheatklatgprgLLKEDAKGCLQKSFRILNEAKK 1983
Cdd:TIGR01612 1416 D--IDECI---KKIKELKNHILSEESNIDTYFKNADENNENVL---------------LLFKNIEMADNKSQHILKIKKD 1475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1984 LA--------NDVKENEDHLNGLKTRIE-NADA--RNGDLL----RTLNDTLGKLSAIpndtaaklqAVKDKARQANDTA 2048
Cdd:TIGR01612 1476 NAtndhdfniNELKEHIDKSKGCKDEADkNAKAieKNKELFeqykKDVTELLNKYSAL---------AIKNKFAKTKKDS 1546
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2049 KDVLAQITELH-----------QNLDGLKKNYNKLADSVAKTNavvkdpSKNKIIADADATVKNLEQEADRLIDKLKPI- 2116
Cdd:TIGR01612 1547 EIIIKEIKDAHkkfileaekseQKIKEIKKEKFRIEDDAAKND------KSNKAAIDIQLSLENFENKFLKISDIKKKIn 1620
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2117 -------------------------KELEDNL-------------KKNISEIKELINQARKQANSIKVSV 2148
Cdd:TIGR01612 1621 dclketesiekkissfsidsqdtelKENGDNLnslqefleslkdqKKNIEDKKKELDELDSEIEKIEIDV 1690
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1717-2145 |
4.81e-08 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 58.69 E-value: 4.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1717 LQKEIDQMIKELrrknlETQKEIAEDELVAAEalLKKVKKL--FGESRGENEEMEKDLRE----KLADYKNKVDDAwdll 1790
Cdd:PRK04778 23 LRKRNYKRIDEL-----EERKQELENLPVNDE--LEKVKKLnlTGQSEEKFEEWRQKWDEivtnSLPDIEEQLFEA---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1791 REATDKIReanrLFAVnQKNMTALEKKKEAVESgkrQIENTLKEGNDIL--DEANRlaDEINSIIDYVEDIQTKL----- 1863
Cdd:PRK04778 92 EELNDKFR----FRKA-KHEINEIESLLDLIEE---DIEQILEELQELLesEEKNR--EEVEQLKDLYRELRKSLlanrf 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1864 --PPMSEELNDKIDDLSQEIKD-RKLAEK--VSQAESHAAQLNDSSAVLDGILDEaknisfnataafkaysnIKDYIDEA 1938
Cdd:PRK04778 162 sfGPALDELEKQLENLEEEFSQfVELTESgdYVEAREILDQLEEELAALEQIMEE-----------------IPELLKEL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1939 EKVakeakdLAHEATKLATGPRGLLKEdakGCLQKSFRILNEAKKLANDVKENEDHLNGLKtrIENADARNGDL---LRT 2015
Cdd:PRK04778 225 QTE------LPDQLQELKAGYRELVEE---GYHLDHLDIEKEIQDLKEQIDENLALLEELD--LDEAEEKNEEIqerIDQ 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2016 LNDTLGKLSAIPNDTAAKLQAVKDKARQANDTAKDVLAQITELHQNL---DGLKKNYNKLADSVAKTNAVVKDPSKNkiI 2092
Cdd:PRK04778 294 LYDILEREVKARKYVEKNSDTLPDFLEHAKEQNKELKEEIDRVKQSYtlnESELESVRQLEKQLESLEKQYDEITER--I 371
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1677500969 2093 ADADATVKNLEQEADRLIDKLKPIKELEDNLKKNISEIKELINQARKQANSIK 2145
Cdd:PRK04778 372 AEQEIAYSELQEELEEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYR 424
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
413-465 |
7.07e-08 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 51.20 E-value: 7.07e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1677500969 413 PCHCDPIGSLNEVCVKDEkharrglapGSCHCKTGFGGVSCDRCARGYTGYPD 465
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGT---------GQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1630-1847 |
9.48e-08 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 58.30 E-value: 9.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1630 ERLIQLAEGNLNTLVTEMNElltRATKVTADGEQTG--------QDAERTNTRAKSLGEFIKELAR------------DA 1689
Cdd:NF041483 1040 DTLITEAAAEADQLTAKAQE---EALRTTTEAEAQAdtmvgaarKEAERIVAEATVEGNSLVEKARtdadellvgarrDA 1116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1690 EAVNEKAiklnETLGTRDEAfernleglqkEIDQMIKELRRKNLETQKEIAE--DELV-AAEallkkvkklfgESRGENE 1766
Cdd:NF041483 1117 TAIRERA----EELRDRITG----------EIEELHERARRESAEQMKSAGErcDALVkAAE-----------EQLAEAE 1171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1767 EMEKDLREKLADYKNK-----VDDAWDLLREATDK----IREANRLFAvnqknmTALEKKKEAVESGKRQIENTLKEGND 1837
Cdd:NF041483 1172 AKAKELVSDANSEASKvriaaVKKAEGLLKEAEQKkaelVREAEKIKA------EAEAEAKRTVEEGKRELDVLVRRRED 1245
|
250
....*....|
gi 1677500969 1838 ILDEANRLAD 1847
Cdd:NF041483 1246 INAEISRVQD 1255
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1617-2145 |
1.19e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.00 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1617 QELKHLLSPQRApERLIQLAEGNLNTLVTEMNELLTRATKVTAdgEQTGQDAERTNTRA----------KSLGEFIKELA 1686
Cdd:COG4913 275 EYLRAALRLWFA-QRRLELLEAELEELRAELARLEAELERLEA--RLDALREELDELEAqirgnggdrlEQLEREIERLE 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1687 RDAEAVNEKAIKLNE---TLGTRDEAFERNLEGLQKEIDQmikelRRKNLETQKEIAEDELVAAEALLKKVKKLFGESRG 1763
Cdd:COG4913 352 RELEERERRRARLEAllaALGLPLPASAEEFAALRAEAAA-----LLEALEEELEALEEALAEAEAALRDLRRELRELEA 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1764 ENEEMEK----------DLREKLADY-KNKVDDAW---DLL---------REA---------------TDKIREANRlfA 1805
Cdd:COG4913 427 EIASLERrksniparllALRDALAEAlGLDEAELPfvgELIevrpeeerwRGAiervlggfaltllvpPEHYAAALR--W 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1806 VNQKNMTA---LEKKKEAVESGKRQI--ENTL------KEGndilDEANRLADEINSIIDY--VEDI------------- 1859
Cdd:COG4913 505 VNRLHLRGrlvYERVRTGLPDPERPRldPDSLagkldfKPH----PFRAWLEAELGRRFDYvcVDSPeelrrhpraitra 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1860 -QTKLPPMSEELNDKIDDLSQEI----KDRKLAEKVSQAeshaAQLNDSSAVLDGILDEAKNISFNATAAFKAYSNIKDY 1934
Cdd:COG4913 581 gQVKGNGTRHEKDDRRRIRSRYVlgfdNRAKLAALEAEL----AELEEELAEAEERLEALEAELDALQERREALQRLAEY 656
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1935 IDE---AEKVAKEAKDLAHEATKLATGPRGLLKedakgcLQKsfrilnEAKKLANDVKENEDHLNGLKTRIENADARNGD 2011
Cdd:COG4913 657 SWDeidVASAEREIAELEAELERLDASSDDLAA------LEE------QLEELEAELEELEEELDELKGEIGRLEKELEQ 724
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2012 LLRTLNDTLGKLSAIPNDTAAKLQAVKDKARQANDTAKDVLAQITELHQNLDGLKKNYNKLADSVAKT----NAVVKDPS 2087
Cdd:COG4913 725 AEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAmrafNREWPAET 804
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1677500969 2088 knkiiADADATVKNLEQ--------EADRLIDKLKPIKELednLKKN-ISEIKELINQARKQANSIK 2145
Cdd:COG4913 805 -----ADLDADLESLPEylalldrlEEDGLPEYEERFKEL---LNENsIEFVADLLSKLRRAIREIK 863
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
757-799 |
1.39e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 50.00 E-value: 1.39e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1677500969 757 CQC--FGHA-ESCDDVTGECLnCKDHTGGPYCDKCLPGFYGEPTKG 799
Cdd:smart00180 1 CDCdpGGSAsGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1663-2114 |
1.58e-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: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1663 QTGQDAERTNTRAKS--LGEFIKELARDAEavnEKAIKLNETLGTRD--EAFERNLEGLQKEI----------DQMIKEL 1728
Cdd:pfam10174 344 QTEVDALRLRLEEKEsfLNKKTKQLQDLTE---EKSTLAGEIRDLKDmlDVKERKINVLQKKIenlqeqlrdkDKQLAGL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1729 RR--KNLETQKEIAEDELVAAEALLKKVKKLFGESRGENEEMEKDLREKLADYKNKVDDAWD----LLREATDKIREANR 1802
Cdd:pfam10174 421 KErvKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERLEELESLKKENKDLKEkvsaLQPELTEKESSLID 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1803 LfavnQKNMTALEKKKEAVESGKRQIENTLKEGndiLDEANRLADEINSIIDYVEDIQTKlppmsEELNDKIDDLSQEIK 1882
Cdd:pfam10174 501 L----KEHASSLASSGLKKDSKLKSLEIAVEQK---KEECSKLENQLKKAHNAEEAVRTN-----PEINDRIRLLEQEVA 568
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1883 DRKLAEKVSQAESHAaqlndssavLDGILDEAKNisfnataafkaYSNIKD-YIDEAEKVA-KEAKDLAHEATKLATGPR 1960
Cdd:pfam10174 569 RYKEESGKAQAEVER---------LLGILREVEN-----------EKNDKDkKIAELESLTlRQMKEQNKKVANIKHGQQ 628
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1961 GLLKEDAKgclqksfrILNEAKKLANDVKEN------EDHLNGL-KTRIEnADARNGDLLRT---LNDTLGKLSAIPNDT 2030
Cdd:pfam10174 629 EMKKKGAQ--------LLEEARRREDNLADNsqqlqlEELMGALeKTRQE-LDATKARLSSTqqsLAEKDGHLTNLRAER 699
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2031 AAKLQAVKDKARQAndtakdVLAQITELHQNLDGLkknynKLADSVAKTNAvvkdpsknkiiadadATVKNLEQEADRLI 2110
Cdd:pfam10174 700 RKQLEEILEMKQEA------LLAAISEKDANIALL-----ELSSSKKKKTQ---------------EEVMALKREKDRLV 753
|
....
gi 1677500969 2111 DKLK 2114
Cdd:pfam10174 754 HQLK 757
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1700-2185 |
1.78e-07 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 57.53 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1700 NETLGTRDEAFERNLEGLQKEIDQMIKE-LRRKN-LETQKEIAEDELVAaeallKKVKKLFGESRGENEEMEKDLREKLA 1777
Cdd:PTZ00440 134 YDDLKKYSDKINEDVEPLNEEIIKNIEQcLGNKNdLDNLIIVLENPEKY-----NVRKTLYDEKFNEYKNKKEAFYNCLK 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1778 DYKNKVDDA--------WDLLR--EATDKIREANR--------LFAVNQKNMTA----LEKKKEAVESG-------KRQI 1828
Cdd:PTZ00440 209 NKKEDYDKKikkinneiRKLLKniKCTGNMCKTDTyvdmvelyLLRVNEVPSNNydnyLNRAKELLESGsdlinkiKKEL 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1829 ENTL---------KEGNDILDEANRLADEINSIIDYVEDIQT--KLPPMSE-ELNDKIDDLSQEIKDRKLAEKvsqaesH 1896
Cdd:PTZ00440 289 GDNKtiysinfiqEEIGDIIKRYNFHLKKIEKGKEYIKRIQNnnIPPQVKKdELKKKYFESAKHYASFKFSLE------M 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1897 AAQLNDSSAVLDGILDEAKNISFN-ATAAFKAYSNIKDYIDEAEKVAKEAKDLAHEATKLATGPRGLLKEDAKGCLQKSF 1975
Cdd:PTZ00440 363 LSMLDSLLIKKEKILNNLFNKLFGdLKEKIETLLDSEYFISKYTNIISLSEHTLKAAEDVLKENSQKIADYALYSNLEII 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1976 RILNEAKKLANDVKENEDHLNGLKTRIENA--------DARNG--DLLRTLNDTLGKLSAIPNdtaaKLQAVKDKARQAN 2045
Cdd:PTZ00440 443 EIKKKYDEKINELKKSINQLKTLISIMKSFydliisekDSMDSkeKKESSDSNYQEKVDELLQ----IINSIKEKNNIVN 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2046 DTAK---DVLAQITELHQNLDGLKKNYNKLADSVakTNAVVKDPSKNKIIADADATVKNLEQEadrlIDKLKPIKELEDN 2122
Cdd:PTZ00440 519 NNFKnieDYYITIEGLKNEIEGLIELIKYYLQSI--ETLIKDEKLKRSMKNDIKNKIKYIEEN----VDHIKDIISLNDE 592
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1677500969 2123 LKKNISEIKELINQARKQANSIKVSVSSGGDCIRTYKPEIKKGSYNNIVVNVKTAVADNLLFY 2185
Cdd:PTZ00440 593 IDNIIQQIEELINEALFNKEKFINEKNDLQEKVKYILNKFYKGDLQELLDELSHFLDDHKYLY 655
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
414-466 |
2.10e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 49.62 E-value: 2.10e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1677500969 414 CHCDPIGSLNEVCVKDEkharrglapGSCHCKTGFGGVSCDRCARGYTG--YPDC 466
Cdd:smart00180 1 CDCDPGGSASGTCDPDT---------GQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1612-1915 |
2.67e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.31 E-value: 2.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1612 LENMTQELKHLLSPQRAPERLIQLaEGNLNTLVTEMNELLTRATKVT---ADGEQTGQDAERTNTRAKSLGEF------- 1681
Cdd:COG4717 114 LREELEKLEKLLQLLPLYQELEAL-EAELAELPERLEELEERLEELReleEELEELEAELAELQEELEELLEQlslatee 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1682 -IKELARDAEAVNEKAIKLNETLgtrdEAFERNLEGLQKEIDQMIKELRRKNLETQKEIAEDELVAAEALL--------- 1751
Cdd:COG4717 193 eLQDLAEELEELQQRLAELEEEL----EEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLallglggsl 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1752 -------------------------KKVKKLFGESRGE-------NEEMEKDLREKLADYKNKVDDAWDLLREATDKIRE 1799
Cdd:COG4717 269 lsliltiagvlflvlgllallflllAREKASLGKEAEElqalpalEELEEEELEELLAALGLPPDLSPEELLELLDRIEE 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1800 ANRLFA------------VNQKNMTAL----------------------EKKKEAVESGKRQIENTLKEGNDILDEAN-- 1843
Cdd:COG4717 349 LQELLReaeeleeelqleELEQEIAALlaeagvedeeelraaleqaeeyQELKEELEELEEQLEELLGELEELLEALDee 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1844 RLADEINSIIDYVEDIQTKLppmsEELNDKIDDLSQEIK----DRKLAEKVSQAESHAAQLND------SSAVLDGILDE 1913
Cdd:COG4717 429 ELEEELEELEEELEELEEEL----EELREELAELEAELEqleeDGELAELLQELEELKAELRElaeewaALKLALELLEE 504
|
..
