|
Name |
Accession |
Description |
Interval |
E-value |
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
291-547 |
1.77e-97 |
|
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: 314.74 E-value: 1.77e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 291 VLSVSSGAAAHRHVNEINATIYLLKTKLSERENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLIQKESMDT 370
Cdd:pfam06008 1 LLSLNSLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 371 IKHASQLVEQAHDMRDKIQEINNKMLYYGEE-HELSPKEISEKLVLAQKMLEEIRRRQpFFTQRELVDEEADEAHELLSQ 449
Cdd:pfam06008 81 LGHAKELAEAIKNLIDNIKEINEKVATLGENdFALPSSDLSRMLAEAQRMLGEIRSRD-FGTQLQNAEAELKAAQDLLSR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 450 AESW-QRLHNETRTLFPVVLEQLDDYNAKLSDLQEALDQALNHVRDAEDMNRATAARQRDHEKQQERVREQMEAVNMSLN 528
Cdd:pfam06008 160 IQTWfQSPQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEETLK 239
|
250
....*....|....*....
gi 387540784 529 TSADSLTTPRLTLSELDDI 547
Cdd:pfam06008 240 TARDSLDAANLLLQEIDDA 258
|
|
| Laminin_II |
pfam06009 |
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 ... |
727-854 |
6.00e-44 |
|
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: 156.49 E-value: 6.00e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 727 SRLITEEANRTTMEVQQATAPMANNLTNWSQNLQHFDSSA---------YNTAVDSARDAVRNLTEVVPQLLDQLRTVEQ 797
Cdd:pfam06009 1 SKELAREANETAKEVLEQLAPLSQNLENTSEKLSGINRSLeetnelvndANKALDDAGRSVKKLEELAPDLLDKLKPLKQ 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 387540784 798 KRPAS-NVSASIQRIRELIAQTRSVASKIQVSMMFDGQSAVEVHSRTSMDDLKAFTSL 854
Cdd:pfam06009 81 LEVNSsSLSDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTSL 138
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
1485-1617 |
3.52e-40 |
|
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: 146.02 E-value: 3.52e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 1485 KSQFSIRLRTRSSHGMIFYVSDQEENDFMTLFLAHGRLVYMFNVGHKKLKIRSQEKYNDGLWHDVVFIREKSSGRLVIDG 1564
Cdd:cd00110 21 RLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDGQWHSVSVERNGRSVTLSVDG 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 387540784 1565 LRVLEESLPPTEATWKIKGPIYLGGVAPGKavKNVQINSIYSFSGCLSNLQLN 1617
Cdd:cd00110 101 ERVVESGSPGGSALLNLDGPLYLGGLPEDL--KSPGLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
1487-1618 |
1.92e-36 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 134.77 E-value: 1.92e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 1487 QFSIRLRTRSSHGMIFYVSDQEENDFMTLFLAHGRLVYMFNVGHKKLKIRSQ-EKYNDGLWHDVVFIREKSSGRLVIDGL 1565
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDpTPLNDGQWHRVAVERNGRSVTLSVDGG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 387540784 1566 RVLEESLPPTEATWKIKGPIYLGGVAPGKavKNVQINSIYSFSGCLSNLQLNG 1618
Cdd:smart00282 81 NRVSGESPGGLTILNLDGPLYLGGLPEDL--KLPPLPVTPGFRGCIRNLKVNG 131
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
1641-1792 |
2.82e-32 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 123.68 E-value: 2.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 1641 GTYFStEGGYVVLDESFNIGLKFEIAFEVRPRSSSGTLVH-GHSVNGEYLNVHMKNGQVIVKVNNGirDFSTSVTPKQSL 1719
Cdd:cd00110 1 GVSFS-GSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYaGSQNGGDFLALELEDGRLVLRYDLG--SGSLVLSSKTPL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 387540784 1720 CDGRWHRITVIRDSNVVQLDVDSE-VNHVVGPLNPKPIDHREPVFVGGVPESLLTPRLAPSKPFTGCIRHFVID 1792
Cdd:cd00110 78 NDGQWHSVSVERNGRSVTLSVDGErVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
1664-1794 |
3.59e-31 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 119.75 E-value: 3.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 1664 EIAFEVRPRSSSGTLVHGHSVNG-EYLNVHMKNGQVIVKVNNGIRDFSTSVTPKQsLCDGRWHRITVIRDSNVVQLDVDS 1742
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGgDYLALELRDGRLVLRYDLGSGPARLTSDPTP-LNDGQWHRVAVERNGRSVTLSVDG 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 387540784 1743 EvNHVVG--PLNPKPIDHREPVFVGGVPESLLTPRLAPSKPFTGCIRHFVIDGH 1794
Cdd:smart00282 80 G-NRVSGesPGGLTILNLDGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
1492-1618 |
5.44e-30 |
|
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: 115.98 E-value: 5.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 1492 LRTRSSHGMIFYVSDQEeNDFMTLFLAHGRLVYMFNVGHKKLKIRSQEK-YNDGLWHDVVFIREKSSGRLVIDGLRVLEE 1570
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGG-SDFLALELVNGRLVLRYDLGSGPESLLSSGKnLNDGQWHSVRVERNGNTLTLSVDGQTVVSS 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 387540784 1571 SLPPTEATWKIKGPIYLGGVAPGKAVKNVQINSiySFSGCLSNLQLNG 1618
Cdd:pfam02210 80 LPPGESLLLNLNGPLYLGGLPPLLLLPALPVRA--GFVGCIRDVRVNG 125
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
1669-1794 |
1.56e-28 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 111.74 E-value: 1.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 1669 VRPRSSSGTLVHGHSVNGEYLNVHMKNGQVIVKVNNGIRDFSTSVTPKqSLCDGRWHRITVIRDSNVVQLDVDSEVNH-V 1747
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDFLALELVNGRLVLRYDLGSGPESLLSSGK-NLNDGQWHSVRVERNGNTLTLSVDGQTVVsS 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 387540784 1748 VGPLNPKPIDHREPVFVGGVPESLLTPRLAPSKPFTGCIRHFVIDGH 1794
Cdd:pfam02210 80 LPPGESLLLNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
1493-1621 |
1.25e-24 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 100.85 E-value: 1.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 1493 RTRSSHGMIFYVSDQEENDFMTLFLAHGRLVYMFNVGHKKLKIRSQEKYNDGLWHDVVFIREKSSGRLVIDGLRVLE-ES 1571
Cdd:pfam00054 2 RTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTgES 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 387540784 1572 LPPTEATWKIKGPIYLGGvAPGKAVKNVQINSIYSFSGCLSNLQLNGASI 1621
Cdd:pfam00054 82 PLGATTDLDVDGPLYVGG-LPSLGVKKRRLAISPSFDGCIRDVIVNGKPL 130
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
1042-1200 |
1.04e-22 |
|
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: 96.33 E-value: 1.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 1042 SYFFDGSGYAAVRDitkRGKFGQVTRFDIEVRTPADNSLILLM--VNGSMFFRLEMRNGYLHVFYDFGfsSGPVHLEDtl 1119
Cdd:cd00110 1 GVSFSGSSYVRLPT---LPAPRTRLSISFSFRTTSPNGLLLYAgsQNGGDFLALELEDGRLVLRYDLG--SGSLVLSS-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 1120 kKAQINDAKYHEISIIyHNDKKMILVVDR-RHVKSMDNEKMKI--PFTDIYIGGAPPEILQSRTLRAHlpldiNFRGCMK 1196
Cdd:cd00110 74 -KTPLNDGQWHSVSVE-RNGRSVTLSVDGeRVVESGSPGGSALlnLDGPLYLGGLPEDLKSPGLPVSP-----GFVGCIR 146
|
....
gi 387540784 1197 GFQF 1200
Cdd:cd00110 147 DLKV 150
|
|
| LamG |
smart00282 |
Laminin G domain; |
1067-1203 |
2.59e-21 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 91.63 E-value: 2.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 1067 RFDIEVRTPADNSLILLM--VNGSMFFRLEMRNGYLHVFYDFGfsSGPVHLedTLKKAQINDAKYHEISIIyHNDKKMIL 1144
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAgsKGGGDYLALELRDGRLVLRYDLG--SGPARL--TSDPTPLNDGQWHRVAVE-RNGRSVTL 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 387540784 1145 VVD---RRHVKSMDNEKMKIPFTDIYIGGAPPEILQSRTLRAHlpldiNFRGCMKGFQFQKK 1203
Cdd:smart00282 76 SVDggnRVSGESPGGLTILNLDGPLYLGGLPEDLKLPPLPVTP-----GFRGCIRNLKVNGK 132
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
1230-1369 |
2.07e-20 |
|
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: 89.40 E-value: 2.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 1230 AYFNGQSFIASIQKISFFDGFEGGFNFRTLQPNGLLFYYASG--SDVFSISLDNGTVVMDV----KGIKVQSvDKQYNDG 1303
Cdd:cd00110 2 VSFSGSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQngGDFLALELEDGRLVLRYdlgsGSLVLSS-KTPLNDG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 387540784 1304 LSHFVIASVSPTRYELIVDKSRVGSKNPTKGKIEQTQagEKKFYFGGSPISAQ------YANFTGCISNAYF 1369
Cdd:cd00110 81 QWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNL--DGPLYLGGLPEDLKspglpvSPGFVGCIRDLKV 150
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
1072-1200 |
7.16e-20 |
|
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: 87.09 E-value: 7.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 1072 VRTPADNSLIL-LMVNGSMFFRLEMRNGYLHVFYDFGfsSGPVHLedTLKKAQINDAKYHEISIIYhNDKKMILVVDRRH 1150
Cdd:pfam02210 1 FRTRQPNGLLLyAGGGGSDFLALELVNGRLVLRYDLG--SGPESL--LSSGKNLNDGQWHSVRVER-NGNTLTLSVDGQT 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 387540784 1151 VKSMDNEKMKIPF---TDIYIGGAPPeilqsRTLRAHLPLDINFRGCMKGFQF 1200
Cdd:pfam02210 76 VVSSLPPGESLLLnlnGPLYLGGLPP-----LLLLPALPVRAGFVGCIRDVRV 123
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
1256-1369 |
8.17e-19 |
|
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: 84.01 E-value: 8.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 1256 FRTLQPNGLLFYYASG-SDVFSISLDNGTVVMDVK----GIKVQSVDKQYNDGLSHFVIASVSPTRYELIVDKSRVGSKN 1330
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGgSDFLALELVNGRLVLRYDlgsgPESLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 387540784 1331 PTKGKIEQTQagEKKFYFGG------SPISAQYANFTGCISNAYF 1369
Cdd:pfam02210 81 PPGESLLLNL--NGPLYLGGlpplllLPALPVRAGFVGCIRDVRV 123
|
|
| LamG |
smart00282 |
Laminin G domain; |
853-1006 |
5.27e-18 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 82.00 E-value: 5.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 853 SLSLYMKppvrqpelTETADQFILYLGSKNaKKEYMGLAIKNDNLVYIYNLGTKDVEIPLDSKPVSswPAYFSIVKIERV 932
Cdd:smart00282 1 SISFSFR--------TTSPNGLLLYAGSKG-GGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLN--DGQWHRVAVERN 69
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 387540784 933 GKHgkVFLTVPSLSSTAEEKFIKKgefsgddSLLDLDpedTVFYVGGVPSNFKLPNSLNLPGFVGCLELATLNN 1006
Cdd:smart00282 70 GRS--VTLSVDGGNRVSGESPGGL-------TILNLD---GPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNG 131
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
828-1005 |
8.98e-18 |
|
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: 82.08 E-value: 8.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 828 SMMFDGQSAVEVhsrTSMDDLKAFTSLSLYMKppvrqpelTETADQFILYLGSKNaKKEYMGLAIKNDNLVYIYNLGTKD 907
Cdd:cd00110 1 GVSFSGSSYVRL---PTLPAPRTRLSISFSFR--------TTSPNGLLLYAGSQN-GGDFLALELEDGRLVLRYDLGSGS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 908 VEIpldSKPVSSWPAYFSIVKIERVGKHgkVFLTVPSLSStaeekfikkGEFSGDDSLLDLDPEDTVfYVGGVPSNFKLP 987
Cdd:cd00110 69 LVL---SSKTPLNDGQWHSVSVERNGRS--VTLSVDGERV---------VESGSPGGSALLNLDGPL-YLGGLPEDLKSP 133
|
170
....*....|....*...
