|
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 ... |
298-554 |
1.35e-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: 326.68 E-value: 1.35e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 298 VLSVSSGAAAHRHVNEINATIYLLKTKLSERENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLVQKESMDT 377
Cdd:pfam06008 1 LLSLNSLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 378 INHASQLVEQAHDMRDKIQEINNKMLYYGEE-HELSPKEISEKLVLAQKMLEEIRSRQpFFTQRELVDEEADEAYELLSQ 456
Cdd:pfam06008 81 LGHAKELAEAIKNLIDNIKEINEKVATLGENdFALPSSDLSRMLAEAQRMLGEIRSRD-FGTQLQNAEAELKAAQDLLSR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 457 AESW-QRLHNETRTLFPVVLEQLDDYNAKLSDLQEALDQALNYVRDAEDMNRATAARQRDHEKQQERVREQMEVVNMSLS 535
Cdd:pfam06008 160 IQTWfQSPQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEETLK 239
|
250
....*....|....*....
gi 2217361438 536 TSADSLTTPRLTLSELDDI 554
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 ... |
734-861 |
2.27e-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: 154.95 E-value: 2.27e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 734 SRLITEEANRTTMEVQQATAPMANNLTNWSQNLQHFDSSA---------YNTAVNSARDAVRNLTEVVPQLLDQLRTVEQ 804
Cdd:pfam06009 1 SKELAREANETAKEVLEQLAPLSQNLENTSEKLSGINRSLeetnelvndANKALDDAGRSVKKLEELAPDLLDKLKPLKQ 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2217361438 805 KRPAS-NVSASIQRIRELIAQTRSVASKIQVSMMFDGQSAVEVHSRTSMDDLKAFTSL 861
Cdd:pfam06009 81 LEVNSsSLSDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTSL 138
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
1492-1624 |
2.00e-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: 2.00e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 1492 KSQFSIRLRTRSSHGMIFYVSDQEENDFMTLFLAHGRLVYMFNVGHKKLKIRSQEKYNDGLWHDVIFIRERSSGRLVIDG 1571
Cdd:cd00110 21 RLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDGQWHSVSVERNGRSVTLSVDG 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2217361438 1572 LRVLEESLPPTEATWKIKGPIYLGGVAPGKavKNVQINSIYSFSGCLSNLQLN 1624
Cdd:cd00110 101 ERVVESGSPGGSALLNLDGPLYLGGLPEDL--KSPGLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
1494-1625 |
1.00e-35 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 132.85 E-value: 1.00e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 1494 QFSIRLRTRSSHGMIFYVSDQEENDFMTLFLAHGRLVYMFNVGHKKLKIRSQ-EKYNDGLWHDVIFIRERSSGRLVIDGL 1572
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDpTPLNDGQWHRVAVERNGRSVTLSVDGG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2217361438 1573 RVLEESLPPTEATWKIKGPIYLGGVAPGKavKNVQINSIYSFSGCLSNLQLNG 1625
Cdd:smart00282 81 NRVSGESPGGLTILNLDGPLYLGGLPEDL--KLPPLPVTPGFRGCIRNLKVNG 131
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
1648-1799 |
2.83e-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: 2.83e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 1648 GTYFStEGGYVVLDESFNIGLKFEIAFEVRPRSSSGTLVH-GHSVNGEYLNVHMKNGQVIVKVNNGirDFSTSVTPKQSL 1726
Cdd:cd00110 1 GVSFS-GSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYaGSQNGGDFLALELEDGRLVLRYDLG--SGSLVLSSKTPL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217361438 1727 CDGRWHRITVIRDSNVVQLDVDSE-VNHVVGPLNPKPIDHREPVFVGGVPESLLTPRLAPSKPFTGCIRHFVID 1799
Cdd:cd00110 78 NDGQWHSVSVERNGRSVTLSVDGErVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
1671-1801 |
3.71e-31 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 119.75 E-value: 3.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 1671 EIAFEVRPRSSSGTLVHGHSVNG-EYLNVHMKNGQVIVKVNNGIRDFSTSVTPKQsLCDGRWHRITVIRDSNVVQLDVDS 1749