gi 1677500969 1914 AK 1915
Cdd:COG4717 505 AR 506
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1684-1885 |
3.21e-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: 3.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1684 ELARDAEAV----NEKAIKLNETLGTRD-----------EAFERNLEGLQKEIDQMIkelrrknlETQKEIAEDELVAAE 1748
Cdd:cd00176 4 QFLRDADELeawlSEKEELLSSTDYGDDlesveallkkhEALEAELAAHEERVEALN--------ELGEQLIEEGHPDAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1749 ALLKKVKKLfgesrgenEEMEKDLREKLADYKNKVDDAWDLLRE----------ATDKIREANRLFAVN-----QKNMTA 1813
Cdd:cd00176 76 EIQERLEEL--------NQRWEELRELAEERRQRLEEALDLQQFfrdaddleqwLEEKEAALASEDLGKdlesvEELLKK 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1677500969 1814 LEKKKEAVESGKRQIENTLKEGNDILDEANRLADeinsiidyvEDIQTKLppmsEELNDKIDDLSQEIKDRK 1885
Cdd:cd00176 148 HKELEEELEAHEPRLKSLNELAEELLEEGHPDAD---------EEIEEKL----EELNERWEELLELAEERQ 206
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1638-2181 |
4.33e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.08 E-value: 4.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1638 GNLNTLVTEM----NELLTRATKVTA---DGEQTGQDAERTNTRAKSLGEfIKELARDAEAvNEKAIKLNETLGTRDEAF 1710
Cdd:COG4913 207 GDLDDFVREYmleePDTFEAADALVEhfdDLERAHEALEDAREQIELLEP-IRELAERYAA-ARERLAELEYLRAALRLW 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1711 --ERNLEGLQKEIDQMIKELRRknLETQKEIAEDELVAAEALLKKVKKLFGESRGEN-EEMEKDLREKLADyKNKVDDAW 1787
Cdd:COG4913 285 faQRRLELLEAELEELRAELAR--LEAELERLEARLDALREELDELEAQIRGNGGDRlEQLEREIERLERE-LEERERRR 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1788 DLLREATDKIREANRL----FAVNQKN----MTALEKKKEAVESGKRQIENTLKEGNDildEANRLADEINSI------I 1853
Cdd:COG4913 362 ARLEALLAALGLPLPAsaeeFAALRAEaaalLEALEEELEALEEALAEAEAALRDLRR---ELRELEAEIASLerrksnI 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1854 D-YVEDIQTKLppmSEELNDKIDDL-----------------------------------------SQEIKDRKLAEKV- 1890
Cdd:COG4913 439 PaRLLALRDAL---AEALGLDEAELpfvgelievrpeeerwrgaiervlggfaltllvppehyaaaLRWVNRLHLRGRLv 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1891 -SQAESHAAQLNDSSAVLDGILDEaknISFNATAaFKAYsnIKDYIDEAEKVAK--EAKDLAHEATKLaTgPRGLLKEDA 1967
Cdd:COG4913 516 yERVRTGLPDPERPRLDPDSLAGK---LDFKPHP-FRAW--LEAELGRRFDYVCvdSPEELRRHPRAI-T-RAGQVKGNG 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1968 K-GCLQKSFRIL--------NEAKK--LANDVKENEDHLNGLKTRIENADARnGDLLRTLNDTLGKLSAIPND------- 2029
Cdd:COG4913 588 TrHEKDDRRRIRsryvlgfdNRAKLaaLEAELAELEEELAEAEERLEALEAE-LDALQERREALQRLAEYSWDeidvasa 666
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2030 --TAAKLQAVKDKARQANDTAKDVLAQITELHQNLDGLKKNYNKLADSVAKTNAVVK------DPSKNKIIADADATVKN 2101
Cdd:COG4913 667 erEIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEqaeeelDELQDRLEAAEDLARLE 746
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2102 LEQEADRLIDKL---KPIKELEDNLKKNISEIKELINQARKQANsikvsvssggDCIRTYKPEikkgsYNNIVVNVKTAV 2178
Cdd:COG4913 747 LRALLEERFAAAlgdAVERELRENLEERIDALRARLNRAEEELE----------RAMRAFNRE-----WPAETADLDADL 811
|
...
gi 1677500969 2179 ADN 2181
Cdd:COG4913 812 ESL 814
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1604-1844 |
4.65e-07 |
|
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: 54.68 E-value: 4.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1604 APYKMLYGLENMTQELKHLLSPQRAP--ERLIQLAEGNLNTLVTEMNELLTRATKVtadgeqtgqdaertntrAKSLGEF 1681
Cdd:cd22656 85 AGGTIDSYYAEILELIDDLADATDDEelEEAKKTIKALLDDLLKEAKKYQDKAAKV-----------------VDKLTDF 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1682 IKELARDAEAVNEKAIKLNETLGTRDEAFER-NLEGLQKEIDQMIKELRRKNLETQKEIaEDELVAAEALLKKVKKLFGE 1760
Cdd:cd22656 148 ENQTEKDQTALETLEKALKDLLTDEGGAIARkEIKDLQKELEKLNEEYAAKLKAKIDEL-KALIADDEAKLAAALRLIAD 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1761 SRGENEEMeKDLREKLADYK---NKVDDAWDLLREATDKIReanrlfavnqKNMTALEKKKEAVESGKRQIENTLKEGND 1837
Cdd:cd22656 227 LTAADTDL-DNLLALIGPAIpalEKLQGAWQAIATDLDSLK----------DLLEDDISKIPAAILAKLELEKAIEKWNE 295
|
....*..
gi 1677500969 1838 ILDEANR 1844
Cdd:cd22656 296 LAEKADK 302
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1607-1843 |
5.67e-07 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 55.23 E-value: 5.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1607 KMLYGLENMTQELKHLLspQRAPERLIQLAegnlNTLVTEMNELLTRATKVTADG---EQTGQDAERTNTRAKsLGEFIK 1683
Cdd:PRK04778 198 EILDQLEEELAALEQIM--EEIPELLKELQ----TELPDQLQELKAGYRELVEEGyhlDHLDIEKEIQDLKEQ-IDENLA 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1684 ELAR-DAEAVNEKAIKLNETLGTRDEAFER------NLEGLQKEIDQMIKELRRKNLETQKEI---------AEDELVAA 1747
Cdd:PRK04778 271 LLEElDLDEAEEKNEEIQERIDQLYDILERevkarkYVEKNSDTLPDFLEHAKEQNKELKEEIdrvkqsytlNESELESV 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1748 EALLKKVKKL-----------------FGESRGENEEMEKDL------------------------REKLADYKNKV--- 1783
Cdd:PRK04778 351 RQLEKQLESLekqydeiteriaeqeiaYSELQEELEEILKQLeeiekeqeklsemlqglrkdeleaREKLERYRNKLhei 430
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1677500969 1784 -------------DDAWDLLREATDKIREANRLFavNQK--NMTALEKKKEAVESgkrQIENTLKEGNDILDEAN 1843
Cdd:PRK04778 431 kryleksnlpglpEDYLEMFFEVSDEIEALAEEL--EEKpiNMEAVNRLLEEATE---DVETLEEETEELVENAT 500
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1613-1849 |
5.90e-07 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 55.82 E-value: 5.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1613 ENMTQELKHLLSPQRAPERLIQLAEGNLNTLVTEMNELLTRATKVTADGEQTGQDAERTNTRAKSLGEFIKELARDAEAV 1692
Cdd:TIGR00606 832 QEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQD 911
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1693 NEKAIKLNETLGTRDEAFERNLEG---LQKEIDQMIKELR-----RKNLETQ-KEIAEDELVAAEALLKKVKKLFGESRG 1763
Cdd:TIGR00606 912 SPLETFLEKDQQEKEELISSKETSnkkAQDKVNDIKEKVKnihgyMKDIENKiQDGKDDYLKQKETELNTVNAQLEECEK 991
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1764 ENEEMEKDLREKLADY-KNKVDDAW---DL-LREATDKIREANRLFAVNQKNMTALE--KKKEAVESGKRQIENTLKEGN 1836
Cdd:TIGR00606 992 HQEKINEDMRLMRQDIdTQKIQERWlqdNLtLRKRENELKEVEEELKQHLKEMGQMQvlQMKQEHQKLEENIDLIKRNHV 1071
|
250
....*....|...
gi 1677500969 1837 DILDEANRLADEI 1849
Cdd:TIGR00606 1072 LALGRQKGYEKEI 1084
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1647-1901 |
6.11e-07 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 54.90 E-value: 6.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1647 MNELLTraTKVTADGEQTGQD-------AERTNTRaksLGEFIKELA---RDAEAVNEKAIKLNETLGTRDEAFERNLEG 1716
Cdd:pfam07888 3 LDELVT--LEEESHGEEGGTDmllvvprAELLQNR---LEECLQERAellQAQEAANRQREKEKERYKRDREQWERQRRE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1717 LQKEIDQMIKELRRKNLETQK-EIAEDELVAAEALLKKVKKLFGESRGENEEMEKDLREKLADYKNKVDDAWDLLREATD 1795
Cdd:pfam07888 78 LESRVAELKEELRQSREKHEElEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1796 KIREANRLFAVNQKNMTALEKKKEAVESGKRQIENTLKEGNDILDE----ANRLADEINSIIDYVEDIQTK---LPPMSE 1868
Cdd:pfam07888 158 RAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQrdtqVLQLQDTITTLTQKLTTAHRKeaeNEALLE 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1677500969 1869 ELNDKIDDL--SQ---EIKDRKLAEKVSQ-----AESH-----AAQLN 1901
Cdd:pfam07888 238 ELRSLQERLnaSErkvEGLGEELSSMAAQrdrtqAELHqarlqAAQLT 285
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1649-1948 |
1.02e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.15 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1649 ELLTRATKVTADGEQTgQDAERTNTRAKSLGEFIKELARDAEAVNekaiKLNETLGTRDEAFERNLEglqkeidqmikEL 1728
Cdd:PTZ00121 1610 EEAKKAEEAKIKAEEL-KKAEEEKKKVEQLKKKEAEEKKKAEELK----KAEEENKIKAAEEAKKAE-----------ED 1673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1729 RRKNLETQKEiAEDELVAAEALLKK---VKKLFGESRGENEEMEKDLREKLADYKNKVDdAWDLLREATDKIREANRL-F 1804
Cdd:PTZ00121 1674 KKKAEEAKKA-EEDEKKAAEALKKEaeeAKKAEELKKKEAEEKKKAEELKKAEEENKIK-AEEAKKEAEEDKKKAEEAkK 1751
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1805 AVNQKNMTALEKKKE--AVESGKRQIENTLKEGNDILDEANRLADE--INSIIDYVEDIQTKLPPMSEELNDKIDDLSQE 1880
Cdd:PTZ00121 1752 DEEEKKKIAHLKKEEekKAEEIRKEKEAVIEEELDEEDEKRRMEVDkkIKDIFDNFANIIEGGKEGNLVINDSKEMEDSA 1831
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1677500969 1881 IKDRKLAEKVSQAESHAAQLNDSSAVLDGILDEAKNISFNataafKAYSNIKDYIDEAEKvAKEAKDL 1948
Cdd:PTZ00121 1832 IKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFN-----KEKDLKEDDEEEIEE-ADEIEKI 1893
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1420-1466 |
1.06e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 47.69 E-value: 1.06e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1420 CQCN--GHSSL-CDPETSICQnCQHHTAGDFCERCALGYYGIVkglPNDC 1466
Cdd:smart00180 1 CDCDpgGSASGtCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDG---PPGC 46
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1650-1905 |
1.14e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 53.68 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1650 LLTRATKVTADGEQTGQDAE--RTNTRAKSLGEFIKELARDAEAVNEKAIKLNETLgtrdEAFERNLEGLQKEIDQMike 1727
Cdd:COG3883 5 ALAAPTPAFADPQIQAKQKElsELQAELEAAQAELDALQAELEELNEEYNELQAEL----EALQAEIDKLQAEIAEA--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1728 lrRKNLETQKEIAEDELVAA----------EALLkkvkklfgESRGeneemekdlrekLADYKNKVDDAWDLLREATDKI 1797
Cdd:COG3883 78 --EAEIEERREELGERARALyrsggsvsylDVLL--------GSES------------FSDFLDRLSALSKIADADADLL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1798 REANRLFAVNQKNMTALEKKKEAVESGKRQIENTLKEGNDILDEANRLADEINSIIDYVEDIQTKLPPMSEELNDKIDDL 1877
Cdd:COG3883 136 EELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAA 215
|
250 260
....*....|....*....|....*...
gi 1677500969 1878 SQEIKDRKLAEKVSQAESHAAQLNDSSA 1905
Cdd:COG3883 216 AAAAAAAAAAAAAAAAAAAAAAAAAAAA 243
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1793-2036 |
1.25e-06 |
|
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: 53.61 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1793 ATDKIREANRLFAVNQKNMTALEKKKEAVESGKRQIENTLKEGNDILDEANRLADEINSIIdyvEDIQTKLppmsEELND 1872
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQEL---AALEAEL----AELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1873 KIDDLSQEIKDRK--LAEKVSqaeshAAQLNDSSAVLDGILDeakniSFNATAAFKAYSNIKDYIDEaekVAKEAKDLAH 1950
Cdd:COG4942 91 EIAELRAELEAQKeeLAELLR-----ALYRLGRQPPLALLLS-----PEDFLDAVRRLQYLKYLAPA---RREQAEELRA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1951 EATKLATGPRGLLKEDAKgcLQKSFRILNEAKK-LANDVKENEDHLNGLKTRIENADARNGDLLR---TLNDTLGKLSAI 2026
Cdd:COG4942 158 DLAELAALRAELEAERAE--LEALLAELEEERAaLEALKAERQKLLARLEKELAELAAELAELQQeaeELEALIARLEAE 235
|
250
....*....|
gi 1677500969 2027 PNDTAAKLQA 2036
Cdd:COG4942 236 AAAAAERTPA 245
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1682-2044 |
1.56e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.17 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1682 IKELARDAEAVNEKAIKLNETLgtrdEAFERNLEGLQKEIDQM---IKELRRKNLETQKEiaEDELVAAEALLKKVKKLF 1758
Cdd:COG1196 234 LRELEAELEELEAELEELEAEL----EELEAELAELEAELEELrleLEELELELEEAQAE--EYELLAELARLEQDIARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1759 GESRGENEEMEKDLREKLADYKNKVDDAWDLLREATDKIREANRLFAVNQKNMTALEKKKEAVESGKRQIENTLKEGN-D 1837
Cdd:COG1196 308 EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAeE 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1838 ILDEANRLADEINSIIDYVEDIQTKLPPMSEELNDKIDDLSQEIKDRKLAEKVSQAESHAAQ-LNDSSAVLDGILDEAKN 1916
Cdd:COG1196 388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEeEAELEEEEEALLELLAE 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1917 ISFNATAAFKAYSNIKDYIDEAEKVAKEAKDLAHEATKLATGPRGLLKEDAKGCLQKSFRILNEAKKLANDVKENEDhLN 1996
Cdd:COG1196 468 LLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAAL-AA 546
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1677500969 1997 GLKTRIENADARNGDLLRTLNDT-LGKLSAIPNDTAAKLQAVKDKARQA 2044
Cdd:COG1196 547 ALQNIVVEDDEVAAAAIEYLKAAkAGRATFLPLDKIRARAALAAALARG 595
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
1688-1842 |
1.56e-06 |
|
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.