gi 387540784 988 NSLNLPGFVGCLELATLN 1005
Cdd:cd00110 134 GLPVSPGFVGCIRDLKVN 151
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
1669-1796 |
5.35e-16 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 76.20 E-value: 5.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 1669 VRPRSSSGTLVHGHSVN-GEYLNVHMKNGQVIVKVNNGIRdfSTSVTPKQSLCDGRWHRITVIRDSNVVQLDVDSEVNHV 1747
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTeRDFLALELRDGRLEVSYDLGSG--AAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPT 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 387540784 1748 V-GPLNPK-PIDHREPVFVGGVPESLLTPRLAP-SKPFTGCIRHFVIDGHPV 1796
Cdd:pfam00054 79 GeSPLGATtDLDVDGPLYVGGLPSLGVKKRRLAiSPSFDGCIRDVIVNGKPL 130
|
|
| LamG |
smart00282 |
Laminin G domain; |
1254-1372 |
6.76e-16 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 75.84 E-value: 6.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 1254 FNFRTLQPNGLLFYYAS--GSDVFSISLDNGTVVMDVKG----IKVQSVDKQYNDGLSHFVIASVSPTRYELIVDksrvg 1327
Cdd:smart00282 4 FSFRTTSPNGLLLYAGSkgGGDYLALELRDGRLVLRYDLgsgpARLTSDPTPLNDGQWHRVAVERNGRSVTLSVD----- 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 387540784 1328 SKNPTKGKIEQTQAG---EKKFYFGGSP------ISAQYANFTGCISNAYFTRV 1372
Cdd:smart00282 79 GGNRVSGESPGGLTIlnlDGPLYLGGLPedlklpPLPVTPGFRGCIRNLKVNGK 132
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
187-238 |
7.46e-16 |
|
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: 73.16 E-value: 7.46e-16
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 387540784 187 CDCSGNSDPNlifEDCDEVTGQCRnCLRNTTGFKCERCAPGYYGDARIAKNC 238
Cdd:cd00055 2 CDCNGHGSLS---GQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
187-232 |
4.61e-14 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 67.76 E-value: 4.61e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 387540784 187 CDCSGNSDPNlifEDCDEVTGQCRnCLRNTTGFKCERCAPGYYGDA 232
Cdd:pfam00053 1 CDCNPHGSLS---DTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLP 42
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
272-716 |
1.31e-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: 76.30 E-value: 1.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 272 DLTDDLRLAALSIEEGKsgVLSVSSGAAAHRHVNEINATIYLL----KTKLSERENQYALRKIQINNAENTMKSLLSDVE 347
Cdd:pfam05483 187 DLNNNIEKMILAFEELR--VQAENARLEMHFKLKEDHEKIQHLeeeyKKEINDKEKQVSLLLIQITEKENKMKDLTFLLE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 348 ELVEKENQASRKGQLiQKESMdtikhaSQLVEQAHDMRDKIQEINNKMlyygEEHELSPKEISEKLVLAQKMLEEIRRRQ 427
Cdd:pfam05483 265 ESRDKANQLEEKTKL-QDENL------KELIEKKDHLTKELEDIKMSL----QRSMSTQKALEEDLQIATKTICQLTEEK 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 428 PffTQRELVDeEADEAH---------------ELLSQAEswQRLHNETRTLFPVVLEqlddYNAKLSDLQEALDQALNHV 492
Cdd:pfam05483 334 E--AQMEELN-KAKAAHsfvvtefeattcsleELLRTEQ--QRLEKNEDQLKIITME----LQKKSSELEEMTKFKNNKE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 493 RDAEDMNRATAARQR--DHEKQQERVREQMEAVNMSLntsADSLTTPRLTLSELD---DIIKNASGIYA-EIDGAKNELQ 566
Cdd:pfam05483 405 VELEELKKILAEDEKllDEKKQFEKIAEELKGKEQEL---IFLLQAREKEIHDLEiqlTAIKTSEEHYLkEVEDLKTELE 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 567 -VKLSNLSNLSH---------DLVQEAIDHAQEL--QQE---ANELSRKLHSSDMNGLVQKALDASNVYENIVNYVSEAN 631
Cdd:pfam05483 482 kEKLKNIELTAHcdklllenkELTQEASDMTLELkkHQEdiiNCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKG 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 632 ETAEFALnttDRIYDAVSGIDTQIIYHKDESENLLNQARELQAKAEsssdeavaDTSRRVGGALARKSALKTRLSDAVKQ 711
Cdd:pfam05483 562 DEVKCKL---DKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIE--------NKNKNIEELHQENKALKKKGSAENKQ 630
|
....*
gi 387540784 712 LQAAE 716
Cdd:pfam05483 631 LNAYE 635
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
318-814 |
8.84e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 73.54 E-value: 8.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 318 LSERENQYALRKIQINNAE--------NTMKSLLSDVEELVEKENQasrkgqliQKESMDTIKHASQLVEQAHdmRDKIQ 389
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEEKEekdlherlNGLESELAELDEEIERYEE--------QREQARETRDEADEVLEEH--EERRE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 390 EInnkmlyygEEHELSPKEISEKLVLAQKMLEEIRRRqpFFTQRELVDEEADEAHELLSQAEsWQRLHNETrtlfpvVLE 469
Cdd:PRK02224 252 EL--------ETLEAEIEDLRETIAETEREREELAEE--VRDLRERLEELEEERDDLLAEAG-LDDADAEA------VEA 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 470 QLDDYNAKLSDLQEALDQALNHVRDAEdmNRATAARQR--DHEKQQERVREQMEAVNMSLNTSADSLTTPRLTLSELDDI 547
Cdd:PRK02224 315 RREELEDRDEELRDRLEECRVAAQAHN--EEAESLREDadDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 548 IKNASGIYA----EIDGAKNELQVKLSNLSNLSHDL---------VQEAIDHAQELQQEAN------------------- 595
Cdd:PRK02224 393 IEELRERFGdapvDLGNAEDFLEELREERDELREREaeleatlrtARERVEEAEALLEAGKcpecgqpvegsphvetiee 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 596 ------ELSRKLhsSDMNGLVQKALDASNVYENIVNYVSEANETAEFALNTTDRIYDAVSGIDTQiiyhKDESENLLNQA 669
Cdd:PRK02224 473 drerveELEAEL--EDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEK----RERAEELRERA 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 670 RELQAKAESSSDEAV-----ADTSRRVGGAL-ARKSALKTRLsDAVKQL--QAAERGDAQQRLGqsRLITEEANRTTMEV 741
Cdd:PRK02224 547 AELEAEAEEKREAAAeaeeeAEEAREEVAELnSKLAELKERI-ESLERIrtLLAAIADAEDEIE--RLREKREALAELND 623
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 387540784 742 QQatapmANNLTNWSQNLQHFDSSAYNTAVDSARDAVRNLTEVVPQLLDQLRTVEQKRPA-----SNVSASIQRIREL 814
Cdd:PRK02224 624 ER-----RERLAEKRERKRELEAEFDEARIEEAREDKERAEEYLEQVEEKLDELREERDDlqaeiGAVENELEELEEL 696
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
132-185 |
1.56e-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: 63.53 E-value: 1.56e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 387540784 132 CPCPlPHlANFAESCYRKNGavRCICKENYAGPNCERCAPGYYGNPlLIGITCK 185
Cdd:cd00055 2 CDCN-GH-GSLSGQCDPGTG--QCECKPNTTGRRCDRCAPGYYGLP-SQGGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
132-184 |
1.96e-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: 63.14 E-value: 1.96e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 387540784 132 CPCPlpHLANFAESCYRKNGavRCICKENYAGPNCERCAPGYYGNPLLIGITC 184
Cdd:pfam00053 1 CDCN--PHGSLSDTCDPETG--QCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
132-177 |
2.83e-12 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 62.71 E-value: 2.83e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 387540784 132 CPCPLPHlaNFAESCYRKNGavRCICKENYAGPNCERCAPGYYGNP 177
Cdd:smart00180 1 CDCDPGG--SASGTCDPDTG--QCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
187-231 |
3.86e-12 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 62.33 E-value: 3.86e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 387540784 187 CDCS--GNSDPnlifeDCDEVTGQCRnCLRNTTGFKCERCAPGYYGD 231
Cdd:smart00180 1 CDCDpgGSASG-----TCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD 41
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
314-640 |
4.88e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 71.63 E-value: 4.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 314 LKTKLSERENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLIQKESMDTIKHASQLVEQA--HDMRDKIQEI 391
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKqiLRERLANLER 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 392 NNKML-YYGEEHELSPKEISEKLVLAQKMLEEIRrrqpffTQRELVDEEADEAHELLSQAESwqrlHNETRTlfpvvlEQ 470
Cdd:TIGR02168 317 QLEELeAQLEELESKLDELAEELAELEEKLEELK------EELESLEAELEELEAELEELES----RLEELE------EQ 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 471 LDDYNAKLSDLQEALDQALNHVRDAED-MNRATAARQRDHEKQQERVRE----QMEAVNMSLNTSADSLTTprlTLSELD 545
Cdd:TIGR02168 381 LETLRSKVAQLELQIASLNNEIERLEArLERLEDRRERLQQEIEELLKKleeaELKELQAELEELEEELEE---LQEELE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 546 DIIKNASGIYAEIDGAKNELQVKLSNLSNLSH--DLVQEAIDHAQELQQEANELsrKLHSSDMNGLVQKALDASNV---Y 620
Cdd:TIGR02168 458 RLEEALEELREELEEAEQALDAAERELAQLQArlDSLERLQENLEGFSEGVKAL--LKNQSGLSGILGVLSELISVdegY 535
|
330 340
....*....|....*....|....*....
gi 387540784 621 E---------NIVNYVSEANETAEFALNT 640
Cdd:TIGR02168 536 EaaieaalggRLQAVVVENLNAAKKAIAF 564
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
1072-1196 |
2.36e-11 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 63.10 E-value: 2.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 1072 VRTPADNSLILLM--VNGSMFFRLEMRNGYLHVFYDFGfsSGPVHLEdtlKKAQINDAKYHEISIIYhNDKKMILVVDRR 1149
Cdd:pfam00054 1 FRTTEPSGLLLYNgtQTERDFLALELRDGRLEVSYDLG--SGAAVVR---SGDKLNDGKWHSVELER-NGRSGTLSVDGE 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 387540784 1150 HVKSMDNEK---MKIPF-TDIYIGGAPPEIlqsrTLRAHLPLDINFRGCMK 1196
Cdd:pfam00054 75 ARPTGESPLgatTDLDVdGPLYVGGLPSLG----VKKRRLAISPSFDGCIR 121
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
81-130 |
4.81e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 59.29 E-value: 4.81e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 387540784 81 PCDCNGN---SNKCLDGSGFCvHCQRNTTGEHCEKCLDGYIGDSIRGAPrfCQ 130
Cdd:cd00055 1 PCDCNGHgslSGQCDPGTGQC-ECKPNTTGRRCDRCAPGYYGLPSQGGG--CQ 50
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
868-1006 |
1.55e-10 |
|
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: 60.51 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 868 TETADQFILYLGSKnaKKEYMGLAIKNDNLVYIYNLGTKDVEIPLDSKPVS--SWpayfSIVKIERVGKHgkVFLTVPSL 945
Cdd:pfam02210 3 TRQPNGLLLYAGGG--GSDFLALELVNGRLVLRYDLGSGPESLLSSGKNLNdgQW----HSVRVERNGNT--LTLSVDGQ 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 387540784 946 SSTAEEKfikkgefSGDDSLLDLDpedTVFYVGGVPSNFKLPNSLNLPGFVGCLELATLNN 1006
Cdd:pfam02210 75 TVVSSLP-------PGESLLLNLN---GPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVNG 125
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
314-736 |
2.55e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.73 E-value: 2.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 314 LKTKLSERENQYALRKIQinNAENTMKSLLSDVEELVEKENQASRKGQLIQKESMDTIKHASQLVEQAHDMRDKIQEINN 393
Cdd:COG1196 218 LKEELKELEAELLLLKLR--ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 394 KMLyyGEEHELSPKEisEKLVLAQKMLEEIRRRqpfftQRELVDEEADEAHELLSQAESWQRLHNETRTLfpvvLEQLDD 473
Cdd:COG1196 296 ELA--RLEQDIARLE--ERRRELEERLEELEEE-----LAELEEELEELEEELEELEEELEEAEEELEEA----EAELAE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 474 YNAKLSDLQEALDQALNHVRDAEDMNRATAARQRDHEKQQERVREQMEAVNMSLNTSADSLTTPRLTLSELDDIIKNASG 553
Cdd:COG1196 363 AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 554 IYAEIDGAKNELQVKLSNLSNLSHDLVQEAIDHAQELQQEANELSRKLHSSDMnglvqkALDASNVYENIVNYVSEANET 633
Cdd:COG1196 443 ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL------LLEAEADYEGFLEGVKAALLL 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 634 AEFALnttdriydaVSGIDTQIIYHKDESENLLNQARELQAKAESSSDEAVADtsRRVGGALARKSALKTRL-SDAVKQL 712
Cdd:COG1196 517 AGLRG---------LAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAA--AAIEYLKAAKAGRATFLpLDKIRAR 585
|
410 420
....*....|....*....|....
gi 387540784 713 QAAERGDAQQRLGQSRLITEEANR 736
Cdd:COG1196 586 AALAAALARGAIGAAVDLVASDLR 609
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
295-826 |
3.09e-10 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 65.52 E-value: 3.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 295 SSGAAAHRHVNEINATIYLLKTKLSERENQYALRKIQINNA--------ENTMKSLLSDVE----ELVEKENQASRKGQL 362
Cdd:pfam15921 217 SLGSAISKILRELDTEISYLKGRIFPVEDQLEALKSESQNKielllqqhQDRIEQLISEHEveitGLTEKASSARSQANS 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 363 IQKEsMDTIKHA-----SQLVEQAHDMRDKIQEINNKMLYYGEEHELSPKEISEKLVLAQKMLEEIRRRQPFFTQRE--- 434
Cdd:pfam15921 297 IQSQ-LEIIQEQarnqnSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESgnl 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 435 -------LVDEEADEAHELLSQAES---WQRLHNETRTLfPVVLEQLDDYNAKLSDLqEALDQALNHVRDAEdMNRATAA 504
Cdd:pfam15921 376 ddqlqklLADLHKREKELSLEKEQNkrlWDRDTGNSITI-DHLRRELDDRNMEVQRL-EALLKAMKSECQGQ-MERQMAA 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 505 RQRDHEKQQE----------------RVREQMEAVNMSLNTSADSLTTPRLTLSELDDIIKNASgiyAEIDGAKNELQVK 568
Cdd:pfam15921 453 IQGKNESLEKvssltaqlestkemlrKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATN---AEITKLRSRVDLK 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 569 LSNLSNLSHDLvqeaiDHAQELQQEANELSRKLHSSD--MNGLVQKaldasnvYENIVNYVSEANETAefalnttdriyd 646
Cdd:pfam15921 530 LQELQHLKNEG-----DHLRNVQTECEALKLQMAEKDkvIEILRQQ-------IENMTQLVGQHGRTA------------ 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 647 avsgidTQIIYHKDESENLLNQAR-ELQakaESSSDEAVADTSRRvggalarksALKTRLSD----AVKQLQAaergdAQ 721
Cdd:pfam15921 586 ------GAMQVEKAQLEKEINDRRlELQ---EFKILKDKKDAKIR---------ELEARVSDleleKVKLVNA-----GS 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 722 QRLGQSRLITEEANRTTMEVQQATAPMaNNLTNWSQNLQ-HF--DSSAYNTAVDSARDAVRNLTEVVPQLLDQLRTVE-Q 797
Cdd:pfam15921 643 ERLRAVKDIKQERDQLLNEVKTSRNEL-NSLSEDYEVLKrNFrnKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEgS 721
|
570 580 590
....*....|....*....|....*....|
gi 387540784 798 KRPASNVSASIQR-IRELIAQTRSVASKIQ 826
Cdd:pfam15921 722 DGHAMKVAMGMQKqITAKRGQIDALQSKIQ 751
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
304-603 |
6.55e-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: 64.31 E-value: 6.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 304 VNEINATIYLLKTKLSERENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLIQKESMDTIKHASQLVEQAHD 383
Cdd:TIGR02168 693 IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE 772
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 384 MRDKIQEINNKMlyygEEHELSPKEISEKLVLAQKMLEEIRRRqpFFTQRELVDEEADEAHELLSQAESWQRLHNETRTL 463
Cdd:TIGR02168 773 AEEELAEAEAEI----EELEAQIEQLKEELKALREALDELRAE--LTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 464 FPVVLEQLDDYNAKLSDLQEALDQAlnhvrdAEDMNRATAARQRdHEKQQERVREQMEAVNMSLNTSADSLTTPRLTLSE 543
Cdd:TIGR02168 847 IEELSEDIESLAAEIEELEELIEEL------ESELEALLNERAS-LEEALALLRSELEELSEELRELESKRSELRRELEE 919
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 544 LDDIIKNASgiyAEIDGAKNELQVKLSNLSNLSHDLVQEAIDHAQELQQEANELSRKLHS 603
Cdd:TIGR02168 920 LREKLAQLE---LRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKR 976
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
320-742 |
1.07e-09 |
|
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: 63.69 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 320 ERENQYALRKIqINNAENTMKSLLSDVEELVEKENQASRKGQLIQKESMDTIKhasQL-VEQAHD--MRDKIQEInnkml 396
Cdd:pfam10174 224 DPAKTKALQTV-IEMKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIK---QMeVYKSHSkfMKNKIDQL----- 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 397 yygeEHELSPKEiSEKLVLaQKMLEEIRRRQPFFTQRELVDEEADEAHEllsqaeswQR---LHNETRTLfPVVLEQ--- 470
Cdd:pfam10174 295 ----KQELSKKE-SELLAL-QTKLETLTNQNSDCKQHIEVLKESLTAKE--------QRaaiLQTEVDAL-RLRLEEkes 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 471 -LDDYNAKLSDLQEALDQALNHVRDAEDM----NRATAARQ----------RDHEKQQERVREQMEAVNMSLNTSADSLT 535
Cdd:pfam10174 360 fLNKKTKQLQDLTEEKSTLAGEIRDLKDMldvkERKINVLQkkienlqeqlRDKDKQLAGLKERVKSLQTDSSNTDTALT 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 536 TPRLTLSELDDIIKNASGIYA--------EIDGAKNELQVKLSNLSNLSHDL------VQEAIDHAQELQQEANELSRKL 601
Cdd:pfam10174 440 TLEEALSEKERIIERLKEQREredrerleELESLKKENKDLKEKVSALQPELtekessLIDLKEHASSLASSGLKKDSKL 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 602 HSSDMNglVQKALDASNVYENIVNYVSEANETAEFALNTTDRIydavSGIDTQIIYHKDES-------ENLLNQARELQA 674
Cdd:pfam10174 520 KSLEIA--VEQKKEECSKLENQLKKAHNAEEAVRTNPEINDRI----RLLEQEVARYKEESgkaqaevERLLGILREVEN 593
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 387540784 675 KaESSSDEAVADTSRRVggalARKSALKTRLSDAVKQLQAAERGDAQQRLGQSRLITEEANRTTMEVQ 742