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGgDYLALELRDGRLVLRYDLGSGPARLTSDPTP-LNDGQWHRVAVERNGRSVTLSVDG 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2217361438 1750 EvNHVVG--PLNPKPIDHREPVFVGGVPESLLTPRLAPSKPFTGCIRHFVIDGH 1801
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 ... |
1499-1625 |
2.37e-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: 2.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 1499 LRTRSSHGMIFYVSDQEeNDFMTLFLAHGRLVYMFNVGHKKLKIRSQEK-YNDGLWHDVIFIRERSSGRLVIDGLRVLEE 1577
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGG-SDFLALELVNGRLVLRYDLGSGPESLLSSGKnLNDGQWHSVRVERNGNTLTLSVDGQTVVSS 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2217361438 1578 SLPPTEATWKIKGPIYLGGVAPGKAVKNVQINSiySFSGCLSNLQLNG 1625
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 ... |
1676-1801 |
1.66e-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: 1.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 1676 VRPRSSSGTLVHGHSVNGEYLNVHMKNGQVIVKVNNGIRDFSTSVTPKqSLCDGRWHRITVIRDSNVVQLDVDSEVNH-V 1754
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDFLALELVNGRLVLRYDLGSGPESLLSSGK-NLNDGQWHSVRVERNGNTLTLSVDGQTVVsS 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2217361438 1755 VGPLNPKPIDHREPVFVGGVPESLLTPRLAPSKPFTGCIRHFVIDGH 1801
Cdd:pfam02210 80 LPPGESLLLNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
1049-1207 |
8.38e-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: 8.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 1049 SYFFDGSGYAvvrDITRRGKFGQVTRFDIEVRTPADNGLILLM--VNGSMFFRLEMRNGYLHVFYDFGfsGGPVHLEDtl 1126
Cdd:cd00110 1 GVSFSGSSYV---RLPTLPAPRTRLSISFSFRTTSPNGLLLYAgsQNGGDFLALELEDGRLVLRYDLG--SGSLVLSS-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 1127 kKAQINDAKYHEISIIyHNDKKMILVVDR-RHVKSMDNEKMKI--PFTDIYIGGAPPEILQSRALRAHlpldiNFRGCMK 1203
Cdd:cd00110 74 -KTPLNDGQWHSVSVE-RNGRSVTLSVDGeRVVESGSPGGSALlnLDGPLYLGGLPEDLKSPGLPVSP-----GFVGCIR 146
|
....
gi 2217361438 1204 GFQF 1207
Cdd:cd00110 147 DLKV 150
|
|
| LamG |
smart00282 |
Laminin G domain; |
1074-1210 |
2.35e-22 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 94.33 E-value: 2.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 1074 RFDIEVRTPADNGLILLM--VNGSMFFRLEMRNGYLHVFYDFGfsGGPVHLedTLKKAQINDAKYHEISIIyHNDKKMIL 1151
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAgsKGGGDYLALELRDGRLVLRYDLG--SGPARL--TSDPTPLNDGQWHRVAVE-RNGRSVTL 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217361438 1152 VVD---RRHVKSMDNEKMKIPFTDIYIGGAPPEILQSralraHLPLDINFRGCMKGFQFQKK 1210
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 ... |
1079-1207 |
1.55e-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: 1.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 1079 VRTPADNGLIL-LMVNGSMFFRLEMRNGYLHVFYDFGfsGGPVHLedTLKKAQINDAKYHEISIIYhNDKKMILVVDRRH 1157
Cdd:pfam02210 1 FRTRQPNGLLLyAGGGGSDFLALELVNGRLVLRYDLG--SGPESL--LSSGKNLNDGQWHSVRVER-NGNTLTLSVDGQT 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2217361438 1158 VKSMDNEKMKIPF---TDIYIGGAPPeilqsRALRAHLPLDINFRGCMKGFQF 1207
Cdd:pfam02210 76 VVSSLPPGESLLLnlnGPLYLGGLPP-----LLLLPALPVRAGFVGCIRDVRV 123
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
1237-1376 |
4.13e-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: 4.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 1237 AYFNGQSFIASIQKISFFDGFEGGFNFRTLQPNGLLFYYASG--SDVFSISLDNGTVIMDV----KGIKVQSvDKQYNDG 1310