Pssm-ID: 403808 [Multi-domain] Cd Length: 142 Bit Score: 50.00 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1688 DAEAVNEKAIKLNEtlgtrdEAFERNLEGLQKEidQMIKELRRKNletqkEIAEDELVAAEALLKKVKKLFGES---RGE 1764
Cdd:pfam12718 8 EAENAQERAEELEE------KVKELEQENLEKE--QEIKSLTHKN-----QQLEEEVEKLEEQLKEAKEKAEESeklKTN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1765 NEEMEK---DLREKLadyknkvDDAWDLLREATDKIREANrlfavnqKNMTALEKKKEAVESGKRQIENTLKEGNDILDE 1841
Cdd:pfam12718 75 NENLTRkiqLLEEEL-------EESDKRLKETTEKLRETD-------VKAEHLERKVQALEQERDEWEKKYEELEEKYKE 140
|
.
gi 1677500969 1842 A 1842
Cdd:pfam12718 141 A 141
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
287-334 |
1.94e-06 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 46.96 E-value: 1.94e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1677500969 287 CICYGHA---RACplDPATnkSRCECEHNTCGDSCDQCCPGFHQKPWRAGT 334
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. |
807-862 |
2.09e-06 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 46.96 E-value: 2.09e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1677500969 807 CACPLNIPSnnfSPTCHldrSLGLICDgCPVGYTGPRCERCAEGYFGQPSVPGGSC 862
Cdd:pfam00053 1 CDCNPHGSL---SDTCD---PETGQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
1826-2078 |
2.24e-06 |
|
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: 51.90 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1826 RQIENTLKEGNDILDEANRLADEINSIIDYVEDIQTKLPPM---SEELNDKIDDLSQEIKD-----RKLAEKVSQAESHA 1897
Cdd:smart00283 4 EAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIaatAQSAAEAAEEGREAVEDaitamDQIREVVEEAVSAV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1898 AQLNDSSAVLDGILDEAKNISF-------NAT--AAfKAysnikdyiDEAEK----VAKEAKDLAHEATKLATGPRGLLK 1964
Cdd:smart00283 84 EELEESSDEIGEIVSVIDDIADqtnllalNAAieAA-RA--------GEAGRgfavVADEVRKLAERSAESAKEIESLIK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1965 E------DAKGCLQKSFRILNEAKKLANDVKENedhLNGLKTRIENAdarngdllrtlNDTLGKLSAIPNDTAAKLQAVK 2038
Cdd:smart00283 155 EiqeetnEAVAAMEESSSEVEEGVELVEETGDA---LEEIVDSVEEI-----------ADLVQEIAAATDEQAAGSEEVN 220
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1677500969 2039 DKARQANDTAKDVLAQITELHQNLDGLKKNYNKLADSVAK 2078
Cdd:smart00283 221 AAIDEIAQVTQETAAMSEEISAAAEELSGLAEELDELVER 260
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1630-1823 |
2.76e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.51 E-value: 2.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1630 ERLIQLAEgnlntLVTEMNELLTRATKVTADGEQTGQDAERTNTRAKSLGEFIKELARDAEAVNEKAIK----------- 1698
Cdd:PRK02224 499 ERAEDLVE-----AEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEaeeeaeearee 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1699 ---LNETLGTRDEAFER--NLEGLQKEIDQMIKELRRKNlETQKEIAEDELVAAEALLKK---VKKLFGESRGENEEMEK 1770
Cdd:PRK02224 574 vaeLNSKLAELKERIESleRIRTLLAAIADAEDEIERLR-EKREALAELNDERRERLAEKrerKRELEAEFDEARIEEAR 652
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1677500969 1771 DLREKLADYKNKVDDAWDLLREATDKIReaNRLFAVNQ--KNMTALEKKKEAVES 1823
Cdd:PRK02224 653 EDKERAEEYLEQVEEKLDELREERDDLQ--AEIGAVENelEELEELRERREALEN 705
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1666-2134 |
3.81e-06 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 53.16 E-value: 3.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1666 QDAERTNTRAKSLGEFIKELARDAEAVNEKAIKLNETLGTRDEAFERNLEGLQKEIDQMIK--ELRRKN-LETQKEIAED 1742
Cdd:COG5022 889 IDVKSISSLKLVNLELESEIIELKKSLSSDLIENLEFKTELIARLKKLLNNIDLEEGPSIEyvKLPELNkLHEVESKLKE 968
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1743 ELVAAEALLKKVKKLFGESRGENEEMEKDLREKLADYKNKvddawDLLREATDKIREANRLFAVNQKNMtalekKKEAVE 1822
Cdd:COG5022 969 TSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQY-----GALQESTKQLKELPVEVAELQSAS-----KIISSE 1038
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1823 SGKRQIENTLKE-GNDILDEANRLADEINSIIDYVEDiqTKLPPMSEELNDKIDDLSQEI--KDRKLAEKVSQAESHAAQ 1899
Cdd:COG5022 1039 STELSILKPLQKlKGLLLLENNQLQARYKALKLRREN--SLLDDKQLYQLESTENLLKTInvKDLEVTNRNLVKPANVLQ 1116
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1900 LNDSSAVLDGILDEAKniSFNAtaafKAYSNIKDY---IDEAEKVAKEAKDLAHEATKLATGPRGLLKEDAKgclqKSFR 1976
Cdd:COG5022 1117 FIVAQMIKLNLLQEIS--KFLS----QLVNTLEPVfqkLSVLQLELDGLFWEANLEALPSPPPFAALSEKRL----YQSA 1186
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1977 ILNEAKKLA-NDVKENEDHLNGLKTRIenadaRNGDLLRTLNDTLGKLSAIPNDTAAKLQAVKD----KARQANDTAKDV 2051
Cdd:COG5022 1187 LYDEKSKLSsSEVNDLKNELIALFSKI-----FSGWPRGDKLKKLISEGWVPTEYSTSLKGFNNlnkkFDTPASMSNEKL 1261
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2052 LAQITELHQNLDGLKKNYNKLADSVAKTNAVVKDPSKNKIIADADA----TVKNLEQEADRLIDKLKPIK------ELED 2121
Cdd:COG5022 1262 LSLLNSIDNLLSSYKLEEEVLPATINSLLQYINVGLFNALRTKASSlrwkSATEVNYNSEELDDWCREFEisdvdeELEE 1341
|
490 500
....*....|....*....|..
gi 1677500969 2122 N---------LKKNISEIKELI 2134
Cdd:COG5022 1342 LiqavkvlqlLKDDLNKLDELL 1363
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1612-1829 |
4.19e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.14 E-value: 4.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1612 LENMTQELKHLLSPQRAPERLIQLAEGNLNTLVTEMNELLTRATKVTADGEQTGQDAERTNTRAKSLGEFIKELARDAEA 1691
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1692 VNEKAIKLNETLGTRD-EAFERNLEGLQKEIDQ---MIKELR--RKNLETQKEIAEDELVAAEALLKkvkklfgesrgEN 1765
Cdd:COG3883 98 SGGSVSYLDVLLGSESfSDFLDRLSALSKIADAdadLLEELKadKAELEAKKAELEAKLAELEALKA-----------EL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1677500969 1766 EEMEKDLREKLADYKNKVDDAWDLLREATDKIREANRLFAVNQKNMTALEKKKEAVESGKRQIE 1829
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
806-863 |
4.30e-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: 46.19 E-value: 4.30e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1677500969 806 PCACPLNIpsnNFSPTCHLDrslGLICDgCPVGYTGPRCERCAEGYFGQPSVPGGsCQ 863
Cdd:cd00055 1 PCDCNGHG---SLSGQCDPG---TGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGG-CQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
468-515 |
6.56e-06 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 45.42 E-value: 6.56e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1677500969 468 ACNCSGLGSKNE--DPCFGPCICKENVEGGDCSRCKSGFFNLQEdNWKGC 515
Cdd:cd00055 1 PCDCNGHGSLSGqcDPGTGQCECKPNTTGRRCDRCAPGYYGLPS-QGGGC 49
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1672-1835 |
8.16e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 50.68 E-value: 8.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1672 NTRAKSLGEFIKELARDAEAVNEKAIKLNETLGTRDEAfERNLEGLQKEIDQMIKELRRKNLETQKEIA--------EDE 1743
Cdd:COG1340 70 NEKVKELKEERDELNEKLNELREELDELRKELAELNKA-GGSIDKLRKEIERLEWRQQTEVLSPEEEKElvekikelEKE 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1744 LVAAEALLK---KVKKLFGESRGENEEMEkDLREKLADYKNKVDDAWDL---LREATDKIR----EANRLFAVNQKNM-- 1811
Cdd:COG1340 149 LEKAKKALEkneKLKELRAELKELRKEAE-EIHKKIKELAEEAQELHEEmieLYKEADELRkeadELHKEIVEAQEKAde 227
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1677500969 1812 ----------------------------TALEKKKEAVESGKRQIENTLKEG 1835
Cdd:COG1340 228 lheeiielqkelrelrkelkklrkkqraLKREKEKEELEEKAEEIFEKLKKG 279
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1469-1524 |
9.20e-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: 45.04 E-value: 9.20e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1677500969 1469 CACPLISSSnnfSPSCVAEGlddYRCTaCPRGYEGQYCERCAPGYTGSPGNPGGSC 1524
Cdd:pfam00053 1 CDCNPHGSL---SDTCDPET---GQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
469-515 |
1.06e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 44.61 E-value: 1.06e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1677500969 469 CNCSGLGSKNE--DPCFGPCICKENVEGGDCSRCKSGFFNlqeDNWKGC 515
Cdd:smart00180 1 CDCDPGGSASGtcDPDTGQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1612-1940 |
1.12e-05 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 51.01 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1612 LENMTQELKHLLspQRAPERLIQLAegnlNTLVTEMNELltratkvtadgEQTGQDAERTNTRAKSLgEFIKELardaEA 1691
Cdd:pfam06160 184 LEEETDALEELM--EDIPPLYEELK----TELPDQLEEL-----------KEGYREMEEEGYALEHL-NVDKEI----QQ 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1692 VNEKAIKLNETLGTRD-EAFERNLEGLQKEIDQM------------------------IKELRRKNLETQKEI------- 1739
Cdd:pfam06160 242 LEEQLEENLALLENLElDEAEEALEEIEERIDQLydllekevdakkyveknlpeiedyLEHAEEQNKELKEELervqqsy 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1740 --AEDELVAAEALLKKVKKLfgesRGENEEMEKDLREKLADYKnkvddawdllrEATDKIREanrlfavNQKNMTALEKK 1817
Cdd:pfam06160 322 tlNENELERVRGLEKQLEEL----EKRYDEIVERLEEKEVAYS-----------ELQEELEE-------ILEQLEEIEEE 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1818 KEAVESGKRQIENTLKEGNDILDEANRladEINSIIDYVEdiQTKLPPMSEELNDKIDDLSQEIKDrkLAEKVSQA---- 1893
Cdd:pfam06160 380 QEEFKESLQSLRKDELEAREKLDEFKL---ELREIKRLVE--KSNLPGLPESYLDYFFDVSDEIED--LADELNEVplnm 452
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1677500969 1894 ESHAAQLNDSSAVLDGILDEAKNISFNATAAFKA--YSN--------IKDYIDEAEK 1940
Cdd:pfam06160 453 DEVNRLLDEAQDDVDTLYEKTEELIDNATLAEQLiqYANryrssnpeVAEALTEAEL 509
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1682-1897 |
1.64e-05 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 48.87 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1682 IKELARDAEAVNEKAI-KLNETLGTRDEAfERNLEGLQKEIDQMIKELRRKN--LETQKEIAEDELVAAEALLKKVKKLf 1758
Cdd:pfam00261 6 IKEELDEAEERLKEAMkKLEEAEKRAEKA-EAEVAALNRRIQLLEEELERTEerLAEALEKLEEAEKAADESERGRKVL- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1759 gesrgENEEMEKDlrEKLADYKNKVDDAWDLLREATDKIREANRLFAVNQKNMTALEKKKEAVESGKRQIENTLKEGndi 1838
Cdd:pfam00261 84 -----ENRALKDE--EKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVV--- 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1677500969 1839 ldeanrladeINSIidyvediqTKLPPMSEELNDKIDDLSQEIKDrkLAEKVSQAESHA 1897
Cdd:pfam00261 154 ----------GNNL--------KSLEASEEKASEREDKYEEQIRF--LTEKLKEAETRA 192
|
|
| CAF-1_p150 |
pfam11600 |
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ... |
1702-1865 |
1.70e-05 |
|
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.
