|
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 |
2.17e-101 |
|
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: 325.91 E-value: 2.17e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 291 VLSVSSGAAAHRHVNEINATIYLLKTKLSERENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLVQKESMDT 370
Cdd:pfam06008 1 LLSLNSLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 371 INHASQLVEQAHDMRDKIQEINNKMLYYGEE-HELSPKEISEKLVLAQKMLEEIRSRQpFFTQRELVDEEADEAYELLSQ 449
Cdd:pfam06008 81 LGHAKELAEAIKNLIDNIKEINEKVATLGENdFALPSSDLSRMLAEAQRMLGEIRSRD-FGTQLQNAEAELKAAQDLLSR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 450 AESW-QRLHNETRTLFPVVLEQLDDYNAKLSDLQEALDQALNYVRDAEDMNRATAARQRDHEKQQERVREQMEVVNMSLS 528
Cdd:pfam06008 160 IQTWfQSPQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEETLK 239
|
250
....*....|....*....
gi 1034650228 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 |
2.59e-43 |
|
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: 154.57 E-value: 2.59e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 727 SRLITEEANRTTMEVQQATAPMANNLTNWSQNLQHFDSSA---------YNTAVNSARDAVRNLTEVVPQLLDQLRTVEQ 797
Cdd:pfam06009 1 SKELAREANETAKEVLEQLAPLSQNLENTSEKLSGINRSLeetnelvndANKALDDAGRSVKKLEELAPDLLDKLKPLKQ 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1034650228 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 |
1.99e-39 |
|
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: 144.10 E-value: 1.99e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 1485 KSQFSIRLRTRSSHGMIFYVSDQEENDFMTLFLAHGRLVYMFNVGHKKLKIRSQEKYNDGLWHDVIFIRERSSGRLVIDG 1564
Cdd:cd00110 21 RLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDGQWHSVSVERNGRSVTLSVDG 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1034650228 1565 LRVLEESLPPTEATWKIKGPIYLGGVAPGKavKNVQINSIYSFSGCLSNLQLN 1617
Cdd:cd00110 101 ERVVESGSPGGSALLNLDGPLYLGGLPEDL--KSPGLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
1487-1618 |
1.09e-35 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 132.46 E-value: 1.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 1487 QFSIRLRTRSSHGMIFYVSDQEENDFMTLFLAHGRLVYMFNVGHKKLKIRSQ-EKYNDGLWHDVIFIRERSSGRLVIDGL 1565
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDpTPLNDGQWHRVAVERNGRSVTLSVDGG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1034650228 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 1034650228 1641 GTYFStEGGYVVLDESFNIGLKFEIAFEVRPRSSSGTLVH-GHSVNGEYLNVHMKNGQVIVKVNNGirDFSTSVTPKQSL 1719
Cdd:cd00110 1 GVSFS-GSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYaGSQNGGDFLALELEDGRLVLRYDLG--SGSLVLSSKTPL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034650228 1720 CDGRWHRITVIRDSNVVQLDVDSE-VNHVVGPLNPKPIDHREPVFVGGVPESLLTPRLAPSKPFTGCIRHFVID 1792
Cdd:cd00110 78 NDGQWHSVSVERNGRSVTLSVDGErVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
1664-1794 |
3.92e-31 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 119.37 E-value: 3.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 1664 EIAFEVRPRSSSGTLVHGHSVNG-EYLNVHMKNGQVIVKVNNGIRDFSTSVTPKQsLCDGRWHRITVIRDSNVVQLDVDS 1742
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGgDYLALELRDGRLVLRYDLGSGPARLTSDPTP-LNDGQWHRVAVERNGRSVTLSVDG 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1034650228 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 |
2.58e-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: 117.14 E-value: 2.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 1492 LRTRSSHGMIFYVSDQEeNDFMTLFLAHGRLVYMFNVGHKKLKIRSQEK-YNDGLWHDVIFIRERSSGRLVIDGLRVLEE 1570
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGG-SDFLALELVNGRLVLRYDLGSGPESLLSSGKnLNDGQWHSVRVERNGNTLTLSVDGQTVVSS 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1034650228 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 |
1.72e-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: 1.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 1669 VRPRSSSGTLVHGHSVNGEYLNVHMKNGQVIVKVNNGIRDFSTSVTPKqSLCDGRWHRITVIRDSNVVQLDVDSEVNH-V 1747
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDFLALELVNGRLVLRYDLGSGPESLLSSGK-NLNDGQWHSVRVERNGNTLTLSVDGQTVVsS 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1034650228 1748 VGPLNPKPIDHREPVFVGGVPESLLTPRLAPSKPFTGCIRHFVIDGH 1794
Cdd:pfam02210 80 LPPGESLLLNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
1042-1200 |
8.35e-24 |
|
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: 99.41 E-value: 8.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 1042 SYFFDGSGYAvvrDITRRGKFGQVTRFDIEVRTPADNGLILLM--VNGSMFFRLEMRNGYLHVFYDFGfsGGPVHLEDtl 1119
Cdd:cd00110 1 GVSFSGSSYV---RLPTLPAPRTRLSISFSFRTTSPNGLLLYAgsQNGGDFLALELEDGRLVLRYDLG--SGSLVLSS-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 1120 kKAQINDAKYHEISIIyHNDKKMILVVDR-RHVKSMDNEKMKI--PFTDIYIGGAPPEILQSRALRAHlpldiNFRGCMK 1196
Cdd:cd00110 74 -KTPLNDGQWHSVSVE-RNGRSVTLSVDGeRVVESGSPGGSALlnLDGPLYLGGLPEDLKSPGLPVSP-----GFVGCIR 146
|
....
gi 1034650228 1197 GFQF 1200
Cdd:cd00110 147 DLKV 150
|
|
| LamG |
smart00282 |
Laminin G domain; |
1067-1203 |
2.45e-22 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 94.33 E-value: 2.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 1067 RFDIEVRTPADNGLILLM--VNGSMFFRLEMRNGYLHVFYDFGfsGGPVHLedTLKKAQINDAKYHEISIIyHNDKKMIL 1144
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAgsKGGGDYLALELRDGRLVLRYDLG--SGPARL--TSDPTPLNDGQWHRVAVE-RNGRSVTL 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034650228 1145 VVD---RRHVKSMDNEKMKIPFTDIYIGGAPPEILQSralraHLPLDINFRGCMKGFQFQKK 1203
Cdd:smart00282 76 SVDggnRVSGESPGGLTILNLDGPLYLGGLPEDLKLP-----PLPVTPGFRGCIRNLKVNGK 132
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
1072-1200 |
1.66e-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: 89.02 E-value: 1.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 1072 VRTPADNGLIL-LMVNGSMFFRLEMRNGYLHVFYDFGfsGGPVHLedTLKKAQINDAKYHEISIIYhNDKKMILVVDRRH 1150
Cdd:pfam02210 1 FRTRQPNGLLLyAGGGGSDFLALELVNGRLVLRYDLG--SGPESL--LSSGKNLNDGQWHSVRVER-NGNTLTLSVDGQT 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1034650228 1151 VKSMDNEKMKIPF---TDIYIGGAPPeilqsRALRAHLPLDINFRGCMKGFQF 1200
Cdd:pfam02210 76 VVSSLPPGESLLLnlnGPLYLGGLPP-----LLLLPALPVRAGFVGCIRDVRV 123
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
1230-1369 |
4.11e-19 |
|
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: 85.93 E-value: 4.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 1230 AYFNGQSFIASIQKISFFDGFEGGFNFRTLQPNGLLFYYASG--SDVFSISLDNGTVIMDV----KGIKVQSvDKQYNDG 1303
Cdd:cd00110 2 VSFSGSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQngGDFLALELEDGRLVLRYdlgsGSLVLSS-KTPLNDG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034650228 1304 LSHFVISSVSPTRYELIVDKSRVGSKNPTKGKIEQTqaSEKKFYFGGSPISAQ------YANFTGCISNAYF 1369
Cdd:cd00110 81 QWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLN--LDGPLYLGGLPEDLKspglpvSPGFVGCIRDLKV 150
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
828-1005 |
1.77e-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: 84.01 E-value: 1.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 828 SMMFDGQSAVEVhsrTSMDDLKAFTSLSLYMKppvkrpelTETADQFILYLGSKNaKKEYMGLAIKNDNLVYVYNLGTKD 907
Cdd:cd00110 1 GVSFSGSSYVRL---PTLPAPRTRLSISFSFR--------TTSPNGLLLYAGSQN-GGDFLALELEDGRLVLRYDLGSGS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 908 VEIpldSKPVSSWPAYFSIVKIERVGKHgkVFLTVPSLSStaeekfikkGEFSGDDSLLDLDPEDTVfYVGGVPSNFKLP 987
Cdd:cd00110 69 LVL---SSKTPLNDGQWHSVSVERNGRS--VTLSVDGERV---------VESGSPGGSALLNLDGPL-YLGGLPEDLKSP 133
|
170
....*....|....*...
gi 1034650228 988 TSLNLPGFVGCLELATLN 1005
Cdd:cd00110 134 GLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
853-1006 |
3.54e-18 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 82.39 E-value: 3.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 853 SLSLYMKppvkrpelTETADQFILYLGSKNaKKEYMGLAIKNDNLVYVYNLGTKDVEIPLDSKPVSswPAYFSIVKIERV 932
Cdd:smart00282 1 SISFSFR--------TTSPNGLLLYAGSKG-GGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLN--DGQWHRVAVERN 69
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034650228 933 GKHgkVFLTVPSLSSTAEEKFIKKgefsgddSLLDLDpedTVFYVGGVPSNFKLPTSLNLPGFVGCLELATLNN 1006
Cdd:smart00282 70 GRS--VTLSVDGGNRVSGESPGGL-------TILNLD---GPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNG 131
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
1256-1369 |
1.57e-17 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 80.54 E-value: 1.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 1256 FRTLQPNGLLFYYASG-SDVFSISLDNGTVIMDVK----GIKVQSVDKQYNDGLSHFVISSVSPTRYELIVDKSRVGSKN 1330
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGgSDFLALELVNGRLVLRYDlgsgPESLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1034650228 1331 PTKGkiEQTQASEKKFYFGG------SPISAQYANFTGCISNAYF 1369
Cdd:pfam02210 81 PPGE--SLLLNLNGPLYLGGlpplllLPALPVRAGFVGCIRDVRV 123
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
187-238 |
7.39e-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: 7.39e-16
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1034650228 187 CDCSGNSDPNlifEDCDEVTGQCRnCLRNTTGFKCERCAPGYYGDARIAKNC 238
Cdd:cd00055 2 CDCNGHGSLS---GQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGGC 49
|
|
| LamG |
smart00282 |
Laminin G domain; |
1254-1372 |
1.16e-14 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 72.37 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 1254 FNFRTLQPNGLLFYYAS--GSDVFSISLDNGTVIMDVKG----IKVQSVDKQYNDGLSHFVISSVSPTRYELIVDksrvg 1327
Cdd:smart00282 4 FSFRTTSPNGLLLYAGSkgGGDYLALELRDGRLVLRYDLgsgpARLTSDPTPLNDGQWHRVAVERNGRSVTLSVD----- 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1034650228 1328 SKNPTKGKIEQTQA---SEKKFYFGGSP------ISAQYANFTGCISNAYFTRV 1372
Cdd:smart00282 79 GGNRVSGESPGGLTilnLDGPLYLGGLPedlklpPLPVTPGFRGCIRNLKVNGK 132
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
187-232 |
4.74e-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: 4.74e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1034650228 187 CDCSGNSDPNlifEDCDEVTGQCRnCLRNTTGFKCERCAPGYYGDA 232
Cdd:pfam00053 1 CDCNPHGSLS---DTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLP 42
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
131-185 |
1.01e-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: 64.30 E-value: 1.01e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1034650228 131 PCPCPlPHlANFAESCYRKNGavRCICNENYAGPNCERCAPGYYGNPlLIGSTCK 185
Cdd:cd00055 1 PCDCN-GH-GSLSGQCDPGTG--QCECKPNTTGRRCDRCAPGYYGLP-SQGGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
187-231 |
4.06e-12 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 62.33 E-value: 4.06e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1034650228 187 CDCS--GNSDPnlifeDCDEVTGQCRnCLRNTTGFKCERCAPGYYGD 231
Cdd:smart00180 1 CDCDpgGSASG-----TCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD 41
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
340-814 |
1.00e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 70.45 E-value: 1.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 340 KSLLSDVEELVEKENQASRKGQL-----VQKESMDTINHASQLVEQAHDMRDKIQEINnkmlyygEEHELSPKEI----S 410
Cdd:PRK02224 186 RGSLDQLKAQIEEKEEKDLHERLnglesELAELDEEIERYEEQREQARETRDEADEVL-------EEHEERREELetleA 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 411 EKLVLAQKMLEEIRSRQPF----FTQRELVDEEADEAYELLSQAEsWQRLHNETrtlfpvVLEQLDDYNAKLSDLQEALD 486
Cdd:PRK02224 259 EIEDLRETIAETEREREELaeevRDLRERLEELEEERDDLLAEAG-LDDADAEA------VEARREELEDRDEELRDRLE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 487 QALNYVRDAEdmNRATAARQR--DHEKQQERVREQMEVVNMSLSTSADSLTTPRLTLSELDDIIKNASGIYA----EIDG 560
Cdd:PRK02224 332 ECRVAAQAHN--EEAESLREDadDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGdapvDLGN 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 561 AKSELQVKLSNLSNLSHDL---------VQEAIDHAQDLQQEAN-------------------------ELSRKLhsSDM 606
Cdd:PRK02224 410 AEDFLEELREERDELREREaeleatlrtARERVEEAEALLEAGKcpecgqpvegsphvetieedrerveELEAEL--EDL 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 607 NGLVQKALDASNVYENIVNYVSEANETAEFALNTTDRIYDAVSGIDTQiiyhKDESENLLNQARELQAKAESSSDEAV-- 684
Cdd:PRK02224 488 EEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEK----RERAEELRERAAELEAEAEEKREAAAea 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 685 ---ADTSRRVGGAL-ARKSALKTRLsDAVKQL--QAAERGDAQQRLGqsRLITEEANRTTMEVQQatapmANNLTNWSQN 758
Cdd:PRK02224 564 eeeAEEAREEVAELnSKLAELKERI-ESLERIrtLLAAIADAEDEIE--RLREKREALAELNDER-----RERLAEKRER 635
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034650228 759 LQHFDSSAYNTAVNSARDAVRNLTEVVPQLLDQLRTVEQKRPA-----SNVSASIQRIREL 814
Cdd:PRK02224 636 KRELEAEFDEARIEEAREDKERAEEYLEQVEEKLDELREERDDlqaeiGAVENELEELEEL 696
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
132-184 |
1.52e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 60.83 E-value: 1.52e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1034650228 132 CPCPlpHLANFAESCYRKNGavRCICNENYAGPNCERCAPGYYGNPLLIGSTC 184
Cdd:pfam00053 1 CDCN--PHGSLSDTCDPETG--QCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
314-640 |
2.51e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 69.32 E-value: 2.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 314 LKTKLSERENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLVQKESMDTINHASQLVEQAHDMRDKIQEINN 393
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLER 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 394 KMLYYGEEHELSPKEISEKLVLAQKMLEEIRSRQPFFT-QRELVDEEADEAYELLSQAESWQRLHNETRTLFPVVLEQLD 472
Cdd:TIGR02168 317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELEsLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 473 DYNAKLSDLQEALDQalnyvrdAEDMNRATAARQRDHEKQQERVreQMEVVNMSLSTSADSLTTprlTLSELDDIIKNAS 552
Cdd:TIGR02168 397 SLNNEIERLEARLER-------LEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEE---LQEELERLEEALE 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 553 GIYAEIDGAKSELQVKLSNLSNLSH--DLVQEAIDHAQDLQQEANELsrKLHSSDMNGLVQKALDASNV---YE------ 621
Cdd:TIGR02168 465 ELREELEEAEQALDAAERELAQLQArlDSLERLQENLEGFSEGVKAL--LKNQSGLSGILGVLSELISVdegYEaaieaa 542
|
330 340
....*....|....*....|..