Cdd:cd00110 2 VSFSGSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQngGDFLALELEDGRLVLRYdlgsGSLVLSS-KTPLNDG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217361438 1311 LSHFVISSVSPTRYELIVDKSRVGSKNPTKGKIEQTqaSEKKFYFGGSPISAQ------YANFTGCISNAYF 1376
Cdd:cd00110 81 QWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLN--LDGPLYLGGLPEDLKspglpvSPGFVGCIRDLKV 150
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
835-1012 |
1.78e-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: 1.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 835 SMMFDGQSAVEVhsrTSMDDLKAFTSLSLYMKppvkrpelTETADQFILYLGSKNaKKEYMGLAIKNDNLVYVYNLGTKD 914
Cdd:cd00110 1 GVSFSGSSYVRL---PTLPAPRTRLSISFSFR--------TTSPNGLLLYAGSQN-GGDFLALELEDGRLVLRYDLGSGS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 915 VEIpldSKPVSSWPAYFSIVKIERVGKHgkVFLTVPSLSStaeekfikkGEFSGDDSLLDLDPEDTVfYVGGVPSNFKLP 994
Cdd:cd00110 69 LVL---SSKTPLNDGQWHSVSVERNGRS--VTLSVDGERV---------VESGSPGGSALLNLDGPL-YLGGLPEDLKSP 133
|
170
....*....|....*...
gi 2217361438 995 TSLNLPGFVGCLELATLN 1012
Cdd:cd00110 134 GLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
860-1013 |
3.32e-18 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 82.77 E-value: 3.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 860 SLSLYMKppvkrpelTETADQFILYLGSKNaKKEYMGLAIKNDNLVYVYNLGTKDVEIPLDSKPVSswPAYFSIVKIERV 939
Cdd:smart00282 1 SISFSFR--------TTSPNGLLLYAGSKG-GGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLN--DGQWHRVAVERN 69
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217361438 940 GKHgkVFLTVPSLSSTAEEKFIKKgefsgddSLLDLDpedTVFYVGGVPSNFKLPTSLNLPGFVGCLELATLNN 1013
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 ... |
1263-1376 |
1.45e-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: 1.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 1263 FRTLQPNGLLFYYASG-SDVFSISLDNGTVIMDVK----GIKVQSVDKQYNDGLSHFVISSVSPTRYELIVDKSRVGSKN 1337
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGgSDFLALELVNGRLVLRYDlgsgPESLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2217361438 1338 PTKGkiEQTQASEKKFYFGG------SPISAQYANFTGCISNAYF 1376
Cdd:pfam02210 81 PPGE--SLLLNLNGPLYLGGlpplllLPALPVRAGFVGCIRDVRV 123
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
187-238 |
8.76e-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: 72.77 E-value: 8.76e-16
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2217361438 187 CDCSGNSDPNlifEDCDEVTGQCRnCLRNTTGFKCERCAPGYYGDARIAKNC 238
Cdd:cd00055 2 CDCNGHGSLS---GQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGGC 49
|
|
| LamG |
smart00282 |
Laminin G domain; |
1261-1379 |
1.13e-14 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 72.37 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 1261 FNFRTLQPNGLLFYYAS--GSDVFSISLDNGTVIMDVKG----IKVQSVDKQYNDGLSHFVISSVSPTRYELIVDksrvg 1334
Cdd:smart00282 4 FSFRTTSPNGLLLYAGSkgGGDYLALELRDGRLVLRYDLgsgpARLTSDPTPLNDGQWHRVAVERNGRSVTLSVD----- 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2217361438 1335 SKNPTKGKIEQTQA---SEKKFYFGGSP------ISAQYANFTGCISNAYFTRV 1379
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 |
5.57e-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: 5.57e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2217361438 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 |
1.14e-12 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 63.91 E-value: 1.14e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2217361438 131 PCPCPlPHlANFAESCYRKNGavRCICNENYAGPNCERCAPGYYGNPlLIGSTCK 185