Pssm-ID: 402959 [Multi-domain] Cd Length: 164 Bit Score: 47.76 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1702 TLGTRDEAFERNLEGLQKEIDQMIKELRRKNLETQKEIAEDElvaAEALLKKVKKlfgESRGENEEmEKDLREKLADYKN 1781
Cdd:pfam11600 3 SQKSVQSQEEKEKQRLEKDKERLRRQLKLEAEKEEKERLKEE---AKAEKERAKE---EARRKKEE-EKELKEKERREKK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1782 KVDDawdllREATDKIR--EANRlfavnQKNMTALEKKKEavESGKRQIENTLKEgndildEANRLADEINSIIDYVEDI 1859
Cdd:pfam11600 76 EKDE-----KEKAEKLRlkEEKR-----KEKQEALEAKLE--EKRKKEEEKRLKE------EEKRIKAEKAEITRFLQKP 137
|
....*.
gi 1677500969 1860 QTKLPP 1865
Cdd:pfam11600 138 KTQQAP 143
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1917-2169 |
1.94e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.76 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1917 ISFNATAAFKAYSNIKDYIDEAEKVAKEAKDLAHEATKLATGPRGLLK--EDAKGCLQKSFRILN-EAKKLANDVKENED 1993
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAalERRIAALARRIRALEqELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1994 HLNGLKTRIENADARNGDLLRTLnDTLGKLSAI--------PNDTAAKLQAVKDKARQANDTAKDVLAQITELHQNLDGL 2065
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRAL-YRLGRQPPLalllspedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2066 KKNYNKLADSVAKTNAVVKDPSKNKiiADADATVKNLEQEADRLIDKLKPIKELEDNLKKNISEIKELINQARKQANSIK 2145
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALK--AERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
250 260 270
....*....|....*....|....*....|.
gi 1677500969 2146 VSVSSG-------GDCIRTYKPEIKKGSYNN 2169
Cdd:COG4942 248 FAALKGklpwpvsGRVVRRFGERDGGGGRNK 278
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1683-2060 |
2.10e-05 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 50.03 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1683 KELARDAEAvnEKAIKLNETLGTRD--EAFERNLEGLQKEIDQMIKELRRKNL---ETQKEIAEDELVAAEALLKKVK-- 1755
Cdd:pfam05701 55 KKQSEAAEA--AKAQVLEELESTKRliEELKLNLERAQTEEAQAKQDSELAKLrveEMEQGIADEASVAAKAQLEVAKar 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1756 --KLFGESRGENEEMEkDLREKLADYKNKVDDAWDLLREATDKIREANR--------LFAVNQK-------NMTALEKKK 1818
Cdd:pfam05701 133 haAAVAELKSVKEELE-SLRKEYASLVSERDIAIKRAEEAVSASKEIEKtveeltieLIATKESlesahaaHLEAEEHRI 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1819 EAV---ESGKRQIENTLKEGNdilDEANRLADEINSiidyVEDIQTKLPPMSE-------ELNDKIDDLSQEIKDRKLAE 1888
Cdd:pfam05701 212 GAAlarEQDKLNWEKELKQAE---EELQRLNQQLLS----AKDLKSKLETASAllldlkaELAAYMESKLKEEADGEGNE 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1889 KVSQAESHAA------QLNDSSAVLDGILDEAKNISFNATA---------------------AFKAYSNIKDYID----E 1937
Cdd:pfam05701 285 KKTSTSIQAAlasakkELEEVKANIEKAKDEVNCLRVAAASlrselekekaelaslrqregmASIAVSSLEAELNrtksE 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1938 AEKVAKEAKDLAHEATKLAtgprgllKEdakgcLQKSFRILNEAKKLANDVKEnedHLNGLKTRIENADArngdllrtln 2017
Cdd:pfam05701 365 IALVQAKEKEAREKMVELP-------KQ-----LQQAAQEAEEAKSLAQAARE---ELRKAKEEAEQAKA---------- 419
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1677500969 2018 dtlgKLSAIpndtAAKLQAVKDKARQANDTAKDVLAQITELHQ 2060
Cdd:pfam05701 420 ----AASTV----ESRLEAVLKEIEAAKASEKLALAAIKALQE 454
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
807-855 |
2.23e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 43.84 E-value: 2.23e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1677500969 807 CACPlniPSNNFSPTCHLDrslGLICDgCPVGYTGPRCERCAEGYFGQP 855
Cdd:smart00180 1 CDCD---PGGSASGTCDPD---TGQCE-CKPNVTGRRCDRCAPGYYGDG 42
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1631-1938 |
2.29e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 50.29 E-value: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1631 RLIQLAEGNLNTLVTEMNElltratkVTADGEQTGQDAERTNTRAKSLGEFIKELARDAEAVNEKAI--KLNETLGTRD- 1707
Cdd:PRK01156 395 EILKIQEIDPDAIKKELNE-------INVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVcpVCGTTLGEEKs 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1708 ----EAFERNLEGLQKEIDQMIKELRRKNLETQKEIAEDELVAAEallkKVKKLFGESRgeneeMEKDLREKLADYKNKV 1783
Cdd:PRK01156 468 nhiiNHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESE----EINKSINEYN-----KIESARADLEDIKIKI 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1784 DDawdlLREATDKIREANRLFavNQKNMTALEKKKEAVESGKRQ-----IENTLKEGNDILDEANRLADEINSIIDYVED 1858
Cdd:PRK01156 539 NE----LKDKHDKYEEIKNRY--KSLKLEDLDSKRTSWLNALAVislidIETNRSRSNEIKKQLNDLESRLQEIEIGFPD 612
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1859 IQTKLPPMSEELNDKIDDLS---QEIKDRKLA-EKVSQAESHaaqLNDSSAVLDGILDEAKNISFNATAAFKAYSNIKDY 1934
Cdd:PRK01156 613 DKSYIDKSIREIENEANNLNnkyNEIQENKILiEKLRGKIDN---YKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKA 689
|
....
gi 1677500969 1935 IDEA 1938
Cdd:PRK01156 690 LDDA 693
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1612-1806 |
2.39e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.44 E-value: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1612 LENMTQELKHLLSPQRAPERLIQLAEGNLNTLVTEMNELLTRATKVTADGEQTGQDAERTNTRaksLGEFIKELARDAEA 1691
Cdd:TIGR02168 868 IEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELR---LEGLEVRIDNLQER 944
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1692 VNEKAIKLNETLGTRDEAFERNLEGLQKEIDQM---IKELRRKNLEtqkeiAEDElvaaealLKKVKKLFGESRGENEEM 1768
Cdd:TIGR02168 945 LSEEYSLTLEEAEALENKIEDDEEEARRRLKRLenkIKELGPVNLA-----AIEE-------YEELKERYDFLTAQKEDL 1012
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1677500969 1769 EKDlREKLADYKNKVDD-AWDLLREATDKIREA-NRLFAV 1806
Cdd:TIGR02168 1013 TEA-KETLEEAIEEIDReARERFKDTFDQVNENfQRVFPK 1051
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1844-2063 |
2.49e-05 |
|
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: 47.26 E-value: 2.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1844 RLADEINSIIDYVEDIQTKLPPMSEELNDKI----DDLSQEIkDRKLAEKVSQAESHAAQLNdssAVLDGILDEAKNIsf 1919
Cdd:pfam01442 1 LLEDSLDELSTYAEELQEQLGPVAQELVDRLeketEALRERL-QKDLEEVRAKLEPYLEELQ---AKLGQNVEELRQR-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1920 nataafkaysnIKDYIDE-AEKVAKEAKDLaheATKLATgprglLKEDAKgclqksfrilneaKKLANDVKENEDHLNGL 1998
Cdd:pfam01442 75 -----------LEPYTEElRKRLNADAEEL---QEKLAP-----YGEELR-------------ERLEQNVDALRARLAPY 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1677500969 1999 KTRI-ENADARNGDLLRTLndtlgklsaipndtAAKLQAVKDKARQANDTAKDVLA-QITELHQNLD 2063
Cdd:pfam01442 123 AEELrQKLAERLEELKESL--------------APYAEEVQAQLSQRLQELREKLEpQAEDLREKLD 175
|
|
| SF-assemblin |
pfam06705 |
SF-assemblin/beta giardin; This family consists of several eukaryotic SF-assemblin and related ... |
1672-1863 |
2.98e-05 |
|
SF-assemblin/beta giardin; This family consists of several eukaryotic SF-assemblin and related beta giardin proteins. During mitosis the SF-assemblin-based cytoskeleton is reorganized; it divides in prophase and is reduced to two dot-like structures at each spindle pole in metaphase. During anaphase, the two dots present at each pole are connected again. In telophase there is an asymmetrical outgrowth of new fibres. It has been suggested that SF-assemblin is involved in re-establishing the microtubular root system characteriztic of interphase cells after mitosis.
Pssm-ID: 284187 [Multi-domain] Cd Length: 247 Bit Score: 48.39 E-value: 2.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1672 NTRAKSLGEFIKELARDAEAVNEKAIKLNETL-----GTRDEAFERNLE---GLQKEIDQMIKELRRK------NLETQK 1737
Cdd:pfam06705 33 DTRVKMIKEAIAHLEKLIQTESKKRQESFEDIqeefkKEIDNMQETIKEeidDMAANFRKALAELNDTinnvetNLQNEI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1738 EIAEDELVA-AEALLKKVKKL---FGESRGENEEMEKDLREKLADYKNKVDDAWDLLREATDKIREANRLFAVNQKNMTA 1813
Cdd:pfam06705 113 AIHNDAIEAlRKEALKSLNDLetgIATENAERKKMYDQLNKKVAEGFARISAAIDTEKNARDSAVSAATTELTNTKLVEK 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1677500969 1814 L--EKKKEAVESGKRQIENTLkegndILDEANRLA--DEI-NSIIDYVEDIQTKL 1863
Cdd:pfam06705 193 CvnEQFENAVLSEIAAIKEEL-----DREKAERKAadDKIvQAVNDYTKALQGGL 242
|
|
| auto_Ata |
NF033481 |
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an ... |
1665-2204 |
3.17e-05 |
|
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an architecture that consists of a long signal peptide, a repetitive passenger domain that varies in length from strain to strain, and a C-terminal domain of four transmembrane beta stands that forms one third of the pore for autotransporter activity and anchoring in the outer membrane.
Pssm-ID: 411124 [Multi-domain] Cd Length: 1862 Bit Score: 49.86 E-value: 3.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1665 GQDAERTNTRAKSLGEFIKELARDAEAVNEKAIKLNET-----------------LGTRDEAFERNLEGLQKeiDQMIKE 1727
Cdd:NF033481 642 GKGAEATNENAAAVGGGAKATGKNAAAIGGGAIADQENavavgqgaqslveggvaLGARSKVEAKNSVALGQ--DAVATE 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1728 LRRKNLETQKEIAEDELVAAEALLKKVKKLFGESRGENEEMEKDLREkladyknkvddawdlLREATDKIREANRLFAVN 1807
Cdd:NF033481 720 ATGTSFLTNRDASQSNGVISVGSAGKERRITNVEDGSADSDAVTVRQ---------------LKNVDSRVNQNTSNIGKN 784
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1808 QKNMTALEKKKEAVESG-KRQIENTLKE--------GNDILDEANRLADEINSIIDYVEDIQTKLPPM----SEELNDKI 1874
Cdd:NF033481 785 TQNITNLNQKLDDTKTNlGNQITDTNKNlndakkdlGNQITDTNTKLNTTKDQLTTQINDTKTELNNTigntKTELNTKI 864
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1875 DDLSQEIKD--------------RKLAEKV-----SQAESHAAQLNDSSAVL----DGI----LDEAK---------NIS 1918
Cdd:NF033481 865 DNTKTELENkglnfagnsgadvhRKLGDKLnivggAAASTPAAKTSGENVITrttqDGIqielLKDSKfdsvttgntTLN 944
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1919 FNATAAFKAYSNIKDYIDEAEKVAKEAKDLAHEATKLATGPRGLLKEDAKGCLQKSFRILNEAKK-LANDVKENEDHLNG 1997
Cdd:NF033481 945 TNGLTIKEGPSITKQGINAGSKQITNVADGINAKDAVNVDQLTKVKENLNGRITDTNNQLNDAKKdLGNQIADTNKNLND 1024
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1998 LKTRIENadaRNGDLLRTLNDTLGKLSAIPNDTAAKLQAV--KDKARQANDTAKDVLAQITELHQNLdGLKKNYNKLADS 2075
Cdd:NF033481 1025 AKKDLGD---QITDTNTKLNNTKDQLTTQINDTKTELNNTigNTKTELENKGLNFAGNSGADVHRKL-GDKLNIVGGAAA 1100
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2076 VAKTNAVVKDPSKNKIIADADATVKNLEQEADRLIDKLKPIKELEDNLKKNISEIKELINQARKQANSIKVSVSSggdci 2155
Cdd:NF033481 1101 STPAAKTSGENVITRTTKDGIQIELLKDSKFDSVTTGNTTLNTNGLTIKEGPSITKDGINAGGKQITNVADGINA----- 1175
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 1677500969 2156 rtyKPEIKKGSYNNIVvnVKTAVADNLLFYLGSAKFIDFLAIEMRKGKV 2204
Cdd:NF033481 1176 ---KDAVNKGQLDNLA--AKQNATDDAAVKYDDAKTKDKVTLKGKDGTV 1219
|
|
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
1772-2136 |
3.19e-05 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 49.63 E-value: 3.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1772 LREKLADYKNKVDDAWDLLREATDKIREANRLFAVNQKNMTALEKKKEAVESGKRQIENTLKEGNDILDEANRLADEINS 1851
Cdd:COG0840 4 LLLLLALLLALLLLALSLLALLAAALLILLALLLAALTALALLLLLSLLALLLLLLLLALALLLVLLALLLLLALVVLLA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1852 IIDYVEDIQTKLPPMSEELNDKIDDLSQEIKDRKLAEKVSQAESHAAQLNDSSAVLDGILDEAKNISFNATAAFKAYSNI 1931
Cdd:COG0840 84 LLLALLLLLLALLALALAALALLAALAALLALLELLLAALLAALAIALLALAALLALAALALALLALALLAAAAAAAAAL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1932 KDYIDEAEKVAKEAKDLAHEATKLATGPRGLLKEDAKGCLQKSFRILNEAKKLANDVKENEdhlngLKTRIEnADARN-- 2009
Cdd:COG0840 164 AALLEAAALALAAAALALALLAAALLALVALAIILALLLSRSITRPLRELLEVLERIAEGD-----LTVRID-VDSKDei 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2010 GDLLRTLNDTLGKLSAIPNDTAAKLQAVKDKARQANDTAKDVLAQITELHQNLDG-------LKKNYNKLADSVAKTNAV 2082
Cdd:COG0840 238 GQLADAFNRMIENLRELVGQVRESAEQVASASEELAASAEELAAGAEEQAASLEEtaaameeLSATVQEVAENAQQAAEL 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1677500969 2083 VKDPSK-----NKIIADADATVKNLEQEADRLIDKlkpIKELEDNLKKnISEIKELINQ 2136
Cdd:COG0840 318 AEEASElaeegGEVVEEAVEGIEEIRESVEETAET---IEELGESSQE-IGEIVDVIDD 372
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1795-1999 |
3.28e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 49.63 E-value: 3.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1795 DKIREANRLFAV--------------NQKNMTALEKK-KEAVESGKRQIENTLKEGNDILDEANRLADEINSIIDYVEDI 1859
Cdd:PHA02562 174 DKIRELNQQIQTldmkidhiqqqiktYNKNIEEQRKKnGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDP 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1860 QTKLppmsEELNDKIDDLSQEI----KDRKLAEKVSQAESHAAQLNDSSAVLDGILDEAKNISfnataafKAYSNIKDYI 1935
Cdd:PHA02562 254 SAAL----NKLNTAAAKIKSKIeqfqKVIKMYEKGGVCPTCTQQISEGPDRITKIKDKLKELQ-------HSLEKLDTAI 322
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1677500969 1936 DEAEKVAKEAKDLAHEATKLATGPRgLLKEDAKGCLQKSFRILNEAKKLANDVKENEDHLNGLK 1999
Cdd:PHA02562 323 DELEEIMDEFNEQSKKLLELKNKIS-TNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQ 385
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1634-1947 |
3.62e-05 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 48.52 E-value: 3.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1634 QLAEGNLNTLVTEMNELLTRATKVTADGEQtgQDAertntrAKSLGEFIKELARDAEAVNEKAIKLNETLGTrdeaFERN 1713
Cdd:cd22656 83 QNAGGTIDSYYAEILELIDDLADATDDEEL--EEA------KKTIKALLDDLLKEAKKYQDKAAKVVDKLTD----FENQ 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1714 LEGLQKEIDQmikelRRKNLetqKEIAEDELvaAEALLKKVKKLfgesrgeNEEMEKDLREKLADYKNKVDDAWDLLREA 1793
Cdd:cd22656 151 TEKDQTALET-----LEKAL---KDLLTDEG--GAIARKEIKDL-------QKELEKLNEEYAAKLKAKIDELKALIADD 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1794 TDKIREANRLFAvnqknmtalekkkeAVESGKRQIENTLkegndildeanrlaDEINSIIDYVEDIQTklppmseelndk 1873
Cdd:cd22656 214 EAKLAAALRLIA--------------DLTAADTDLDNLL--------------ALIGPAIPALEKLQG------------ 253
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1677500969 1874 iddlsqeikdrklaekvsqaesHAAQLNDSsavLDGILDEAKNISFNATAAFKAYSNIKDYIDEAEKVAKEAKD 1947
Cdd:cd22656 254 ----------------------AWQAIATD---LDSLKDLLEDDISKIPAAILAKLELEKAIEKWNELAEKADK 302
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1992-2145 |
3.62e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.06 E-value: 3.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1992 EDHLNGLKTRIENADARNGDLLRTLNDTLGKLSAipndTAAKLQAVKDKARQANDTAKDVLAQITELHQNLDGLKKNYNK 2071
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEE----LNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2072 LADSVAKTNAVV---------KDPS---------------KNKIIADADATVKNLEQEADRLIDKLKPIKELEDNLKKNI 2127
Cdd:COG3883 91 RARALYRSGGSVsyldvllgsESFSdfldrlsalskiadaDADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAK 170
|
170
....*....|....*...