gi 1034650228 622 ---NIVNYVSEANETAEFALNT 640
Cdd:TIGR02168 543 lggRLQAVVVENLNAAKKAIAF 564
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
81-130 |
2.83e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 60.06 E-value: 2.83e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1034650228 81 PCDCNGN---SNECLDGSGYCvHCQRNTTGEHCEKCLDGYIGDSIRGAPqfCQ 130
Cdd:cd00055 1 PCDCNGHgslSGQCDPGTGQC-ECKPNTTGRRCDRCAPGYYGLPSQGGG--CQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
132-177 |
3.55e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 59.63 E-value: 3.55e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1034650228 132 CPCPLPHlaNFAESCYRKNGavRCICNENYAGPNCERCAPGYYGNP 177
Cdd:smart00180 1 CDCDPGG--SASGTCDPDTG--QCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
868-1006 |
9.20e-11 |
|
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: 61.28 E-value: 9.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 868 TETADQFILYLGSKnaKKEYMGLAIKNDNLVYVYNLGTKDVEIPLDSKPVS--SWpayfSIVKIERVGKHgkVFLTVPSL 945
Cdd:pfam02210 3 TRQPNGLLLYAGGG--GSDFLALELVNGRLVLRYDLGSGPESLLSSGKNLNdgQW----HSVRVERNGNT--LTLSVDGQ 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034650228 946 SSTAEEKfikkgefSGDDSLLDLDpedTVFYVGGVPSNFKLPTSLNLPGFVGCLELATLNN 1006
Cdd:pfam02210 75 TVVSSLP-------PGESLLLNLN---GPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVNG 125
|
|
| TNFRSF16 |
cd13416 |
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 ... |
65-257 |
2.01e-10 |
|
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: 61.16 E-value: 2.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 65 EKCNAGFFhTLSGECvpCDcngnsnECLDGSGYCVHCQRNTTGehCEKCLDGYIGDSIRGAPQFCQPC-PCplPHLANFA 143
Cdd:cd13416 1 EACPSGQY-TSSGEC--CE------QCPPGEGVARPCGDNQTV--CEPCLDGVTFSDVVSHTEPCQPCtRC--PGLMSMR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 144 ESCYRKNGAVrcicnenyagpnCErCAPGYYGNPLliGSTCKKCDCsgnsdpnlifedCDEVTGQCRNC--LRNTtgfKC 221
Cdd:cd13416 68 APCTATHDTV------------CE-CAYGYYLDED--SGTCEPCTV------------CPPGQGVVQSCgpNQDT---VC 117
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1034650228 222 ERCAPGYYGDARIAKN----CAVCncggGPCDSVTGECLE 257
Cdd:cd13416 118 EACPEGTYSDEDSSTDpclpCTVC----EDGEVELRECTP 153
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
82-129 |
5.62e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 56.21 E-value: 5.62e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1034650228 82 CDCNGN---SNECLDGSGYCvHCQRNTTGEHCEKCLDGYIGDSIrGAPQFC 129
Cdd:pfam00053 1 CDCNPHgslSDTCDPETGQC-LCKPGVTGRHCDRCKPGYYGLPS-DPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
82-121 |
3.92e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 53.85 E-value: 3.92e-09
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1034650228 82 CDCNGN---SNECLDGSGYCvHCQRNTTGEHCEKCLDGYIGDS 121
Cdd:smart00180 1 CDCDPGgsaSGTCDPDTGQC-ECKPNVTGRRCDRCAPGYYGDG 42
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
312-724 |
2.42e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.01 E-value: 2.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 312 YLLKTKLseRENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLVQKESmdtinhasQLVEQAHDMRDKIQEI 391
Cdd:COG4717 45 AMLLERL--EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELE--------ELEEELEELEAELEEL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 392 NNKMLYYgeEHELSPKEISEKLVLAQKMLEEIRSRQPFFTQRELVDEEADEAYE-LLSQAESWQR-LHNETRTLFPVVLE 469
Cdd:COG4717 115 REELEKL--EKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEeLEAELAELQEeLEELLEQLSLATEE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 470 QLDDYNAKLSDLQEALDQALNYVRDAEDmNRATAARQRD-------HEKQQERVREQMEVVN-----MSLSTSADSLTTP 537
Cdd:COG4717 193 ELQDLAEELEELQQRLAELEEELEEAQE-ELEELEEELEqleneleAAALEERLKEARLLLLiaaalLALLGLGGSLLSL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 538 RLTL----------------------SELDDIIKNASGIYAEIDGAKSELQVKLSNL---SNLSHDLVQEAIDHAQDLQQ 592
Cdd:COG4717 272 ILTIagvlflvlgllallflllarekASLGKEAEELQALPALEELEEEELEELLAALglpPDLSPEELLELLDRIEELQE 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 593 ---EANELSRKLHSSDMNGLVQKALDASNV-----YENIVNYVSEANETAEfalnttdriydAVSGIDTQIIYHKDESEN 664
Cdd:COG4717 352 llrEAEELEEELQLEELEQEIAALLAEAGVedeeeLRAALEQAEEYQELKE-----------ELEELEEQLEELLGELEE 420
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034650228 665 LLNQARELQAKAE-SSSDEAVADTSRRVGGALARKSALKTRLSDAVKQLQAAERGDAQQRL 724
Cdd:COG4717 421 LLEALDEEELEEElEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEEL 481
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
522-750 |
2.61e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.84 E-value: 2.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 522 VVNMSLSTSADslTTPRLTLSELDDIIKNASGIYAEIDGAKSELQVKLSNLSNLSHDL--VQEAIDhaqDLQQEANELSR 599
Cdd:COG3883 5 ALAAPTPAFAD--PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELeaLQAEID---KLQAEIAEAEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 600 KLhsSDMNGLVQKALDASNVYENIVNYVS---EANETAEFA--LNTTDRIYDAVSGIDTQIIYHKDESENLLNQARELQA 674
Cdd:COG3883 80 EI--EERREELGERARALYRSGGSVSYLDvllGSESFSDFLdrLSALSKIADADADLLEELKADKAELEAKKAELEAKLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 675 KAESSSDEAvADTSRRVGGALARKSALKTRLSDAVKQLQA------AERGDAQQRLGQSRLITEEANRTTMEVQQATAPM 748
Cdd:COG3883 158 ELEALKAEL-EAAKAELEAQQAEQEALLAQLSAEEAAAEAqlaeleAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
..
gi 1034650228 749 AN 750
Cdd:COG3883 237 AA 238
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
347-848 |
9.79e-07 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 54.06 E-value: 9.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 347 EELVEKENQASRKgqlvQKESMDTINHASQLVEQahdmrdkiqeinnkmlyygeEHELSPKEISEKLVLAQKMLEEIRSR 426
Cdd:NF041483 699 EALAAAQEEAARR----RREAEETLGSARAEADQ--------------------ERERAREQSEELLASARKRVEEAQAE 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 427 qpffTQReLVdEEADE-AYELLSQAESwqrlhnetrtlfpvVLEQLDDynaKLSDLQEALDQALNYVRDAEDMnraTAAR 505
Cdd:NF041483 755 ----AQR-LV-EEADRrATELVSAAEQ--------------TAQQVRD---SVAGLQEQAEEEIAGLRSAAEH---AAER 808
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 506 QRDhEKQQE--RVReqmevvnmslstsADSLTTpRLTLSEldDIIKNASGIYAEIDGAKSelqvklsnlsnLSHDLVQEA 583
Cdd:NF041483 809 TRT-EAQEEadRVR-------------SDAYAE-RERASE--DANRLRREAQEETEAAKA-----------LAERTVSEA 860
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 584 IDHAQDLQQEANELSRKLHSSDMNGLVQKALDASNVYenivnyvSEANETAefalnttDRI-YDAVSGIDTQIIYHKDES 662
Cdd:NF041483 861 IAEAERLRSDASEYAQRVRTEASDTLASAEQDAARTR-------ADAREDA-------NRIrSDAAAQADRLIGEATSEA 926
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 663 ENLLNQARelqAKAESSSDEAVADTSRRVGGALARKSALKTRLSDAVKQL--QAAER-GDAQQRLGQSRlitEEANRTTM 739
Cdd:NF041483 927 ERLTAEAR---AEAERLRDEARAEAERVRADAAAQAEQLIAEATGEAERLraEAAETvGSAQQHAERIR---TEAERVKA 1000
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 740 EvqqaTAPMANNLTNWSQN-----LQHFDSSAYNTAVNSARDAVRNLTEVVPQlLDQLRTVEQKRPASNVSASIQRIREL 814
Cdd:NF041483 1001 E----AAAEAERLRTEAREeadrtLDEARKDANKRRSEAAEQADTLITEAAAE-ADQLTAKAQEEALRTTTEAEAQADTM 1075
|
490 500 510
....*....|....*....|....*....|....
gi 1034650228 815 IAQTRSVASKIQVSMMFDGQSAVEvHSRTSMDDL 848
Cdd:NF041483 1076 VGAARKEAERIVAEATVEGNSLVE-KARTDADEL 1108
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
433-814 |
4.50e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.88 E-value: 4.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 433 RELVDEEAD---EAYELLSQAESWQRLHNETRtlfpvvlEQLDDYNAKLSDLQEALDQA---LNYVRDAEDMNRATAARQ 506
Cdd:PRK04863 282 RVHLEEALElrrELYTSRRQLAAEQYRLVEMA-------RELAELNEAESDLEQDYQAAsdhLNLVQTALRQQEKIERYQ 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 507 RDHEKQQERVREQMEVVNMSLSTSADSLTTPRLTLSELD-------------DIIKNASGIYAE----IDGAKSELQVKL 569
Cdd:PRK04863 355 ADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDelksqladyqqalDVQQTRAIQYQQavqaLERAKQLCGLPD 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 570 SNLSNLShDLVQEAIDHAQDLQQEANELSRKLHSSDMnglvqkaldasnvyenivnyvseANETAEFALNTTDRIYDAVS 649
Cdd:PRK04863 435 LTADNAE-DWLEEFQAKEQEATEELLSLEQKLSVAQA-----------------------AHSQFEQAYQLVRKIAGEVS 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 650 GIDTQiiyhkDESENLLNQARELQAKAEsssdeavadtsrRVGGALARKSALKTRLsdavKQLQAAER--GDAQQRLGQS 727
Cdd:PRK04863 491 RSEAW-----DVARELLRRLREQRHLAE------------QLQQLRMRLSELEQRL----RQQQRAERllAEFCKRLGKN 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 728 --------RLITE-EANRTTMEVQQATA-----PMANNLTNWSQNLQHFDSSA-----YNTAVNSARDAV-------RNL 781
Cdd:PRK04863 550 lddedeleQLQEElEARLESLSESVSEArerrmALRQQLEQLQARIQRLAARApawlaAQDALARLREQSgeefedsQDV 629
|
410 420 430
....*....|....*....|....*....|....*
gi 1034650228 782 TEVVPQLLDQLR--TVEQKRPASNVSASIQRIREL 814
Cdd:PRK04863 630 TEYMQQLLERERelTVERDELAARKQALDEEIERL 664
|
|
| ApoLp-III_like |
cd13769 |
Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles ... |
703-829 |
4.70e-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: 4.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 703 TRLSDAVKQLQAAERGDAQQRLGQSRL-ITEEANRTtmeVQQATAPMANNLTNWSQNLQHFDSSAYNTAVNSARDAVRNL 781
Cdd:cd13769 1 TQLSELIQKAQEAINNLAQQVQKQLGLqNPEEVVNT---LKEQSDNFANNLQEVSSSLKEEAKKKQGEVEEAWNEFKTKL 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1034650228 782 TEVVPQLLDQLRTVEQkrpASNVSASIQ-RIRELIAQTRSVASKIQVSM 829
Cdd:cd13769 78 SETVPELRKSLPVEEK---AQELQAKLQsGLQTLVTESQKLAKAISENS 123
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
514-757 |
2.40e-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: 49.66 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 514 ERVREQMEVVNMSLSTSADSLTTPRLTLSELDDIIKnaSGIYAEIDGAKSELQVKLSNLSNLSHDLVQEAIDHAQD---L 590
Cdd:TIGR01612 500 MRMKDFKDIIDFMELYKPDEVPSKNIIGFDIDQNIK--AKLYKEIEAGLKESYELAKNWKKLIHEIKKELEEENEDsihL 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 591 QQEAN---------------------ELSRKLHS-SDMNGLVQKALDASNVYENIVNYVSEANETAEFA----LNTTDRI 644
Cdd:TIGR01612 578 EKEIKdlfdkyleiddeiiyinklklELKEKIKNiSDKNEYIKKAIDLKKIIENNNAYIDELAKISPYQvpehLKNKDKI 657
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 645 YDAVSGIDTQI--------------IYHKDESENLLNQAR--ELQAKAESSSDEAVADTSRRVGGALARKSALKTRLSDA 708
Cdd:TIGR01612 658 YSTIKSELSKIyeddidalynelssIVKENAIDNTEDKAKldDLKSKIDKEYDKIQNMETATVELHLSNIENKKNELLDI 737
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1034650228 709 VKQLQAAERGDaqqrlgqsrlITEEANRTTMEVQQATAPMANNLTNWSQ 757
Cdd:TIGR01612 738 IVEIKKHIHGE----------INKDLNKILEDFKNKEKELSNKINDYAK 776
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
659-817 |
1.38e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 659 KDESENLLNQARELQAK-AESSSDEAVADTSRR--------VGGAlaRKSALKTRLSDAVKQLQAAE--RGDAQQRLGQS 727
Cdd:COG4913 294 EAELEELRAELARLEAElERLEARLDALREELDeleaqirgNGGD--RLEQLEREIERLERELEERErrRARLEALLAAL 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 728 RLiTEEANRTTMEVQQATAPMAnnLTNWSQnlqhfDSSAYNTAVNSARDAVRNLTEVVPQLLDQLRTVEQKRpaSNVSAS 807
Cdd:COG4913 372 GL-PLPASAEEFAALRAEAAAL--LEALEE-----ELEALEEALAEAEAALRDLRRELRELEAEIASLERRK--SNIPAR 441
|
170
....*....|
gi 1034650228 808 IQRIRELIAQ 817
Cdd:COG4913 442 LLALRDALAE 451
|
|
| |
|
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 |
2.17e-101 |
|
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: 325.91 E-value: 2.17e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 291 VLSVSSGAAAHRHVNEINATIYLLKTKLSERENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLVQKESMDT 370
Cdd:pfam06008 1 LLSLNSLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 371 INHASQLVEQAHDMRDKIQEINNKMLYYGEE-HELSPKEISEKLVLAQKMLEEIRSRQpFFTQRELVDEEADEAYELLSQ 449
Cdd:pfam06008 81 LGHAKELAEAIKNLIDNIKEINEKVATLGENdFALPSSDLSRMLAEAQRMLGEIRSRD-FGTQLQNAEAELKAAQDLLSR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 450 AESW-QRLHNETRTLFPVVLEQLDDYNAKLSDLQEALDQALNYVRDAEDMNRATAARQRDHEKQQERVREQMEVVNMSLS 528
Cdd:pfam06008 160 IQTWfQSPQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEETLK 239
|
250
....*....|....*....