Cdd:pfam10174 594 E-KNDKDKKIAELESLT----LRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQ 656
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
304-744 |
1.88e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.03 E-value: 1.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 304 VNEINATIYLLKTKLSERENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLIQKESMDTIKHASQLVEQAHD 383
Cdd:COG1196 283 LEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 384 MRDKIQEINNKMLyyGEEHELSpKEISEKLVLAQKMLEEIRRRQpffTQRELVDEEADEAHELLSQAESWQRLHNETRTL 463
Cdd:COG1196 363 AEEALLEAEAELA--EAEEELE-ELAEELLEALRAAAELAAQLE---ELEEAEEALLERLERLEEELEELEEALAELEEE 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 464 FPVVLEQLDDYNAKLSDLQEALDQALNHVRDAE------DMNRATAARQRDHEKQQERVREQMEAVNMSLNTSADSLTTP 537
Cdd:COG1196 437 EEEEEEALEEAAEEEAELEEEEEALLELLAELLeeaallEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLL 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 538 RLTLSELDDIIKNASGIYAEIDGAKNELQVKLSNLSNLSHDLVQEAIDHAQE-----------LQQEANELSRKLHSSDM 606
Cdd:COG1196 517 AGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAakagratflplDKIRARAALAAALARGA 596
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 607 NGLVQKALDASNVYENIVNYV-----------SEANETAEFALNTTDRIYDAVSGIDTQIIYHKDESENLLNQARELQAK 675
Cdd:COG1196 597 IGAAVDLVASDLREADARYYVlgdtllgrtlvAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLE 676
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 387540784 676 AESSSDEAVADTSRRVGGALARKSALKTRLSDAVKQLQAAERGDAQQRLGQSRLITEEANRTTMEVQQA 744
Cdd:COG1196 677 AEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEE 745
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
82-129 |
3.09e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 54.28 E-value: 3.09e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 387540784 82 CDCNGN---SNKCLDGSGFCvHCQRNTTGEHCEKCLDGYIGDSIrGAPRFC 129
Cdd:pfam00053 1 CDCNPHgslSDTCDPETGQC-LCKPGVTGRHCDRCKPGYYGLPS-DPPQGC 49
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
311-738 |
4.65e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.49 E-value: 4.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 311 IYLLKTKLSERENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLIQKESMDTIKHASQLVEQAHDMRDKIQE 390
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 391 INNKMLYYGEEHElspkEISEKLVLAQKMLEEIrrrqpfftQRELVDEEADEAHELLSQAESWQRLHNETRTLFPVVLEQ 470
Cdd:COG1196 314 LEERLEELEEELA----ELEEELEELEEELEEL--------EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 471 LDDYNAKLSDLQEALDQAlNHVRDAEDMNRATAARQRDHEKQQERVREQMEAVNMSLNTSADSLTTPRLTLSELDDIIKN 550
Cdd:COG1196 382 EELAEELLEALRAAAELA-AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 551 ASGIYAEIDGAKNELQVKLSNLSNLSHDLVQ--EAIDHAQELQQEANELSRKLHSSDMNGLVQKALDAsnvyENIVNYVS 628
Cdd:COG1196 461 LLELLAELLEEAALLEAALAELLEELAEAAArlLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAV----LIGVEAAY 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 629 EANETAEFALNTTDRIYDAVSGIDTQIIYHKDESEN-----LLNQARELQAKAESSSDEAVADTSRRVGGALARKSALKT 703
Cdd:COG1196 537 EAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGratflPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYY 616
|
410 420 430
....*....|....*....|....*....|....*
gi 387540784 704 RLSDAVkQLQAAERGDAQQRLGQSRLITEEANRTT 738
Cdd:COG1196 617 VLGDTL-LGRTLVAARLEAALRRAVTLAGRLREVT 650
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
82-121 |
9.65e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 52.70 E-value: 9.65e-09
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 387540784 82 CDCNGN---SNKCLDGSGFCvHCQRNTTGEHCEKCLDGYIGDS 121
Cdd:smart00180 1 CDCDPGgsaSGTCDPDTGQC-ECKPNVTGRRCDRCAPGYYGDG 42
|
|
| TNFRSF16 |
cd13416 |
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 ... |
65-257 |
9.77e-09 |
|
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: 56.16 E-value: 9.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 65 EKCNAGFFRTlSGECvpCDcngnsnKCLDGSGFCVHCQRNTTGehCEKCLDGYIGDSIRGAPRFCQLC-PCPlpHLANFA 143
Cdd:cd13416 1 EACPSGQYTS-SGEC--CE------QCPPGEGVARPCGDNQTV--CEPCLDGVTFSDVVSHTEPCQPCtRCP--GLMSMR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 144 ESCYRKNGAVrcickenyagpnCErCAPGYYGNPLliGITCKKCDCsgnsdpnlifedCDEVTGQCRNC--LRNTtgfKC 221
Cdd:cd13416 68 APCTATHDTV------------CE-CAYGYYLDED--SGTCEPCTV------------CPPGQGVVQSCgpNQDT---VC 117
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 387540784 222 ERCAPGYYGDARIAKN----CAVCncggGPCDSVTGECLE 257
Cdd:cd13416 118 EACPEGTYSDEDSSTDpclpCTVC----EDGEVELRECTP 153
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
305-521 |
1.84e-08 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 58.00 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 305 NEINATIYLLKTKLSERENQYAlrkiQINNAENTMKSLLSDVEEL----------VEKENQ----ASRKGQLIQ--KESM 368
Cdd:COG1340 81 DELNEKLNELREELDELRKELA----ELNKAGGSIDKLRKEIERLewrqqtevlsPEEEKElvekIKELEKELEkaKKAL 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 369 DTIKHASQLVEQAHDMRDKIQEINNKMlyygeehelspKEISEKlvlAQKMLEEIrrrQPFFTQRELVDEEADEAHELLS 448
Cdd:COG1340 157 EKNEKLKELRAELKELRKEAEEIHKKI-----------KELAEE---AQELHEEM---IELYKEADELRKEADELHKEIV 219
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 387540784 449 QA-ESWQRLHnetrtlfpvvlEQLDDYNAKLSDLQEALDQALNHVRDAEdmnrataaRQRDHEKQQERVREQME 521
Cdd:COG1340 220 EAqEKADELH-----------EEIIELQKELRELRKELKKLRKKQRALK--------REKEKEELEEKAEEIFE 274
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
312-724 |
1.89e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.40 E-value: 1.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 312 YLLKTKLseRENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLIQKESmdtikhasQLVEQAHDMRDKIQEI 391
Cdd:COG4717 45 AMLLERL--EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELE--------ELEEELEELEAELEEL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 392 NNKMLYYGEEHELSP-----KEISEKLVLAQKMLEEIRRRQPFFTQRElvdEEADEAHELLSQAEswQRLHNETRTLFPV 466
Cdd:COG4717 115 REELEKLEKLLQLLPlyqelEALEAELAELPERLEELEERLEELRELE---EELEELEAELAELQ--EELEELLEQLSLA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 467 VLEQLDDYNAKLSDLQEALDQALNHVRDAEDmNRATAARQRD-------HEKQQERVREQM-----EAVNMSLNTSADSL 534
Cdd:COG4717 190 TEEELQDLAEELEELQQRLAELEEELEEAQE-ELEELEEELEqleneleAAALEERLKEARlllliAAALLALLGLGGSL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 535 TTPRLTL----------------------SELDDIIKNASGIYAEIDGAKNELQVKLSNL---SNLSHDLVQEAIDHAQE 589
Cdd:COG4717 269 LSLILTIagvlflvlgllallflllarekASLGKEAEELQALPALEELEEEELEELLAALglpPDLSPEELLELLDRIEE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 590 LQQ---EANELSRKLHSSDMNGLVQKALDASNV-----YENIVNYVSEANETAEfalnttdriydAVSGIDTQIIYHKDE 661
Cdd:COG4717 349 LQEllrEAEELEEELQLEELEQEIAALLAEAGVedeeeLRAALEQAEEYQELKE-----------ELEELEEQLEELLGE 417
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 387540784 662 SENLLNQARELQAKAE-SSSDEAVADTSRRVGGALARKSALKTRLSDAVKQLQAAERGDAQQRL 724
Cdd:COG4717 418 LEELLEALDEEELEEElEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEEL 481
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
418-824 |
2.05e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.57 E-value: 2.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 418 KMLEEI--------RRRQpffTQRELvdEEADE--------AHELLSQ----------AESWQRLHNETRtlfpvVLE-- 469
Cdd:COG1196 159 AIIEEAagiskykeRKEE---AERKL--EATEEnlerlediLGELERQleplerqaekAERYRELKEELK-----ELEae 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 470 ----QLDDYNAKLSDLQEALDQALNHVRDAEdmnrataARQRDHEKQQERVREQMEAVNMSLNTSADSLttpRLTLSELd 545
Cdd:COG1196 229 llllKLRELEAELEELEAELEELEAELEELE-------AELAELEAELEELRLELEELELELEEAQAEE---YELLAEL- 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 546 diiknasgiyAEIDGAKNELQVKLSNLSNLSHDLVQEAIDHAQELQQEANELSRKLHSSDMngLVQKALDASNVYENIVN 625
Cdd:COG1196 298 ----------ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE--AEEELEEAEAELAEAEE 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 626 YVSEANETAEFALNTTDRIYDAVSGIDTQIIYHKDESENLLNQARELQAKAESSSDEAVADTSRRVGGALARKSALKTRL 705
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 706 SDAVKQLQAAERGDAQQR----LGQSRLITEEANRTTMEVQQATAPMANNLTNWSQNLQHFDSSAyntavdsARDAVRNL 781
Cdd:COG1196 446 EAAEEEAELEEEEEALLEllaeLLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGV-------KAALLLAG 518
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 387540784 782 TEVVPQLLDQLRTVEQKRPASNVSASIQRIRELIAQTRSVASK 824
Cdd:COG1196 519 LRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAA 561
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
419-878 |
4.74e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.86 E-value: 4.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 419 MLEEI--RRRQPFFT----QRELVDEEADEAHELLSQAESWQRLHNETRtlfpvvlEQLDDYNAKLSDLQEALDQALNHV 492
Cdd:COG4717 46 MLLERleKEADELFKpqgrKPELNLKELKELEEELKEAEEKEEEYAELQ-------EELEELEEELEELEAELEELREEL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 493 RDAEDMNRAtaarqRDHEKQQERVREQMEavnmSLNTSADSLTTPRLTLSELDDIIKNASgiyAEIDGAKNELQVKLSNL 572
Cdd:COG4717 119 EKLEKLLQL-----LPLYQELEALEAELA----ELPERLEELEERLEELRELEEELEELE---AELAELQEELEELLEQL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 573 SNLSHDLVQEAIDHAQELQQEANELSRKL---------HSSDMNGLVQKALDAsNVYENIVNY-------------VSEA 630
Cdd:COG4717 187 SLATEEELQDLAEELEELQQRLAELEEELeeaqeeleeLEEELEQLENELEAA-ALEERLKEArlllliaaallalLGLG 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 631 NETAEFALNTTDRIYDAVSGIDTQIIYHKDESENLLNQARELQAKAESSS--DEAVADTSRRVGGALARKSALKTRLSDA 708
Cdd:COG4717 266 GSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEEleEEELEELLAALGLPPDLSPEELLELLDR 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 709 VKQLQAA--ERGDAQQRLGQSRLITE------------------------EANRTTMEVQQATAPMANNLTNWSQNLQHF 762
Cdd:COG4717 346 IEELQELlrEAEELEEELQLEELEQEiaallaeagvedeeelraaleqaeEYQELKEELEELEEQLEELLGELEELLEAL 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 763 DSSAYNTAVDSARDAVRNLTEVVPQLLDQLRTVEQK----RPASNVSASIQRIRELIAQTRSVASKIQVSMMfdGQSAVE 838
Cdd:COG4717 426 DEEELEEELEELEEELEELEEELEELREELAELEAEleqlEEDGELAELLQELEELKAELRELAEEWAALKL--ALELLE 503
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 387540784 839 VHSRTSMDDlkaftslslymkppvRQPELTETADQFILYL 878
Cdd:COG4717 504 EAREEYREE---------------RLPPVLERASEYFSRL 528
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
408-848 |
9.54e-08 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 57.53 E-value: 9.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 408 EISEKLVLAQKmlEEIRRRQpfftqrelvdeeadEAHELLSQA--ESWQ---RLHNETRTLFPVVLEQLDDYNAKLSDLQ 482
Cdd:NF041483 696 EAAEALAAAQE--EAARRRR--------------EAEETLGSAraEADQereRAREQSEELLASARKRVEEAQAEAQRLV 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 483 EALDQ-ALNHVRDAEDmnraTAARQRD-----HEKQQERVREQMEAVNMSlntsADSltTPRLTLSELDDIIKNAsgiYA 556
Cdd:NF041483 760 EEADRrATELVSAAEQ----TAQQVRDsvaglQEQAEEEIAGLRSAAEHA----AER--TRTEAQEEADRVRSDA---YA 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 557 EIDGA-------KNELQVKLSNLSNLSHDLVQEAIDHAQELQQEANELSRKLHSSDMNGLVQKALDASNVYenivnyvSE 629
Cdd:NF041483 827 ERERAsedanrlRREAQEETEAAKALAERTVSEAIAEAERLRSDASEYAQRVRTEASDTLASAEQDAARTR-------AD 899
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 630 ANETAefalnttDRI-YDAVSGIDTQIIYHKDESENLLNQARelqAKAESSSDEAVADTSRRVGGALARKSALKTRLSDA 708
Cdd:NF041483 900 AREDA-------NRIrSDAAAQADRLIGEATSEAERLTAEAR---AEAERLRDEARAEAERVRADAAAQAEQLIAEATGE 969
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 709 VKQL--QAAER-GDAQQRLGQSRlitEEANRTTMEvqqaTAPMANNLTNWSQN-----LQHFDSSAYNTAVDSARDAVRN 780
Cdd:NF041483 970 AERLraEAAETvGSAQQHAERIR---TEAERVKAE----AAAEAERLRTEAREeadrtLDEARKDANKRRSEAAEQADTL 1042
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 387540784 781 LTEVVPQlLDQLRTVEQKRPASNVSASIQRIRELIAQTRSVASKIQVSMMFDGQSAVEvHSRTSMDDL 848
Cdd:NF041483 1043 ITEAAAE-ADQLTAKAQEEALRTTTEAEAQADTMVGAARKEAERIVAEATVEGNSLVE-KARTDADEL 1108
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
314-593 |
2.09e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 56.23 E-value: 2.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 314 LKTKLSERENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLIQKEsmdtikhASQLVEQAHDMRDKIQEINN 393
Cdd:TIGR02169 679 LRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQE-------EEKLKERLEELEEDLSSLEQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 394 KMLYYGEEHELSPKEIS---EKLVLAQKMLEEIRRR---QPFFTQRELVDEEADEAHELLSQAESWQRLHNEtRTLFPVV 467
Cdd:TIGR02169 752 EIENVKSELKELEARIEeleEDLHKLEEALNDLEARlshSRIPEIQAELSKLEEEVSRIEARLREIEQKLNR-LTLEKEY 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 468 LE----------------------QLDDYNAKLSDLQEALDQALNHVRDAEDmnrataaRQRDHEKQQERVREQMEAVNM 525
Cdd:TIGR02169 831 LEkeiqelqeqridlkeqiksiekEIENLNGKKEELEEELEELEAALRDLES-------RLGDLKKERDELEAQLRELER 903
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 387540784 526 SLNTSADSLTTPRLTLSELDDIIKNASGIYAEIDGAKNELQVKLSNLsnLSHDLVQEAIdhaQELQQE 593
Cdd:TIGR02169 904 KIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEE--LSLEDVQAEL---QRVEEE 966
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
522-787 |
2.13e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.22 E-value: 2.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 522 AVNMSLNTSADSLTTPRLTLSELDDIIKNASGIYAEIDGAKNELQVKLSNLSNLSHDL--VQEAIDhaqELQQEANELSR 599
Cdd:COG3883 3 ALALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELeaLQAEID---KLQAEIAEAEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 600 KLhsSDMNGLVQKALDASNVYENIVNYVS---EANETAEFA--LNTTDRIYDAVSGIDTQIIYHKDESENLLNQARELQA 674
Cdd:COG3883 80 EI--EERREELGERARALYRSGGSVSYLDvllGSESFSDFLdrLSALSKIADADADLLEELKADKAELEAKKAELEAKLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 675 KAESSSDEAvADTSRRVGGALARKSALKTRLSDAVKQLQAA-ERGDAQQRLGQSRLITEEANRTTMEVQQATAPMANNLT 753
Cdd:COG3883 158 ELEALKAEL-EAAKAELEAQQAEQEALLAQLSAEEAAAEAQlAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
250 260 270
....*....|....*....|....*....|....
gi 387540784 754 NWSQNLQHFDSSAYNTAVDSARDAVRNLTEVVPQ 787
Cdd:COG3883 237 AAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAG 270
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
431-900 |
2.55e-07 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 55.68 E-value: 2.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 431 TQRELVDEEADEAHELLSQAESWQR------------LHNETRTLFPVVLEQLDDYNA-------KLSDLQEALDQ---A 488
Cdd:COG5278 43 EHTYEVLRALEELLSALLDAETGQRgylltgdesflePYEEARAEIDELLAELRSLTAdnpeqqaRLDELEALIDQwlaE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 489 LNHVRDAEDMNRATAARQRDHEKQQERVREQMEAVNMSLNTSADSLTTPRLTLSELDDIIKNASGIYAEIDGAKNELQVK 568
Cdd:COG5278 123 LEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 569 LSNLSNLSHDLVQEAIDHAQELQQEANELSRKLHSSDMNGLVQKALDAsnvyenIVNYVSEANETAEFALNTTDRIYDAV 648
Cdd:COG5278 203 LLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALL------LALLAALALAALLAAALLALAALLLA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 649 SGIDTQIIYHKDESENLLNQARELQAKAESSSDEAVADTSRRVGGALARKSALKTRLSDAVKQLQAAERGDAQQRLGQSR 728
Cdd:COG5278 277 LAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAA 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 729 LITEEANRTTMEVQQATAPMANNLTNWSQNLQHFDSSAYNTAVDSARDAVRNLTEVVPQLLDQLRTVEQKRPASNVSASI 808
Cdd:COG5278 357 AAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAE 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 809 QRIRELIAQTRSVASKIQVSMMFDGQSAVEVHSRTSMDDLKAFTSLSLYMKPPVRQPELTETADQFILYLGSKNAKKEYM 888
Cdd:COG5278 437 EEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAA 516
|
490
....*....|..