gi 1677500969 2128 SEIKELINQARKQANSIK 2145
Cdd:COG3883 171 AELEAQQAEQEALLAQLS 188
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1930-2137 |
3.98e-05 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 47.72 E-value: 3.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1930 NIKDYIDEAEKVAKEAKDLAHEATKLATGPRG----------LLKED---AKGCLQKSFRILNEAKKLAndvKENEdhlN 1996
Cdd:pfam00261 5 QIKEELDEAEERLKEAMKKLEEAEKRAEKAEAevaalnrriqLLEEElerTEERLAEALEKLEEAEKAA---DESE---R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1997 GLKTrIENADARNGDLLRTLNDTLGKLSAIPNDT-------AAKLQAVKDKARQANDTAKDVLAQITELHQNLDGLKKNY 2069
Cdd:pfam00261 79 GRKV-LENRALKDEEKMEILEAQLKEAKEIAEEAdrkyeevARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2070 NKLADSVAKTNAVvKDPSKNKI-------------IADADATVKNLEQEADRLIDKLkpikELEdnlKKNISEIKELINQ 2136
Cdd:pfam00261 158 KSLEASEEKASER-EDKYEEQIrflteklkeaetrAEFAERSVQKLEKEVDRLEDEL----EAE---KEKYKAISEELDQ 229
|
.
gi 1677500969 2137 A 2137
Cdd:pfam00261 230 T 230
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1836-2076 |
4.20e-05 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 48.52 E-value: 4.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1836 NDILDEANRLAdeiNSIIDYVEDIQTKLPPMSEELNDKIDDLSQEIKDRKLAEKVSQAEshaaqlndssAVLDGILDEAK 1915
Cdd:cd22656 65 DDTYPSIVSLA---GDIYNYAQNAGGTIDSYYAEILELIDDLADATDDEELEEAKKTIK----------ALLDDLLKEAK 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1916 NIsfnATAAFKAYSNIKDYIDEAEKVAKEAKDLAHEATKLATGPRGLLKEDAKGCLQKSFRILNE--AKKLANDVKENED 1993
Cdd:cd22656 132 KY---QDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLLTDEGGAIARKEIKDLQKELEKLNEeyAAKLKAKIDELKA 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1994 HLNGLKTRIEnADARNGDLLRTLNDTLGKLS-----AIP---------NDTAAKLQAVKDKArqANDTAKDVLAQITELh 2059
Cdd:cd22656 209 LIADDEAKLA-AALRLIADLTAADTDLDNLLaligpAIPaleklqgawQAIATDLDSLKDLL--EDDISKIPAAILAKL- 284
|
250
....*....|....*..
gi 1677500969 2060 qNLDGLKKNYNKLADSV 2076
Cdd:cd22656 285 -ELEKAIEKWNELAEKA 300
|
|
| Phage_GP20 |
pfam06810 |
Phage minor structural protein GP20; This family consists of several phage minor structural ... |
1679-1809 |
4.42e-05 |
|
Phage minor structural protein GP20; This family consists of several phage minor structural protein GP20 sequences of around 180 residues in length. The function of this family is unknown.
Pssm-ID: 429131 [Multi-domain] Cd Length: 149 Bit Score: 46.20 E-value: 4.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1679 GEFIKELARDAeaVNEKAIKLNETLGTRD---EAFE---RNLEGLQKEIDQMIKELRRKNLETQKEIAEDELVAAeallk 1752
Cdd:pfam06810 12 GKDIPKAKFDE--VNTERDTLKEQLATRDkqlKDLKkvaKDNEELQKQIDELQAKNKDAEADYEAKIADLKFDNA----- 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1753 kVKKLFGESRGENeemEKDLREKLADYKNKVDDAWDL--LREATDKIREANR-LFAVNQK 1809
Cdd:pfam06810 85 -IKLALKGAKAKN---EKAVKALLDKDKLKLKDDGTLigLDEQIEGLKESDKyLFEQEQK 140
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1630-1859 |
5.21e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 5.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1630 ERLIQLAEGNLNTLVTEMNELLTRATKVTADGEQTGQDAERTNTRAKSLGEFI--KELARDAEAVNEKAIKLN------E 1701
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvASAEREIAELEAELERLDassddlA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1702 TLGTRDEAFERNLEGLQKEIDQMIKEL-----RRKNLETQKEIAEDELVAAEALLKKVK-----KLFGESRGEN--EEME 1769
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIgrlekELEQAEEELDELQDRLEAAEDLARLELralleERFAAALGDAveRELR 768
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1770 KDLREKLADYKNKVDDAWDLLREAtdkIREANRLFAVNQKNMTA--------LEKKKEAVESG----KRQIENTLKE--G 1835
Cdd:COG4913 769 ENLEERIDALRARLNRAEEELERA---MRAFNREWPAETADLDAdleslpeyLALLDRLEEDGlpeyEERFKELLNEnsI 845
|
250 260
....*....|....*....|....
gi 1677500969 1836 NDILDEANRLADEINSIIDYVEDI 1859
Cdd:COG4913 846 EFVADLLSKLRRAIREIKERIDPL 869
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
1612-1955 |
5.26e-05 |
|
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.
Pssm-ID: 427715 [Multi-domain] Cd Length: 360 Bit Score: 48.54 E-value: 5.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1612 LENMTQELKHLLSpqrAPERLIQLAEGNLNTLVTEMNELL--TRATKVTADGEQTGQDAertntraKSLGEFIkelarDA 1689
Cdd:pfam04108 47 LEKVREGLEKVLN---ELKKDFKQLLKDLDAALERLEETLdkLRNTPVEPALPPGEEKQ-------KTLLDFI-----DE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1690 EAVNekaiKLNETLGTRDEAFERNLEGLQKEIDQMIKELRrknlETQKEIaeDELVAAEALLKKVKKLFGEsrgeNEEME 1769
Cdd:pfam04108 112 DSVE----ILRDALKELIDELQAAQESLDSDLKRFDDDLR----DLQKEL--ESLSSPSESISLIPTLLKE----LESLE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1770 KDLREKLadyKNKVDDawdllreaTDKIREANRLFAVNQKNMTALEKKKEavesgkRQIENTLKEGNDILDE-------A 1842
Cdd:pfam04108 178 EEMASLL---ESLTNH--------YDQCVTAVKLTEGGRAEMLEVLENDA------RELDDVVPELQDRLDEmennyerL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1843 NRLADEINSIIDYV-------EDIQTKLPpmseELNDKIDDLSQEIKDRKLAekvsqAESHAAQLNDSSAVLDGILDeak 1915
Cdd:pfam04108 241 QKLLEQKNSLIDELlsalqliAEIQSRLP----EYLAALKEFEERWEEEKET-----IEDYLSELEDLREFYEGFPS--- 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1677500969 1916 nisfnataafkAYsniKDYIDEA-------EKVAKEAKDLAHEATKL 1955
Cdd:pfam04108 309 -----------AY---GSLLLEVerrrewaEKMKKILRKLAEELDRL 341
|
|
| alph_xenorhab_A |
NF033928 |
alpha-xenorhabdolysin family binary toxin subunit A; Alpha-xenorhabdolysin was the founding ... |
1904-2145 |
5.91e-05 |
|
alpha-xenorhabdolysin family binary toxin subunit A; Alpha-xenorhabdolysin was the founding member of a family of alpha-helical pore-forming binary toxins. YaxAB from Yersinia enterocolitica has been studied structurally. This HMM represents subunit A proteins such as XaxA and YaxA, capable of binding to the membrane even in the absence of the B subunit. This family is related to the Bacillus haemolytic enterotoxin family (see PF05791.9), although thresholds for this HMM are set to exclude that family.
Pssm-ID: 468250 [Multi-domain] Cd Length: 340 Bit Score: 48.06 E-value: 5.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1904 SAVLDGILDEAKNISfNATAAFKAYSN-IKDYIDEAeKVAKEAKDLAHEATKLATGPRGLLKEDAKGCLQKsfrILneaK 1982
Cdd:NF033928 62 SNLEPKIKQLANDLA-NYARNIVVTGNpIIDLINEM-PIIKRGDLTEEELSELPPIPLSSDDKEIVKELKE---IL---E 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1983 KLANDVKENEDHLNGLKTRIenadarnGDLLRTLNDTLgklsaipndtAAKLQAVKDKAR--QANDTAKDVLAQITELHQ 2060
Cdd:NF033928 134 DLKNDIKDYQQKADDVKKEL-------DDFENDLREEL----------LPQLKLKKKLYDdnLGSDSIEELREKIDQLEK 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2061 NLDGLKKNYNKLADSVAKT----NAVVkdpsknkII---------ADADATVKNLEQEADRLIDKLK---PIKELEDNLK 2124
Cdd:NF033928 197 EIEQLNKEYDDYVKLSFTGlaggPIGL-------AItggifgskaEKIRKEKNALIQEIDELQEQLKkknALLGSLERLQ 269
|
250 260
....*....|....*....|.