Cdd:cd00055 1 PCDCN-GH-GSLSGQCDPGTG--QCECKPNTTGRRCDRCAPGYYGLP-SQGGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
187-231 |
4.76e-12 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 61.94 E-value: 4.76e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2217361438 187 CDCS--GNSDPnlifeDCDEVTGQCRnCLRNTTGFKCERCAPGYYGD 231
Cdd:smart00180 1 CDCDpgGSASG-----TCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD 41
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
347-821 |
9.47e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 70.45 E-value: 9.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 347 KSLLSDVEELVEKENQASRKGQL-----VQKESMDTINHASQLVEQAHDMRDKIQEINnkmlyygEEHELSPKEI----S 417
Cdd:PRK02224 186 RGSLDQLKAQIEEKEEKDLHERLnglesELAELDEEIERYEEQREQARETRDEADEVL-------EEHEERREELetleA 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 418 EKLVLAQKMLEEIRSRQPF----FTQRELVDEEADEAYELLSQAEsWQRLHNETrtlfpvVLEQLDDYNAKLSDLQEALD 493
Cdd:PRK02224 259 EIEDLRETIAETEREREELaeevRDLRERLEELEEERDDLLAEAG-LDDADAEA------VEARREELEDRDEELRDRLE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 494 QALNYVRDAEdmNRATAARQR--DHEKQQERVREQMEVVNMSLSTSADSLTTPRLTLSELDDIIKNASGIYA----EIDG 567
Cdd:PRK02224 332 ECRVAAQAHN--EEAESLREDadDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGdapvDLGN 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 568 AKSELQVKLSNLSNLSHDL---------VQEAIDHAQDLQQEAN-------------------------ELSRKLhsSDM 613
Cdd:PRK02224 410 AEDFLEELREERDELREREaeleatlrtARERVEEAEALLEAGKcpecgqpvegsphvetieedrerveELEAEL--EDL 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 614 NGLVQKALDASNVYENIVNYVSEANETAEFALNTTDRIYDAVSGIDTQiiyhKDESENLLNQARELQAKAESSSDEAV-- 691
Cdd:PRK02224 488 EEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEK----RERAEELRERAAELEAEAEEKREAAAea 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 692 ---ADTSRRVGGAL-ARKSALKTRLsDAVKQL--QAAERGDAQQRLGqsRLITEEANRTTMEVQQatapmANNLTNWSQN 765
Cdd:PRK02224 564 eeeAEEAREEVAELnSKLAELKERI-ESLERIrtLLAAIADAEDEIE--RLREKREALAELNDER-----RERLAEKRER 635
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217361438 766 LQHFDSSAYNTAVNSARDAVRNLTEVVPQLLDQLRTVEQKRPA-----SNVSASIQRIREL 821
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 |
1.72e-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: 60.44 E-value: 1.72e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2217361438 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 ... |
321-647 |
2.19e-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: 2.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 321 LKTKLSERENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLVQKESMDTINHASQLVEQAHDMRDKIQEINN 400
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLER 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 401 KMLYYGEEHELSPKEISEKLVLAQKMLEEIRSRQPFFT-QRELVDEEADEAYELLSQAESWQRLHNETRTLFPVVLEQLD 479
Cdd:TIGR02168 317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELEsLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 480 DYNAKLSDLQEALDQalnyvrdAEDMNRATAARQRDHEKQQERVreQMEVVNMSLSTSADSLTTprlTLSELDDIIKNAS 559
Cdd:TIGR02168 397 SLNNEIERLEARLER-------LEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEE---LQEELERLEEALE 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 560 GIYAEIDGAKSELQVKLSNLSNLSH--DLVQEAIDHAQDLQQEANELsrKLHSSDMNGLVQKALDASNV---YE------ 628
Cdd:TIGR02168 465 ELREELEEAEQALDAAERELAQLQArlDSLERLQENLEGFSEGVKAL--LKNQSGLSGILGVLSELISVdegYEaaieaa 542
|
330 340
....*....|....*....|..