gi 387540784 889 GLAIKNDNLVYI 900
Cdd:COG5278 517 LAAALAAALASA 528
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
300-820 |
8.36e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 54.20 E-value: 8.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 300 AHRHVNEINATIYLLKTKLSERENQYALRKiqiNNAENTMKSLLSDVEELVEKENQASRKGQLiQKESMDTIKHASQLVE 379
Cdd:TIGR00618 192 LHGKAELLTLRSQLLTLCTPCMPDTYHERK---QVLEKELKHLREALQQTQQSHAYLTQKREA-QEEQLKKQQLLKQLRA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 380 QAHDMRDKIQEINNKMlyygEEHELSPKeiSEKLVLAQKMLEEIRR---------------RQPFFTQRELVDEEADEAH 444
Cdd:TIGR00618 268 RIEELRAQEAVLEETQ----ERINRARK--AAPLAAHIKAVTQIEQqaqrihtelqskmrsRAKLLMKRAAHVKQQSSIE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 445 ELLSQAESWQRLHNETRTLFPVVLEQLDDYNAKLSDLQ------------EALDQALNHVRDAEDMNRATA----ARQRD 508
Cdd:TIGR00618 342 EQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQhihtlqqqkttlTQKLQSLCKELDILQREQATIdtrtSAFRD 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 509 HEKQQERVREQMEAvnmslntSADSLTTPRLTLSELDDIIKNASGIYAEIDGAKNELQVKLSNLSNLshdLVQEAIDHAQ 588
Cdd:TIGR00618 422 LQGQLAHAKKQQEL-------QQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQI---HLQETRKKAV 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 589 ELQ--QEANELSRKLHSSDMNgLVQKALDAsnvyenivnYVSEANetaefalntTDRiydaVSGIDTQIIYHKDESENL- 665
Cdd:TIGR00618 492 VLArlLELQEEPCPLCGSCIH-PNPARQDI---------DNPGPL---------TRR----MQRGEQTYAQLETSEEDVy 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 666 ------LNQARELQAKAESSSDEAVADTSRRvggalARKSALKTRLSDAVKQLQaaERGDAQQRLGQSRLITEEANRTTM 739
Cdd:TIGR00618 549 hqltseRKQRASLKEQMQEIQQSFSILTQCD-----NRSKEDIPNLQNITVRLQ--DLTEKLSEAEDMLACEQHALLRKL 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 740 EVQQATAPMANNLTNWSQNLQ----HFDSSAYNTAVDSARDAVRNLTEVVPQLLDQLRTVEQKrpASNVSASIQRIRELI 815
Cdd:TIGR00618 622 QPEQDLQDVRLHLQQCSQELAlkltALHALQLTLTQERVREHALSIRVLPKELLASRQLALQK--MQSEKEQLTYWKEML 699
|
....*
gi 387540784 816 AQTRS 820
Cdd:TIGR00618 700 AQCQT 704
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
331-783 |
8.87e-07 |
|
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: 53.70 E-value: 8.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 331 QINNAENTMKSLLSDVEELVEKEnqasrkgqliqKESMDTIKHAsqlveqahdmRDKIQEINNKMLYYGeeHELSPKEis 410
Cdd:pfam06160 94 LLDDIEEDIKQILEELDELLESE-----------EKNREEVEEL----------KDKYRELRKTLLANR--FSYGPAI-- 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 411 EKLvlaQKMLEEIrrrQPFFTQRELVDEEAD--EAHELLSQaeswqrLHNETRTL------FPVVLEQL-DDYNAKLSDL 481
Cdd:pfam06160 149 DEL---EKQLAEI---EEEFSQFEELTESGDylEAREVLEK------LEEETDALeelmedIPPLYEELkTELPDQLEEL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 482 QEALDQ------ALNHVRDAEDMNRATAARQRD----HEKQQERVREQMEAVNMSLNTSADSLTTprltlsELD---DII 548
Cdd:pfam06160 217 KEGYREmeeegyALEHLNVDKEIQQLEEQLEENlallENLELDEAEEALEEIEERIDQLYDLLEK------EVDakkYVE 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 549 KNASGIYAEIDGAK---NELQVKLSNLsNLSHDLVQEAIDHAQELQQEANELSRKLHSsdmngLVQKALDASNVYENIVN 625
Cdd:pfam06160 291 KNLPEIEDYLEHAEeqnKELKEELERV-QQSYTLNENELERVRGLEKQLEELEKRYDE-----IVERLEEKEVAYSELQE 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 626 YVSEanetaefalnttdrIYDAVSGIDTQIIYHKDESENLLNQarELQAKAESSS-DEAVADTSRRVggalaRKSAL--- 701
Cdd:pfam06160 365 ELEE--------------ILEQLEEIEEEQEEFKESLQSLRKD--ELEAREKLDEfKLELREIKRLV-----EKSNLpgl 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 702 ----KTRLSDAVKQLQaaergDAQQRLGQSRLITEEANRTTMEVQQAtapmannltnwsqnLQHFDSSAYNTaVDSARda 777
Cdd:pfam06160 424 pesyLDYFFDVSDEIE-----DLADELNEVPLNMDEVNRLLDEAQDD--------------VDTLYEKTEEL-IDNAT-- 481
|
....*.
gi 387540784 778 vrnLTE 783
Cdd:pfam06160 482 ---LAE 484
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
408-760 |
1.41e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.60 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 408 EISEKLVLAQKMLEEIRRR--QPFFTQRELVDEEADEAHELLSQAESWQRLHNETRTLFPVVLEQLDDYNAKLSDLQEAL 485
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKtgILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 486 DQALNHVRDAEDMNRATAARQRDHEKQQERVREQMEAVNmslntsadslttprltlSELDDIIKNASGIYAEIDGAKNEL 565
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQ-----------------KERQDLEQQRKQLEAQIAELQSEI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 566 QVKLSNLSNLSHDLvQEAIDHAQELQQEANELSRKLHSSDMNGLVQKAldasnvyENIVNYVSEANETAEFALNTTDRIY 645
Cdd:COG4372 146 AEREEELKELEEQL-ESLQEELAALEQELQALSEAEAEQALDELLKEA-------NRNAEKEEELAEAEKLIESLPRELA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 646 DAVSGIDTQIIYHKDESENLLNQARELQAKAESSSDEAVADTSRRVGGALARKSALKTRLSDAVKQLQAAERGDAQQRLG 725
Cdd:COG4372 218 EELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKL 297
|
330 340 350
....*....|....*....|....*....|....*
gi 387540784 726 QSRLITEEANRTTMEVQQATAPMANNLTNWSQNLQ 760
Cdd:COG4372 298 LALLLNLAALSLIGALEDALLAALLELAKKLELAL 332
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
1256-1369 |
2.28e-06 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 48.47 E-value: 2.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 1256 FRTLQPNGLLFYYAS--GSDVFSISLDNG--TVVMDV-KGIKVQSVDKQYNDGLSHFVIASVSPTRYELIVDK-SRVGSK 1329
Cdd:pfam00054 1 FRTTEPSGLLLYNGTqtERDFLALELRDGrlEVSYDLgSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGeARPTGE 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 387540784 1330 NPTKGKieQTQAGEKKFYFGGSPISAQYA-------NFTGCISNAYF 1369
Cdd:pfam00054 81 SPLGAT--TDLDVDGPLYVGGLPSLGVKKrrlaispSFDGCIRDVIV 125
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
313-601 |
2.84e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.84 E-value: 2.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 313 LLKTKLSERENQYALRKiqinNAENTMKsllsdVEELVEKENQASRKGQLIQKESMDTIKHASQLVEQAHDMRDKIQEIN 392
Cdd:PTZ00121 1680 AKKAEEDEKKAAEALKK----EAEEAKK-----AEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAK 1750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 393 nkmlyygeehelspKEISEKLVLAQKMLEEIRRRQPFFTQRELV-DEEADEAHEllSQAESWQRLHNETRTLFPVVLEQL 471
Cdd:PTZ00121 1751 --------------KDEEEKKKIAHLKKEEEKKAEEIRKEKEAViEEELDEEDE--KRRMEVDKKIKDIFDNFANIIEGG 1814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 472 DDYNAKLSDLQEALDQALNHVRDAEDMNRATAARQRDHEKQQERVREQMEAVNMSLNTSADSLTTPRLTLSELDDIIKna 551
Cdd:PTZ00121 1815 KEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEK-- 1892
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 387540784 552 sgiyaeIDGAKNELQVKLSNLSNLSHDLVQEAIDHAQELQQEANELSRKL 601
Cdd:PTZ00121 1893 ------IDKDDIEREIPNNNMAGKNNDIIDDKLDKDEYIKRDAEETREEI 1936
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
306-667 |
2.97e-06 |
|
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: 52.33 E-value: 2.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 306 EINATIYLLKTKLSERENQYALRKIQINNAENTMKSL---LSDVEELVEKENQASRKGQ--LIQKESM-DTIK-HASQLV 378
Cdd:TIGR04523 430 RLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLetqLKVLSRSINKIKQNLEQKQkeLKSKEKElKKLNeEKKELE 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 379 EQAHDMRDKIQEINNKMlyygEEHELSPKEISEKLVLAQKMLEEIRrrqpFFTQRELVDEEADEAHELLSQaeswqrLHN 458
Cdd:TIGR04523 510 EKVKDLTKKISSLKEKI----EKLESEKKEKESKISDLEDELNKDD----FELKKENLEKEIDEKNKEIEE------LKQ 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 459 ETRTLfpvvleqlddyNAKLSDLQEALDQalnhvrdaedmnrataarqrdHEKQQERVREQMEAVNMSLNTSADSLTTPR 538
Cdd:TIGR04523 576 TQKSL-----------KKKQEEKQELIDQ---------------------KEKEKKDLIKEIEEKEKKISSLEKELEKAK 623
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 539 LTLSELDDIIKNasgiyaeIDGAKNELQVKLSNLsnlsHDLVQEAIDHAQELQQEANELSRKLhsSDMNGLVQKALDASN 618
Cdd:TIGR04523 624 KENEKLSSIIKN-------IKSKKNKLKQEVKQI----KETIKEIRNKWPEIIKKIKESKTKI--DDIIELMKDWLKELS 690
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 387540784 619 VYENivNYVSEANETAEfaLNTTDRIYDAVSGIDTQIIYHKDESENLLN 667
Cdd:TIGR04523 691 LHYK--KYITRMIRIKD--LPKLEEKYKEIEKELKKLDEFSKELENIIK 735
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
314-604 |
3.25e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 52.38 E-value: 3.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 314 LKTKLSEREnQYALrkiqinnaentMKSLLSDVEELVEKENQASRkgqlIQKESMDTIKHASQLVEQAHDMRDKIQEINN 393
Cdd:TIGR02169 216 LLKEKREYE-GYEL-----------LKEKEALERQKEAIERQLAS----LEEELEKLTEEISELEKRLEEIEQLLEELNK 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 394 KMLYYGEEHELspkEISEKLVLAQKMLEEIRRRQPfFTQRELVDEEADEA------HELLSQAESWQRLHNETRTlfpvv 467
Cdd:TIGR02169 280 KIKDLGEEEQL---RVKEKIGELEAEIASLERSIA-EKERELEDAEERLAkleaeiDKLLAEIEELEREIEEERK----- 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 468 leQLDDYNAKLSDLQEALDQALNHVRDAEDMNRATAARQRDHEKQQERVREQMEAVNMSLNTSADSLTTPRLTLSELDDI 547
Cdd:TIGR02169 351 --RRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAA 428
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 387540784 548 IKNASGIYAEIDGAKNELQVKLS----NLSNLSHDLVQEAIDHAQeLQQEANELSRKLHSS 604
Cdd:TIGR02169 429 IAGIEAKINELEEEKEDKALEIKkqewKLEQLAADLSKYEQELYD-LKEEYDRVEKELSKL 488
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
302-573 |
3.36e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 52.38 E-value: 3.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 302 RHVNEINATIYLLKTKLSERENQYALRKIQINNAENTMKSLLSDvEELVEKENQASRKGQLIQKEsmDTIKHASQLVEQA 381
Cdd:TIGR02169 244 RQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEE-EQLRVKEKIGELEAEIASLE--RSIAEKERELEDA 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 382 HDMRDKIQEINNKMLyygEEHELSPKEISEKLVLAQKMLEEIrrrqpfftqrelvDEEADEAHELLSQAESWQRLHNETR 461
Cdd:TIGR02169 321 EERLAKLEAEIDKLL---AEIEELEREIEEERKRRDKLTEEY-------------AELKEELEDLRAELEEVDKEFAETR 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 462 TLFPVVLEQLDDYNAKLSDLQEALDQALNHVRDAEdmnrataARQRDHEKQQERVREQMEAVNMSLNTSADSLTTPRLTL 541
Cdd:TIGR02169 385 DELKDYREKLEKLKREINELKRELDRLQEELQRLS-------EELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKL 457
|
250 260 270
....*....|....*....|....*....|..
gi 387540784 542 SELDDIIKNASGIYAEIDGAKNELQVKLSNLS 573
Cdd:TIGR02169 458 EQLAADLSKYEQELYDLKEEYDRVEKELSKLQ 489
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
314-671 |
4.10e-06 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 52.36 E-value: 4.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 314 LKTKLS--ERENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLIQKESMDTIKHASQLVEQAHDMRDKIQEI 391
Cdd:TIGR01612 2049 IKEKIDnyEKEKEKFGIDFDVKAMEEKFDNDIKDIEKFENNYKHSEKDNHDFSEEKDNIIQSKKKLKELTEAFNTEIKII 2128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 392 NNKMLyygEEHELSPKeiseklvlaqkmLEEIRRRQPFFTQRELVDEeadeaheLLSQAESWQRLHNETRTLFPVVLEQL 471
Cdd:TIGR01612 2129 EDKII---EKNDLIDK------------LIEMRKECLLFSYATLVET-------LKSKVINHSEFITSAAKFSKDFFEFI 2186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 472 DDYNAKLSDLQEALDQALNHVRDAEDMNRATAARQRDHEKQQERVREQMEAVNM--------SLNTSADSLTTPRLTL-- 541
Cdd:TIGR01612 2187 EDISDSLNDDIDALQIKYNLNQTKKHMISILADATKDHNNLIEKEKEATKIINNltelftidFNNADADILHNNKIQIiy 2266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 542 --SELDDIIKNASGIYAEIDGAKnelqvklsnLSNLSHdLVQEAIDHAQE----LQQEANELSRKLHssDMNGLVQKALD 615
Cdd:TIGR01612 2267 fnSELHKSIESIKKLYKKINAFK---------LLNISH-INEKYFDISKEfdniIQLQKHKLTENLN--DLKEIDQYISD 2334
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 387540784 616 ASNVYENIVNyvseanETAEFALNTTDRIYDAVSGIDTQIiyhkDESENLLNQARE 671
Cdd:TIGR01612 2335 KKNIFLHALN------ENTNFNFNALKEIYDDIINRENKA----DEIENINNKENE 2380
|
|
| ApoLp-III_like |
cd13769 |
Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles ... |
703-829 |
4.11e-06 |
|
Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles in the transport of lipids and lipoprotein metabolism. Apolipophorin III (apoLp-III) assists in the loading of diacylglycerol, generated from triacylglycerol stores in the fat body through the action of adipokinetic hormone, into lipophorin, the hemolymph lipoprotein. ApoLp-III increases the lipid carrying capacity of lipophorin by covering the expanding hydrophobic surface resulting from diacylglycerol uptake. It plays a critical role in the transport of lipids during insect flight, and may also play a role in defense mechanisms and innate immunity.