gi 1034650228 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 |
2.59e-43 |
|
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: 154.57 E-value: 2.59e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 727 SRLITEEANRTTMEVQQATAPMANNLTNWSQNLQHFDSSA---------YNTAVNSARDAVRNLTEVVPQLLDQLRTVEQ 797
Cdd:pfam06009 1 SKELAREANETAKEVLEQLAPLSQNLENTSEKLSGINRSLeetnelvndANKALDDAGRSVKKLEELAPDLLDKLKPLKQ 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1034650228 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 |
1.99e-39 |
|
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: 144.10 E-value: 1.99e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 1485 KSQFSIRLRTRSSHGMIFYVSDQEENDFMTLFLAHGRLVYMFNVGHKKLKIRSQEKYNDGLWHDVIFIRERSSGRLVIDG 1564
Cdd:cd00110 21 RLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDGQWHSVSVERNGRSVTLSVDG 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1034650228 1565 LRVLEESLPPTEATWKIKGPIYLGGVAPGKavKNVQINSIYSFSGCLSNLQLN 1617
Cdd:cd00110 101 ERVVESGSPGGSALLNLDGPLYLGGLPEDL--KSPGLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
1487-1618 |
1.09e-35 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 132.46 E-value: 1.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 1487 QFSIRLRTRSSHGMIFYVSDQEENDFMTLFLAHGRLVYMFNVGHKKLKIRSQ-EKYNDGLWHDVIFIRERSSGRLVIDGL 1565
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDpTPLNDGQWHRVAVERNGRSVTLSVDGG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1034650228 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 1034650228 1641 GTYFStEGGYVVLDESFNIGLKFEIAFEVRPRSSSGTLVH-GHSVNGEYLNVHMKNGQVIVKVNNGirDFSTSVTPKQSL 1719
Cdd:cd00110 1 GVSFS-GSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYaGSQNGGDFLALELEDGRLVLRYDLG--SGSLVLSSKTPL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034650228 1720 CDGRWHRITVIRDSNVVQLDVDSE-VNHVVGPLNPKPIDHREPVFVGGVPESLLTPRLAPSKPFTGCIRHFVID 1792
Cdd:cd00110 78 NDGQWHSVSVERNGRSVTLSVDGErVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
1664-1794 |
3.92e-31 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 119.37 E-value: 3.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 1664 EIAFEVRPRSSSGTLVHGHSVNG-EYLNVHMKNGQVIVKVNNGIRDFSTSVTPKQsLCDGRWHRITVIRDSNVVQLDVDS 1742
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGgDYLALELRDGRLVLRYDLGSGPARLTSDPTP-LNDGQWHRVAVERNGRSVTLSVDG 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1034650228 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 |
2.58e-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: 117.14 E-value: 2.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 1492 LRTRSSHGMIFYVSDQEeNDFMTLFLAHGRLVYMFNVGHKKLKIRSQEK-YNDGLWHDVIFIRERSSGRLVIDGLRVLEE 1570
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGG-SDFLALELVNGRLVLRYDLGSGPESLLSSGKnLNDGQWHSVRVERNGNTLTLSVDGQTVVSS 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1034650228 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 |
1.72e-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: 1.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 1669 VRPRSSSGTLVHGHSVNGEYLNVHMKNGQVIVKVNNGIRDFSTSVTPKqSLCDGRWHRITVIRDSNVVQLDVDSEVNH-V 1747
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDFLALELVNGRLVLRYDLGSGPESLLSSGK-NLNDGQWHSVRVERNGNTLTLSVDGQTVVsS 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1034650228 1748 VGPLNPKPIDHREPVFVGGVPESLLTPRLAPSKPFTGCIRHFVIDGH 1794
Cdd:pfam02210 80 LPPGESLLLNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
1493-1621 |
7.30e-24 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 98.54 E-value: 7.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 1493 RTRSSHGMIFYVSDQEENDFMTLFLAHGRLVYMFNVGHKKLKIRSQEKYNDGLWHDVIFIRERSSGRLVIDGLRVLE-ES 1571
Cdd:pfam00054 2 RTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTgES 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1034650228 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 |
8.35e-24 |
|
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: 99.41 E-value: 8.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 1042 SYFFDGSGYAvvrDITRRGKFGQVTRFDIEVRTPADNGLILLM--VNGSMFFRLEMRNGYLHVFYDFGfsGGPVHLEDtl 1119
Cdd:cd00110 1 GVSFSGSSYV---RLPTLPAPRTRLSISFSFRTTSPNGLLLYAgsQNGGDFLALELEDGRLVLRYDLG--SGSLVLSS-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 1120 kKAQINDAKYHEISIIyHNDKKMILVVDR-RHVKSMDNEKMKI--PFTDIYIGGAPPEILQSRALRAHlpldiNFRGCMK 1196
Cdd:cd00110 74 -KTPLNDGQWHSVSVE-RNGRSVTLSVDGeRVVESGSPGGSALlnLDGPLYLGGLPEDLKSPGLPVSP-----GFVGCIR 146
|
....
gi 1034650228 1197 GFQF 1200
Cdd:cd00110 147 DLKV 150
|
|
| LamG |
smart00282 |
Laminin G domain; |
1067-1203 |
2.45e-22 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 94.33 E-value: 2.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 1067 RFDIEVRTPADNGLILLM--VNGSMFFRLEMRNGYLHVFYDFGfsGGPVHLedTLKKAQINDAKYHEISIIyHNDKKMIL 1144
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAgsKGGGDYLALELRDGRLVLRYDLG--SGPARL--TSDPTPLNDGQWHRVAVE-RNGRSVTL 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034650228 1145 VVD---RRHVKSMDNEKMKIPFTDIYIGGAPPEILQSralraHLPLDINFRGCMKGFQFQKK 1203
Cdd:smart00282 76 SVDggnRVSGESPGGLTILNLDGPLYLGGLPEDLKLP-----PLPVTPGFRGCIRNLKVNGK 132
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
1072-1200 |
1.66e-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: 89.02 E-value: 1.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 1072 VRTPADNGLIL-LMVNGSMFFRLEMRNGYLHVFYDFGfsGGPVHLedTLKKAQINDAKYHEISIIYhNDKKMILVVDRRH 1150
Cdd:pfam02210 1 FRTRQPNGLLLyAGGGGSDFLALELVNGRLVLRYDLG--SGPESL--LSSGKNLNDGQWHSVRVER-NGNTLTLSVDGQT 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1034650228 1151 VKSMDNEKMKIPF---TDIYIGGAPPeilqsRALRAHLPLDINFRGCMKGFQF 1200
Cdd:pfam02210 76 VVSSLPPGESLLLnlnGPLYLGGLPP-----LLLLPALPVRAGFVGCIRDVRV 123
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
1230-1369 |
4.11e-19 |
|
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: 85.93 E-value: 4.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 1230 AYFNGQSFIASIQKISFFDGFEGGFNFRTLQPNGLLFYYASG--SDVFSISLDNGTVIMDV----KGIKVQSvDKQYNDG 1303
Cdd:cd00110 2 VSFSGSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQngGDFLALELEDGRLVLRYdlgsGSLVLSS-KTPLNDG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034650228 1304 LSHFVISSVSPTRYELIVDKSRVGSKNPTKGKIEQTqaSEKKFYFGGSPISAQ------YANFTGCISNAYF 1369
Cdd:cd00110 81 QWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLN--LDGPLYLGGLPEDLKspglpvSPGFVGCIRDLKV 150
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
828-1005 |
1.77e-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: 84.01 E-value: 1.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 828 SMMFDGQSAVEVhsrTSMDDLKAFTSLSLYMKppvkrpelTETADQFILYLGSKNaKKEYMGLAIKNDNLVYVYNLGTKD 907
Cdd:cd00110 1 GVSFSGSSYVRL---PTLPAPRTRLSISFSFR--------TTSPNGLLLYAGSQN-GGDFLALELEDGRLVLRYDLGSGS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 908 VEIpldSKPVSSWPAYFSIVKIERVGKHgkVFLTVPSLSStaeekfikkGEFSGDDSLLDLDPEDTVfYVGGVPSNFKLP 987
Cdd:cd00110 69 LVL---SSKTPLNDGQWHSVSVERNGRS--VTLSVDGERV---------VESGSPGGSALLNLDGPL-YLGGLPEDLKSP 133
|
170
....*....|....*...
gi 1034650228 988 TSLNLPGFVGCLELATLN 1005
Cdd:cd00110 134 GLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
853-1006 |
3.54e-18 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 82.39 E-value: 3.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 853 SLSLYMKppvkrpelTETADQFILYLGSKNaKKEYMGLAIKNDNLVYVYNLGTKDVEIPLDSKPVSswPAYFSIVKIERV 932
Cdd:smart00282 1 SISFSFR--------TTSPNGLLLYAGSKG-GGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLN--DGQWHRVAVERN 69
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034650228 933 GKHgkVFLTVPSLSSTAEEKFIKKgefsgddSLLDLDpedTVFYVGGVPSNFKLPTSLNLPGFVGCLELATLNN 1006
Cdd:smart00282 70 GRS--VTLSVDGGNRVSGESPGGL-------TILNLD---GPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNG 131
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
1256-1369 |
1.57e-17 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 80.54 E-value: 1.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 1256 FRTLQPNGLLFYYASG-SDVFSISLDNGTVIMDVK----GIKVQSVDKQYNDGLSHFVISSVSPTRYELIVDKSRVGSKN 1330
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGgSDFLALELVNGRLVLRYDlgsgPESLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1034650228 1331 PTKGkiEQTQASEKKFYFGG------SPISAQYANFTGCISNAYF 1369
Cdd:pfam02210 81 PPGE--SLLLNLNGPLYLGGlpplllLPALPVRAGFVGCIRDVRV 123
|
|
| 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 1034650228 1669 VRPRSSSGTLVHGHSVN-GEYLNVHMKNGQVIVKVNNGIRdfSTSVTPKQSLCDGRWHRITVIRDSNVVQLDVDSEVNHV 1747
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTeRDFLALELRDGRLEVSYDLGSG--AAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPT 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1034650228 1748 V-GPLNPK-PIDHREPVFVGGVPESLLTPRLAP-SKPFTGCIRHFVIDGHPV 1796
Cdd:pfam00054 79 GeSPLGATtDLDVDGPLYVGGLPSLGVKKRRLAiSPSFDGCIRDVIVNGKPL 130
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
187-238 |
7.39e-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: 7.39e-16
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1034650228 187 CDCSGNSDPNlifEDCDEVTGQCRnCLRNTTGFKCERCAPGYYGDARIAKNC 238
Cdd:cd00055 2 CDCNGHGSLS---GQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGGC 49
|
|
| LamG |
smart00282 |
Laminin G domain; |
1254-1372 |
1.16e-14 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 72.37 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 1254 FNFRTLQPNGLLFYYAS--GSDVFSISLDNGTVIMDVKG----IKVQSVDKQYNDGLSHFVISSVSPTRYELIVDksrvg 1327
Cdd:smart00282 4 FSFRTTSPNGLLLYAGSkgGGDYLALELRDGRLVLRYDLgsgpARLTSDPTPLNDGQWHRVAVERNGRSVTLSVD----- 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1034650228 1328 SKNPTKGKIEQTQA---SEKKFYFGGSP------ISAQYANFTGCISNAYFTRV 1372
Cdd:smart00282 79 GGNRVSGESPGGLTilnLDGPLYLGGLPedlklpPLPVTPGFRGCIRNLKVNGK 132
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
187-232 |
4.74e-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: 4.74e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1034650228 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 |
7.40e-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: 73.99 E-value: 7.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 272 DLTDDLRLAALSIEEGKsgVLSVSSGAAAHRHVNEINATIYLL----KTKLSERENQYALRKIQINNAENTMKSLLSDVE 347
Cdd:pfam05483 187 DLNNNIEKMILAFEELR--VQAENARLEMHFKLKEDHEKIQHLeeeyKKEINDKEKQVSLLLIQITEKENKMKDLTFLLE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 348 ELVEKENQASRKGQLvQKESMdtinhaSQLVEQAHDMRDKIQEINNKMlyygEEHELSPKEISEKLVLAQKMLEEIRSrq 427
Cdd:pfam05483 265 ESRDKANQLEEKTKL-QDENL------KELIEKKDHLTKELEDIKMSL----QRSMSTQKALEEDLQIATKTICQLTE-- 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 428 pfftQRELVDEEADEAY------------------ELLSQAEswQRLHNETRTLFPVVLEqlddYNAKLSDLQEALDQAL 489
Cdd:pfam05483 332 ----EKEAQMEELNKAKaahsfvvtefeattcsleELLRTEQ--QRLEKNEDQLKIITME----LQKKSSELEEMTKFKN 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 490 NYVRDAEDMNRATAARQR--DHEKQQERVREQMEVVNMSLSTsadSLTTPRLTLSELD---DIIKNASGIYA-EIDGAKS 563
Cdd:pfam05483 402 NKEVELEELKKILAEDEKllDEKKQFEKIAEELKGKEQELIF---LLQAREKEIHDLEiqlTAIKTSEEHYLkEVEDLKT 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 564 ELQ-VKLSNLSNLSH---------DLVQEAID-------HAQDLQQEANELSRKLhsSDMNGLVQKALDASNVYENIVNY 626
Cdd:pfam05483 479 ELEkEKLKNIELTAHcdklllenkELTQEASDmtlelkkHQEDIINCKKQEERML--KQIENLEEKEMNLRDELESVREE 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 627 VSEANETAEFALnttDRIYDAVSGIDTQIIYHKDESENLLNQARELQAKAEsssdeavaDTSRRVGGALARKSALKTRLS 706
Cdd:pfam05483 557 FIQKGDEVKCKL---DKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIE--------NKNKNIEELHQENKALKKKGS 625
|
490
....*....|
gi 1034650228 707 DAVKQLQAAE 716
Cdd:pfam05483 626 AENKQLNAYE 635
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
131-185 |
1.01e-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: 64.30 E-value: 1.01e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1034650228 131 PCPCPlPHlANFAESCYRKNGavRCICNENYAGPNCERCAPGYYGNPlLIGSTCK 185
Cdd:cd00055 1 PCDCN-GH-GSLSGQCDPGTG--QCECKPNTTGRRCDRCAPGYYGLP-SQGGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
187-231 |
4.06e-12 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 62.33 E-value: 4.06e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1034650228 187 CDCS--GNSDPnlifeDCDEVTGQCRnCLRNTTGFKCERCAPGYYGD 231
Cdd:smart00180 1 CDCDpgGSASG-----TCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD 41
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
1072-1196 |