gi 2217361438 629 ---NIVNYVSEANETAEFALNT 647
Cdd:TIGR02168 543 lggRLQAVVVENLNAAKKAIAF 564
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
81-130 |
3.23e-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: 3.23e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2217361438 81 PCDCNGN---SNECLDGSGYCvHCQRNTTGEHCEKCLDGYIGDSIRGAPqfCQ 130
Cdd:cd00055 1 PCDCNGHgslSGQCDPGTGQC-ECKPNTTGRRCDRCAPGYYGLPSQGGG--CQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
132-177 |
4.17e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 59.25 E-value: 4.17e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2217361438 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 ... |
875-1013 |
8.80e-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: 8.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 875 TETADQFILYLGSKnaKKEYMGLAIKNDNLVYVYNLGTKDVEIPLDSKPVS--SWpayfSIVKIERVGKHgkVFLTVPSL 952
Cdd:pfam02210 3 TRQPNGLLLYAGGG--GSDFLALELVNGRLVLRYDLGSGPESLLSSGKNLNdgQW----HSVRVERNGNT--LTLSVDGQ 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217361438 953 SSTAEEKfikkgefSGDDSLLDLDpedTVFYVGGVPSNFKLPTSLNLPGFVGCLELATLNN 1013
Cdd:pfam02210 75 TVVSSLP-------PGESLLLNLN---GPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVNG 125
|
|
| TNFRSF16 |
cd13416 |
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 ... |
65-257 |
2.80e-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: 60.78 E-value: 2.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 65 EKCNAGFFhTLSGECvpCDcngnsnECLDGSGYCVHCQRNTTGehCEKCLDGYIGDSIRGAPQFCQPC-PCplPHLANFA 143
Cdd:cd13416 1 EACPSGQY-TSSGEC--CE------QCPPGEGVARPCGDNQTV--CEPCLDGVTFSDVVSHTEPCQPCtRC--PGLMSMR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 144 ESCYRKNGAVrcicnenyagpnCErCAPGYYGNPLliGSTCKKCDCsgnsdpnlifedCDEVTGQCRNC--LRNTtgfKC 221
Cdd:cd13416 68 APCTATHDTV------------CE-CAYGYYLDED--SGTCEPCTV------------CPPGQGVVQSCgpNQDT---VC 117
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2217361438 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 |
6.47e-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: 6.47e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2217361438 82 CDCNGN---SNECLDGSGYCvHCQRNTTGEHCEKCLDGYIGDSIrGAPQFC 129
Cdd:pfam00053 1 CDCNPHgslSDTCDPETGQC-LCKPGVTGRHCDRCKPGYYGLPS-DPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
82-121 |
4.70e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 53.47 E-value: 4.70e-09
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2217361438 82 CDCNGN---SNECLDGSGYCvHCQRNTTGEHCEKCLDGYIGDS 121
Cdd:smart00180 1 CDCDPGgsaSGTCDPDTGQC-ECKPNVTGRRCDRCAPGYYGDG 42
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
319-731 |
2.43e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.01 E-value: 2.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 319 YLLKTKLseRENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLVQKESmdtinhasQLVEQAHDMRDKIQEI 398
Cdd:COG4717 45 AMLLERL--EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELE--------ELEEELEELEAELEEL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 399 NNKMLYYgeEHELSPKEISEKLVLAQKMLEEIRSRQPFFTQRELVDEEADEAYE-LLSQAESWQR-LHNETRTLFPVVLE 476
Cdd:COG4717 115 REELEKL--EKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEeLEAELAELQEeLEELLEQLSLATEE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 477 QLDDYNAKLSDLQEALDQALNYVRDAEDmNRATAARQRD-------HEKQQERVREQMEVVN-----MSLSTSADSLTTP 544