Pssm-ID: 259842 [Multi-domain] Cd Length: 158 Bit Score: 48.47 E-value: 4.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 703 TRLSDAVKQLQAAERGDAQQRLGQSRL-ITEEANRTtmeVQQATAPMANNLTNWSQNLQHFDSSAYNTAVDSARDAVRNL 781
Cdd:cd13769 1 TQLSELIQKAQEAINNLAQQVQKQLGLqNPEEVVNT---LKEQSDNFANNLQEVSSSLKEEAKKKQGEVEEAWNEFKTKL 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 387540784 782 TEVVPQLLDQLRTVEQkrpASNVSASIQ-RIRELIAQTRSVASKIQVSM 829
Cdd:cd13769 78 SETVPELRKSLPVEEK---AQELQAKLQsGLQTLVTESQKLAKAISENS 123
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
332-524 |
4.53e-06 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 49.75 E-value: 4.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 332 INNAENTMKSL-----LSDVEELVEKeNQASRKGQLIQKESMDTI-KHASQLVEQAHDMRDKIQE----INNKMlyygee 401
Cdd:cd00176 16 LSEKEELLSSTdygddLESVEALLKK-HEALEAELAAHEERVEALnELGEQLIEEGHPDAEEIQErleeLNQRW------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 402 helspKEISEKLVLAQKMLEEIRRRQPFFTQrelVDEEADEAHELLSQAESWQRLHNETRtlfpvVLEQLDdynaKLSDL 481
Cdd:cd00176 89 -----EELRELAEERRQRLEEALDLQQFFRD---ADDLEQWLEEKEAALASEDLGKDLES-----VEELLK----KHKEL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 387540784 482 QEALDQALNHVRDAEDMNRATAARQrdHEKQQERVREQMEAVN 524
Cdd:cd00176 152 EEELEAHEPRLKSLNELAEELLEEG--HPDADEEIEEKLEELN 192
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
314-670 |
7.85e-06 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 50.60 E-value: 7.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 314 LKTKLSERENQY--ALRKI--QINNAEntmkSLLSDVEELVEKEN--QASR-----KGQLIQ-KESMDTIKhaSQLVEQA 381
Cdd:PRK04778 152 LRKSLLANRFSFgpALDELekQLENLE----EEFSQFVELTESGDyvEAREildqlEEELAAlEQIMEEIP--ELLKELQ 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 382 HDMRDKIQEINN---KML---YYGEEHELSP--KEISEKLVLAQKMLEEIrrrqpfftqrelvdeEADEAHELLSQAESw 453
Cdd:PRK04778 226 TELPDQLQELKAgyrELVeegYHLDHLDIEKeiQDLKEQIDENLALLEEL---------------DLDEAEEKNEEIQE- 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 454 qRL-------------HNETRTLFPVVLEQLDDYNAKLSDLQEALDQ-----ALNHvRDAEdmnrataaRQRDHEKQQER 515
Cdd:PRK04778 290 -RIdqlydilerevkaRKYVEKNSDTLPDFLEHAKEQNKELKEEIDRvkqsyTLNE-SELE--------SVRQLEKQLES 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 516 VREQMEAVnmslntsADSLTTPRLTLSELDDIIKNASGIYAEIdgakNELQVKLSN-LSNLSHDlVQEAIDHAQELQQEA 594
Cdd:PRK04778 360 LEKQYDEI-------TERIAEQEIAYSELQEELEEILKQLEEI----EKEQEKLSEmLQGLRKD-ELEAREKLERYRNKL 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 595 NELSRKLHSSDMNGLVQKALDAsnvYENIVNYVSEANEtaefALNTT----DRIYDAVSGIDTQIIYHKDESENLLNQAR 670
Cdd:PRK04778 428 HEIKRYLEKSNLPGLPEDYLEM---FFEVSDEIEALAE----ELEEKpinmEAVNRLLEEATEDVETLEEETEELVENAT 500
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
332-822 |
7.93e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 50.99 E-value: 7.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 332 INNAENTMKSLLSDVE----ELVEKENQASRKgQLIQKESMDTIKhaSQLVEQAHDMRDKIQEINNkmlyygeehELSPK 407
Cdd:pfam12128 246 LQQEFNTLESAELRLShlhfGYKSDETLIASR-QEERQETSAELN--QLLRTLDDQWKEKRDELNG---------ELSAA 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 408 EisEKLVLAQKMLEEIRRRQpfftqRELVDEEADEAHELLSQAESWQRLHNETRTLFPVVLEQLDDYNAKLSDLQEALDQ 487
Cdd:pfam12128 314 D--AAVAKDRSELEALEDQH-----GAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKE 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 488 ALNhvRDAEDMN------RATAARQR-----DHEKQQERVREQMEAVNMSLNTSADSLttpRLTLSELDDIIKNASgiya 556
Cdd:pfam12128 387 QNN--RDIAGIKdklakiREARDRQLavaedDLQALESELREQLEAGKLEFNEEEYRL---KSRLGELKLRLNQAT---- 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 557 eidgAKNELQVKLSNLsnlshdlvQEAIDHAQELQQEANELSRKLHSSD--MNGLVQKALDASNVYENIVNYVSEANETA 634
Cdd:pfam12128 458 ----ATPELLLQLENF--------DERIERAREEQEAANAEVERLQSELrqARKRRDQASEALRQASRRLEERQSALDEL 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 635 EFALnttdriyDAVSG-----IDTQIIYHKDESENLLNQARELQAKAESSSDEAVADTSRRVGGA------------LAR 697
Cdd:pfam12128 526 ELQL-------FPQAGtllhfLRKEAPDWEQSIGKVISPELLHRTDLDPEVWDGSVGGELNLYGVkldlkridvpewAAS 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 698 KSALKTRLSDAVKQLQAAERGDAQQ--RLGQSRLITEEANRttmEVQQATAPMANN------LTNWSQNLQHFDSSAYNT 769
Cdd:pfam12128 599 EEELRERLDKAEEALQSAREKQAAAeeQLVQANGELEKASR---EETFARTALKNArldlrrLFDEKQSEKDKKNKALAE 675
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 387540784 770 AVDSARDAVRNLTEVVPQLLDQLRTV--EQKRPASNVSASIQRIRELIAQTRSVA 822
Cdd:pfam12128 676 RKDSANERLNSLEAQLKQLDKKHQAWleEQKEQKREARTEKQAYWQVVEGALDAQ 730
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
284-814 |
8.46e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.11 E-value: 8.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 284 IEEGKSGVlsvssgAAAH-RHVNEINAtiyLLKTKLSERENQYALRKiQINNAENTMKSLLSDVEELVEKEnqasrkgql 362
Cdd:PRK04863 263 ITESTNYV------AADYmRHANERRV---HLEEALELRRELYTSRR-QLAAEQYRLVEMARELAELNEAE--------- 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 363 iqkesmdtikhaSQLVEQAHDMRDKIQEINNKMLYYG--EEHELSPKEISEKLVlAQKMLeeirrrqpfftqRELVDEEA 440
Cdd:PRK04863 324 ------------SDLEQDYQAASDHLNLVQTALRQQEkiERYQADLEELEERLE-EQNEV------------VEEADEQQ 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 441 DEAHELLSQAEswqrlhnetrtlfpvvlEQLDDYNAKLSDLQEALDQAlnhvrdaedmnrATAARQRDHEKQQ-ERVReq 519
Cdd:PRK04863 379 EENEARAEAAE-----------------EEVDELKSQLADYQQALDVQ------------QTRAIQYQQAVQAlERAK-- 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 520 meavnmslntsadslttprlTLSELDDIiknasgiyaEIDGAKnelqvklsnlsnlshDLVQEAIDHAQELQQEANELSR 599
Cdd:PRK04863 428 --------------------QLCGLPDL---------TADNAE---------------DWLEEFQAKEQEATEELLSLEQ 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 600 KLHSSDMnglvqkaldasnvyenivnyvseANETAEFALNTTDRIYDAVSGIDTQiiyhkDESENLLNQARELQAKAEss 679
Cdd:PRK04863 464 KLSVAQA-----------------------AHSQFEQAYQLVRKIAGEVSRSEAW-----DVARELLRRLREQRHLAE-- 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 680 sdeavadtsrRVGGALARKSALKTRLsdavKQLQAAER--GDAQQRLGQS--------RLITE-EANRTTMEVQQATA-- 746
Cdd:PRK04863 514 ----------QLQQLRMRLSELEQRL----RQQQRAERllAEFCKRLGKNlddedeleQLQEElEARLESLSESVSEAre 579
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 747 ---PMANNLTNWSQNLQHFDSSAynTAVDSARDAVRNLTEVVP--------------QLLDQLR--TVEQKRPASNVSAS 807
Cdd:PRK04863 580 rrmALRQQLEQLQARIQRLAARA--PAWLAAQDALARLREQSGeefedsqdvteymqQLLERERelTVERDELAARKQAL 657
|
....*..
gi 387540784 808 IQRIREL 814
Cdd:PRK04863 658 DEEIERL 664
|
|
| VSP |
pfam03302 |
Giardia variant-specific surface protein; |
67-300 |
9.91e-06 |
|
Giardia variant-specific surface protein;
Pssm-ID: 146106 [Multi-domain] Cd Length: 397 Bit Score: 49.97 E-value: 9.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 67 CNAGFFRTlSGECVPCD-----CNGNS----NKCLDG-----------------------SGFCVHCQRNTTG-EHCEKC 113
Cdd:pfam03302 96 CNDGFYKS-GDACSPCHescktCSGGTasdcTECLTGkalrygndgtkgtcgegcttgtgAGACKTCGLTIDGtSYCSEC 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 114 -------LDGYIGDSIRGAPRFCQLCPCPLPHLANFAESCYRKNGAV--------RCICKENYAGPNCERCAPGYYGNPL 178
Cdd:pfam03302 175 ateteypQNGVCTSTAARATATCKASSVANGMCSSCANGYFRMNGGCyettkfpgKSVCEEANSGGTCQKEAPGYKLNNG 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 179 LIGITCKKCD-CSGNSDPNLIFED-------CDEVTGQCRNCLRNTTgfKCERCAPGYYGDARIAKNCAVCNCGGGpcds 250
Cdd:pfam03302 255 DLVTCSPGCKtCTSNTVCTTCMDGyvktsdsCTKCDSSCETCTGATT--TCKTCATGYYKSGTGCVSCTSSESDNG---- 328
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 387540784 251 VTG--ECLEegLEPPTGCDKCVwdltddlrLAALSIEEGKSGVLSVSSGAAA 300
Cdd:pfam03302 329 ITGvkGCLN--CAPPSNNKGSV--------LCYLIKDSGSTNKSGLSTGAIA 370
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
314-567 |
1.26e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 50.43 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 314 LKTKLSERENQYA--LRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLIQKESMDTikhasqlVEQAHDMRDKIQEI 391
Cdd:TIGR00606 797 FQMELKDVERKIAqqAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQ-------QEQIQHLKSKTNEL 869
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 392 NNKMLYYGEehelspkEISEKLVLAQKMLEEIRRRQpfftqrELVDEEADEAHELLSQAESWQRLHNETRTLFPVVLEQL 471
Cdd:TIGR00606 870 KSEKLQIGT-------NLQRRQQFEEQLVELSTEVQ------SLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSN 936
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 472 DDYNAKLSDLQEALDQALNHVRDAED----------MNRAT-----AARQRDHEKQQERVREQMEAVNMSLNTS--ADSL 534
Cdd:TIGR00606 937 KKAQDKVNDIKEKVKNIHGYMKDIENkiqdgkddylKQKETelntvNAQLEECEKHQEKINEDMRLMRQDIDTQkiQERW 1016
|
250 260 270
....*....|....*....|....*....|...
gi 387540784 535 TTPRLTLSELDDIIKNASGIYAEIDGAKNELQV 567
Cdd:TIGR00606 1017 LQDNLTLRKRENELKEVEEELKQHLKEMGQMQV 1049
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
467-700 |
1.53e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.44 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 467 VLEQLDDYNAKLSDLQEALDQALNHVRDAE----DMNRATAARQRDHEKQQERVREQMEAVNMSLNT--------SADSL 534
Cdd:COG3883 35 AQAELDALQAELEELNEEYNELQAELEALQaeidKLQAEIAEAEAEIEERREELGERARALYRSGGSvsyldvllGSESF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 535 TT--PRLTLseLDDIIKNASGIYAEIDGAKNELQVKLSNLSnlshDLVQEAIDHAQELQQEANELSRKLhsSDMNGLVQK 612
Cdd:COG3883 115 SDflDRLSA--LSKIADADADLLEELKADKAELEAKKAELE----AKLAELEALKAELEAAKAELEAQQ--AEQEALLAQ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 613 ALDASNVYENIVNYVSEANETAEFALNTTDRIYDAVSGIDTQIIYHKDESENLLNQARELQAKAESSSDEAVADTSRRVG 692
Cdd:COG3883 187 LSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAG 266
|
....*...
gi 387540784 693 GALARKSA 700
Cdd:COG3883 267 AAAGAAGA 274
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
277-658 |
1.72e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.13 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 277 LRLAALSIEEGKSGVLSVSSGAAAHRHVNEINATIYLLKTKLSERENQYALRKIQINNAENTMKSLLSDVEELvEKENQA 356
Cdd:COG4372 13 LSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL-NEQLQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 357 SRKGQLIQKESMDTIKhasqlvEQAHDMRDKIQEINnkmlyygeehelspKEISEKLVLAQKMLEEIRRRQPFFTQRElv 436
Cdd:COG4372 92 AQAELAQAQEELESLQ------EEAEELQEELEELQ--------------KERQDLEQQRKQLEAQIAELQSEIAERE-- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 437 deeaDEAHELLSQAESWQRLhnetrtlfpvvLEQLDDYNAKLSD--LQEALDQALNHVRDAEDMNRATAARQRDHEKQQE 514
Cdd:COG4372 150 ----EELKELEEQLESLQEE-----------LAALEQELQALSEaeAEQALDELLKEANRNAEKEEELAEAEKLIESLPR 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 515 RVREQMEAVNMSLNTSADSLTTPRLTLSELDDIIKNASGIYAEIDGAKNELQVKLSNLSNLSHDLVQEAIDHAQELQQEA 594
Cdd:COG4372 215 ELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALE 294
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 387540784 595 NELSRKLHSSDMNGLVQKALDASNVYENIVNYVSEANETAEFALNTTDRIYDAVSGIDTQIIYH 658
Cdd:COG4372 295 LKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLEL 358
|
|
| PLU-1 |
pfam08429 |
PLU-1-like protein; Sequences in this family bear similarity to the central region of PLU-1. ... |
314-597 |
2.54e-05 |
|
PLU-1-like protein; Sequences in this family bear similarity to the central region of PLU-1. This is a nuclear protein that may have a role in DNA-binding and transcription, and is closely associated with the malignant phenotype of breast cancer. This region is found in various other Jumonji/ARID domain-containing proteins (see pfam02373, pfam01388).