9.58e-12 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 63.88 E-value: 9.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 1072 VRTPADNGLILLM--VNGSMFFRLEMRNGYLHVFYDFGfsGGPVHLEdtlKKAQINDAKYHEISIIYhNDKKMILVVDRR 1149
Cdd:pfam00054 1 FRTTEPSGLLLYNgtQTERDFLALELRDGRLEVSYDLG--SGAAVVR---SGDKLNDGKWHSVELER-NGRSGTLSVDGE 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1034650228 1150 HVKSMDNEK---MKIPF-TDIYIGGAPPEILqsraLRAHLPLDINFRGCMK 1196
Cdd:pfam00054 75 ARPTGESPLgatTDLDVdGPLYVGGLPSLGV----KKRRLAISPSFDGCIR 121
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
340-814 |
1.00e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 70.45 E-value: 1.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 340 KSLLSDVEELVEKENQASRKGQL-----VQKESMDTINHASQLVEQAHDMRDKIQEINnkmlyygEEHELSPKEI----S 410
Cdd:PRK02224 186 RGSLDQLKAQIEEKEEKDLHERLnglesELAELDEEIERYEEQREQARETRDEADEVL-------EEHEERREELetleA 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 411 EKLVLAQKMLEEIRSRQPF----FTQRELVDEEADEAYELLSQAEsWQRLHNETrtlfpvVLEQLDDYNAKLSDLQEALD 486
Cdd:PRK02224 259 EIEDLRETIAETEREREELaeevRDLRERLEELEEERDDLLAEAG-LDDADAEA------VEARREELEDRDEELRDRLE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 487 QALNYVRDAEdmNRATAARQR--DHEKQQERVREQMEVVNMSLSTSADSLTTPRLTLSELDDIIKNASGIYA----EIDG 560
Cdd:PRK02224 332 ECRVAAQAHN--EEAESLREDadDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGdapvDLGN 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 561 AKSELQVKLSNLSNLSHDL---------VQEAIDHAQDLQQEAN-------------------------ELSRKLhsSDM 606
Cdd:PRK02224 410 AEDFLEELREERDELREREaeleatlrtARERVEEAEALLEAGKcpecgqpvegsphvetieedrerveELEAEL--EDL 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 607 NGLVQKALDASNVYENIVNYVSEANETAEFALNTTDRIYDAVSGIDTQiiyhKDESENLLNQARELQAKAESSSDEAV-- 684
Cdd:PRK02224 488 EEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEK----RERAEELRERAAELEAEAEEKREAAAea 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 685 ---ADTSRRVGGAL-ARKSALKTRLsDAVKQL--QAAERGDAQQRLGqsRLITEEANRTTMEVQQatapmANNLTNWSQN 758
Cdd:PRK02224 564 eeeAEEAREEVAELnSKLAELKERI-ESLERIrtLLAAIADAEDEIE--RLREKREALAELNDER-----RERLAEKRER 635
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034650228 759 LQHFDSSAYNTAVNSARDAVRNLTEVVPQLLDQLRTVEQKRPA-----SNVSASIQRIREL 814
Cdd:PRK02224 636 KRELEAEFDEARIEEAREDKERAEEYLEQVEEKLDELREERDDlqaeiGAVENELEELEEL 696
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
295-826 |
1.51e-11 |
|
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: 69.76 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 295 SSGAAAHRHVNEINATIYLLKTKLSERENQYALRKIQINNA--------ENTMKSLLSDVE----ELVEKENQASRKGQL 362
Cdd:pfam15921 217 SLGSAISKILRELDTEISYLKGRIFPVEDQLEALKSESQNKielllqqhQDRIEQLISEHEveitGLTEKASSARSQANS 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 363 VQKEsMDTI-----NHASQLVEQAHDMRDKIQEINNKMLYYGEEHELSPKEISEKLVLAQKMLEEIRSRQPFFTQR---- 433
Cdd:pfam15921 297 IQSQ-LEIIqeqarNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQEsgnl 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 434 ---------ELVDEEADEAYELLSQAESWQRLHNETRTLfPVVLEQLDDYNAKLSDLqEALDQALNYVRDAEdMNRATAA 504
Cdd:pfam15921 376 ddqlqkllaDLHKREKELSLEKEQNKRLWDRDTGNSITI-DHLRRELDDRNMEVQRL-EALLKAMKSECQGQ-MERQMAA 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 505 RQRDHEKQQE----------------RVREQMEVVNMSLSTSADSLTTPRLTLSELDDIIKNASgiyAEIDGAKSELQVK 568
Cdd:pfam15921 453 IQGKNESLEKvssltaqlestkemlrKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATN---AEITKLRSRVDLK 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 569 LSNLSNLSHDLvqeaiDHAQDLQQEANELSRKLHSSD--MNGLVQKaldasnvYENIVNYVSEANETAefalnttdriyd 646
Cdd:pfam15921 530 LQELQHLKNEG-----DHLRNVQTECEALKLQMAEKDkvIEILRQQ-------IENMTQLVGQHGRTA------------ 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 647 avsgidTQIIYHKDESENLLNQAR-ELQakaESSSDEAVADTSRRvggalarksALKTRLSD----AVKQLQAaergdAQ 721
Cdd:pfam15921 586 ------GAMQVEKAQLEKEINDRRlELQ---EFKILKDKKDAKIR---------ELEARVSDleleKVKLVNA-----GS 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 722 QRLGQSRLITEEANRTTMEVQQATAPMaNNLTNWSQNLQ-HF--DSSAYNTAVNSARDAVRNLTEVVPQLLDQLRTVE-Q 797
Cdd:pfam15921 643 ERLRAVKDIKQERDQLLNEVKTSRNEL-NSLSEDYEVLKrNFrnKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEgS 721
|
570 580 590
....*....|....*....|....*....|
gi 1034650228 798 KRPASNVSASIQR-IRELIAQTRSVASKIQ 826
Cdd:pfam15921 722 DGHAMKVAMGMQKqITAKRGQIDALQSKIQ 751
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
132-184 |
1.52e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 60.83 E-value: 1.52e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1034650228 132 CPCPlpHLANFAESCYRKNGavRCICNENYAGPNCERCAPGYYGNPLLIGSTC 184
Cdd:pfam00053 1 CDCN--PHGSLSDTCDPETG--QCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
314-640 |
2.51e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 69.32 E-value: 2.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 314 LKTKLSERENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLVQKESMDTINHASQLVEQAHDMRDKIQEINN 393
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLER 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 394 KMLYYGEEHELSPKEISEKLVLAQKMLEEIRSRQPFFT-QRELVDEEADEAYELLSQAESWQRLHNETRTLFPVVLEQLD 472
Cdd:TIGR02168 317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELEsLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 473 DYNAKLSDLQEALDQalnyvrdAEDMNRATAARQRDHEKQQERVreQMEVVNMSLSTSADSLTTprlTLSELDDIIKNAS 552
Cdd:TIGR02168 397 SLNNEIERLEARLER-------LEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEE---LQEELERLEEALE 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 553 GIYAEIDGAKSELQVKLSNLSNLSH--DLVQEAIDHAQDLQQEANELsrKLHSSDMNGLVQKALDASNV---YE------ 621
Cdd:TIGR02168 465 ELREELEEAEQALDAAERELAQLQArlDSLERLQENLEGFSEGVKAL--LKNQSGLSGILGVLSELISVdegYEaaieaa 542
|
330 340
....*....|....*....|..
gi 1034650228 622 ---NIVNYVSEANETAEFALNT 640
Cdd:TIGR02168 543 lggRLQAVVVENLNAAKKAIAF 564
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
81-130 |
2.83e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 60.06 E-value: 2.83e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1034650228 81 PCDCNGN---SNECLDGSGYCvHCQRNTTGEHCEKCLDGYIGDSIRGAPqfCQ 130
Cdd:cd00055 1 PCDCNGHgslSGQCDPGTGQC-ECKPNTTGRRCDRCAPGYYGLPSQGGG--CQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
132-177 |
3.55e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 59.63 E-value: 3.55e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1034650228 132 CPCPLPHlaNFAESCYRKNGavRCICNENYAGPNCERCAPGYYGNP 177
Cdd:smart00180 1 CDCDPGG--SASGTCDPDTG--QCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
868-1006 |
9.20e-11 |
|
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: 61.28 E-value: 9.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 868 TETADQFILYLGSKnaKKEYMGLAIKNDNLVYVYNLGTKDVEIPLDSKPVS--SWpayfSIVKIERVGKHgkVFLTVPSL 945
Cdd:pfam02210 3 TRQPNGLLLYAGGG--GSDFLALELVNGRLVLRYDLGSGPESLLSSGKNLNdgQW----HSVRVERNGNT--LTLSVDGQ 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034650228 946 SSTAEEKfikkgefSGDDSLLDLDpedTVFYVGGVPSNFKLPTSLNLPGFVGCLELATLNN 1006
Cdd:pfam02210 75 TVVSSLP-------PGESLLLNLN---GPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVNG 125
|
|
| TNFRSF16 |
cd13416 |
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 ... |
65-257 |
2.01e-10 |
|
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: 61.16 E-value: 2.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 65 EKCNAGFFhTLSGECvpCDcngnsnECLDGSGYCVHCQRNTTGehCEKCLDGYIGDSIRGAPQFCQPC-PCplPHLANFA 143
Cdd:cd13416 1 EACPSGQY-TSSGEC--CE------QCPPGEGVARPCGDNQTV--CEPCLDGVTFSDVVSHTEPCQPCtRC--PGLMSMR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 144 ESCYRKNGAVrcicnenyagpnCErCAPGYYGNPLliGSTCKKCDCsgnsdpnlifedCDEVTGQCRNC--LRNTtgfKC 221
Cdd:cd13416 68 APCTATHDTV------------CE-CAYGYYLDED--SGTCEPCTV------------CPPGQGVVQSCgpNQDT---VC 117
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1034650228 222 ERCAPGYYGDARIAKN----CAVCncggGPCDSVTGECLE 257
Cdd:cd13416 118 EACPEGTYSDEDSSTDpclpCTVC----EDGEVELRECTP 153
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
82-129 |
5.62e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 56.21 E-value: 5.62e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1034650228 82 CDCNGN---SNECLDGSGYCvHCQRNTTGEHCEKCLDGYIGDSIrGAPQFC 129
Cdd:pfam00053 1 CDCNPHgslSDTCDPETGQC-LCKPGVTGRHCDRCKPGYYGLPS-DPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
82-121 |
3.92e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 53.85 E-value: 3.92e-09
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1034650228 82 CDCNGN---SNECLDGSGYCvHCQRNTTGEHCEKCLDGYIGDS 121
Cdd:smart00180 1 CDCDPGgsaSGTCDPDTGQC-ECKPNVTGRRCDRCAPGYYGDG 42
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
312-724 |
2.42e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.01 E-value: 2.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 312 YLLKTKLseRENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLVQKESmdtinhasQLVEQAHDMRDKIQEI 391
Cdd:COG4717 45 AMLLERL--EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELE--------ELEEELEELEAELEEL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 392 NNKMLYYgeEHELSPKEISEKLVLAQKMLEEIRSRQPFFTQRELVDEEADEAYE-LLSQAESWQR-LHNETRTLFPVVLE 469
Cdd:COG4717 115 REELEKL--EKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEeLEAELAELQEeLEELLEQLSLATEE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 470 QLDDYNAKLSDLQEALDQALNYVRDAEDmNRATAARQRD-------HEKQQERVREQMEVVN-----MSLSTSADSLTTP 537
Cdd:COG4717 193 ELQDLAEELEELQQRLAELEEELEEAQE-ELEELEEELEqleneleAAALEERLKEARLLLLiaaalLALLGLGGSLLSL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 538 RLTL----------------------SELDDIIKNASGIYAEIDGAKSELQVKLSNL---SNLSHDLVQEAIDHAQDLQQ 592
Cdd:COG4717 272 ILTIagvlflvlgllallflllarekASLGKEAEELQALPALEELEEEELEELLAALglpPDLSPEELLELLDRIEELQE 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 593 ---EANELSRKLHSSDMNGLVQKALDASNV-----YENIVNYVSEANETAEfalnttdriydAVSGIDTQIIYHKDESEN 664
Cdd:COG4717 352 llrEAEELEEELQLEELEQEIAALLAEAGVedeeeLRAALEQAEEYQELKE-----------ELEELEEQLEELLGELEE 420
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034650228 665 LLNQARELQAKAE-SSSDEAVADTSRRVGGALARKSALKTRLSDAVKQLQAAERGDAQQRL 724
Cdd:COG4717 421 LLEALDEEELEEElEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEEL 481
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
304-603 |
3.16e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.91 E-value: 3.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 304 VNEINATIYLLKTKLSERENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLVQKESMDTINHASQLVEQAHD 383
Cdd:TIGR02168 693 IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE 772
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 384 MRDKIQEINNKMlyygEEHELSPKEISEKLVLAQKMLEEIRSRqpFFTQRELVDEEADEAYELLSQAESWQRLHNETRTL 463
Cdd:TIGR02168 773 AEEELAEAEAEI----EELEAQIEQLKEELKALREALDELRAE--LTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 464 FPVVLEQLDDYNAKLSDLQEALDQAlnyvrdAEDMNRATAARQRdHEKQQERVREQMEVVNMSLSTSADSLTTPRLTLSE 543
Cdd:TIGR02168 847 IEELSEDIESLAAEIEELEELIEEL------ESELEALLNERAS-LEEALALLRSELEELSEELRELESKRSELRRELEE 919
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 544 LDDIIKNASgiyAEIDGAKSELQVKLSNLSNLSHDLVQEAIDHAQDLQQEANELSRKLHS 603
Cdd:TIGR02168 920 LREKLAQLE---LRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKR 976
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
314-736 |
3.20e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.79 E-value: 3.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 314 LKTKLSERENQYALRKIQinNAENTMKSLLSDVEELVEKENQASRKGQLVQKESMDTINHASQLVEQAHDMRDKIQEINN 393
Cdd:COG1196 218 LKEELKELEAELLLLKLR--ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 394 KMLyyGEEHELSPKEisEKLVLAQKMLEEIRSRqpfftQRELVDEEADEAYELLSQAESWQRLHNETRTLfpvvLEQLDD 473
Cdd:COG1196 296 ELA--RLEQDIARLE--ERRRELEERLEELEEE-----LAELEEELEELEEELEELEEELEEAEEELEEA----EAELAE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 474 YNAKLSDLQEALDQALNYVRDAEDMNRATAARQRDHEKQQERVREQMEVVNMSLSTSADSLTTPRLTLSELDDIIKNASG 553
Cdd:COG1196 363 AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 554 IYAEIDGAKSELQVKLSNLSNLSHDLVQEAIDHAQDLQQEANELSRKLHSSDMnglvqkALDASNVYENIVNYVSEANET 633
Cdd:COG1196 443 ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL------LLEAEADYEGFLEGVKAALLL 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 634 AEFALnttdriydaVSGIDTQIIYHKDESENLLNQARELQAKAESSSDEAVADtsRRVGGALARKSALKTRL-SDAVKQL 712
Cdd:COG1196 517 AGLRG---------LAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAA--AAIEYLKAAKAGRATFLpLDKIRAR 585
|
410 420
....*....|....*....|....