gi 1677500969 2125 KNISEIKELINQARKQANSIK 2145
Cdd:NF033928 270 TSLDDILTRMEDALPALKKLK 290
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1688-1875 |
1.08e-04 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 45.33 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1688 DAEAVNEKAIKLNETLG--TRD--EAFERNLEGLQKEIDQMIKELRRKnLET-----QKEIAE--DELVA-AEALLKKVK 1755
Cdd:pfam01442 5 SLDELSTYAEELQEQLGpvAQElvDRLEKETEALRERLQKDLEEVRAK-LEPyleelQAKLGQnvEELRQrLEPYTEELR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1756 KLFgesRGENEEMEKDLREKLADYKNKvddawdlLREATDKIREAnrlfavnqknmtaLEkkkEAVESGKRQIENTLKEG 1835
Cdd:pfam01442 84 KRL---NADAEELQEKLAPYGEELRER-------LEQNVDALRAR-------------LA---PYAEELRQKLAERLEEL 137
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1677500969 1836 NDILDE-ANRLADEINSiidYVEDIQTKLPPMSEELNDKID 1875
Cdd:pfam01442 138 KESLAPyAEEVQAQLSQ---RLQELREKLEPQAEDLREKLD 175
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1663-1878 |
1.11e-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: 46.56 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1663 QTGQDAERTNTRAKSLGEFIKEL-ARDAEAVNEKAiKLNETLGTRDEAFERNLEGLQK---EIDQMIK-----ELRRKNL 1733
Cdd:pfam00261 5 QIKEELDEAEERLKEAMKKLEEAeKRAEKAEAEVA-ALNRRIQLLEEELERTEERLAEaleKLEEAEKaadesERGRKVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1734 ETqKEIAEDELVAA-EALLKkvkklfgESRGENEEMEKDLRE---KLADYKNKVDDAWDLLREATDKIREANRLFAVNQK 1809
Cdd:pfam00261 84 EN-RALKDEEKMEIlEAQLK-------EAKEIAEEADRKYEEvarKLVVVEGDLERAEERAELAESKIVELEEELKVVGN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1810 NMTALE-------KKKEAVESGKRQIENTLKEGNDILDEANRLADEINSIIDYVED----IQTKLPPMSEELNDKIDDLS 1878
Cdd:pfam00261 156 NLKSLEaseekasEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDeleaEKEKYKAISEELDQTLAELN 235
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1976-2175 |
1.17e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.46 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1976 RILNEAKKLANDVKENEDHLNGLKTRIENADARNGDLLRTLNDTLGKLSaipnDTAAKLQavKDKARQAN-DTAKDVLAQ 2054
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIE----EVEARIK--KYEEQLGNvRNNKEYEAL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2055 ITElhqnLDGLKKNYNKLADSVAKtnavvkdpsKNKIIADADATVKNLEQEADRLIDKLkpiKELEDNLKKNISEIKELI 2134
Cdd:COG1579 95 QKE----IESLKRRISDLEDEILE---------LMERIEELEEELAELEAELAELEAEL---EEKKAELDEELAELEAEL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1677500969 2135 NQARKQANSIKVSVSSggDCIRTYKpEIKKGSYNNIVVNVK 2175
Cdd:COG1579 159 EELEAEREELAAKIPP--ELLALYE-RIRKRKNGLAVVPVE 196
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1585-1805 |
1.26e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1585 DLARLEQMVMSINLTGPLPAPYKMLYGLENMTQELKHLLSPQRAPERLIQLAEgnlntLVTEMNELLTRAtKVTADGE-- 1662
Cdd:COG4717 315 ELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEE-----LEQEIAALLAEA-GVEDEEElr 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1663 ---QTGQDAERTNTRAKSLGEFIKELARDAEAVNEKAIKlnETLGTRDEAFERNLEGLQKEIDQMIKELRRknLETQKEI 1739
Cdd:COG4717 389 aalEQAEEYQELKEELEELEEQLEELLGELEELLEALDE--EELEEELEELEEELEELEEELEELREELAE--LEAELEQ 464
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1677500969 1740 AEDELVAAEALLKKvkklfgesrgenEEMEKDLREKLADY-KNKVddAWDLLREATDKIRE---------ANRLFA 1805
Cdd:COG4717 465 LEEDGELAELLQEL------------EELKAELRELAEEWaALKL--ALELLEEAREEYREerlppvlerASEYFS 526
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1731-1894 |
1.41e-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: 46.18 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1731 KNLETQKEIAEDELVAAEALLKKVKKLFGESRGENEEMEKDLREKLADyknkVDDAWDLLREATDKIREANRLFAVNQKN 1810
Cdd:pfam00261 4 QQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEE----LERTEERLAEALEKLEEAEKAADESERG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1811 MTALEKKKEAVESGKRQIENTLKEGNDILDEANRLADEINSIIDYVEDIQTKLPPMSEELNDKIDDLSQEIKD-----RK 1885
Cdd:pfam00261 80 RKVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVvgnnlKS 159
|
170
....*....|..
gi 1677500969 1886 L---AEKVSQAE 1894
Cdd:pfam00261 160 LeasEEKASERE 171
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
1766-1899 |
1.44e-04 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 43.75 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1766 EEMEKD---LREKLADYKNKVDDAWDLLREATDKIREANRLFAVNQKNMTALEKKKEAVESGKRQIEntlKEGNDILDEA 1842
Cdd:pfam20492 2 EEAEREkqeLEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLE---ESAEMEAEEK 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1677500969 1843 NRLADEInsiidyvediqtklppmsEELNDKIDDLSQEiKDRKLAEKVS-QAESHAAQ 1899
Cdd:pfam20492 79 EQLEAEL------------------AEAQEEIARLEEE-VERKEEEARRlQEELEEAR 117
|
|
| NtpH |
COG2811 |
Archaeal/vacuolar-type H+-ATPase subunit H [Energy production and conversion]; Archaeal ... |
1813-1916 |
1.72e-04 |
|
Archaeal/vacuolar-type H+-ATPase subunit H [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase subunit H is part of the Pathway/BioSystem: A/V-type ATP synthase
Pssm-ID: 442060 [Multi-domain] Cd Length: 108 Bit Score: 43.36 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1813 ALEKKKEAVESGKRQIENTLKEGNDILDEANRLADEInsiidyVEDIQTKlppMSEELNDKIDDLSQEIKDRKlAEKVSQ 1892
Cdd:COG2811 6 VLKEIKEAEEEADEIIEEAKEEREERIAEAREEAEEI------IEQAEEE---AEEEAQERLEEAREEAEAEA-EEIIEE 75
|
90 100
....*....|....*....|....*
gi 1677500969 1893 AESHA-AQLNDSSAVLDGILDEAKN 1916
Cdd:COG2811 76 GEKEAeALKKKAEDKLDKAVELLVE 100
|
|
| YkaA |
COG1392 |
Phosphate transport regulator YkaA, distantly related to PhoU, UPF0111/DUF47 family [Inorganic ... |
1769-1954 |
2.05e-04 |
|
Phosphate transport regulator YkaA, distantly related to PhoU, UPF0111/DUF47 family [Inorganic ion transport and metabolism];
Pssm-ID: 441002 [Multi-domain] Cd Length: 205 Bit Score: 45.25 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1769 EKDLREKLADYKNKVDDAWDLLREATDKIREANRLfavnQKNMTALEKKKEAVesgKRQIENTLKEG-------NDILde 1841
Cdd:COG1392 5 EKSFFDLLEEHAEKVVEAAELLVELLEDYEDVEEL----AEEIKELEHEADEI---KREIREELNKTfitpfdrEDIL-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1842 anRLADEINSIIDYVEDIqtklppmSEEL-NDKIDDLSQEIkdRKLAEKVSQAeshAAQLNDSSAVLDGILDEAKnisfn 1920
Cdd:COG1392 76 --ELASALDDIADYIEDI-------AGRLvLYKIEELDEEL--LELAELLVEA---AEELVEAVKELRELLKKAE----- 136
|
170 180 190
....*....|....*....|....*....|....
gi 1677500969 1921 ataafkaysNIKDYIDEAEKVAKEAKDLAHEATK 1954
Cdd:COG1392 137 ---------EVLELIIEINRLENEADDLYREALA 161
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1770-1915 |
2.09e-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: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1770 KDLREKLADYKnkvDDAWDLLREATDKIRE--ANRLFAVNQKNMTALEKKKEAVESGKRQIENTLKE-GNDILDEANRLA 1846
Cdd:pfam01442 14 EELQEQLGPVA---QELVDRLEKETEALRErlQKDLEEVRAKLEPYLEELQAKLGQNVEELRQRLEPyTEELRKRLNADA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1847 DEI------------NSIIDYVEDIQTKLPPMSEELNDKIDDLSQEIKDRkLAEKVSQAESHAAQ-LNDSSAVLDGILDE 1913
Cdd:pfam01442 91 EELqeklapygeelrERLEQNVDALRARLAPYAEELRQKLAERLEELKES-LAPYAEEVQAQLSQrLQELREKLEPQAED 169
|
..
gi 1677500969 1914 AK 1915
Cdd:pfam01442 170 LR 171
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1672-1889 |
2.40e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.82 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1672 NTRAKSLGEFIKELARDAEAVNEKA---IKLNETLGTRD----EAFERNLEGLQKEI-DQMIKE---------------- 1727
Cdd:PRK01156 475 NEKKSRLEEKIREIEIEVKDIDEKIvdlKKRKEYLESEEinksINEYNKIESARADLeDIKIKInelkdkhdkyeeiknr 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1728 --------LRRKNLETQKEIAEDELVAAEALLKK---VKKLFGESRGENEEME--------------KDLREKLADYKNK 1782
Cdd:PRK01156 555 ykslkledLDSKRTSWLNALAVISLIDIETNRSRsneIKKQLNDLESRLQEIEigfpddksyidksiREIENEANNLNNK 634
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1783 VDDAWDLLReATDKIREANRLFAVNQKNMTALEKKKEAVESGKRQIENTLKEGNDILDEANRLADEINSIIdyvEDIQTK 1862
Cdd:PRK01156 635 YNEIQENKI-LIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTI---EILRTR 710
|
250 260
....*....|....*....|....*..
gi 1677500969 1863 LppmsEELNDKIDDLSQEIKDRKLAEK 1889
Cdd:PRK01156 711 I----NELSDRINDINETLESMKKIKK 733
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1570-1897 |
2.58e-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: 46.89 E-value: 2.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1570 ECVFCGDEC--------TGLLLGDLARLEQMvmsINLTGPLPAPYKMLYGleNMTQELKHLLSPQRAPERLIQlAEGNLN 1641
Cdd:TIGR00618 503 PCPLCGSCIhpnparqdIDNPGPLTRRMQRG---EQTYAQLETSEEDVYH--QLTSERKQRASLKEQMQEIQQ-SFSILT 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1642 TLVTEMNELLTRATKVTADGEQTGQdaERTNTRAKSLGEFIKELARDAEAVNEKAIKLNETlgtrdeafernleglQKEI 1721
Cdd:TIGR00618 577 QCDNRSKEDIPNLQNITVRLQDLTE--KLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQ---------------QCSQ 639
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1722 DQMIKELRRKNLETqkEIAEDELVAAEALLKKVKKLFGESRGENEEMEKDLREKLADYKNKVDDAWDLLREATDKIREAN 1801
Cdd:TIGR00618 640 ELALKLTALHALQL--TLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYD 717
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1802 RLFavnqknmtalEKKKEAVESGKRQIENTLKEGNDILDEANRLADEinSIIDYVEDIQTKLP--PMSEELNDKIDDLSQ 1879
Cdd:TIGR00618 718 REF----------NEIENASSSLGSDLAAREDALNQSLKELMHQART--VLKARTEAHFNNNEevTAALQTGAELSHLAA 785
|
330 340
....*....|....*....|....*..
gi 1677500969 1880 EIKDRK---------LAEKVSQAESHA 1897
Cdd:TIGR00618 786 EIQFFNrlreedthlLKTLEAEIGQEI 812
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1727-1883 |
2.83e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 45.78 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1727 ELRRKNLETQKEIAE---DELVAAEALLKKvkklfgesrgeNEEMEKDLREKLADYKNKVDDAWDLLREATDKIreanrl 1803
Cdd:smart00787 136 EWRMKLLEGLKEGLDenlEGLKEDYKLLMK-----------ELELLNSIKPKLRDRKDALEEELRQLKQLEDEL------ 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1804 favNQKNMTALEKKKEAVESGKRQIENTLKEGNDILDEANRLADEInsiidyvediqtklppmsEELNDKIDDLSQEIKD 1883
Cdd:smart00787 199 ---EDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKI------------------EDLTNKKSELNTEIAE 257
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
1783-2108 |
2.85e-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: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1783 VDDAWDLLREATDKIREANRLF-AVNQ--KNMTALEKKKEAV-ESGKRQIENTLKEGNDILDEANRLADEINSIIdyved 1858
Cdd:pfam04108 16 LTDARSLLEELVVLLAKIAFLRrGLSVqlANLEKVREGLEKVlNELKKDFKQLLKDLDAALERLEETLDKLRNTP----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1859 IQTKLPPMSEE---LNDKIDDLSQEIKDRKLAEKVSQAESHAAQLNDSSAVLDGILDEAKNISFNATAAFKAYSNIKDYI 1935
Cdd:pfam04108 91 VEPALPPGEEKqktLLDFIDEDSVEILRDALKELIDELQAAQESLDSDLKRFDDDLRDLQKELESLSSPSESISLIPTLL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1936 DEAEKVAKEAKDLA-----H-----EATKLATGPR----GLLKEDAkgclQKSFRILNEAKKLANDVKENEDHLNGLKTR 2001
Cdd:pfam04108 171 KELESLEEEMASLLesltnHydqcvTAVKLTEGGRaemlEVLENDA----RELDDVVPELQDRLDEMENNYERLQKLLEQ 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2002 IENADARNGDLLRTLNDTLGKLSAIPndtaAKLQAVKDKARQANDTAKDVLAQITELHQNLDGLKKNYNKLADSVAKTNA 2081
Cdd:pfam04108 247 KNSLIDELLSALQLIAEIQSRLPEYL----AALKEFEERWEEEKETIEDYLSELEDLREFYEGFPSAYGSLLLEVERRRE 322
|
330 340
....*....|....*....|....*..
gi 1677500969 2082 VvkDPSKNKIIADADATVKNLeQEADR 2108
Cdd:pfam04108 323 W--AEKMKKILRKLAEELDRL-QEEER 346
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1469-1520 |
2.85e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 40.76 E-value: 2.85e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1677500969 1469 CACPLissSNNFSPSCVaegLDDYRCTaCPRGYEGQYCERCAPGYTGSPGNP 1520
Cdd:smart00180 1 CDCDP---GGSASGTCD---PDTGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| V_Alix_like |
cd08915 |
Protein-interacting V-domain of mammalian Alix and related domains; This superfamily contains ... |
1971-2133 |
3.01e-04 |
|
Protein-interacting V-domain of mammalian Alix and related domains; This superfamily contains the V-shaped (V) domain of mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, and related domains. Alix, HD-PTP, Bro1, and Rim20 all interact with the ESCRT (Endosomal Sorting Complexes Required for Transport) system. Alix, also known as apoptosis-linked gene-2 interacting protein 1 (AIP1), participates in membrane remodeling processes during the budding of enveloped viruses, vesicle budding inside late endosomal multivesicular bodies (MVBs), and the abscission reactions of mammalian cell division. It also functions in apoptosis. HD-PTP functions in cell migration and endosomal trafficking, Bro1 in endosomal trafficking, and Rim20 in the response to the external pH via the Rim101 pathway. The Alix V-domain contains a binding site, partially conserved in this superfamily, for the retroviral late assembly (L) domain YPXnL motif. The Alix V-domain is also a dimerization domain. Members of this superfamily have an N-terminal Bro1-like domain, which binds components of the ESCRT-III complex. The Bro1-like domains of Alix and HD-PTP can also bind human immunodeficiency virus type 1 (HIV-1) nucleocapsid. Many members, including Alix, HD-PTP, and Bro1, also have a proline-rich region (PRR), which binds multiple partners in Alix, including Tsg101 (tumor susceptibility gene 101, a component of ESCRT-1) and the apoptotic protein ALG-2. The C-terminal portion (V-domain and PRR) of Bro1 interacts with Doa4, a ubiquitin thiolesterase needed to remove ubiquitin from MVB cargoes; it interacts with a YPxL motif in Doa4s catalytic domain to stimulate its deubiquitination activity. Rim20 may bind the ESCRT-III subunit Snf7, bringing the protease Rim13 (a YPxL-containing transcription factor) into proximity with Rim101, and promoting the proteolytic activation of Rim101. HD-PTP is encoded by the PTPN23 gene, a tumor suppressor gene candidate often absent in human kidney, breast, lung, and cervical tumors. HD-PTP has a C-terminal catalytically inactive tyrosine phosphatase domain.