Cdd:COG4717 193 ELQDLAEELEELQQRLAELEEELEEAQE-ELEELEEELEqleneleAAALEERLKEARLLLLiaaalLALLGLGGSLLSL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 545 RLTL----------------------SELDDIIKNASGIYAEIDGAKSELQVKLSNL---SNLSHDLVQEAIDHAQDLQQ 599
Cdd:COG4717 272 ILTIagvlflvlgllallflllarekASLGKEAEELQALPALEELEEEELEELLAALglpPDLSPEELLELLDRIEELQE 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 600 ---EANELSRKLHSSDMNGLVQKALDASNV-----YENIVNYVSEANETAEfalnttdriydAVSGIDTQIIYHKDESEN 671
Cdd:COG4717 352 llrEAEELEEELQLEELEQEIAALLAEAGVedeeeLRAALEQAEEYQELKE-----------ELEELEEQLEELLGELEE 420
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217361438 672 LLNQARELQAKAE-SSSDEAVADTSRRVGGALARKSALKTRLSDAVKQLQAAERGDAQQRL 731
Cdd:COG4717 421 LLEALDEEELEEElEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEEL 481
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
529-757 |
2.62e-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: 2.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 529 VVNMSLSTSADslTTPRLTLSELDDIIKNASGIYAEIDGAKSELQVKLSNLSNLSHDL--VQEAIDhaqDLQQEANELSR 606
Cdd:COG3883 5 ALAAPTPAFAD--PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELeaLQAEID---KLQAEIAEAEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 607 KLhsSDMNGLVQKALDASNVYENIVNYVS---EANETAEFA--LNTTDRIYDAVSGIDTQIIYHKDESENLLNQARELQA 681
Cdd:COG3883 80 EI--EERREELGERARALYRSGGSVSYLDvllGSESFSDFLdrLSALSKIADADADLLEELKADKAELEAKKAELEAKLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 682 KAESSSDEAvADTSRRVGGALARKSALKTRLSDAVKQLQA------AERGDAQQRLGQSRLITEEANRTTMEVQQATAPM 755
Cdd:COG3883 158 ELEALKAEL-EAAKAELEAQQAEQEALLAQLSAEEAAAEAqlaeleAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
..
gi 2217361438 756 AN 757
Cdd:COG3883 237 AA 238
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
354-855 |
7.63e-07 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 54.45 E-value: 7.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 354 EELVEKENQASRKgqlvQKESMDTINHASQLVEQahdmrdkiqeinnkmlyygeEHELSPKEISEKLVLAQKMLEEIRSR 433
Cdd:NF041483 699 EALAAAQEEAARR----RREAEETLGSARAEADQ--------------------ERERAREQSEELLASARKRVEEAQAE 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 434 qpffTQReLVdEEADE-AYELLSQAESwqrlhnetrtlfpvVLEQLDDynaKLSDLQEALDQALNYVRDAEDMnraTAAR 512
Cdd:NF041483 755 ----AQR-LV-EEADRrATELVSAAEQ--------------TAQQVRD---SVAGLQEQAEEEIAGLRSAAEH---AAER 808
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 513 QRDhEKQQE--RVReqmevvnmslstsADSLTTpRLTLSEldDIIKNASGIYAEIDGAKSelqvklsnlsnLSHDLVQEA 590
Cdd:NF041483 809 TRT-EAQEEadRVR-------------SDAYAE-RERASE--DANRLRREAQEETEAAKA-----------LAERTVSEA 860
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 591 IDHAQDLQQEANELSRKLHSSDMNGLVQKALDASNVYenivnyvSEANETAefalnttDRI-YDAVSGIDTQIIYHKDES 669
Cdd:NF041483 861 IAEAERLRSDASEYAQRVRTEASDTLASAEQDAARTR-------ADAREDA-------NRIrSDAAAQADRLIGEATSEA 926
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 670 ENLLNQARelqAKAESSSDEAVADTSRRVGGALARKSALKTRLSDAVKQL--QAAER-GDAQQRLGQSRlitEEANRTTM 746
Cdd:NF041483 927 ERLTAEAR---AEAERLRDEARAEAERVRADAAAQAEQLIAEATGEAERLraEAAETvGSAQQHAERIR---TEAERVKA 1000
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 747 EvqqaTAPMANNLTNWSQN-----LQHFDSSAYNTAVNSARDAVRNLTEVVPQlLDQLRTVEQKRPASNVSASIQRIREL 821
Cdd:NF041483 1001 E----AAAEAERLRTEAREeadrtLDEARKDANKRRSEAAEQADTLITEAAAE-ADQLTAKAQEEALRTTTEAEAQADTM 1075
|
490 500 510
....*....|....*....|....*....|....