Pssm-ID: 462475 [Multi-domain] Cd Length: 336 Bit Score: 48.36 E-value: 2.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 314 LKTKLSERENqyalRKIQINNAENTMKSLLSDVEELVEKENQ-------ASRKGQLIQKE---SMDTIKHASQLVEQAHD 383
Cdd:pfam08429 21 LRALLNEAEK----IKFPLPELLQDLRAFVQRANKWVEEAQQllsrkqqTRRKNEAEEDErerEKRTVEELRKLLEEADN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 384 MRDKIQEInnkmlyygeeHELspKEISEKLV----LAQKMLEEirrrqpfftqrELVDEEADEAHELLSQAESwqrlhne 459
Cdd:pfam08429 97 LPFDCPEI----------EQL--KELLEEIEefqkRAREALSE-----------EPPSLSIEELEELLEEGKS------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 460 trtlFPVVLEQLDDynaklsdLQEALDQA--LNHVRDAEDMNRAT-------------AARQRDHEKQQERVREQMEAVN 524
Cdd:pfam08429 147 ----FNVDLPELEE-------LEKVLEQLkwLEEVRETSRKKSLTledvrelieegveLGIPPPYEDLMAELQELLTAGE 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 387540784 525 MSLNTSADSLTTPRLTLSELDDIIKNASGIyaeidgaknelQVKLSNLSNLshdlvQEAIDHAQELQQEANEL 597
Cdd:pfam08429 216 RWEEKAKELLSRERVSLAQLEALSKEAQEI-----------PVSLPNLAAL-----DEILKKAREWQRQIEAL 272
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
433-819 |
3.96e-05 |
|
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: 48.80 E-value: 3.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 433 RELVDEEADEAHELLSQAESW---QRLHNETRtlfpvvlEQLDDYNAKLSDLQEALDQA---LNHVRDAEDMNRATAARQ 506
Cdd:COG3096 281 RELSERALELRRELFGARRQLaeeQYRLVEMA-------RELEELSARESDLEQDYQAAsdhLNLVQTALRQQEKIERYQ 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 507 RDHEKQQERVREQMEAVnmslNTSADSLTTPRLTLSELDDIIKNASGIYAEIDGAKNELQVK----------------LS 570
Cdd:COG3096 354 EDLEELTERLEEQEEVV----EEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRaiqyqqavqalekaraLC 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 571 NLSNLS----HDLVQEAIDHAQELQQEANELSRKLHSSDM-NGLVQKALDAsnvYENIVNYV--SEANETAEFALnTTDR 643
Cdd:COG3096 430 GLPDLTpenaEDYLAAFRAKEQQATEEVLELEQKLSVADAaRRQFEKAYEL---VCKIAGEVerSQAWQTARELL-RRYR 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 644 IYDAVSGIDTQIIYHKDESENLLNQarelQAKAESSSDEavadTSRRVGGALARKSALKTRLSDAVKQLQ--AAERGDAQ 721
Cdd:COG3096 506 SQQALAQRLQQLRAQLAELEQRLRQ----QQNAERLLEE----FCQRIGQQLDAAEELEELLAELEAQLEelEEQAAEAV 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 722 QRLGQSRLiTEEANRTTMEVQQATAPM-------ANNLTNwsQNLQHFDSSAyntAVDSARDavrnltevvpQLLDQLRT 794
Cdd:COG3096 578 EQRSELRQ-QLEQLRARIKELAARAPAwlaaqdaLERLRE--QSGEALADSQ---EVTAAMQ----------QLLERERE 641
|
410 420
....*....|....*....|....*
gi 387540784 795 VEQKRpasnvSASIQRIRELIAQTR 819
Cdd:COG3096 642 ATVER-----DELAARKQALESQIE 661
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
514-757 |
4.07e-05 |
|
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: 48.89 E-value: 4.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 514 ERVREQMEAVNMSLNTSADSLTTPRLTLSELDDIIKnaSGIYAEIDGAKNELQVKLSNLSNLSHDL---VQEAIDHAQEL 590
Cdd:TIGR01612 500 MRMKDFKDIIDFMELYKPDEVPSKNIIGFDIDQNIK--AKLYKEIEAGLKESYELAKNWKKLIHEIkkeLEEENEDSIHL 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 591 QQEAN---------------------ELSRKLHS-SDMNGLVQKALDASNVYENIVNYVSEANETAEFA----LNTTDRI 644
Cdd:TIGR01612 578 EKEIKdlfdkyleiddeiiyinklklELKEKIKNiSDKNEYIKKAIDLKKIIENNNAYIDELAKISPYQvpehLKNKDKI 657
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 645 YDAVSGIDTQI--------------IYHKDESENLLNQAR--ELQAKAESSSDEAVADTSRRVGGALARKSALKTRLSDA 708
Cdd:TIGR01612 658 YSTIKSELSKIyeddidalynelssIVKENAIDNTEDKAKldDLKSKIDKEYDKIQNMETATVELHLSNIENKKNELLDI 737
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 387540784 709 VKQLQAAERGDaqqrlgqsrlITEEANRTTMEVQQATAPMANNLTNWSQ 757
Cdd:TIGR01612 738 IVEIKKHIHGE----------INKDLNKILEDFKNKEKELSNKINDYAK 776
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
314-824 |
4.28e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 48.63 E-value: 4.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 314 LKTKLSERENqyalRKIQINNAENTMKSLLSDVEELVEKENQASRKGQL--------IQKESMDTIKHASQ---LVEQAH 382
Cdd:pfam01576 80 LESRLEEEEE----RSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLekvtteakIKKLEEDILLLEDQnskLSKERK 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 383 DMRDKIQEINNKMlyyGEEHELSpKEISeKLVLAQKML---EEIRRRQPFFTQREL------VDEEADEAHE----LLSQ 449
Cdd:pfam01576 156 LLEERISEFTSNL---AEEEEKA-KSLS-KLKNKHEAMisdLEERLKKEEKGRQELekakrkLEGESTDLQEqiaeLQAQ 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 450 AE----SWQRLHNETRTLfpvvLEQLDDYNAKLSDLQEALDQALNHVRDA-EDMNRATAARQRdHEKQQERVREQMEAVN 524
Cdd:pfam01576 231 IAelraQLAKKEEELQAA----LARLEEETAQKNNALKKIRELEAQISELqEDLESERAARNK-AEKQRRDLGEELEALK 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 525 MSLNTSADS------LTTPRLT------------------------------LSELDDIIKNASGIYAEIDGAK------ 562
Cdd:pfam01576 306 TELEDTLDTtaaqqeLRSKREQevtelkkaleeetrsheaqlqemrqkhtqaLEELTEQLEQAKRNKANLEKAKqalese 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 563 -NELQVKLSNLSNLSHDLVQ---EAIDHAQELQQEANELSRklHSSDMNGLVQKaldASNVYENIVNYVSEANETAEfal 638
Cdd:pfam01576 386 nAELQAELRTLQQAKQDSEHkrkKLEGQLQELQARLSESER--QRAELAEKLSK---LQSELESVSSLLNEAEGKNI--- 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 639 nttdRIYDAVSGIDTQIiyhkDESENLLNQarELQAKAESSSdeavadtsrRVGGALARKSALKTRLSDAVKQLQAAER- 717
Cdd:pfam01576 458 ----KLSKDVSSLESQL----QDTQELLQE--ETRQKLNLST---------RLRQLEDERNSLQEQLEEEEEAKRNVERq 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 718 -GDAQQRLGQSRLITEEANRTTMEVQQATAPMANNLTNWSQNLQHfDSSAYNTaVDSARDAVRnltevvpQLLDQLrTVE 796
Cdd:pfam01576 519 lSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEE-KAAAYDK-LEKTKNRLQ-------QELDDL-LVD 588
|
570 580 590
....*....|....*....|....*....|.
gi 387540784 797 QKRPASNVSASIQRIR---ELIAQTRSVASK 824
Cdd:pfam01576 589 LDHQRQLVSNLEKKQKkfdQMLAEEKAISAR 619
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
875-1006 |
9.23e-05 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 43.84 E-value: 9.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 875 ILYLGSKNaKKEYMGLAIKNDNLVYIYNLGTKDVEIPldSKPVSSwPAYFSIVKIERVGKHGkvFLTV---PSLSSTAEe 951
Cdd:pfam00054 10 LLYNGTQT-ERDFLALELRDGRLEVSYDLGSGAAVVR--SGDKLN-DGKWHSVELERNGRSG--TLSVdgeARPTGESP- 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 387540784 952 kfikkgefSGDDSLLDLDpedTVFYVGGVPSNFKLPNSL-NLPGFVGCLELATLNN 1006
Cdd:pfam00054 83 --------LGATTDLDVD---GPLYVGGLPSLGVKKRRLaISPSFDGCIRDVIVNG 127
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
347-600 |
1.31e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 46.61 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 347 EELVEKENQASRKGQLIQKEsMDTIKHASQLVEQAHDM-RDKIQEINNKMLYYGEEHELSpKEIsEKLVLAQKMLEEIRR 425
Cdd:COG0497 154 EELLEEYREAYRAWRALKKE-LEELRADEAERARELDLlRFQLEELEAAALQPGEEEELE-EER-RRLSNAEKLREALQE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 426 rqpfftQRELVDEEADEAHELLSQAESWqrlhnetrtlfpvvLEQLDDYNAKLSDLQEALDQALNHVRDAEDMNRATAAR 505
Cdd:COG0497 231 ------ALEALSGGEGGALDLLGQALRA--------------LERLAEYDPSLAELAERLESALIELEEAASELRRYLDS 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 506 QRDHEKQQERVREQMEAVNmslntsadslttpRLTL---SELDDIIKnasgiYAEidgaknELQVKLSNLSNLSHDL--V 580
Cdd:COG0497 291 LEFDPERLEEVEERLALLR-------------RLARkygVTVEELLA-----YAE------ELRAELAELENSDERLeeL 346
|
250 260
....*....|....*....|.
gi 387540784 581 QEAIDHA-QELQQEANELSRK 600
Cdd:COG0497 347 EAELAEAeAELLEAAEKLSAA 367
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
304-826 |
1.36e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.82 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 304 VNEINATIYLLKTKLSERENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLIqKESMDTIKHASQLVEQAHD 383
Cdd:PRK01156 199 LENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEI-KTAESDLSMELEKNNYYKE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 384 MRDKIQEINNKMLYYGEEHELSPKEISEKLVLAQKMLEEIrrrqpfftqrelvDEEADEAHELLSQAESWQRLHNEtrtl 463
Cdd:PRK01156 278 LEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNI-------------DAEINKYHAIIKKLSVLQKDYND---- 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 464 FPVVLEQLDDYNAKLSDLQEALDQALNHVRDAEDMNRataaRQRDHEKQQERVREQMEAVNMSLNTSADSLTTPRLTL-S 542
Cdd:PRK01156 341 YIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKK----KIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEInV 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 543 ELDDIIKNASGIYAEIDGAKNELQVKLSNLSNL-----------------SHDLVQEAIDHAQELQQEANELSRKLHSSD 605
Cdd:PRK01156 417 KLQDISSKVSSLNQRIRALRENLDELSRNMEMLngqsvcpvcgttlgeekSNHIINHYNEKKSRLEEKIREIEIEVKDID 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 606 MNGLVQKALDASNVYENIVNYVSEANETAEFALNTTDrIYDAVSgidtQIIYHKDESENLLNQAR-----ELQAKAESSS 680
Cdd:PRK01156 497 EKIVDLKKRKEYLESEEINKSINEYNKIESARADLED-IKIKIN----ELKDKHDKYEEIKNRYKslkleDLDSKRTSWL 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 681 DEAVADTSRRVGGALARKSALKTRLSDAVKQLQAAERG--DAQQRLGQS-RLITEEANRTTMEVQQATAPMAnNLTNWSQ 757
Cdd:PRK01156 572 NALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGfpDDKSYIDKSiREIENEANNLNNKYNEIQENKI-LIEKLRG 650
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 387540784 758 NLQHFDSSAynTAVDSARDAVRNLTEVVPQLLDQLRTVEQKRPASNVSASiqRIRELIAQTRSVASKIQ 826
Cdd:PRK01156 651 KIDNYKKQI--AEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRA--RLESTIEILRTRINELS 715
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
469-680 |
1.56e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.55 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 469 EQLDDYNAKLSDLQEALD--QALNHVRDAEDMNRATAARQRDHEKQQERVREQMEAVNMSLNTSADSLTTPRLTLSELdd 546
Cdd:COG3206 182 EQLPELRKELEEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL-- 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 547 iikNASGIYAEIDGAKNELQVKLSNLSNL---SHDLVQEAIDHAQELQQE-ANELSRKLHS--SDMNGLVQKALDASNVY 620
Cdd:COG3206 260 ---LQSPVIQQLRAQLAELEAELAELSARytpNHPDVIALRAQIAALRAQlQQEAQRILASleAELEALQAREASLQAQL 336
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 621 ENIVNYVSEANETaEFALNTTDRIYDAvsgidTQIIYhkdesENLLNQARELQAKAESSS 680
Cdd:COG3206 337 AQLEARLAELPEL-EAELRRLEREVEV-----ARELY-----ESLLQRLEEARLAEALTV 385
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
337-600 |
1.57e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 45.67 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 337 NTMKSLLSDVEELVEKENQASRK-GQLIQKESmdtikhasQLVEQAHDMRDKIQEINNKMlyygeehelspKEISEKlvl 415
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEiEELKEKRD--------ELNEELKELAEKRDELNAQV-----------KELREE--- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 416 AQKMleeirrrqpfftqRELVDEEADEAHELLSQAESWQrlhNETRTLFpvvlEQLDDYNAKLSDLQ------EALDQAL 489
Cdd:COG1340 59 AQEL-------------REKRDELNEKVKELKEERDELN---EKLNELR----EELDELRKELAELNkaggsiDKLRKEI 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 490 NHVRDAEDmnraTAARQRDHEKQ----QERVREQMEAVNMSLNTSadslttprltlSELDDIIKNASGIYAEIDGAKNEL 565
Cdd:COG1340 119 ERLEWRQQ----TEVLSPEEEKElvekIKELEKELEKAKKALEKN-----------EKLKELRAELKELRKEAEEIHKKI 183
|
250 260 270
....*....|....*....|....*....|....*
gi 387540784 566 QvKLSNLSNLSHDLVQEAIDHAQELQQEANELSRK 600
Cdd:COG1340 184 K-ELAEEAQELHEEMIELYKEADELRKEADELHKE 217
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
306-568 |
2.64e-04 |
|
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: 46.21 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 306 EINATIYLLKTKLSERENQYALRKIQINNAE-NTMKSLLSDVEELVE----KENQASRKGQLIQKESMDTIKHASQLVEQ 380
Cdd:TIGR02169 769 ELEEDLHKLEEALNDLEARLSHSRIPEIQAElSKLEEEVSRIEARLReieqKLNRLTLEKEYLEKEIQELQEQRIDLKEQ 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 381 AHDMRDKIQEIN---NKMLYYGEEHELSPKEISEKLV-------LAQKMLEEIRRRQpfftqRELvDEEADEAHELLSQ- 449
Cdd:TIGR02169 849 IKSIEKEIENLNgkkEELEEELEELEAALRDLESRLGdlkkerdELEAQLRELERKI-----EEL-EAQIEKKRKRLSEl 922
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 450 AESWQRLHNETRTLFPVVLEQLDDYNAKLS--DLQEALDQALNHVRDAEDMN-RA------TAARQRDHEKQQERVREQM 520
Cdd:TIGR02169 923 KAKLEALEEELSEIEDPKGEDEEIPEEELSleDVQAELQRVEEEIRALEPVNmLAiqeyeeVLKRLDELKEKRAKLEEER 1002
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 387540784 521 EAVnmsLNTSADSLTTPRLTLSE-LDDIIKNASGIYAEIDGAKNELQVK 568
Cdd:TIGR02169 1003 KAI---LERIEEYEKKKREVFMEaFEAINENFNEIFAELSGGTGELILE 1048
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
469-672 |
3.15e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.39 E-value: 3.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 469 EQLDDYNAKLSDLQEALDQALNHVRDAEDMNRATAarqRDHEKQQERVREQMEAVNMSLNTSADSLTTPRLTLSELDDII 548
Cdd:PHA02562 195 QQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEA---KTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKI 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 549 KNASGI---YAE----------IDGAKNELQVKLSNLSNLSH--DLVQEAIDHAQELQQEANELSRKLHssDMNGlvqka 613
Cdd:PHA02562 272 EQFQKVikmYEKggvcptctqqISEGPDRITKIKDKLKELQHslEKLDTAIDELEEIMDEFNEQSKKLL--ELKN----- 344
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 387540784 614 lDASNVYENIVNYVSEAnetaefalnttDRIYDAVSGIDTQIIYHKDESENLLNQAREL 672
Cdd:PHA02562 345 -KISTNKQSLITLVDKA-----------KKVKAAIEELQAEFVDNAEELAKLQDELDKI 391
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
361-601 |
3.33e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 361 QLIQKESMDTIKHASQLVEQAHDMRDKIQEINNKMLYYGEEHELSPKEISEKLvlaqKMLEEIRRRQpffTQRELVDEEA 440
Cdd:COG4717 291 LLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELL----DRIEELQELL---REAEELEEEL 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 441 DEAHELLSQAESWQRLHNETRTLFPVVLEQLDDYNAKLSDLQEALDQALNHVRDAEDMNRATaarqrdhekQQERVREQM 520
Cdd:COG4717 364 QLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEAL---------DEEELEEEL 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 521 EAVNMSLNTSADSLTTPRLTLSELDDIIKNA--SGIYAEIDGAKNELQVKLSNLS------NLSHDLVQEAIDHAQE--- 589
Cdd:COG4717 435 EELEEELEELEEELEELREELAELEAELEQLeeDGELAELLQELEELKAELRELAeewaalKLALELLEEAREEYREerl 514
|
250
....*....|....