Pssm-ID: 185746 [Multi-domain] Cd Length: 342 Bit Score: 45.80 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1971 LQKSFrilNEAKKLAndvKENEDHLNGLKTRIEnADARNGDLLR----TLNDTLGKLSAIPNDTAAKLQAVKDKARQAND 2046
Cdd:cd08915 75 IEQSF---KELSKLR---QNVEELLQECEELLE-EEAAEDDQLRakfgTLRWRRPSSDEAAKELYEKVTKLRGYLEQASN 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2047 TAKDVLAQITELHQNLDGLKKNYNKLADSVAKTNaVVKDPSKNKIIADADAT---VKNLEQEADRLIDKLKpIKELEDN- 2122
Cdd:cd08915 148 SDNEVLQCYESIDPNLVLLCGGYKELKAFIPSPY-PALDPEVSEVVSSLRPLlneVSELEKERERFISELE-IKSRNNDi 225
|
170
....*....|.
gi 1677500969 2123 LKKNISEIKEL 2133
Cdd:cd08915 226 LPKLITEYKKN 236
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
306-330 |
3.64e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 40.37 E-value: 3.64e-04
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1728-1953 |
3.74e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.92 E-value: 3.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1728 LRRKNLETQKEIAEDElvaAEALLKKVKKlfgESRGENEEMEKDLREKLADYKNKVDdawdllREATDKIREANRLFA-V 1806
Cdd:PRK12704 24 VRKKIAEAKIKEAEEE---AKRILEEAKK---EAEAIKKEALLEAKEEIHKLRNEFE------KELRERRNELQKLEKrL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1807 NQKNMTaLEKKKEAVESGKRQIENTLKEGNDILDEANRLADEINSIIDYVEDIQTKLPPMSEElndkiddlsqEIKDRKL 1886
Cdd:PRK12704 92 LQKEEN-LDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAE----------EAKEILL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1677500969 1887 AEKVSQAESHAAQLndssavldgildeaknisfnataafkaysnIKDYIDEAEKVA-KEAKDLAHEAT 1953
Cdd:PRK12704 161 EKVEEEARHEAAVL------------------------------IKEIEEEAKEEAdKKAKEILAQAI 198
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1469-1525 |
4.19e-04 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 40.42 E-value: 4.19e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1677500969 1469 CACPLISSSNnfsPSCVAEGLddyRCTaCPRGYEGQYCERCAPGYTGSPGNPGGsCQ 1525
Cdd:cd00055 2 CDCNGHGSLS---GQCDPGTG---QCE-CKPNTTGRRCDRCAPGYYGLPSQGGG-CQ 50
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1740-1946 |
4.57e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.53 E-value: 4.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1740 AEDELVAAEALLKKVKKlfgesrgeneEMEKdLREKLADYKNKVDDAWDLLREATDKIREANRLFAVNQKNMTALEKKKE 1819
Cdd:COG4942 18 QADAAAEAEAELEQLQQ----------EIAE-LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1820 AVESGKRQIENTLKEGNDIL-------------------------DEANRLADEINSIIDYVEDIQTKLPPMSEELNDKI 1874
Cdd:COG4942 87 ELEKEIAELRAELEAQKEELaellralyrlgrqpplalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1677500969 1875 DDLSQEIKD--RKLAEKVSQAESHAAQLNDSSAVLDGILDEAKNISFNATAAFKAYSNIKDYIDEAEKVAKEAK 1946
Cdd:COG4942 167 AELEAERAEleALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1682-1902 |
5.49e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 44.91 E-value: 5.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1682 IKELAR---DAEAVNEKAIKLNETLGTRDEAFERNleglqKEIDQMIKELRRKNLETQKEI----AEDELVAAEALLKKV 1754
Cdd:pfam13868 8 LRELNSkllAAKCNKERDAQIAEKKRIKAEEKEEE-----RRLDEMMEEERERALEEEEEKeeerKEERKRYRQELEEQI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1755 KklfgesrgENEEMEKDLREKLADYKNKVDDAWDL-----LREATDKIREANRL------FAVNQKNMTALEKKKEAVEs 1823
Cdd:pfam13868 83 E--------EREQKRQEEYEEKLQEREQMDEIVERiqeedQAEAEEKLEKQRQLreeideFNEEQAEWKELEKEEEREE- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1824 gKRQIENTL--KEGNDILDEANRLAD------EINSIIDYVEDIQTKLppmsEELNDKIDDLSQEIKDRKLAEK-VSQAE 1894
Cdd:pfam13868 154 -DERILEYLkeKAEREEEREAEREEIeeekerEIARLRAQQEKAQDEK----AERDELRAKLYQEEQERKERQKeREEAE 228
|
....*...
gi 1677500969 1895 SHAAQLND 1902
Cdd:pfam13868 229 KKARQRQE 236
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1692-2057 |
6.80e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 45.71 E-value: 6.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1692 VNEKAIKLNETLGTRDEAFE--RNLEGLQKEIDQMIKEL-----RRKNLETQKEIAEDELVAAEALLKkvkklfgesrge 1764
Cdd:COG3096 277 ANERRELSERALELRRELFGarRQLAEEQYRLVEMARELeelsaRESDLEQDYQAASDHLNLVQTALR------------ 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1765 neemekdLREKLADYKNKVDDAWDLLREATDKIREANRLFAVNQknmTALEKKKEAVESGKRQIENtLKEGNDI------ 1838
Cdd:COG3096 345 -------QQEKIERYQEDLEELTERLEEQEEVVEEAAEQLAEAE---ARLEAAEEEVDSLKSQLAD-YQQALDVqqtrai 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1839 --------LDEANRLADEINSIIDYVEDIQtklppmsEELNDKIDDLSQEIkdRKLAEKVSQAESHAAQLNDSSAVLDGI 1910
Cdd:COG3096 414 qyqqavqaLEKARALCGLPDLTPENAEDYL-------AAFRAKEQQATEEV--LELEQKLSVADAARRQFEKAYELVCKI 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1911 LDEAknisfNATAAFkaysnikdyiDEAEKVAKEAKDLAHEATKLATgPRGLLKEdakgcLQKSFRILNEAKKLA----- 1985
Cdd:COG3096 485 AGEV-----ERSQAW----------QTARELLRRYRSQQALAQRLQQ-LRAQLAE-----LEQRLRQQQNAERLLeefcq 543
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1677500969 1986 ------NDVKENEDHLNGLKTRIENADarngDLLRTLNDTLGKLSAIPNDTAAKLQAVKDKArQANDTAKDVLAQITE 2057
Cdd:COG3096 544 rigqqlDAAEELEELLAELEAQLEELE----EQAAEAVEQRSELRQQLEQLRARIKELAARA-PAWLAAQDALERLRE 616
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1720-1890 |
9.45e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.82 E-value: 9.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1720 EIDQMIKEL--RRKNLETQKEIAEDELVAAEALLKKVKKLFgesrGENEEMEKDLREKLAD-YKNKVDDAwdlLREATDK 1796
Cdd:PRK00409 517 KLNELIASLeeLERELEQKAEEAEALLKEAEKLKEELEEKK----EKLQEEEDKLLEEAEKeAQQAIKEA---KKEADEI 589
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1797 IREANRLfavnQKNMTALEKKKEAVESGKRqientlkegndiLDEANRLADEInsiidyvediqtKLPPMSEELNDKIDD 1876
Cdd:PRK00409 590 IKELRQL----QKGGYASVKAHELIEARKR------------LNKANEKKEKK------------KKKQKEKQEELKVGD 641
|
170
....*....|....
gi 1677500969 1877 lsqEIKDRKLAEKV 1890
Cdd:PRK00409 642 ---EVKYLSLGQKG 652
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1641-1776 |
1.01e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.13 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1641 NTLVTEMNELLTRATKVtadgeqtgQDAERTNTRAKSLGEFIKEL---ARDA-EAVNEKAIKLNETLGTRDEAFERnLEG 1716
Cdd:COG1340 136 KELVEKIKELEKELEKA--------KKALEKNEKLKELRAELKELrkeAEEIhKKIKELAEEAQELHEEMIELYKE-ADE 206
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1677500969 1717 LQKEIDQM----------IKELRRKNLETQKEIAE--DELVAAEALLKKVKKlfGESRGENEEMEKDLREKL 1776
Cdd:COG1340 207 LRKEADELhkeiveaqekADELHEEIIELQKELRElrKELKKLRKKQRALKR--EKEKEELEEKAEEIFEKL 276
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1691-2134 |
1.35e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.56 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1691 AVNEKAIKLNETLGTRDEAFE--RNLEGLQKEIDQMIKEL-----RRKNLETQKEIAEDEL---VAAEALLKKVKKlfge 1760
Cdd:PRK04863 277 HANERRVHLEEALELRRELYTsrRQLAAEQYRLVEMARELaelneAESDLEQDYQAASDHLnlvQTALRQQEKIER---- 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1761 SRGENEEMEKDLREKLAdyknkvddawdlLREATDKIREANRlfavnqknmTALEKKKEAVESGKRQIENtLKEGNDILD 1840
Cdd:PRK04863 353 YQADLEELEERLEEQNE------------VVEEADEQQEENE---------ARAEAAEEEVDELKSQLAD-YQQALDVQQ 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1841 -------EANRLADEINSIIDYVEDIQTKLPPMSEELNDKIDDLSQEIkdRKLAEKVSQAESHAAQLndssavldgilde 1913
Cdd:PRK04863 411 traiqyqQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEEL--LSLEQKLSVAQAAHSQF------------- 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1914 aknisfnaTAAFKAYSNIKDYID--EAEKVAKE----AKDLAHEATKLAtGPRGLLKEdAKGCL---QKSFRILNEAKKL 1984
Cdd:PRK04863 476 --------EQAYQLVRKIAGEVSrsEAWDVAREllrrLREQRHLAEQLQ-QLRMRLSE-LEQRLrqqQRAERLLAEFCKR 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1985 ANDVKENEDHLNGLKTRIEnadarngdllrtlndtlgklsaipndtaAKLQAVKDKARQANdtakdvlAQITELHQNLDG 2064
Cdd:PRK04863 546 LGKNLDDEDELEQLQEELE----------------------------ARLESLSESVSEAR-------ERRMALRQQLEQ 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2065 LKKNYNKLA----------DSVAKTNAvvkdpsknkIIADADATVKNLEQEADRLIDKLKPIKELEDNLKKNISEIKELI 2134
Cdd:PRK04863 591 LQARIQRLAarapawlaaqDALARLRE---------QSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEI 661
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1684-1902 |
1.43e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 43.75 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1684 ELARDAEAVNEKAIKLNEtlgtRDEA-----FERNLEgLQKEIDQMIKEL-RRKNLETQKEIAEDELVAAEALLK--KVK 1755
Cdd:pfam13868 95 EKLQEREQMDEIVERIQE----EDQAeaeekLEKQRQ-LREEIDEFNEEQaEWKELEKEEEREEDERILEYLKEKaeREE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1756 KLFGESRGENEEMEKdLREKLADYKNKVDDAWDLLREATDKIREANRLFAVNQKNMTALEKKKEAvesgKRQIENTLKEg 1835
Cdd:pfam13868 170 EREAEREEIEEEKER-EIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQ----RQELQQAREE- 243
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1677500969 1836 nDILDEANRLADEINsiidyvEDIQTKLPPMseELNDKIDDLSQEIKDRKLAEKVSQAESHAAQLND 1902
Cdd:pfam13868 244 -QIELKERRLAEEAE------REEEEFERML--RKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEE 301
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1719-1892 |
1.51e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.06 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1719 KEIDQMIKELRRKNLETQKEIAEDELVAAEALLKKVkklfgesrgeNEEMEK--DLREKLADYKNKVDDAWDLLREATDK 1796
Cdd:PRK04778 252 LDIEKEIQDLKEQIDENLALLEELDLDEAEEKNEEI----------QERIDQlyDILEREVKARKYVEKNSDTLPDFLEH 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1797 IREANRLFA-----VNQkNMTALEKKKEAVESGKRQIENTLKEGNDILDE-ANR------LADEINSIIDYVEDIQTKlp 1864
Cdd:PRK04778 322 AKEQNKELKeeidrVKQ-SYTLNESELESVRQLEKQLESLEKQYDEITERiAEQeiayseLQEELEEILKQLEEIEKE-- 398
|
170 180
....*....|....*....|....*....
gi 1677500969 1865 pmSEELNDKIDDLSQ-EIKDRKLAEKVSQ 1892
Cdd:PRK04778 399 --QEKLSEMLQGLRKdELEAREKLERYRN 425
|
|
| TNFRSF16 |
cd13416 |
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 ... |
785-919 |
1.68e-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: 41.52 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 785 CDKCLPGFYGEPTKGTSEDCQPCA-CPLNIPsnnfsPTCHLDRSLGLICdgcpvgytgprceRCAEGYFgqPSVPGGSCQ 863
Cdd:cd13416 35 CEPCLDGVTFSDVVSHTEPCQPCTrCPGLMS-----MRAPCTATHDTVC-------------ECAYGYY--LDEDSGTCE 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1677500969 864 PCQcndnldfsipgSCDSLSGSCLICKPGTTGRyCELCADGYFGDAV-DAKNCQPCR 919
Cdd:cd13416 95 PCT-----------VCPPGQGVVQSCGPNQDTV-CEACPEGTYSDEDsSTDPCLPCT 139
|
|
| SerH |
pfam06873 |
Cell surface immobilization antigen SerH; This family consists of several cell surface ... |
884-1133 |
2.31e-03 |
|
Cell surface immobilization antigen SerH; This family consists of several cell surface immobilization antigen SerH proteins which seem to be specific to Tetrahymena thermophila. The SerH locus of Tetrahymena thermophila is one of several paralogous loci with genes encoding variants of the major cell surface protein known as the immobilization antigen (i-ag).