gi 1034650228 713 QAAERGDAQQRLGQSRLITEEANR 736
Cdd:COG1196 586 AALAAALARGAIGAAVDLVASDLR 609
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
320-742 |
3.65e-08 |
|
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: 58.68 E-value: 3.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 320 ERENQYALRKIqINNAENTMKSLLSDVEELVEKENQASRKGQLVQKESMDTINhasQL-VEQAHD--MRDKIQEInnkml 396
Cdd:pfam10174 224 DPAKTKALQTV-IEMKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIK---QMeVYKSHSkfMKNKIDQL----- 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 397 yygeEHELSPKEiSEKLVLaQKMLEEIRSRQPFFTQRELVDEEADEAYEllsqaeswQR---LHNETRTLfPVVLEQ--- 470
Cdd:pfam10174 295 ----KQELSKKE-SELLAL-QTKLETLTNQNSDCKQHIEVLKESLTAKE--------QRaaiLQTEVDAL-RLRLEEkes 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 471 -LDDYNAKLSDLQEALDQALNYVRDAEDM----NRATAARQ----------RDHEKQQERVREQMEVVNMSLSTSADSLT 535
Cdd:pfam10174 360 fLNKKTKQLQDLTEEKSTLAGEIRDLKDMldvkERKINVLQkkienlqeqlRDKDKQLAGLKERVKSLQTDSSNTDTALT 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 536 TPRLTLSELDDIIKNASGIYA--------EIDGAKSELQVKLSNLSNLSHDL------VQEAIDHAQDLQQEANELSRKL 601
Cdd:pfam10174 440 TLEEALSEKERIIERLKEQREredrerleELESLKKENKDLKEKVSALQPELtekessLIDLKEHASSLASSGLKKDSKL 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 602 HSSDMNglVQKALDASNVYENIVNYVSEANETAEFALNTTDRIydavSGIDTQIIYHKDES-------ENLLNQARELQA 674
Cdd:pfam10174 520 KSLEIA--VEQKKEECSKLENQLKKAHNAEEAVRTNPEINDRI----RLLEQEVARYKEESgkaqaevERLLGILREVEN 593
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034650228 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 |
5.50e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.02 E-value: 5.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 304 VNEINATIYLLKTKLSERENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLVQKESMDTINHASQLVEQAHD 383
Cdd:COG1196 283 LEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 384 MRDKIQEINNkmlyygEEHELSPKEISEKLVLAQKMLEEIRSRQPFFTQRELVDEEADEAYELLSQAESWQRLHNETRTL 463
Cdd:COG1196 363 AEEALLEAEA------ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 464 FPVVLEQLDDYNAKLSDLQEALDQALNYVRDAE------DMNRATAARQRDHEKQQERVREQMEVVNMSLSTSADSLTTP 537
Cdd:COG1196 437 EEEEEEALEEAAEEEAELEEEEEALLELLAELLeeaallEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLL 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 538 RLTLSELDDIIKNASGIYAEIDGAKSELQVKLSNLSNLSHDLVQEAIDHAQD-----------LQQEANELSRKLHSSDM 606
Cdd:COG1196 517 AGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAakagratflplDKIRARAALAAALARGA 596
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 607 NGLVQKALDASNVYENIVNYV-----------SEANETAEFALNTTDRIYDAVSGIDTQIIYHKDESENLLNQARELQAK 675
Cdd:COG1196 597 IGAAVDLVASDLREADARYYVlgdtllgrtlvAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLE 676
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034650228 676 AESSSDEAVADTSRRVGGALARKSALKTRLSDAVKQLQAAERGDAQQRLGQSRLITEEANRTTMEVQQA 744
Cdd:COG1196 677 AEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEE 745
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
311-746 |
2.15e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.10 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 311 IYLLKTKLSERENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLVQKESMDTINHASQLVEQAHDMRDKIQE 390
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 391 INNKMLYYGEEHElspkEISEKLVLAQKMLEEIRsrqpffTQRELVDEEADEAYELLSQAEswQRLHNETRTLFPVVLEQ 470
Cdd:COG1196 314 LEERLEELEEELA----ELEEELEELEEELEELE------EELEEAEEELEEAEAELAEAE--EALLEAEAELAEAEEEL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 471 LDDYNAKLSDLQEALDQAlNYVRDAEDMNRATAARQRDHEKQQERVREQMEVVNMSLSTSADSLTTPRLTLSELDDIIKN 550
Cdd:COG1196 382 EELAEELLEALRAAAELA-AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 551 ASGIYAEIDGAKSELQVKLSNLSNLSHDLVQ--EAIDHAQDLQQEANELSRKLHSSDMNGLVQKALDAsnvyENIVNYVS 628
Cdd:COG1196 461 LLELLAELLEEAALLEAALAELLEELAEAAArlLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAV----LIGVEAAY 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 629 EANETAEFALNTTDRIYDAVSGIDTQIIYHKDESEN-----LLNQARELQAKAESSSDEAVADTSRRVGGALARKSALKT 703
Cdd:COG1196 537 EAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGratflPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYY 616
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1034650228 704 RLSDAVkQLQAAERGDAQQRLGQSRLITEEANRTTMEVQQATA 746
Cdd:COG1196 617 VLGDTL-LGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSA 658
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
291-746 |
2.40e-07 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 55.68 E-value: 2.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 291 VLSVSSGAAAHRHVNEINATIYLLKTklsERENQYALRKIQ--INNAENTMKS-LLSDVEELVEKENQAsrkgqlvQKES 367
Cdd:COG5278 19 LLLLVLGVLSYLSLNRLREASEWVEH---TYEVLRALEELLsaLLDAETGQRGyLLTGDESFLEPYEEA-------RAEI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 368 MDTINHASQLVEQAHDMRDKIQEINNKMLYYGEEHELS-------PKEISEKLVLA---QKMLEEIRSRQpfFTQRELVD 437
Cdd:COG5278 89 DELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVialrragGLEAALALVRSgegKALMDEIRARL--LLLALALA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 438 EEADEAYELLSQAESWQRLHNETRTLFPVVLEQLDDYNAKLSDLQEALDQALNYVRDAEDMNRATAARQRDHEKQQERVR 517
Cdd:COG5278 167 ALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 518 EQMEVVNMSLSTSADSLTTPRLTLSELDDIIKNAsgiyAEIDGAKSELQVKLSNLSNLSHDLVQEAIDHAQDLQQEANEL 597
Cdd:COG5278 247 AALLLALLAALALAALLAAALLALAALLLALAAA----AALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 598 SRKLHSSDMNGLVQKALDASNVYENIVNYVSEANETAEFALNTTDRIYDAVSGIDTQIIYHKDESENLLNQARELQAKAE 677
Cdd:COG5278 323 AALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAA 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034650228 678 SSSDEAVADTSRRVGGALARKSALKTRLSDAVKQLQAAERGDAQQRLGQSRLITEEANRTTMEVQQATA 746
Cdd:COG5278 403 AAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAV 471
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
367-844 |
2.44e-07 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 55.68 E-value: 2.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 367 SMDTINHASQLVEQAHDMRDKIQEINNKM----------LYYGEEHELspkeiseklvlaqkmleeirsrQPFFTQRELV 436
Cdd:COG5278 31 SLNRLREASEWVEHTYEVLRALEELLSALldaetgqrgyLLTGDESFL----------------------EPYEEARAEI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 437 DEEADEAYELLSQAESWQRLhnetrtlfpvvLEQLDD-YNAKLSDLQEAL--------DQALNYVRDAEDMNRATAARQR 507
Cdd:COG5278 89 DELLAELRSLTADNPEQQAR-----------LDELEAlIDQWLAELEQVIalrragglEAALALVRSGEGKALMDEIRAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 508 DHEKQQERVREQMEVVNMSLSTSADSLTTPRLTLSELDDIIKNASGIYAEIDGAKSELQVKLSNLSNLSHDLVQEAIDHA 587
Cdd:COG5278 158 LLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 588 QDLQQEANELSRKLHSSDMNGLVQKALDASNVYENIVNYVSEANETAEFALNTTDRIYDAVSGIDTQIIYHKDESENLLN 667
Cdd:COG5278 238 LALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 668 QARELQAKAESSSDEAVADTSRRVGGALARKSALKTRLSDAVKQLQAAERGDAQQRLGQSRLITEEANRTTMEVQQATAP 747
Cdd:COG5278 318 AAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 748 MANNLTNWSQNLQHFDSSAYNTAVNSARDAVRNLTEVVPQLLDQLRTVEQKRPASNVSASIQRIRELIAQTRSVASKIQV 827
Cdd:COG5278 398 AAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAAL 477
|
490
....*....|....*..
gi 1034650228 828 SMMFDGQSAVEVHSRTS 844
Cdd:COG5278 478 AAAAAALAEAEAAAALA 494
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
522-750 |
2.61e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.84 E-value: 2.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 522 VVNMSLSTSADslTTPRLTLSELDDIIKNASGIYAEIDGAKSELQVKLSNLSNLSHDL--VQEAIDhaqDLQQEANELSR 599
Cdd:COG3883 5 ALAAPTPAFAD--PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELeaLQAEID---KLQAEIAEAEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 600 KLhsSDMNGLVQKALDASNVYENIVNYVS---EANETAEFA--LNTTDRIYDAVSGIDTQIIYHKDESENLLNQARELQA 674
Cdd:COG3883 80 EI--EERREELGERARALYRSGGSVSYLDvllGSESFSDFLdrLSALSKIADADADLLEELKADKAELEAKKAELEAKLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 675 KAESSSDEAvADTSRRVGGALARKSALKTRLSDAVKQLQA------AERGDAQQRLGQSRLITEEANRTTMEVQQATAPM 748
Cdd:COG3883 158 ELEALKAEL-EAAKAELEAQQAEQEALLAQLSAEEAAAEAqlaeleAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
..
gi 1034650228 749 AN 750
Cdd:COG3883 237 AA 238
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
305-521 |
3.26e-07 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 54.15 E-value: 3.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 305 NEINATIYLLKTKLSERENQYAlrkiQINNAENTMKSLLSDVEEL----------VEKENQ----ASRKGQLVQ--KESM 368
Cdd:COG1340 81 DELNEKLNELREELDELRKELA----ELNKAGGSIDKLRKEIERLewrqqtevlsPEEEKElvekIKELEKELEkaKKAL 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 369 DTINHASQLVEQAHDMRDKIQEINNKMlyygeehelspKEISEKlvlAQKMLEEIRSRqpfFTQRELVDEEADEAYELLS 448
Cdd:COG1340 157 EKNEKLKELRAELKELRKEAEEIHKKI-----------KELAEE---AQELHEEMIEL---YKEADELRKEADELHKEIV 219
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034650228 449 QA-ESWQRLHnetrtlfpvvlEQLDDYNAKLSDLQEALDQALNYVRDAEdmnrataaRQRDHEKQQERVREQME 521
Cdd:COG1340 220 EAqEKADELH-----------EEIIELQKELRELRKELKKLRKKQRALK--------REKEKEELEEKAEEIFE 274
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
411-826 |
4.06e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.16 E-value: 4.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 411 EKLVLAQKMLEEIRSRQPfftqrELVDEEADEAYELLSQAESWQRLHNETRtlfpvvlEQLDDYNAKLSDLQEALDQALN 490
Cdd:COG4717 49 ERLEKEADELFKPQGRKP-----ELNLKELKELEEELKEAEEKEEEYAELQ-------EELEELEEELEELEAELEELRE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 491 YVRDAEDMNRAtaarqRDHEKQQERVREQMEvvnmSLSTSADSLTTPRLTLSELDDIIKNASgiyAEIDGAKSELQVKLS 570
Cdd:COG4717 117 ELEKLEKLLQL-----LPLYQELEALEAELA----ELPERLEELEERLEELRELEEELEELE---AELAELQEELEELLE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 571 NLSNLSHDLVQEAIDHAQDLQQEANELSRKL---------HSSDMNGLVQKALDAsNVYENIVNY-------------VS 628
Cdd:COG4717 185 QLSLATEEELQDLAEELEELQQRLAELEEELeeaqeeleeLEEELEQLENELEAA-ALEERLKEArlllliaaallalLG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 629 EANETAEFALNTTDRIYDAVSGIDTQIIYHKDESENLLNQARELQAKAESSS--DEAVADTSRRVGGALARKSALKTRLS 706
Cdd:COG4717 264 LGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEEleEEELEELLAALGLPPDLSPEELLELL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 707 DAVKQLQAA--ERGDAQQRLGQSRLITE------------------------EANRTTMEVQQATAPMANNLTNWSQNLQ 760
Cdd:COG4717 344 DRIEELQELlrEAEELEEELQLEELEQEiaallaeagvedeeelraaleqaeEYQELKEELEELEEQLEELLGELEELLE 423
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034650228 761 HFDSSAYNTAVNSARDAVRNLTEVVPQLLDQLRTVEQKRpaSNVSASiQRIRELIAQTRSVASKIQ 826
Cdd:COG4717 424 ALDEEELEEELEELEEELEELEEELEELREELAELEAEL--EQLEED-GELAELLQELEELKAELR 486
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
314-670 |
6.26e-07 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 54.46 E-value: 6.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 314 LKTKLSERENQY--ALRKI--QINNAEntmkSLLSDVEELVEKEN-QASRKGQLVQKESMDTINH-----ASQLVEQAHD 383
Cdd:PRK04778 152 LRKSLLANRFSFgpALDELekQLENLE----EEFSQFVELTESGDyVEAREILDQLEEELAALEQimeeiPELLKELQTE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 384 MRDKIQEINN---KML---YYGEEHELSP--KEISEKLVLAQKMLEEI---RSRQpfftQRELVDEEADEAYELLsQAES 452
Cdd:PRK04778 228 LPDQLQELKAgyrELVeegYHLDHLDIEKeiQDLKEQIDENLALLEELdldEAEE----KNEEIQERIDQLYDIL-EREV 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 453 wqRLHNETRTLFPVVLEQLDDYNAKLSDLQEALDQ-ALNYVRDAEDMnrataARQRDHEKQQERVREQMEVVnmslstsA 531
Cdd:PRK04778 303 --KARKYVEKNSDTLPDFLEHAKEQNKELKEEIDRvKQSYTLNESEL-----ESVRQLEKQLESLEKQYDEI-------T 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 532 DSLTTPRLTLSELDDIIKNASGIYAEIDgaksELQVKLSN-LSNLSHDlVQEAIDHAQDLQQEANELSRKLHSSDMNGLV 610
Cdd:PRK04778 369 ERIAEQEIAYSELQEELEEILKQLEEIE----KEQEKLSEmLQGLRKD-ELEAREKLERYRNKLHEIKRYLEKSNLPGLP 443
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034650228 611 QKALDAsnvYENIVNYVSEANEtaefALNTT----DRIYDAVSGIDTQIIYHKDESENLLNQAR 670
Cdd:PRK04778 444 EDYLEM---FFEVSDEIEALAE----ELEEKpinmEAVNRLLEEATEDVETLEEETEELVENAT 500
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
347-848 |
9.79e-07 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 54.06 E-value: 9.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 347 EELVEKENQASRKgqlvQKESMDTINHASQLVEQahdmrdkiqeinnkmlyygeEHELSPKEISEKLVLAQKMLEEIRSR 426
Cdd:NF041483 699 EALAAAQEEAARR----RREAEETLGSARAEADQ--------------------ERERAREQSEELLASARKRVEEAQAE 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 427 qpffTQReLVdEEADE-AYELLSQAESwqrlhnetrtlfpvVLEQLDDynaKLSDLQEALDQALNYVRDAEDMnraTAAR 505
Cdd:NF041483 755 ----AQR-LV-EEADRrATELVSAAEQ--------------TAQQVRD---SVAGLQEQAEEEIAGLRSAAEH---AAER 808
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 506 QRDhEKQQE--RVReqmevvnmslstsADSLTTpRLTLSEldDIIKNASGIYAEIDGAKSelqvklsnlsnLSHDLVQEA 583
Cdd:NF041483 809 TRT-EAQEEadRVR-------------SDAYAE-RERASE--DANRLRREAQEETEAAKA-----------LAERTVSEA 860
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 584 IDHAQDLQQEANELSRKLHSSDMNGLVQKALDASNVYenivnyvSEANETAefalnttDRI-YDAVSGIDTQIIYHKDES 662
Cdd:NF041483 861 IAEAERLRSDASEYAQRVRTEASDTLASAEQDAARTR-------ADAREDA-------NRIrSDAAAQADRLIGEATSEA 926
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 663 ENLLNQARelqAKAESSSDEAVADTSRRVGGALARKSALKTRLSDAVKQL--QAAER-GDAQQRLGQSRlitEEANRTTM 739
Cdd:NF041483 927 ERLTAEAR---AEAERLRDEARAEAERVRADAAAQAEQLIAEATGEAERLraEAAETvGSAQQHAERIR---TEAERVKA 1000
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 740 EvqqaTAPMANNLTNWSQN-----LQHFDSSAYNTAVNSARDAVRNLTEVVPQlLDQLRTVEQKRPASNVSASIQRIREL 814
Cdd:NF041483 1001 E----AAAEAERLRTEAREeadrtLDEARKDANKRRSEAAEQADTLITEAAAE-ADQLTAKAQEEALRTTTEAEAQADTM 1075
|
490 500 510
....*....|....*....|....*....|....