gi 387540784 590 --LQQEANELSRKL 601
Cdd:COG4717 515 ppVLERASEYFSRL 528
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
299-760 |
3.64e-04 |
|
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: 45.73 E-value: 3.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 299 AAHRHVNEINATIYLLKTKLSERENQYA-LRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLIQKESMDTIKhASQL 377
Cdd:pfam02463 227 LYLDYLKLNEERIDLLQELLRDEQEEIEsSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSE-LLKL 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 378 VEQAHDMRDKIQEinnkmlyygeeHELSPKEISEKLVLAQK--------MLEEIRRRQPF-----FTQRELVDEEADEAH 444
Cdd:pfam02463 306 ERRKVDDEEKLKE-----------SEKEKKKAEKELKKEKEeieelekeLKELEIKREAEeeeeeELEKLQEKLEQLEEE 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 445 ELLSQAESWQRLHNETRTLFPVVLEQLDDYNAKLSDLQEAldqalnhvRDAEDMNRATAARQRDHEKQQERVREQMEAvn 524
Cdd:pfam02463 375 LLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELA--------RQLEDLLKEEKKEELEILEEEEESIELKQG-- 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 525 mSLNTSADSLTTPRLTLSELDDIIKNASGIYAEIDGAKNELQVKLsnlsnLSHDLVQEAIDHAQELQQEANELSRKLHSS 604
Cdd:pfam02463 445 -KLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLEL-----LLSRQKLEERSQKESKARSGLKVLLALIKD 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 605 DMNGLVQKALDASNVYENIVNYVSEANETAEFALNTTDRI--------YDAVSGIDTQIIYHKDESENLLNQARELQ--- 673
Cdd:pfam02463 519 GVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADeveerqklVRALTELPLGARKLRLLIPKLKLPLKSIAvle 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 674 -------AKAESSSDEAVADTSRRVGGALARKSALKTRLSDAVKQLQaaERGDAQQRLGQSRLITEEANRTTMEVQQATA 746
Cdd:pfam02463 599 idpilnlAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKE--SGLRKGVSLEEGLAEKSEVKASLSELTKELL 676
|
490
....*....|....
gi 387540784 747 PMANNLTNWSQNLQ 760
Cdd:pfam02463 677 EIQELQEKAESELA 690
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
659-817 |
3.73e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 3.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 659 KDESENLLNQARELQAK-AESSSDEAVADTSRR--------VGGAlaRKSALKTRLSDAVKQLQAAE--RGDAQQRLGQS 727
Cdd:COG4913 294 EAELEELRAELARLEAElERLEARLDALREELDeleaqirgNGGD--RLEQLEREIERLERELEERErrRARLEALLAAL 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 728 RLiTEEANRTTMEVQQATAPMAnnLTNWSQnlqhfDSSAYNTAVDSARDAVRNLTEVVPQLLDQLRTVEQKRpaSNVSAS 807
Cdd:COG4913 372 GL-PLPASAEEFAALRAEAAAL--LEALEE-----ELEALEEALAEAEAALRDLRRELRELEAEIASLERRK--SNIPAR 441
|
170
....*....|
gi 387540784 808 IQRIRELIAQ 817
Cdd:COG4913 442 LLALRDALAE 451
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
316-543 |
3.99e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 3.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 316 TKLSERENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLIQKEsMDT----IKHASQLVEQAhdmRDKIQEI 391
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAE-IDKlqaeIAEAEAEIEER---REELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 392 NNKMlyYGEEHELSPKEIseklVLAQKMLEEirrrqpFFTQRELVDEEADEAHELLSQAESWQRLHNETRTLfpvVLEQL 471
Cdd:COG3883 92 ARAL--YRSGGSVSYLDV----LLGSESFSD------FLDRLSALSKIADADADLLEELKADKAELEAKKAE---LEAKL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 387540784 472 DDYNAKLSDLQEALDQALNHVRDAEDMNRATAARQRDHEKQQERVREQMEAVNMSLNTSADSLTTPRLTLSE 543
Cdd:COG3883 157 AELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
407-603 |
4.17e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 4.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 407 KEISEKLVLAQKMLEEIRRrqpfftQRELVDEEADEAHELLSQAES---WQRLHNETRTLfPVVLEQLDDYNAKLSDLQE 483
Cdd:COG4913 620 AELEEELAEAEERLEALEA------ELDALQERREALQRLAEYSWDeidVASAEREIAEL-EAELERLDASSDDLAALEE 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 484 ALDQALNHVRDAEDMNRATAARQRDHEKQQERVREQMEAVNMSLNT-SADSLTTPRLTLSELddiiknasgiYAEIDGAK 562
Cdd:COG4913 693 QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAaEDLARLELRALLEER----------FAAALGDA 762
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 387540784 563 NELQVKlsnlSNLSHDLVQEaidhAQELQQEANELSRKLHS 603
Cdd:COG4913 763 VERELR----ENLEERIDAL----RARLNRAEEELERAMRA 795
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
501-807 |
4.90e-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: 44.37 E-value: 4.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 501 ATAARQRDHEKQQERVREQMEAVNMSLNTSADSLTTPRLTLSELDDIIKNASGIYAEIDGAKNELQVKLsnlsnlshdlv 580
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL----------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 581 qeaidhaQELQQEANELSRKLHSsdmnglvQKALDASNVYeniVNYVSEANETAEFALNTTDriydaVSGIDTQIIYHKD 660
Cdd:COG4942 86 -------AELEKEIAELRAELEA-------QKEELAELLR---ALYRLGRQPPLALLLSPED-----FLDAVRRLQYLKY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 661 ESENLLNQARELQAKaesssdeavadtsrrvggaLARKSALKTRLSDAVKQLQAAErgdAQQRLGQSRLITEEANRTTME 740
Cdd:COG4942 144 LAPARREQAEELRAD-------------------LAELAALRAELEAERAELEALL---AELEEERAALEALKAERQKLL 201
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 387540784 741 VQQATapmannltnwsqnlqhfDSSAYNTAVDSARDAVRNLTEVVPQLLDQLRTVEQKRPASNVSAS 807
Cdd:COG4942 202 ARLEK-----------------ELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
336-675 |
5.25e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.33 E-value: 5.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 336 ENTMKSLLSDVEELVEKENQASRKGQLIQKesmdTIKHASQLV------------EQA-HDMRDKIQEINNKMlyygEEH 402
Cdd:PRK04863 785 EKRIEQLRAEREELAERYATLSFDVQKLQR----LHQAFSRFIgshlavafeadpEAElRQLNRRRVELERAL----ADH 856
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 403 ELSPKEISEKLVLAQKMLEEIRRRQPFFT--QRELVDEEADEAHELLSQAESWQR-LHNETRTLfpvvlEQLDDYNAKLS 479
Cdd:PRK04863 857 ESQEQQQRSQLEQAKEGLSALNRLLPRLNllADETLADRVEEIREQLDEAEEAKRfVQQHGNAL-----AQLEPIVSVLQ 931
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 480 DLQEALDQAlnhvrdaedmnrataarQRDH---EKQQERVREQMEAVnmslntsaDSLTTPRLTLSelddiIKNASGIYA 556
Cdd:PRK04863 932 SDPEQFEQL-----------------KQDYqqaQQTQRDAKQQAFAL--------TEVVQRRAHFS-----YEDAAEMLA 981
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 557 EIDGAKNELQVKLSNLSNLSHDLVQEAIDHAQELQQeANELSRKLHSSdMNGLVQKALDASNVYENI-VNYVSEANETAE 635
Cdd:PRK04863 982 KNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQ-YNQVLASLKSS-YDAKRQMLQELKQELQDLgVPADSGAEERAR 1059
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 387540784 636 falNTTDRIYDAVSG-------IDTQIIYHKDESENLLNQARELQAK 675
Cdd:PRK04863 1060 ---ARRDELHARLSAnrsrrnqLEKQLTFCEAEMDNLTKKLRKLERD 1103
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
305-671 |
5.44e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.89 E-value: 5.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 305 NEINATIYLLKTKLSerenqyalrkiqinNAENTMKSLLSDVEELveKENQASRKGQ---------LIQKESMDTIKHAS 375
Cdd:PRK01156 412 NEINVKLQDISSKVS--------------SLNQRIRALRENLDEL--SRNMEMLNGQsvcpvcgttLGEEKSNHIINHYN 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 376 qlvEQAHDMRDKIQEINNKMlyygeehelspKEISEKLVLAQKMLE-----EIRRRQPFFTQ-----RELVDEEADEAhE 445
Cdd:PRK01156 476 ---EKKSRLEEKIREIEIEV-----------KDIDEKIVDLKKRKEyleseEINKSINEYNKiesarADLEDIKIKIN-E 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 446 LLSQAESWQRLHNETRTLFPVVLEQ-LDDYNAKLS--------DLQEALDQALNHVRDAED-MNRATAARQRDHEKQQER 515
Cdd:PRK01156 541 LKDKHDKYEEIKNRYKSLKLEDLDSkRTSWLNALAvislidieTNRSRSNEIKKQLNDLESrLQEIEIGFPDDKSYIDKS 620
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 516 VREQMEAVNmSLNTSADSLTTPRLTLSELDDIIKNASGIYAEIDG---AKNELQVKLSNlSNLSHDLVQEAIDHAQELQQ 592
Cdd:PRK01156 621 IREIENEAN-NLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSiipDLKEITSRIND-IEDNLKKSRKALDDAKANRA 698
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 387540784 593 EANELSRKLHSsDMNGLVQKALDasnvyeniVNYVSEANETAEFALNTTDRIYDAVSGIDTQIIYHKDESENLLNQARE 671
Cdd:PRK01156 699 RLESTIEILRT-RINELSDRIND--------INETLESMKKIKKAIGDLKRLREAFDKSGVPAMIRKSASQAMTSLTRK 768
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
304-602 |
6.10e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 6.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 304 VNEINATIYLLKTKLSERENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLIQKESMDTIKHASQLVEQAHD 383
Cdd:COG4372 82 LEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLES 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 384 MRDKIQEINNkmlyygEEHELSPKEISEKLvlaQKMLEEIRRRQPFFTQRELVDEEADEAHELLSQAESwQRLHNETRTL 463
Cdd:COG4372 162 LQEELAALEQ------ELQALSEAEAEQAL---DELLKEANRNAEKEEELAEAEKLIESLPRELAEELL-EAKDSLEAKL 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 464 FPVVLEQLDDYNAKLSDLQEALDQALNHVRDAEDMNRATAARQRDHEKQQERVREQMEAVNmslNTSADSLTTPRLTLSE 543
Cdd:COG4372 232 GLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAA---LELKLLALLLNLAALS 308
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 387540784 544 LDDIIKNASGIYAEIDGAKNELQVKLSNLSNLSHDLVQEAIDHAQELQQEANELSRKLH 602
Cdd:COG4372 309 LIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGV 367
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
298-596 |
6.99e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 6.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 298 AAAHRHVNEINATIYLLKTKLSERENQYALRKIQINNAENTMKSLLSDVEELVEKEnqasrkgqliqKESMDTIKHASQL 377
Cdd:PRK02224 373 EEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRERE-----------AELEATLRTARER 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 378 VEQAHDMRD--KIQEInnkmlyyGEEHELSP--KEISEKLVLAQKM---LEEIRrrqpffTQRELVDEEADEAHELLSQA 450
Cdd:PRK02224 442 VEEAEALLEagKCPEC-------GQPVEGSPhvETIEEDRERVEELeaeLEDLE------EEVEEVEERLERAEDLVEAE 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 451 ESWQRLHNETRTLFPVVLEQLDDYNAKLSDLQEALDQALNHVRDAEDmNRATAARQRDhekQQERVREQMEAVN---MSL 527
Cdd:PRK02224 509 DRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEE-KREAAAEAEE---EAEEAREEVAELNsklAEL 584
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 387540784 528 NTSADSLTTPRLTLSELDDIIKNASGI------YAEI-DGAKNELQVKLSNLSNLSHDLVQEAIDHAQELQQEANE 596
Cdd:PRK02224 585 KERIESLERIRTLLAAIADAEDEIERLrekreaLAELnDERRERLAEKRERKRELEAEFDEARIEEAREDKERAEE 660
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
417-677 |
1.06e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.98 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 417 QKMLEEIRRrqpfftQRELVDEEADEA----HELLSQAESW--QR--LHNETRTL---FPVVLEQLDDYNAKLSDLQEAL 485
Cdd:COG1340 7 SSSLEELEE------KIEELREEIEELkekrDELNEELKELaeKRdeLNAQVKELreeAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 486 D---QALNHVRDAEDMNRATAARQRDHEKQQERVREQMEAVNMSLNTSAdslttprLTLSELDDIIKNASGIYAEIDGAK 562
Cdd:COG1340 81 DelnEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEV-------LSPEEEKELVEKIKELEKELEKAK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 563 --NELQVKLSNLSNLS----------HDLVQEAIDHAQELQQEANELSRKLhssdmNGLVQKALDAsnvYENIVNYVSEA 630
Cdd:COG1340 154 kaLEKNEKLKELRAELkelrkeaeeiHKKIKELAEEAQELHEEMIELYKEA-----DELRKEADEL---HKEIVEAQEKA 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 387540784 631 NET-AEFalnttDRIYDAVSGIDTQIIYHKDESENLL--NQARELQAKAE 677
Cdd:COG1340 226 DELhEEI-----IELQKELRELRKELKKLRKKQRALKreKEKEELEEKAE 270
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
469-600 |
1.08e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.60 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 469 EQLDDYNAKLSDLQEALDQALNHVRDAEDMNRATAARQRDHEKQQERVR--EQMEAVNMSLntsaDSLttpRLTLSELDD 546
Cdd:COG1579 38 DELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnKEYEALQKEI----ESL---KRRISDLED 110
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 387540784 547 IIKNasgIYAEIDGAKNELQVKLSNLSNLSHDL--VQEAIDHA-QELQQEANELSRK 600
Cdd:COG1579 111 EILE---LMERIEELEEELAELEAELAELEAELeeKKAELDEElAELEAELEELEAE 164
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
525-744 |
1.08e-03 |
|
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: 42.78 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 525 MSLNTSADSLTTPRLTLSELDDIIKNASgiyaEIDGAKNELQVKLSNLSNLSHDLVQEaidhAQELQQEANELSRK--LH 602
Cdd:pfam06008 2 LSLNSLTGALPAPYKINYNLENLTKQLQ----EYLSPENAHKIQIEILEKELSSLAQE----TEELQKKATQTLAKaqQV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 603 SSDMNGLVQKALDASNVYENIVNYVSEANETAEfALNTTDriyDAVSGidTQIIYHKDESENLLNQARELQAKAESSSDE 682
Cdd:pfam06008 74 NAESERTLGHAKELAEAIKNLIDNIKEINEKVA-TLGEND---FALPS--SDLSRMLAEAQRMLGEIRSRDFGTQLQNAE 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 387540784 683 AVADTSRRVggaLAR---------------KSALKTRLSDAVKQLQaaergDAQQRLGQSRLITEEANRTTMEVQQA 744
Cdd:pfam06008 148 AELKAAQDL---LSRiqtwfqspqeenkalANALRDSLAEYEAKLS-----DLRELLREAAAKTRDANRLNLANQAN 216
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
339-601 |
1.90e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 339 MKSLLSDVEELVEKENQASRKGQLIQKEsmdtIKHASQLVEQaHDMRDKIQEINNKMLYYGEEhELSPK-----EISEKL 413
Cdd:PRK03918 461 LKRIEKELKEIEEKERKLRKELRELEKV----LKKESELIKL-KELAEQLKELEEKLKKYNLE-ELEKKaeeyeKLKEKL 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 414 VLAQK----MLEEIRRRQPFFTQRELVDEEADEAHELLSQaeswqrLHNETRTLFpvvLEQLDDYNAKLSDLQEALDQAL 489
Cdd:PRK03918 535 IKLKGeiksLKKELEKLEELKKKLAELEKKLDELEEELAE------LLKELEELG---FESVEELEERLKELEPFYNEYL 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 490 NhVRDAEDmnrataaRQRDHEKQQERVREqmeavnmslntsadslttprltlsELDDIIKNASGIYAEIDGAKNELQVKL 569
Cdd:PRK03918 606 E-LKDAEK-------ELEREEKELKKLEE------------------------ELDKAFEELAETEKRLEELRKELEELE 653
|
250 260 270
....*....|....*....|....*....|..
gi 387540784 570 SNLSNLSHdlvqeaidhaQELQQEANELSRKL 601
Cdd:PRK03918 654 KKYSEEEY----------EELREEYLELSREL 675
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
366-599 |
2.03e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 366 ESMDTIKHASQLVEQAHDMRDKIQ------EINNKMLYYGEEHElspKEISEKLVLAQKmLEEIRRRQPFFTQRelVDEE 439
Cdd:COG4717 341 ELLDRIEELQELLREAEELEEELQleeleqEIAALLAEAGVEDE---EELRAALEQAEE-YQELKEELEELEEQ--LEEL 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 440 ADEAHELLSQA--ESWQRLHNETRtlfpvvlEQLDDYNAKLSDLQEALDQALNHVRDAEDMNRATAARQrdhekQQERVR 517
Cdd:COG4717 415 LGELEELLEALdeEELEEELEELE-------EELEELEEELEELREELAELEAELEQLEEDGELAELLQ-----ELEELK 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 518 EQMEAV---NMSLNTSADSLTTPRLTLSE--LDDIIKNASGIYAEI-DGAKNELQVklsnlsNLSHDLVqeaIDHAQELQ 591
Cdd:COG4717 483 AELRELaeeWAALKLALELLEEAREEYREerLPPVLERASEYFSRLtDGRYRLIRI------DEDLSLK---VDTEDGRT 553
|
....*...