Pssm-ID: 284327 [Multi-domain] Cd Length: 418 Bit Score: 43.38 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 884 GSCLICKPGT--------TGRYCELCADGYFG--DAvdakNCQPCRCNAGGSFSEVCHSQTGQcECRANvqGQRCDKCKA 953
Cdd:pfam06873 123 GDCTLCNPSTpaavsdksTCVSCTACSSITSGwtDA----NCNACATTASPKGNNVFANSAGS-ACVAA--SASCGSTSR 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 954 GTFGLQSArGCVPCN-----CNSFGSKSFDCEESGQCWCQPGVTGKKCDRCAHGYFN-----FQEGGCTACECSHLGnnc 1023
Cdd:pfam06873 196 GSTAWTDA-DCLACTpatpyASADKSSCVASSCAACSTVTSGWTDSDCNACATTASPatknlFANAAGSSCVASSAS--- 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1024 dpKTGRCICPPNTIGEKCSKCAPNT------WGHSITTGCKACNCSTVGSLDFQCN--VNTGQCNCHPKF---------- 1085
Cdd:pfam06873 272 --CTTASRGTTAWTDSDCTLCTPSTpaasldASPCVVSSCVACNSITSGWTDANCNscAMTASPSTKNVFanadgsacva 349
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1086 SGAKCTECSRGH--WNYPRCNLCDcflpGT----------DATTCDSeTKKCSCSDQTGQ 1133
Cdd:pfam06873 350 SSYSCNQTARGSnkWTDADCALCN----GTasnanqyasaDGSSCQS-TKQSSSSTFSGQ 404
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1635-1883 |
2.47e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.77 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1635 LAEGNLNTLVTEMNELLTRATKVTADGEQTGQDAERTNTRAKSLGEFIKELARDAEAVNEKAIKLNETLGTRDEAFERNL 1714
Cdd:COG1196 627 LVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEE 706
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1715 EGLQKEIDQMIKELRRKNLETQKEIAEDELVAAEALlkkvkklfgESRGENEEMEKDLREKLADyknkVDDAWDLLREAT 1794
Cdd:COG1196 707 RELAEAEEERLEEELEEEALEEQLEAEREELLEELL---------EEEELLEEEALEELPEPPD----LEELERELERLE 773
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1795 DKIReanRLFAVNqknMTALEkkkEAVEsgkrqientLKEgndildeanRLadeinsiidyvediqtklppmsEELNDKI 1874
Cdd:COG1196 774 REIE---ALGPVN---LLAIE---EYEE---------LEE---------RY----------------------DFLSEQR 804
|
....*....
gi 1677500969 1875 DDLSQEIKD 1883
Cdd:COG1196 805 EDLEEARET 813
|
|
| F5_F8_type_C |
pfam00754 |
F5/8 type C domain; This domain is also known as the discoidin (DS) domain family. |
90-174 |
2.60e-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: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 90 SSNPNQRHPITNAIDGK-NTWWQSPSIKNGieyhyVTITLDLQQVFQIAYVIVKAANSPRPGN---WILERSLDDVEYKP 165
Cdd:pfam00754 5 SSSYSGEGPAAAALDGDpNTAWSAWSGDDP-----QWIQVDLGKPKKITGVVTQGRQDGSNGYvtsYKIEYSLDGENWTT 79
|
....*....
gi 1677500969 166 WQYHAVTDT 174
Cdd:pfam00754 80 VKDEKIPGN 88
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1613-1902 |
2.92e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.47 E-value: 2.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1613 ENMTQELKHLLSP---QRAPERLiQLAEGNLNTLVTE--MNELLTRATKVTADGEQ-------TGQDAERTNTRAKSLGE 1680
Cdd:COG3206 81 SPLETQIEILKSRpvlERVVDKL-NLDEDPLGEEASReaAIERLRKNLTVEPVKGSnvieisyTSPDPELAAAVANALAE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1681 -FIKELARDAEAVNEKAIK-LNETLgtrdEAFERNLEGLQKEIdqmiKELRRKN------------------LETQKEIA 1740
Cdd:COG3206 160 aYLEQNLELRREEARKALEfLEEQL----PELRKELEEAEAAL----EEFRQKNglvdlseeaklllqqlseLESQLAEA 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1741 EDELVAAEALLKKVKKLFGESRGENEEMEKDlrEKLADYKNKvddawdlLREATDKIREANRLFAVNQKNMTALEKKKEA 1820
Cdd:COG3206 232 RAELAEAEARLAALRAQLGSGPDALPELLQS--PVIQQLRAQ-------LAELEAELAELSARYTPNHPDVIALRAQIAA 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1821 VESGKRQientlkEGNDILDEANRladEINSIIDYVEDIQTKLppmsEELNDKIDDLSQeiKDRKLAEKVSQAESHAAQL 1900
Cdd:COG3206 303 LRAQLQQ------EAQRILASLEA---ELEALQAREASLQAQL----AQLEARLAELPE--LEAELRRLEREVEVARELY 367
|
..
gi 1677500969 1901 ND 1902
Cdd:COG3206 368 ES 369
|
|
| DivIVA |
pfam05103 |
DivIVA protein; The Bacillus subtilis divIVA1 mutation causes misplacement of the septum ... |
1738-1860 |
3.19e-03 |
|
DivIVA protein; The Bacillus subtilis divIVA1 mutation causes misplacement of the septum during cell division, resulting in the formation of small, circular, anucleate mini-cells. Inactivation of divIVA produces a mini-cell phenotype, whereas overproduction of DivIVA results in a filamentation phenotype. These proteins appear to contain coiled-coils.
Pssm-ID: 428304 [Multi-domain] Cd Length: 131 Bit Score: 40.24 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1738 EIAEDelvaAEALLKkvkklfgesrgENEEME---KDLREKLADYKNkvddawdllREatDKIREAnrlFAVNQKnmTAL 1814
Cdd:pfam05103 29 QVAED----YEALIR-----------ENAELKekiEELEEKLAHYKN---------LE--ETLQNT---LILAQE--TAE 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1815 EKKKEAvesgKRQIENTLKE----GNDILDEANRLADEINsiiDYVEDIQ 1860
Cdd:pfam05103 78 EVKANA----QKEAELIIKEaeakAERIVDDANNEVKKIN---DEIEELK 120
|
|
| 4HB_MCP_1 |
pfam12729 |
Four helix bundle sensory module for signal transduction; This family is a four helix bundle ... |
1609-1783 |
4.37e-03 |
|
Four helix bundle sensory module for signal transduction; This family is a four helix bundle that operates as a ubiquitous sensory module in prokaryotic signal-transduction. The 4HB_MCP is always found between two predicted transmembrane helices indicating that it detects only extracellular signals. In many cases the domain is associated with a cytoplasmic HAMP domain suggesting that most proteins carrying the bundle might share the mechanism of transmembrane signalling which is well-characterized in E coli chemoreceptors. This domain recognizes citrate and TCA cycle intermediates, cis-aconitate, boric acid, Phenanthrene, pyrene and benzopyrene (Matilla et el., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 432749 [Multi-domain] Cd Length: 181 Bit Score: 40.70 E-value: 4.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1609 LYGLENMTQELKHLLSpqrapERLIQLAE-GNLNTLVTEMNELLTRATKVTadgeqtgqDAERTNTRAKSLGEFIKElar 1687
Cdd:pfam12729 27 LYSLKQINDNLDTMYE-----DRLLPIKWlGDIRANLLELRANLLELILTT--------DPAERDELLKDIEELRAE--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1688 daeaVNEKAIKLNETLGTRDE-----AFERNLEGLQKEIDQMIKELRRKNLETqkeiaedelvAAEALLKKVKKLFgesr 1762
Cdd:pfam12729 91 ----IDKLLEKYEKTILTDEEkklfaEFKENLNAYRAVRNKVLELAKAGNKDE----------AYQLYKTEGRPAR---- 152
|
170 180
....*....|....*....|.
gi 1677500969 1763 genEEMEKDLrEKLADYKNKV 1783
Cdd:pfam12729 153 ---EAMIEAL-EELVDYNLKV 169
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
1696-1786 |
4.48e-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: 4.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1696 AIKLNETLGTRDEAFERNLEGLQKEIDQMIKELRRKN--LETQKEIAEDELVAAEALLKKVKKLFgesrgeNEEMEKDLR 1773
Cdd:pfam03938 17 GKAAQAQLEKKFKKRQAELEAKQKELQKLYEELQKDGalLEEEREEKEQELQKKEQELQQLQQKA------QQELQKKQQ 90
|
90
....*....|...
gi 1677500969 1774 EKLADYKNKVDDA 1786
Cdd:pfam03938 91 ELLQPIQDKINKA 103
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1708-1899 |
4.78e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 42.37 E-value: 4.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1708 EAFERNLEGLQKEIDQM---IKELRRKNLetqKEIAEDELVAAEALLKKVKKLFGESRG------ENE------------ 1766
Cdd:COG0497 175 EELRADEAERARELDLLrfqLEELEAAAL---QPGEEEELEEERRRLSNAEKLREALQEalealsGGEggaldllgqalr 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1767 EMEK--DLREKLADYKNKVDDAWDLLREATDKIR------EAN--RLFAVNQKnMTALE--KKKEAVEsgkrqIEntlke 1834
Cdd:COG0497 252 ALERlaEYDPSLAELAERLESALIELEEAASELRryldslEFDpeRLEEVEER-LALLRrlARKYGVT-----VE----- 320
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1677500969 1835 gnDILDEANRLADEINSIIDYVEDIqtklppmsEELNDKIDDLSQEIkdRKLAEKVSQAESHAAQ 1899
Cdd:COG0497 321 --ELLAYAEELRAELAELENSDERL--------EELEAELAEAEAEL--LEAAEKLSAARKKAAK 373
|
|
| TNFRSF9 |
cd13410 |
Tumor necrosis factor receptor superfamily member 9 (TNFRSF9), also known as CD137; TNFRSF9 ... |
948-1060 |
5.33e-03 |
|
Tumor necrosis factor receptor superfamily member 9 (TNFRSF9), also known as CD137; TNFRSF9 (also known as CD137, ILA, 4-1BB) plays a role in the immunobiology of human cancer where it is preferentially expressed on tumor-reactive subset of tumor-infiltrating lymphocytes. It can be expressed by activated T cells, but to a larger extent on CD8 than on CD4 T cells. In addition, CD137 expression is found on dendritic cells, follicular dendritic cells, natural killer cells, granulocytes and cells of blood vessel walls at sites of inflammation. It transduces signals that lead to the activation of NF-kappaB, mediated by the TRAF adaptor proteins. CD137 contributes to the clonal expansion, survival, and development of T cells. It can also induce proliferation in peripheral monocytes, enhance T cell apoptosis induced by TCR/CD3 triggered activation, and regulate CD28 co-stimulation to promote Th1 cell responses. CD137 is modulated by SAHA treatment in breast cancer cells, suggesting that the combination of SAHA with this receptor could be a new therapeutic approach for the treatment of tumors.
Pssm-ID: 276915 [Multi-domain] Cd Length: 138 Bit Score: 39.72 E-value: 5.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 948 CDKCKAGTF-GLQSARGCVPCNCNSFGSKsfdceeSGQCWCQpgvtgkKCDRCAhGYFNFQEggctacECSHLGNncdpk 1026
Cdd:cd13410 6 CSNCPAGTFcGKNKDQTCIPCPPNSFSST------GGQQTCD------ICRKCE-GVFRTKK------PCSSTSN----- 61
|
90 100 110
....*....|....*....|....*....|....*...
gi 1677500969 1027 tGRCICPP--NTIGEKCSKCAPN-TWGHSIT-TGCKAC 1060
Cdd:cd13410 62 -AECECVPgfHCLGPGCSMCEPDcKQGQELTkEGCKDC 98
|
|
| ClyA-like |
cd21116 |
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ... |
2028-2147 |
6.01e-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: 40.86 E-value: 6.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 2028 NDTAAKLQAVKDKARQANDTAKDVLAQITELHQNLDGLKKNYNKLADSVAKTNAVVKDPSKNkiiadadatVKNLEQEAD 2107
Cdd:cd21116 94 QQLLQGLEALQSQVTKKQTSVTSFINELTTFKNDLDDDSRNLQTDATKAQAQVAVLNALKNQ---------LNSLAEQID 164
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1677500969 2108 RLIDKLKPIKELEDNLKKNISEIKELINQARKQANSIKVS 2147
Cdd:cd21116 165 AAIDALEKLSNDWQTLDSDIKELITDLEDAESSIDAAFLQ 204
|
|
| TNFRSF4 |
cd13406 |
Tumor necrosis factor receptor superfamily member 4 (TNFRSF4), also known as CD134 or OXO40; ... |
886-973 |
6.85e-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: 39.69 E-value: 6.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 886 CLICKPG---------TTGRYCELCADGYFGDAVDAKNCQPC-RCNAGGSFSEV--C-HSQTGQCECRANVQ-------G 945
Cdd:cd13406 15 CHECPPGegmesrctgTQDTVCSPCEPGFYNEAVNYEPCKPCtQCNQRSGSEEKqkCtKTSDTVCRCRPGTQpldsykpG 94
|
90 100
....*....|....*....|....*....
gi 1677500969 946 QRCDKCKAGTFGLQSARGCVP-CNCNSFG 973
Cdd:cd13406 95 VDCVPCPPGHFSRGDNQACKPwTNCSLAG 123
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1674-1834 |
7.00e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.15 E-value: 7.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1674 RAKSLGEFIKELARDAEAVNEKAIKLNETlgtrdeAFERNLEGLQKEI---DQMIKELRRKNLETQKEIAE--DELVAAE 1748
Cdd:COG2433 374 RGLSIEEALEELIEKELPEEEPEAEREKE------HEERELTEEEEEIrrlEEQVERLEAEVEELEAELEEkdERIERLE 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677500969 1749 ALLKKVKklfgesRGENEEMEKDlrekladyknkvddawdllREATDKIREANRLfavnQKnmtALEKKKEAVESGKRQI 1828
Cdd:COG2433 448 RELSEAR------SEERREIRKD-------------------REISRLDREIERL----ER---ELEEERERIEELKRKL 495
|
....*.
gi 1677500969 1829 EnTLKE 1834
Cdd:COG2433 496 E-RLKE 500
|
|
| |