gi 1034650228 815 IAQTRSVASKIQVSMMFDGQSAVEvHSRTSMDDL 848
Cdd:NF041483 1076 VGAARKEAERIVAEATVEGNSLVE-KARTDADEL 1108
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
408-760 |
1.44e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.60 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 408 EISEKLVLAQKMLEEIRSR--QPFFTQRELVDEEADEAYELLSQAESWQRLHNETRtlfpvvlEQLDDYNAKLSDLQEAL 485
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKtgILIAALSEQLRKALFELDKLQEELEQLREELEQAR-------EELEQLEEELEQARSEL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 486 DQALNYVRDAEDMNRATAARQRDHEKQQERVREQMEvvnmSLSTSADSLttprltLSELDDIIKNASGIYAEIDGAKSEL 565
Cdd:COG4372 76 EQLEEELEELNEQLQAAQAELAQAQEELESLQEEAE----ELQEELEEL------QKERQDLEQQRKQLEAQIAELQSEI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 566 QVKLSNLSNLSHDLvQEAIDHAQDLQQEANELSRKLHSSDMNGLVQKAldasnvyENIVNYVSEANETAEFALNTTDRIY 645
Cdd:COG4372 146 AEREEELKELEEQL-ESLQEELAALEQELQALSEAEAEQALDELLKEA-------NRNAEKEEELAEAEKLIESLPRELA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 646 DAVSGIDTQIIYHKDESENLLNQARELQAKAESSSDEAVADTSRRVGGALARKSALKTRLSDAVKQLQAAERGDAQQRLG 725
Cdd:COG4372 218 EELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKL 297
|
330 340 350
....*....|....*....|....*....|....*
gi 1034650228 726 QSRLITEEANRTTMEVQQATAPMANNLTNWSQNLQ 760
Cdd:COG4372 298 LALLLNLAALSLIGALEDALLAALLELAKKLELAL 332
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
306-667 |
1.64e-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: 53.10 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 306 EINATIYLLKTKLSERENQYALRKIQINNAENTMKSL---LSDVEELVEKENQASRKGQ--LVQKESM-DTIN-HASQLV 378
Cdd:TIGR04523 430 RLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLetqLKVLSRSINKIKQNLEQKQkeLKSKEKElKKLNeEKKELE 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 379 EQAHDMRDKIQEINNKMlyygEEHELSPKEISEKLVLAQKMLEEIRSRqpffTQRELVDEEADEAYELLSQaeswqrLHN 458
Cdd:TIGR04523 510 EKVKDLTKKISSLKEKI----EKLESEKKEKESKISDLEDELNKDDFE----LKKENLEKEIDEKNKEIEE------LKQ 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 459 ETRTLfpvvleqlddyNAKLSDLQEALDQalnyvrdaedmnrataarqrdHEKQQERVREQMEVVNMSLSTSADSLTTPR 538
Cdd:TIGR04523 576 TQKSL-----------KKKQEEKQELIDQ---------------------KEKEKKDLIKEIEEKEKKISSLEKELEKAK 623
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 539 LTLSELDDIIKNasgiyaeIDGAKSELQVKLSNLsnlsHDLVQEAIDHAQDLQQEANELSRKLhsSDMNGLVQKALDASN 618
Cdd:TIGR04523 624 KENEKLSSIIKN-------IKSKKNKLKQEVKQI----KETIKEIRNKWPEIIKKIKESKTKI--DDIIELMKDWLKELS 690
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1034650228 619 VYENivNYVSEANETAEfaLNTTDRIYDAVSGIDTQIIYHKDESENLLN 667
Cdd:TIGR04523 691 LHYK--KYITRMIRIKD--LPKLEEKYKEIEKELKKLDEFSKELENIIK 735
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
331-604 |
2.40e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 51.45 E-value: 2.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 331 QINNAENTMKSLLSDVEELVEKENQASRKGQLVQKESMDTINHASQLVEQAHDMRDKIQEINNKMlyygEEHELSPKEIS 410
Cdd:COG1340 9 SLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKV----KELKEERDELN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 411 EKLVLAQKMLEEIRSRQPfftQRELVDEEADEAYELLSQAEsWQRlhnETRTLFP----VVLEQLDDYNAKLSDLQEALD 486
Cdd:COG1340 85 EKLNELREELDELRKELA---ELNKAGGSIDKLRKEIERLE-WRQ---QTEVLSPeeekELVEKIKELEKELEKAKKALE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 487 QALNYVrdaEDMNRATAARqrdheKQQERVREQMEvvnmSLSTSADSLTTprltlsELDDIIKNASGIYAEIDGAKSELq 566
Cdd:COG1340 158 KNEKLK---ELRAELKELR-----KEAEEIHKKIK----ELAEEAQELHE------EMIELYKEADELRKEADELHKEI- 218
|
250 260 270
....*....|....*....|....*....|....*...
gi 1034650228 567 VKLSNLSNLSHDLVQEAIDHAQDLQQEANELSRKLHSS 604
Cdd:COG1340 219 VEAQEKADELHEEIIELQKELRELRKELKKLRKKQRAL 256
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
449-824 |
2.48e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.63 E-value: 2.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 449 QAESWQRLHNETRTLfpvvleQLDDYNAKLSDLQEALDQALNYVRDAEDMNRATAARQRDHEKQQERVREQMEVVNMSLS 528
Cdd:COG1196 211 KAERYRELKEELKEL------EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 529 TSADSLttpRLTLSELddiiknasgiyAEIDGAKSELQVKLSNLSNLSHDLVQEAIDHAQDLQQEANELSRKLHSSDMng 608
Cdd:COG1196 285 EAQAEE---YELLAEL-----------ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE-- 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 609 LVQKALDASNVYENIVNYVSEANETAEFALNTTDRIYDAVSGIDTQIIYHKDESENLLNQARELQAKAESSSDEAVADTS 688
Cdd:COG1196 349 AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 689 RRVGGALARKSALKTRLSDAVKQLQAAERGDAQQR----LGQSRLITEEANRTTMEVQQATAPMANNLTNWSQNLQHFDS 764
Cdd:COG1196 429 ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEllaeLLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 765 SAYNTAVNSARDAvrnltevVPQLLDQLRTVEQKRPASNVSASIQRIRELIAQTRSVASK 824
Cdd:COG1196 509 GVKAALLLAGLRG-------LAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAA 561
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
302-566 |
3.17e-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: 3.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 302 RHVNEINATIYLLKTKLSERENQYAlrkiQINNAENTMKSLLSDVEELVEKENQAsrkgQLVQKESMDTIN-HASQLVEQ 380
Cdd:TIGR02169 702 NRLDELSQELSDASRKIGEIEKEIE----QLEQEEEKLKERLEELEEDLSSLEQE----IENVKSELKELEaRIEELEED 773
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 381 AHDMRDKIQEInnkmlyygeEHELSPKEISEKLVLAQKmLEEIRSRQPFFTQ---RELVDEEADEAY------ELLSQAE 451
Cdd:TIGR02169 774 LHKLEEALNDL---------EARLSHSRIPEIQAELSK-LEEEVSRIEARLReieQKLNRLTLEKEYlekeiqELQEQRI 843
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 452 SWQRLHNETRtlfpvvlEQLDDYNAKLSDLQEALDQALNYVRDAEDmnrataaRQRDHEKQQERVREQMEVVNMSLSTSA 531
Cdd:TIGR02169 844 DLKEQIKSIE-------KEIENLNGKKEELEEELEELEAALRDLES-------RLGDLKKERDELEAQLRELERKIEELE 909
|
250 260 270
....*....|....*....|....*....|....*
gi 1034650228 532 DSLTTPRLTLSELDDIIKNASGIYAEIDGAKSELQ 566
Cdd:TIGR02169 910 AQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDE 944
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
307-567 |
3.94e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 51.97 E-value: 3.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 307 INATIYLLKTKLSERENQYAlrkiQINNAENTMKSLLSDV---EELVEKENQASRK-GQLVQK-ESMDTINHASQLVEQA 381
Cdd:TIGR00606 756 VNRDIQRLKNDIEEQETLLG----TIMPEEESAKVCLTDVtimERFQMELKDVERKiAQQAAKlQGSDLDRTVQQVNQEK 831
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 382 HDMRDKIQEINNKmlyyGEEHELSPKEISEKLVLAQKMLEEIRS-----------RQPFFTQRELVDEEADEAYELLSQA 450
Cdd:TIGR00606 832 QEKQHELDTVVSK----IELNRKLIQDQQEQIQHLKSKTNELKSeklqigtnlqrRQQFEEQLVELSTEVQSLIREIKDA 907
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 451 --------ESWQRLHNETRTLFPVVLEQLDDYNAKLSDLQEALDQAL-------NYVRDAED---MNRAT-----AARQR 507
Cdd:TIGR00606 908 keqdspleTFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHgymkdieNKIQDGKDdylKQKETelntvNAQLE 987
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034650228 508 DHEKQQERVREQMEVVNMSLSTS--ADSLTTPRLTLSELDDIIKNASGIYAEIDGAKSELQV 567
Cdd:TIGR00606 988 ECEKHQEKINEDMRLMRQDIDTQkiQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQV 1049
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
306-711 |
4.13e-06 |
|
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: 51.89 E-value: 4.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 306 EINATIYLLKTKLSERENQYALRKIQINNAENTMKSLLSDVEEL---VEKENQASRKGQLVQKESMDTINHASQLVEQAH 382
Cdd:TIGR00618 553 SERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLqdlTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRL 632
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 383 DMRDKIQEINNKMLY-YGEEHELSPKEISEKLVLA---QKMLEEIRSRQPFFTQRELVDEEADEayELLSQAESWQR-LH 457
Cdd:TIGR00618 633 HLQQCSQELALKLTAlHALQLTLTQERVREHALSIrvlPKELLASRQLALQKMQSEKEQLTYWK--EMLAQCQTLLReLE 710
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 458 NETRTLFPVVLEQLDDYNAKLSDLQ---EALDQALNYVR-------------DAEDMNRATAARQRDHEKQQerVREQME 521
Cdd:TIGR00618 711 THIEEYDREFNEIENASSSLGSDLAareDALNQSLKELMhqartvlkarteaHFNNNEEVTAALQTGAELSH--LAAEIQ 788
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 522 VVNMSLSTSADSLttpRLTLSEL------DDIIKNASGIyaEIDGAKSELQVKLSNLSNLSHDLVQEAIDHAQDLQQEAn 595
Cdd:TIGR00618 789 FFNRLREEDTHLL---KTLEAEIgqeipsDEDILNLQCE--TLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLA- 862
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 596 ELSRKlhSSDMNGLVQKAldasNVYENIVNYVsEANETAEFALNTTdriYDAVsgIDTQIIYH-------KDESENllnq 668
Cdd:TIGR00618 863 QLTQE--QAKIIQLSDKL----NGINQIKIQF-DGDALIKFLHEIT---LYAN--VRLANQSEgrfhgryADSHVN---- 926
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1034650228 669 ARELQAKAE---SSSDEAVADTSRRVGGALARKS-ALKTRLSDAVKQ 711
Cdd:TIGR00618 927 ARKYQGLALlvaDAYTGSVRPSATLSGGETFLASlSLALALADLLST 973
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
433-814 |
4.50e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.88 E-value: 4.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 433 RELVDEEAD---EAYELLSQAESWQRLHNETRtlfpvvlEQLDDYNAKLSDLQEALDQA---LNYVRDAEDMNRATAARQ 506
Cdd:PRK04863 282 RVHLEEALElrrELYTSRRQLAAEQYRLVEMA-------RELAELNEAESDLEQDYQAAsdhLNLVQTALRQQEKIERYQ 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 507 RDHEKQQERVREQMEVVNMSLSTSADSLTTPRLTLSELD-------------DIIKNASGIYAE----IDGAKSELQVKL 569
Cdd:PRK04863 355 ADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDelksqladyqqalDVQQTRAIQYQQavqaLERAKQLCGLPD 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 570 SNLSNLShDLVQEAIDHAQDLQQEANELSRKLHSSDMnglvqkaldasnvyenivnyvseANETAEFALNTTDRIYDAVS 649
Cdd:PRK04863 435 LTADNAE-DWLEEFQAKEQEATEELLSLEQKLSVAQA-----------------------AHSQFEQAYQLVRKIAGEVS 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 650 GIDTQiiyhkDESENLLNQARELQAKAEsssdeavadtsrRVGGALARKSALKTRLsdavKQLQAAER--GDAQQRLGQS 727
Cdd:PRK04863 491 RSEAW-----DVARELLRRLREQRHLAE------------QLQQLRMRLSELEQRL----RQQQRAERllAEFCKRLGKN 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 728 --------RLITE-EANRTTMEVQQATA-----PMANNLTNWSQNLQHFDSSA-----YNTAVNSARDAV-------RNL 781
Cdd:PRK04863 550 lddedeleQLQEElEARLESLSESVSEArerrmALRQQLEQLQARIQRLAARApawlaAQDALARLREQSgeefedsQDV 629
|
410 420 430
....*....|....*....|....*....|....*
gi 1034650228 782 TEVVPQLLDQLR--TVEQKRPASNVSASIQRIREL 814
Cdd:PRK04863 630 TEYMQQLLERERelTVERDELAARKQALDEEIERL 664
|
|
| ApoLp-III_like |
cd13769 |
Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles ... |
703-829 |
4.70e-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: 4.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 703 TRLSDAVKQLQAAERGDAQQRLGQSRL-ITEEANRTtmeVQQATAPMANNLTNWSQNLQHFDSSAYNTAVNSARDAVRNL 781
Cdd:cd13769 1 TQLSELIQKAQEAINNLAQQVQKQLGLqNPEEVVNT---LKEQSDNFANNLQEVSSSLKEEAKKKQGEVEEAWNEFKTKL 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1034650228 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 |
4.79e-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: 49.37 E-value: 4.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 332 INNAENTMKSL-----LSDVEELVEKeNQASRKGQLVQKESMDTIN-HASQLVEQAHDMRDKIQE----INNKMlyygee 401
Cdd:cd00176 16 LSEKEELLSSTdygddLESVEALLKK-HEALEAELAAHEERVEALNeLGEQLIEEGHPDAEEIQErleeLNQRW------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 402 helspKEISEKLVLAQKMLEEIRSRQPFFTQrelVDEEADEAYELLSQAESWQRLHNETRtlfpvVLEQLDdynaKLSDL 481
Cdd:cd00176 89 -----EELRELAEERRQRLEEALDLQQFFRD---ADDLEQWLEEKEAALASEDLGKDLES-----VEELLK----KHKEL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1034650228 482 QEALDQALNYVRDAEDMNRATAARQrdHEKQQERVREQMEVVN 524
Cdd:cd00176 152 EEELEAHEPRLKSLNELAEELLEEG--HPDADEEIEEKLEELN 192
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
302-572 |
7.49e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.22 E-value: 7.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 302 RHVNEINATIYLLKTKLSERENQYALRKIQINNAENTMKSLLSDvEELVEKENQASRKGQLVQKEsmDTINHASQLVEQA 381
Cdd:TIGR02169 244 RQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEE-EQLRVKEKIGELEAEIASLE--RSIAEKERELEDA 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 382 HDMRDKIQEINNKMLyygEEHELSPKEISEKLVLAQKMLEEIRSRQpfftqrelvdeeaDEAYELLSQAESWQRLHNETR 461
Cdd:TIGR02169 321 EERLAKLEAEIDKLL---AEIEELEREIEEERKRRDKLTEEYAELK-------------EELEDLRAELEEVDKEFAETR 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 462 TLFPVVLEQLDDYNAKLSDLQEALDQALNYVRDAEdmnrataARQRDHEKQQERVREQ-------MEVVNMSLSTSADSL 534
Cdd:TIGR02169 385 DELKDYREKLEKLKREINELKRELDRLQEELQRLS-------EELADLNAAIAGIEAKineleeeKEDKALEIKKQEWKL 457
|
250 260 270
....*....|....*....|....*....|....*...