gi 387540784 592 QEANELSR 599
Cdd:COG4717 554 RPVEELSR 561
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
359-675 |
2.68e-03 |
|
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: 41.99 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 359 KGQLIQKESMDTIKHASQLVEQAHDMRDKIQEINnkmlyygeehelspKEISEKLVLAQKMLEEIRRRqpfftQRELVDE 438
Cdd:pfam04108 4 SAQDLCRWANELLTDARSLLEELVVLLAKIAFLR--------------RGLSVQLANLEKVREGLEKV-----LNELKKD 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 439 EADEAHELLSQAESWQR-LHNETRTLFPVVLEQLDDYNAKLSDL--QEALDQALNHVRdaedmnrataarqrdheKQQER 515
Cdd:pfam04108 65 FKQLLKDLDAALERLEEtLDKLRNTPVEPALPPGEEKQKTLLDFidEDSVEILRDALK-----------------ELIDE 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 516 VREQMEAVNMSLNTSADSLTTPRLTLSELDDIIKNASGIYaeidgaknelqVKLSNLSNLSHDLVQ--EAIDHAQELQQE 593
Cdd:pfam04108 128 LQAAQESLDSDLKRFDDDLRDLQKELESLSSPSESISLIP-----------TLLKELESLEEEMASllESLTNHYDQCVT 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 594 ANELSRKLHSSDMNGLVQKALDASNVYENIVNYVSEANETAEFALNTTDRIYDAvsgidtqiiyhKDESENLLNQARELQ 673
Cdd:pfam04108 197 AVKLTEGGRAEMLEVLENDARELDDVVPELQDRLDEMENNYERLQKLLEQKNSL-----------IDELLSALQLIAEIQ 265
|
..
gi 387540784 674 AK 675
Cdd:pfam04108 266 SR 267
|
|
| DivIVA |
pfam05103 |
DivIVA protein; The Bacillus subtilis divIVA1 mutation causes misplacement of the septum ... |
376-460 |
2.84e-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: 39.86 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 376 QLVEQAHDMRDKIQEINNKMLYYGEEHElspkEISEKLVLAQKMLEEIRRRQPffTQRELVDEEA-DEAHELLSQAES-W 453
Cdd:pfam05103 36 ALIRENAELKEKIEELEEKLAHYKNLEE----TLQNTLILAQETAEEVKANAQ--KEAELIIKEAeAKAERIVDDANNeV 109
|
....*..
gi 387540784 454 QRLHNET 460
Cdd:pfam05103 110 KKINDEI 116
|
|
| Laminin_G_3 |
pfam13385 |
Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin ... |
1490-1612 |
4.16e-03 |
|
Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin A-like lectin/glucanases superfamily.
Pssm-ID: 463865 [Multi-domain] Cd Length: 151 Bit Score: 39.67 E-value: 4.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 1490 IRLRTRSSHGMIFYVSDQEeNDFMTLFLAHGRLVYMFNVGHKKLK-IRSQEKYNDGLWHDVVFIREKSSGRLVIDGLRVL 1568
Cdd:pfam13385 25 VKPDSLPGWARAIISSSGG-GGYSLGLDGDGRLRFAVNGGNGGWDtVTSGASVPLGQWTHVAVTYDGGTLRLYVNGVLVG 103
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 387540784 1569 EESLPPTeATWKIKGPIYLGGVAPGKAVKNVQINSIYSFSGCLS 1612
Cdd:pfam13385 104 SSTLTGG-PPPGTGGPLYIGRSPGGDDYFNGLIDEVRIYDRALS 146
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
407-601 |
4.27e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.93 E-value: 4.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 407 KEISEKLVLAQKMLEEIRRRQPFFTqrelVDEEADEAHELLSQAESwQRlhNETRTlfpvvleQLDDYNAKLSDLQEALD 486
Cdd:COG3206 185 PELRKELEEAEAALEEFRQKNGLVD----LSEEAKLLLQQLSELES-QL--AEARA-------ELAEAEARLAALRAQLG 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 487 QALNHVRDAEDMNRATAARQRDHEKQQERVReqmeavnMSLNTSADSlttPRLT-----LSELDDIIKN-ASGIYAEIDG 560
Cdd:COG3206 251 SGPDALPELLQSPVIQQLRAQLAELEAELAE-------LSARYTPNH---PDVIalraqIAALRAQLQQeAQRILASLEA 320
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 387540784 561 AKNELQVKLSNLSNLSHDLvQEAIDHAQELQQEANELSRKL 601
Cdd:COG3206 321 ELEALQAREASLQAQLAQL-EARLAELPELEAELRRLEREV 360
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
317-451 |
4.52e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.05 E-value: 4.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 317 KLSERENQYALRKiQINNAENTMKSLLSDVEELVEKENQASRK----GQLIQK--ESMDTI-KHASQLVEQAHDMRDKIQ 389
Cdd:COG1340 141 KIKELEKELEKAK-KALEKNEKLKELRAELKELRKEAEEIHKKikelAEEAQElhEEMIELyKEADELRKEADELHKEIV 219
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 387540784 390 EINNKMlyyGEEHEL------SPKEISEKLVLAQKMLEEIRRRQpfftQRELVDEEADEAHELLSQAE 451
Cdd:COG1340 220 EAQEKA---DELHEEiielqkELRELRKELKKLRKKQRALKREK----EKEELEEKAEEIFEKLKKGE 280
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
469-727 |
4.73e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.29 E-value: 4.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 469 EQLDDYNAKLSDLQEALDQalnhvrdaedmnraTAARQRDHEKQQERVREQMEAVNMSLNTSADSLTTPRLTLSELDDII 548
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAE--------------LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 549 KNASgiyAEIDGAKNELQVKLSNLSNLshdlvqeaIDHAQELQQeANELSRKLHSSDMNGLVQKAldasnvyeNIVNYVS 628
Cdd:COG4942 86 AELE---KEIAELRAELEAQKEELAEL--------LRALYRLGR-QPPLALLLSPEDFLDAVRRL--------QYLKYLA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 629 EANETAEFALNTTdriYDAVSGIDTQIIYHKDESENLLNQARELQA---KAESSSDEAVADTSRRVGGALARKSALK--- 702
Cdd:COG4942 146 PARREQAEELRAD---LAELAALRAELEAERAELEALLAELEEERAaleALKAERQKLLARLEKELAELAAELAELQqea 222
|
250 260
....*....|....*....|....*
gi 387540784 703 TRLSDAVKQLQAAERGDAQQRLGQS 727
Cdd:COG4942 223 EELEALIARLEAEAAAAAERTPAAG 247
|
|
| Rcc_KIF21A |
cd22263 |
regulatory coiled-coil domain found in kinesin-like protein KIF21A; KIF21A, also called ... |
328-395 |
4.84e-03 |
|
regulatory coiled-coil domain found in kinesin-like protein KIF21A; KIF21A, also called kinesin-like protein KIF2 or renal carcinoma antigen NY-REN-62, is a microtubule-binding motor protein involved in neuronal axonal transport. It works as a microtubule stabilizer that regulates axonal morphology, suppressing cortical microtubule dynamics in neurons. Mutations in KIF21A cause congenital fibrosis of the extraocular muscles type 1 (CFEOM1). In vitro, it has a plus-end directed motor activity. This model corresponds to the regulatory coiled-coil domain of KIF21A, which folds into an intramolecular antiparallel coiled-coil monomer in solution, but crystallizes into a dimeric domain-swapped antiparallel coiled-coil.
Pssm-ID: 410204 [Multi-domain] Cd Length: 82 Bit Score: 37.98 E-value: 4.84e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 387540784 328 RKIQINNAENTMKSLLSDVEELVEKENQASRKGQLIQKESMDTIKHASQLVEQAHDMRDKIQEINNKM 395
Cdd:cd22263 1 QRMTISNMEADMNRLLKQREELTKRREKLSKKREKIIKENGEGDKNVHNINEEMESLTANIDYINDSI 68
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
314-678 |
5.32e-03 |
|
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: 41.54 E-value: 5.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 314 LKTKLSERENQYALRKIQINNAENTMKSLLSDVEEL------VEKENQaSRKGQLIQKES-MDTIKHASQ-LVEQAHDMR 385
Cdd:TIGR04523 312 LKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLkkeltnSESENS-EKQRELEEKQNeIEKLKKENQsYKQEIKNLE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 386 DKIQEINNKMLYYGEEHELSPKEISEKLVLAQKMLEEIRRrqpfftQRELVDEEADEAHELLSQAESWQRLHNETRTLFP 465
Cdd:TIGR04523 391 SQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIER------LKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRE 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 466 VVLEQLDDYNAKLSDLQEALDQALNHVRDAEDMNRATAARQRDHEKQQERVREQMEavnmSLNTSADSLTTprlTLSELD 545
Cdd:TIGR04523 465 SLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKIS----SLKEKIEKLES---EKKEKE 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 546 DiiknasgiyaEIDGAKNELqvkLSNLSNLSHDLVQEAIDhaqELQQEANELSrklhssdmngLVQKALDASN--VYENI 623
Cdd:TIGR04523 538 S----------KISDLEDEL---NKDDFELKKENLEKEID---EKNKEIEELK----------QTQKSLKKKQeeKQELI 591
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 387540784 624 VNYVSEANE-TAEFALNTTdriydAVSGIDTQIIYHKDESENLLNQARELQAKAES 678
Cdd:TIGR04523 592 DQKEKEKKDlIKEIEEKEK-----KISSLEKELEKAKKENEKLSSIIKNIKSKKNK 642
|
|
| Prefoldin_alpha_GimC |
cd23160 |
Prefoldin alpha subunit, archaeal; Archaeal alpha subunit of prefoldin (GimC), a hexameric ... |
510-601 |
5.73e-03 |
|
Prefoldin alpha subunit, archaeal; Archaeal alpha subunit of prefoldin (GimC), a hexameric molecular chaperone complex, found in both eukaryotes and archaea. Prefoldin binds and stabilizes newly synthesized polypeptides allowing them to fold correctly. The complex contains two alpha and four beta subunits, the two subunits being evolutionarily related. In archaea, there is usually only one gene for each subunit while in eukaryotes there two or more paralogous genes encoding each subunit adding heterogeneity to the structure of the hexamer. The structure of the complex consists of a double beta barrel assembly with six protruding coiled-coils.
Pssm-ID: 467476 [Multi-domain] Cd Length: 127 Bit Score: 38.62 E-value: 5.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 510 EKQQERVREQMEAVNMSLNtsadSLTTPRLTLSELDDI-------------------IKNA--------SGIYAE--IDG 560
Cdd:cd23160 13 EQQAEALQQQIELLQASIN----ELNRAKETLEELKKLkegteilvpigggsfvkakIKDTdkvlvnigAGVVVEktIDE 88
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 387540784 561 AKNELQVKLSNLSNLSHDLVQEaidhAQELQQEANELSRKL 601
Cdd:cd23160 89 AIEILEKRIKELEKALEKLQEQ----LQQIAQRLEELEAEL 125
|
|
| DivIVA |
COG3599 |
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle ... |
376-463 |
6.17e-03 |
|
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442818 [Multi-domain] Cd Length: 125 Bit Score: 38.68 E-value: 6.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 376 QLVEQAHDMRDKIQEINNKMLYYGEEHElspkEISEKLVLAQKMLEEIRR--RQpfftQRELVDEEAD-EAHELLSQAES 452
Cdd:COG3599 38 RLIRENKELKEKLEELEEELEEYRELEE----TLQKTLVVAQETAEEVKEnaEK----EAELIIKEAElEAEKIIEEAQE 109
|
90
....*....|..
gi 387540784 453 -WQRLHNETRTL 463
Cdd:COG3599 110 kARKIVREIEEL 121
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
302-717 |
6.42e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 6.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 302 RHVNEIN--ATIYLlktKLSERENQYALRKIQINNAENTMKSLLSDVEELVEK-ENQASRKGQLIQKESmDTIKHASQLV 378
Cdd:PRK03918 283 KELKELKekAEEYI---KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKElEEKEERLEELKKKLK-ELEKRLEELE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 379 EQAHDMRDKIQEINNKMLYYGEEHELSPKEISEKLVLAQKMLEEIRRRQPFFTQR--ELVDEEAD--EAHELLSQAES-- 452
Cdd:PRK03918 359 ERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARigELKKEIKElkKAIEELKKAKGkc 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 453 ---WQRLHNETRtlfpvvLEQLDDYNAKLSDLQEALDQALNHVRDAED---------MNRATAARQRDHEKQQERVREQM 520
Cdd:PRK03918 439 pvcGRELTEEHR------KELLEEYTAELKRIEKELKEIEEKERKLRKelrelekvlKKESELIKLKELAEQLKELEEKL 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 521 EAVNMS-LNTSADSLttpRLTLSELDDIIKNASGIYAEID------GAKNELQVKLSN----LSNLSHDLVQEAIDHAQE 589
Cdd:PRK03918 513 KKYNLEeLEKKAEEY---EKLKEKLIKLKGEIKSLKKELEkleelkKKLAELEKKLDEleeeLAELLKELEELGFESVEE 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 590 LQQEANELsRKLHSSDMnglvqKALDASNVYENIVNYVSEANETAEFALNTTDRIYDAVSGIDTQI-----IYHKDESEN 664
Cdd:PRK03918 590 LEERLKEL-EPFYNEYL-----ELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELeelekKYSEEEYEE 663
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 387540784 665 LLNQARELqakaesssdeavadtSRRVGGALARKSALKTRLSDAVKQLQAAER 717
Cdd:PRK03918 664 LREEYLEL---------------SRELAGLRAELEELEKRREEIKKTLEKLKE 701
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
469-726 |
6.93e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 6.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 469 EQLDDYNAKLSDLQEALDQALNHVRDAEDMNRATAARQRDHEKQQER---------VREQMEAVNMSLntsaDSLTTPRL 539
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYswdeidvasAEREIAELEAEL----ERLDASSD 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 540 TLSELDDIIKNASGIYAEIDGAKNELQVKLSNLSNlSHDLVQEAIDHAQELQQEANELSRKLHSSDMNGLVQKALDasnv 619
Cdd:COG4913 686 DLAALEEQLEELEAELEELEEELDELKGEIGRLEK-ELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALG---- 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 620 yENIVNYVSEanetaefalnttdRIYDAVSGIDTQIIYHKDESENLLNQ--------ARELQAKAESSSD-EAVADTSRR 690
Cdd:COG4913 761 -DAVERELRE-------------NLEERIDALRARLNRAEEELERAMRAfnrewpaeTADLDADLESLPEyLALLDRLEE 826
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 387540784 691 VGgaLAR-----KSALKTRLSDAVKQLQAA---ERGDAQQRLGQ 726
Cdd:COG4913 827 DG--LPEyeerfKELLNENSIEFVADLLSKlrrAIREIKERIDP 868
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
364-596 |
7.65e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.44 E-value: 7.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 364 QKESMDTIKHASQLVEQAHDMRDKIQEINNKMLYYGEEHELSPKEISEklvlAQKMLEEIRrrqpfftqrELVDEEADEA 443
Cdd:PRK11281 51 QKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQ----AQAELEALK---------DDNDEETRET 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 444 HELLSQAESWQRLhNETRTLFPVVLEQLDDYNAKLSDLQEALDQALNHVrdaedmnraTAARQRdhekqqervreqMEAV 523
Cdd:PRK11281 118 LSTLSLRQLESRL-AQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAAL---------YANSQR------------LQQI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387540784 524 NMSLNTSADSLTTPRLTLSELddiiknasgIYAEID--GAKNELQVK-------LSNLSNLSHDLVQEAIDHAQE----L 590
Cdd:PRK11281 176 RNLLKGGKVGGKALRPSQRVL---------LQAEQAllNAQNDLQRKslegntqLQDLLQKQRDYLTARIQRLEHqlqlL 246
|
....*.
gi 387540784 591 QQEANE 596
Cdd:PRK11281 247 QEAINS 252
|
|
|