gi 1034650228 535 TTPRLTLSELDDIIKNASGIYAEIDGAKSELQVKLSNL 572
Cdd:TIGR02169 458 EQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEA 495
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
1256-1369 |
9.61e-06 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 46.93 E-value: 9.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 1256 FRTLQPNGLLFYYAS--GSDVFSISLDNG--TVIMDV-KGIKVQSVDKQYNDGLSHFVISSVSPTRYELIVDK-SRVGSK 1329
Cdd:pfam00054 1 FRTTEPSGLLLYNGTqtERDFLALELRDGrlEVSYDLgSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGeARPTGE 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1034650228 1330 NPTKGKieQTQASEKKFYFGGSPISAQYA-------NFTGCISNAYF 1369
Cdd:pfam00054 81 SPLGAT--TDLDVDGPLYVGGLPSLGVKKrrlaispSFDGCIRDVIV 125
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
313-601 |
1.08e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 313 LLKTKLSERENQYALRKiqinNAENTMKsllsdVEELVEKENQASRKGQLVQKESMDTINHASQLVEQAHDMRDKIQEIN 392
Cdd:PTZ00121 1680 AKKAEEDEKKAAEALKK----EAEEAKK-----AEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAK 1750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 393 NkmlyygEEHElsPKEISEKLVLAQKMLEEIRSRQPFFTQRELVDEEADEAYELlsqaeswQRLHNETRTLFPVVLEQLD 472
Cdd:PTZ00121 1751 K------DEEE--KKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEV-------DKKIKDIFDNFANIIEGGK 1815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 473 DYNAKLSDLQEALDQALNYVRDAEDMNRATAARQRDHEKQQERVREQMEVVNMSLSTSADSLTTPRLTLSELDDIIKnas 552
Cdd:PTZ00121 1816 EGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEK--- 1892
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1034650228 553 giyaeIDGAKSELQVKLSNLSNLSHDLVQEAIDHAQDLQQEANELSRKL 601
Cdd:PTZ00121 1893 -----IDKDDIEREIPNNNMAGKNNDIIDDKLDKDEYIKRDAEETREEI 1936
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
314-671 |
2.28e-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: 49.66 E-value: 2.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 314 LKTKLS--ERENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLVQKESMDTINHASQLVEQAHDMRDKIQEI 391
Cdd:TIGR01612 2049 IKEKIDnyEKEKEKFGIDFDVKAMEEKFDNDIKDIEKFENNYKHSEKDNHDFSEEKDNIIQSKKKLKELTEAFNTEIKII 2128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 392 NNKMLyygEEHELSPKeiseklvlaqkmLEEIRSRQPFFTQRELVDEeadeayeLLSQAESWQRLHNETRTLFPVVLEQL 471
Cdd:TIGR01612 2129 EDKII---EKNDLIDK------------LIEMRKECLLFSYATLVET-------LKSKVINHSEFITSAAKFSKDFFEFI 2186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 472 DDYNAKLSDLQEALDQALNYVRDAEDMNRATAARQRDHEKQQERVREQMEVVNM--------SLSTSADSLTTPRLTL-- 541
Cdd:TIGR01612 2187 EDISDSLNDDIDALQIKYNLNQTKKHMISILADATKDHNNLIEKEKEATKIINNltelftidFNNADADILHNNKIQIiy 2266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 542 --SELDDIIKNASGIYAEIDGakselqVKLSNLSNLSHDLVQEAIDHAQDLQQEANELSRKLHssDMNGLVQKALDASNV 619
Cdd:TIGR01612 2267 fnSELHKSIESIKKLYKKINA------FKLLNISHINEKYFDISKEFDNIIQLQKHKLTENLN--DLKEIDQYISDKKNI 2338
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1034650228 620 YENIVNyvseanETAEFALNTTDRIYDAVSGIDTQIiyhkDESENLLNQARE 671
Cdd:TIGR01612 2339 FLHALN------ENTNFNFNALKEIYDDIINRENKA----DEIENINNKENE 2380
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
514-757 |
2.40e-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: 49.66 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 514 ERVREQMEVVNMSLSTSADSLTTPRLTLSELDDIIKnaSGIYAEIDGAKSELQVKLSNLSNLSHDLVQEAIDHAQD---L 590
Cdd:TIGR01612 500 MRMKDFKDIIDFMELYKPDEVPSKNIIGFDIDQNIK--AKLYKEIEAGLKESYELAKNWKKLIHEIKKELEEENEDsihL 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 591 QQEAN---------------------ELSRKLHS-SDMNGLVQKALDASNVYENIVNYVSEANETAEFA----LNTTDRI 644
Cdd:TIGR01612 578 EKEIKdlfdkyleiddeiiyinklklELKEKIKNiSDKNEYIKKAIDLKKIIENNNAYIDELAKISPYQvpehLKNKDKI 657
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 645 YDAVSGIDTQI--------------IYHKDESENLLNQAR--ELQAKAESSSDEAVADTSRRVGGALARKSALKTRLSDA 708
Cdd:TIGR01612 658 YSTIKSELSKIyeddidalynelssIVKENAIDNTEDKAKldDLKSKIDKEYDKIQNMETATVELHLSNIENKKNELLDI 737
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1034650228 709 VKQLQAAERGDaqqrlgqsrlITEEANRTTMEVQQATAPMANNLTNWSQ 757
Cdd:TIGR01612 738 IVEIKKHIHGE----------INKDLNKILEDFKNKEKELSNKINDYAK 776
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
314-604 |
3.37e-05 |
|
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: 48.91 E-value: 3.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 314 LKTKLSEREnQYALRKiQINNAENTMKSLLSDVEELvEKEnQASRKGQLvqkesmdtinhaSQLVEQAHDMRDKIQEINN 393
Cdd:TIGR02169 216 LLKEKREYE-GYELLK-EKEALERQKEAIERQLASL-EEE-LEKLTEEI------------SELEKRLEEIEQLLEELNK 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 394 KMLYYGEEHELSPKE---------------ISEKLVLAQKMLEEIRSRQpfftqrELVDEEADEAYELLSQAESWQRlhn 458
Cdd:TIGR02169 280 KIKDLGEEEQLRVKEkigeleaeiaslersIAEKERELEDAEERLAKLE------AEIDKLLAEIEELEREIEEERK--- 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 459 ETRTLFPVVLEQLDDYNAKLSDLQEAldqalnyvrDAEdmNRATAARQRDHEKQQERVREQMEVVNMSLSTSADSLTTPR 538
Cdd:TIGR02169 351 RRDKLTEEYAELKEELEDLRAELEEV---------DKE--FAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLS 419
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 539 LTLSELDDIIKNASGIYAEIDGAKSELQVKLS----NLSNLSHDLVQEAIDHaQDLQQEANELSRKLHSS 604
Cdd:TIGR02169 420 EELADLNAAIAGIEAKINELEEEKEDKALEIKkqewKLEQLAADLSKYEQEL-YDLKEEYDRVEKELSKL 488
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
303-759 |
4.31e-05 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 48.31 E-value: 4.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 303 HVNEINATIYLLKTKLSERenqyALRKI--QINNAENTMKSLLSDVEELVEKEnqasrkgqlvqKESMDTINHAsqlveq 380
Cdd:pfam06160 68 LLFEAEELNDKYRFKKAKK----ALDEIeeLLDDIEEDIKQILEELDELLESE-----------EKNREEVEEL------ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 381 ahdmRDKIQEINNKMLYYGeeHELSPKEisEKLvlaQKMLEEIRSRqpfFTQRELVDEEAD--EAYELLSQaeswqrLHN 458
Cdd:pfam06160 127 ----KDKYRELRKTLLANR--FSYGPAI--DEL---EKQLAEIEEE---FSQFEELTESGDylEAREVLEK------LEE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 459 ETRTL------FPVVLEQL-DDYNAKLSDLQEALDQAL--NYVRD----AEDMNRATAARQRD----HEKQQERVREQME 521
Cdd:pfam06160 187 ETDALeelmedIPPLYEELkTELPDQLEELKEGYREMEeeGYALEhlnvDKEIQQLEEQLEENlallENLELDEAEEALE 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 522 VVNMSLSTSADSLTTprltlsELD---DIIKNASGIYAEIDGAKS---ELQVKLSNLsNLSHDLVQEAIDHAQDLQQEAN 595
Cdd:pfam06160 267 EIEERIDQLYDLLEK------EVDakkYVEKNLPEIEDYLEHAEEqnkELKEELERV-QQSYTLNENELERVRGLEKQLE 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 596 ELSRKLHSsdmngLVQKALDASNVYENIVNYVSEanetaefalnttdrIYDAVSGIDTQIIYHKDESENLLNQarELQAK 675
Cdd:pfam06160 340 ELEKRYDE-----IVERLEEKEVAYSELQEELEE--------------ILEQLEEIEEEQEEFKESLQSLRKD--ELEAR 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 676 AESSS-DEAVADTSRRVggalaRKSAL-------KTRLSDAVKQLQaaergDAQQRLGQSRLITEEANRttmEVQQATAP 747
Cdd:pfam06160 399 EKLDEfKLELREIKRLV-----EKSNLpglpesyLDYFFDVSDEIE-----DLADELNEVPLNMDEVNR---LLDEAQDD 465
|
490
....*....|..
gi 1034650228 748 MaNNLTNWSQNL 759
Cdd:pfam06160 466 V-DTLYEKTEEL 476
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
306-572 |
5.91e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.14 E-value: 5.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 306 EINATIYLLKTKLSERENQyalrKIQINNAENTMKSLLSDVEELVEKENQASRKGQLVQKEsmdtinhasqlVEQAHDMR 385
Cdd:PRK03918 173 EIKRRIERLEKFIKRTENI----EELIKEKEKELEEVLREINEISSELPELREELEKLEKE-----------VKELEELK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 386 DKIQEINNKMlyygEEHELSPKEISEKLVLAQKMLEEIRSRqpfftQRELvDEEADEAYELLSQAESWQRL---HNETRT 462
Cdd:PRK03918 238 EEIEELEKEL----ESLEGSKRKLEEKIRELEERIEELKKE-----IEEL-EEKVKELKELKEKAEEYIKLsefYEEYLD 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 463 LFPVVLEQLDDYNAKLSDLQEALDQALNYVRDAEDMNRATAARQRDHEKQQERVREQMEVvnMSLSTSADSLTTpRLTLS 542
Cdd:PRK03918 308 ELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEA--KAKKEELERLKK-RLTGL 384
|
250 260 270
....*....|....*....|....*....|
gi 1034650228 543 ELDDIIKNasgiYAEIDGAKSELQVKLSNL 572
Cdd:PRK03918 385 TPEKLEKE----LEELEKAKEEIEEEISKI 410
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
875-1006 |
8.30e-05 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 44.23 E-value: 8.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 875 ILYLGSKNaKKEYMGLAIKNDNLVYVYNLGTKDVEIPldSKPVSSwPAYFSIVKIERVGKHGkvFLTV---PSLSSTAEe 951
Cdd:pfam00054 10 LLYNGTQT-ERDFLALELRDGRLEVSYDLGSGAAVVR--SGDKLN-DGKWHSVELERNGRSG--TLSVdgeARPTGESP- 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034650228 952 kfikkgefSGDDSLLDLDpedTVFYVGGVPSNFKLPTSL-NLPGFVGCLELATLNN 1006
Cdd:pfam00054 83 --------LGATTDLDVD---GPLYVGGLPSLGVKKRRLaISPSFDGCIRDVIVNG 127
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
277-658 |
1.38e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.43 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 277 LRLAALSIEEGKSGVLSVSSGAAAHRHVNEINATIYLLKTKLSERENQYALRKIQINNAENTMKSLLSDVEELvEKENQA 356
Cdd:COG4372 13 LSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL-NEQLQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 357 SRKGQLVQKESMDTINhasqlvEQAHDMRDKIQEINnkmlyygeehelspKEISEKLVLAQKMLEEIRSRQPFFTQRElv 436
Cdd:COG4372 92 AQAELAQAQEELESLQ------EEAEELQEELEELQ--------------KERQDLEQQRKQLEAQIAELQSEIAERE-- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 437 deeaDEAYELLSQAESWQRLhnetrtlfpvvLEQLDDYNAKLSD--LQEALDQALNYVRDAEDMNRATAARQRDHEKQQE 514
Cdd:COG4372 150 ----EELKELEEQLESLQEE-----------LAALEQELQALSEaeAEQALDELLKEANRNAEKEEELAEAEKLIESLPR 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 515 RVREQMEVVNMSLSTSADSLTTPRLTLSELDDIIKNASGIYAEIDGAKSELQVKLSNLSNLSHDLVQEAIDHAQDLQQEA 594
Cdd:COG4372 215 ELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALE 294
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034650228 595 NELSRKLHSSDMNGLVQKALDASNVYENIVNYVSEANETAEFALNTTDRIYDAVSGIDTQIIYH 658
Cdd:COG4372 295 LKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLEL 358
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
304-718 |
4.18e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 45.28 E-value: 4.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 304 VNEINATIYLLKTKLSERENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRkgqlvqkesmdtinhasqLVEQAHD 383
Cdd:PRK01156 199 LENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNR------------------YESEIKT 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 384 MRDKIQEINNKMLYYGEEHELSPKEISEKLVLAQKMLEE-IRSRQPFFTQREL---VDEEADEAYELLSQAESWQRLHNE 459
Cdd:PRK01156 261 AESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDyFKYKNDIENKKQIlsnIDAEINKYHAIIKKLSVLQKDYND 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 460 trtlFPVVLEQLDDYNAKLSDLQEALDQALNYVRDAEDMNRataaRQRDHEKQQERVREQMEVVNMSLSTSADSLTTPRL 539
Cdd:PRK01156 341 ----YIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKK----KIEEYSKNIERMSAFISEILKIQEIDPDAIKKELN 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 540 TL-SELDDIIKNASGIYAEIDGAKSELQVKLSNLSNL-----------------SHDLVQEAIDHAQDLQQEANELSRKL 601
Cdd:PRK01156 413 EInVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLngqsvcpvcgttlgeekSNHIINHYNEKKSRLEEKIREIEIEV 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 602 HSSDMNGLVQKALDASNVYENIVNYVSEANETAEFALNTTDrIYDAVSgidtQIIYHKDESENLLNQAR-----ELQAKA 676
Cdd:PRK01156 493 KDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLED-IKIKIN----ELKDKHDKYEEIKNRYKslkleDLDSKR 567
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1034650228 677 ESSSDEAVADTSRRVGGALARKSALKTRLSDAVKQLQAAERG 718
Cdd:PRK01156 568 TSWLNALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIG 609
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
306-568 |
4.38e-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: 45.44 E-value: 4.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 306 EINATIYLLKTKLSERENQYALRKIQINNAE-NTMKSLLSDVEELVE----KENQASRKGQLVQKESMDTINHASQLVEQ 380
Cdd:TIGR02169 769 ELEEDLHKLEEALNDLEARLSHSRIPEIQAElSKLEEEVSRIEARLReieqKLNRLTLEKEYLEKEIQELQEQRIDLKEQ 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 381 AHDMRDKIQEIN---NKMLYYGEEHELSPKEISEKLVLAQKMLEEIRS--RQPFFTQRELvDEEADEAYELLSQ-AESWQ 454
Cdd:TIGR02169 849 IKSIEKEIENLNgkkEELEEELEELEAALRDLESRLGDLKKERDELEAqlRELERKIEEL-EAQIEKKRKRLSElKAKLE 927
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 455 RLHNETRTLFPVVLEQLDDYNAKLS--DLQEALDQALNYVRDAEDMN-RA------TAARQRDHEKQQERVREQMEvvnm 525
Cdd:TIGR02169 928 ALEEELSEIEDPKGEDEEIPEEELSleDVQAELQRVEEEIRALEPVNmLAiqeyeeVLKRLDELKEKRAKLEEERK---- 1003
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1034650228 526 SLSTSADSLTTPR--LTLSELDDIIKNASGIYAEIDGAKSELQVK 568
Cdd:TIGR02169 1004 AILERIEEYEKKKreVFMEAFEAINENFNEIFAELSGGTGELILE 1048
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
304-602 |
4.75e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 4.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 304 VNEINATIYLLKTKLSERENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLVQKESMDTINHASQLVEQAHD 383
Cdd:COG4372 82 LEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLES 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 384 MRDKIQEINNkmlyygEEHELSPKEISEKLvlaQKMLEEIRSRQPFFTQRELVDEEADEAYELLSQAESwQRLHNETRTL 463
Cdd:COG4372 162 LQEELAALEQ------ELQALSEAEAEQAL---DELLKEANRNAEKEEELAEAEKLIESLPRELAEELL-EAKDSLEAKL 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 464 FPVVLEQLDDYNAKLSDLQEALDQALNYVRDAEDMNRATAARQRDHEKQQERVREQMEVVNMSLSTSAdslTTPRLTLSE 543
Cdd:COG4372 232 GLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLA---LLLNLAALS 308
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034650228 544 LDDIIKNASGIYAEIDGAKSELQVKLSNLSNLSHDLVQEAIDHAQDLQQEANELSRKLH 602
Cdd:COG4372 309 LIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGV 367
|
|
| VSP |
pfam03302 |
Giardia variant-specific surface protein; |
87-212 |
8.39e-04 |
|
Giardia variant-specific surface protein;
Pssm-ID: 146106 [Multi-domain] Cd Length: 397 Bit Score: 43.80 E-value: 8.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 87 NSNECLDGSGYCVHCQRNTTgehCEKCLDGYIGDSirgapQFCQPCpcplphlanfAESCYRKNGAVRcicnenyagpNC 166
Cdd:pfam03302 252 NNGDLVTCSPGCKTCTSNTV---CTTCMDGYVKTS-----DSCTKC----------DSSCETCTGATT----------TC 303
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1034650228 167 ERCAPGYYGNplliGSTCKKCDCSgNSDPNLIfedcdEVTGqCRNC 212
Cdd:pfam03302 304 KTCATGYYKS----GTGCVSCTSS-ESDNGIT-----GVKG-CLNC 338
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
359-675 |
9.07e-04 |
|
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.
Pssm-ID: 427715 [Multi-domain] Cd Length: 360 Bit Score: 43.53 E-value: 9.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 359 KGQLVQKESMDTINHASQLVEQAHDMRDKIQEINnkmlyygeehelspKEISEKLVLAQKMLEEIRSRqpfftqRELVDE 438
Cdd:pfam04108 4 SAQDLCRWANELLTDARSLLEELVVLLAKIAFLR--------------RGLSVQLANLEKVREGLEKV------LNELKK 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 439 EADEAYELLSQA-ESWQR-LHNETRTLFPVVLEQLDDYNAKLSDL--QEALDQALNYVRdaedmnrataarqrdheKQQE 514
Cdd:pfam04108 64 DFKQLLKDLDAAlERLEEtLDKLRNTPVEPALPPGEEKQKTLLDFidEDSVEILRDALK-----------------ELID 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 515 RVREQMEvvnmSLSTSADSLTTprlTLSELDDIIKNASGIYAEIDGAKSELQvklsNLSNLSHDLVQ--EAIDHAQDLQQ 592
Cdd:pfam04108 127 ELQAAQE----SLDSDLKRFDD---DLRDLQKELESLSSPSESISLIPTLLK----ELESLEEEMASllESLTNHYDQCV 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 593 EANELSRKLHSSDMNGLVQKALDASNVYENIVNYVSEANETAEFALNTTDRIYDAvsgidtqiiyhKDESENLLNQAREL 672
Cdd:pfam04108 196 TAVKLTEGGRAEMLEVLENDARELDDVVPELQDRLDEMENNYERLQKLLEQKNSL-----------IDELLSALQLIAEI 264
|
...
gi 1034650228 673 QAK 675
Cdd:pfam04108 265 QSR 267
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
469-672 |
9.81e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.85 E-value: 9.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 469 EQLDDYNAKLSDLQEALDQALNYVRDAEDMNRATAarqRDHEKQQERVREQMEVVNMSLSTSADSLTTPRLTLSELDDII 548
Cdd:PHA02562 195 QQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEA---KTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKI 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 549 KNASGI----------------YAEIDGAKSELQVKLSNLsNLSHDLVQEAIDHAQDLQQEANELSRKLHssDMNGlvqk 612
Cdd:PHA02562 272 EQFQKVikmyekggvcptctqqISEGPDRITKIKDKLKEL-QHSLEKLDTAIDELEEIMDEFNEQSKKLL--ELKN---- 344
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 613 alDASNVYENIVNYVSEAnetaefalnttDRIYDAVSGIDTQIIYHKDESENLLNQAREL 672
Cdd:PHA02562 345 --KISTNKQSLITLVDKA-----------KKVKAAIEELQAEFVDNAEELAKLQDELDKI 391
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
659-817 |
1.38e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 659 KDESENLLNQARELQAK-AESSSDEAVADTSRR--------VGGAlaRKSALKTRLSDAVKQLQAAE--RGDAQQRLGQS 727
Cdd:COG4913 294 EAELEELRAELARLEAElERLEARLDALREELDeleaqirgNGGD--RLEQLEREIERLERELEERErrRARLEALLAAL 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 728 RLiTEEANRTTMEVQQATAPMAnnLTNWSQnlqhfDSSAYNTAVNSARDAVRNLTEVVPQLLDQLRTVEQKRpaSNVSAS 807
Cdd:COG4913 372 GL-PLPASAEEFAALRAEAAAL--LEALEE-----ELEALEEALAEAEAALRDLRRELRELEAEIASLERRK--SNIPAR 441
|
170
....*....|
gi 1034650228 808 IQRIRELIAQ 817
Cdd:COG4913 442 LLALRDALAE 451
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
316-543 |
1.48e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 316 TKLSERENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLVQKEsMDT----INHASQLVEQAhdmRDKIQEI 391
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAE-IDKlqaeIAEAEAEIEER---REELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 392 NNKMlyYGEEHELSPKEIseklVLAQKMLEEirsrqpFFTQRELVDEEADEAYELLSQAESWQRLHNETRTLfpvVLEQL 471
Cdd:COG3883 92 ARAL--YRSGGSVSYLDV----LLGSESFSD------FLDRLSALSKIADADADLLEELKADKAELEAKKAE---LEAKL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034650228 472 DDYNAKLSDLQEALDQALNYVRDAEDMNRATAARQRDHEKQQERVREQMEVVNMSLSTSADSLTTPRLTLSE 543
Cdd:COG3883 157 AELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
398-601 |
1.76e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 398 YGEEHELSPKEISEKLvlaqKMLEEIRSRQpffTQRELVDEEADEAYELLSQAESWQRLHNETRTLFPVVLEQLDDYN-- 475
Cdd:COG4717 328 LGLPPDLSPEELLELL----DRIEELQELL---REAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQel 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 476 -AKLSDLQEALDQALNYVRDAEDMNrataarqrdhekQQERVREQMEVVNMSLSTSADSLTTPRLTLSELDDIIKNA--S 552
Cdd:COG4717 401 kEELEELEEQLEELLGELEELLEAL------------DEEELEEELEELEEELEELEEELEELREELAELEAELEQLeeD 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 553 GIYAEIDGAKSELQVKLSNLS------NLSHDLVQEAIDHAQD-----LQQEANELSRKL 601
Cdd:COG4717 469 GELAELLQELEELKAELRELAeewaalKLALELLEEAREEYREerlppVLERASEYFSRL 528
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
469-680 |
2.13e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.08 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 469 EQLDDYNAKLSDLQEALD--QALNYVRDAEDMNRATAARQRDHEKQQERVREQMEVVNMSLSTSADSLTTPRLTLSELdd 546
Cdd:COG3206 182 EQLPELRKELEEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL-- 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 547 iikNASGIYAEIDGAKSELQVKLSNLSNL---SHDLVQEAIDHAQDLQQE-ANELSRKLHS--SDMNGLVQKALDASNVY 620
Cdd:COG3206 260 ---LQSPVIQQLRAQLAELEAELAELSARytpNHPDVIALRAQIAALRAQlQQEAQRILASleAELEALQAREASLQAQL 336
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 621 ENIVNYVSEANETaEFALNTTDRIYDAvsgidTQIIYhkdesENLLNQARELQAKAESSS 680
Cdd:COG3206 337 AQLEARLAELPEL-EAELRRLEREVEV-----ARELY-----ESLLQRLEEARLAEALTV 385
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
317-451 |
3.38e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.43 E-value: 3.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 317 KLSERENQYALRKiQINNAENTMKSLLSDVEELVEKENQASRK-GQLVQK-----ESMDTI-NHASQLVEQAHDMRDKIQ 389
Cdd:COG1340 141 KIKELEKELEKAK-KALEKNEKLKELRAELKELRKEAEEIHKKiKELAEEaqelhEEMIELyKEADELRKEADELHKEIV 219
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034650228 390 EINNKMlyyGEEHEL------SPKEISEKLVLAQKMLEEIRSRQpfftQRELVDEEADEAYELLSQAE 451
Cdd:COG1340 220 EAQEKA---DELHEEiielqkELRELRKELKKLRKKQRALKREK----EKEELEEKAEEIFEKLKKGE 280
|
|
| DivIVA |
pfam05103 |
DivIVA protein; The Bacillus subtilis divIVA1 mutation causes misplacement of the septum ... |
376-460 |
5.20e-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: 39.09 E-value: 5.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 376 QLVEQAHDMRDKIQEINNKMLYYGEEHElspkEISEKLVLAQKMLEEIRSRQPffTQRELVDEEA-DEAYELLSQAES-W 453
Cdd:pfam05103 36 ALIRENAELKEKIEELEEKLAHYKNLEE----TLQNTLILAQETAEEVKANAQ--KEAELIIKEAeAKAERIVDDANNeV 109
|
....*..
gi 1034650228 454 QRLHNET 460
Cdd:pfam05103 110 KKINDEI 116
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
339-600 |
5.95e-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: 5.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 339 MKSLlSDVEELVekenqasRKGQLVQKESMDTINHASQLVEQAHDMRDKIQEINNKMlyygeehelspkeiseklvlaqK 418
Cdd:COG4913 203 FKPI-GDLDDFV-------REYMLEEPDTFEAADALVEHFDDLERAHEALEDAREQI----------------------E 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 419 MLEEIRSRQpffTQRELVDEEADEAYELLSQAESWQR------LHNETRTLfpvvLEQLDDYNAKLSDLQEALDQALNYV 492
Cdd:COG4913 253 LLEPIRELA---ERYAAARERLAELEYLRAALRLWFAqrrlelLEAELEEL----RAELARLEAELERLEARLDALREEL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 493 RDAE----------------DMNRATAARQRdHEKQQERVREQMEVVNMSLSTSADslttprltlsELDDIIKNASGIYA 556
Cdd:COG4913 326 DELEaqirgnggdrleqlerEIERLERELEE-RERRRARLEALLAALGLPLPASAE----------EFAALRAEAAALLE 394
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1034650228 557 EIDGAKSELQVKLSNLSNLSHDLVQEaidhAQDLQQEANELSRK 600
Cdd:COG4913 395 ALEEELEALEEALAEAEAALRDLRRE----LRELEAEIASLERR 434
|
|
| TNFRSF6_teleost |
cd13423 |
Tumor necrosis factor receptor superfamily member 6 (TNFRSF6) in teleosts; also known as fas ... |
157-249 |
6.27e-03 |
|
Tumor necrosis factor receptor superfamily member 6 (TNFRSF6) in teleosts; also known as fas cell surface death receptor (FasR); This subfamily of TNFRSF6 (also known as fas cell surface death receptor (FasR) or Fas; APT1; CD95; FAS1; APO-1; FASTM; ALPS1A) is found in teleosts. It contains a death domain and plays a central role in the physiological regulation of programmed cell death. In humans, it has been implicated in the pathogenesis of various malignancies and diseases of the immune system. The receptor interactions with the Fas ligand (FasL), allowing the formation of a death-inducing signaling complex that includes Fas-associated death domain protein (FADD), caspase 8, and caspase 10; autoproteolytic processing of the caspases in the complex triggers a downstream caspase cascade, leading to apoptosis. This receptor has also been shown to activate NF-kappaB, MAPK3/ERK1, and MAPK8/JNK, and is involved in transducing the proliferating signals in normal diploid fibroblast and T cells. In channel catfish and the Japanese rice fish, medaka, homologs of Fas receptor (FasR), as well as FADD and caspase 8, have been identified and characterized, and likely constitute the teleost equivalent of the death-inducing signaling complex (DISC). FasL/FasR are involved in the initiation of apoptosis and suggest that mechanisms of cell-mediated cytotoxicity in teleosts are similar to those used by mammals; presumably, the mechanism of apoptosis induction via death receptors was evolutionarily established during the appearance of vertebrates.
Pssm-ID: 276928 [Multi-domain] Cd Length: 103 Bit Score: 38.18 E-value: 6.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 157 CNENYAGPNCERCAPGYYGNPLLIGSTCKKCD-CSGNSdpNLIFED-CdeVTGQCRNClrnttgfkceRCAPGYYGDARi 234
Cdd:cd13423 27 CTNNGTDGECEACEDGTYNSHPNSLDSCEPCTsCDPNA--NLEVEErC--TPSSDTVC----------RCKEGHYCDKG- 91
|
90
....*....|....*
gi 1034650228 235 aKNCAVCNcgggPCD 249
Cdd:cd13423 92 -EECKVCY----PCD 101
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
407-686 |
6.48e-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: 6.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 407 KEISEKLVLAQKMLEEIRsrqpffTQRELVDEEADEAYELLSQAES---WQRLHNETRTLfPVVLEQLDDYNAKLSDLQE 483
Cdd:COG4913 620 AELEEELAEAEERLEALE------AELDALQERREALQRLAEYSWDeidVASAEREIAEL-EAELERLDASSDDLAALEE 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 484 ALDQALNYVRDAEDMNRATAARQRDHEKQQERVREQMEVVNMSLST-SADSLTTPRLTLSE-LDDIIKNASG------IY 555
Cdd:COG4913 693 QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAaEDLARLELRALLEErFAAALGDAVErelrenLE 772
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 556 AEIDGAKSELQVKLSNLSNLSHDLVQEAIDHAQDLQ------QEANELSRKLHSSDMNGLVQKALDA--SNVYENIVNYV 627
Cdd:COG4913 773 ERIDALRARLNRAEEELERAMRAFNREWPAETADLDadleslPEYLALLDRLEEDGLPEYEERFKELlnENSIEFVADLL 852
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034650228 628 SEANETAEFALNTTDRIYDAVSGIDtqiiYHKDesenllnqaRELQAKAESSSDEAVAD 686
Cdd:COG4913 853 SKLRRAIREIKERIDPLNDSLKRIP----FGPG---------RYLRLEARPRPDPEVRE 898
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
469-600 |
8.35e-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: 39.91 E-value: 8.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650228 469 EQLDDYNAKLSDLQEALDQALNYVRDAEDMNRATAARQRDHEKQQERVREQMEVVNMSlstsaDSLTTPRLTLSELDDII 548
Cdd:COG1579 38 DELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEALQ-----KEIESLKRRISDLEDEI 112
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1034650228 549 KNasgIYAEIDGAKSELQVKLSNLSNLSHDL--VQEAIDHA-QDLQQEANELSRK 600
Cdd:COG1579 113 LE---LMERIEELEEELAELEAELAELEAELeeKKAELDEElAELEAELEELEAE 164
|
|
| |