gi 2217361438 822 IAQTRSVASKIQVSMMFDGQSAVEvHSRTSMDDL 855
Cdd:NF041483 1076 VGAARKEAERIVAEATVEGNSLVE-KARTDADEL 1108
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
440-821 |
4.05e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 52.27 E-value: 4.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 440 RELVDEEAD---EAYELLSQAESWQRLHNETRtlfpvvlEQLDDYNAKLSDLQEALDQA---LNYVRDAEDMNRATAARQ 513
Cdd:PRK04863 282 RVHLEEALElrrELYTSRRQLAAEQYRLVEMA-------RELAELNEAESDLEQDYQAAsdhLNLVQTALRQQEKIERYQ 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 514 RDHEKQQERVREQMEVVNMSLSTSADSLTTPRLTLSELD-------------DIIKNASGIYAE----IDGAKSELQVKL 576
Cdd:PRK04863 355 ADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDelksqladyqqalDVQQTRAIQYQQavqaLERAKQLCGLPD 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 577 SNLSNLShDLVQEAIDHAQDLQQEANELSRKLHSSDMnglvqkaldasnvyenivnyvseANETAEFALNTTDRIYDAVS 656
Cdd:PRK04863 435 LTADNAE-DWLEEFQAKEQEATEELLSLEQKLSVAQA-----------------------AHSQFEQAYQLVRKIAGEVS 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 657 GIDTQiiyhkDESENLLNQARELQAKAEsssdeavadtsrRVGGALARKSALKTRLsdavKQLQAAER--GDAQQRLGQS 734
Cdd:PRK04863 491 RSEAW-----DVARELLRRLREQRHLAE------------QLQQLRMRLSELEQRL----RQQQRAERllAEFCKRLGKN 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 735 --------RLITE-EANRTTMEVQQATA-----PMANNLTNWSQNLQHFDSSA-----YNTAVNSARDAV-------RNL 788
Cdd:PRK04863 550 lddedeleQLQEElEARLESLSESVSEArerrmALRQQLEQLQARIQRLAARApawlaAQDALARLREQSgeefedsQDV 629
|
410 420 430
....*....|....*....|....*....|....*
gi 2217361438 789 TEVVPQLLDQLR--TVEQKRPASNVSASIQRIREL 821
Cdd:PRK04863 630 TEYMQQLLERERelTVERDELAARKQALDEEIERL 664
|
|
| ApoLp-III_like |
cd13769 |
Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles ... |
710-836 |
4.17e-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: 4.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 710 TRLSDAVKQLQAAERGDAQQRLGQSRL-ITEEANRTtmeVQQATAPMANNLTNWSQNLQHFDSSAYNTAVNSARDAVRNL 788
Cdd:cd13769 1 TQLSELIQKAQEAINNLAQQVQKQLGLqNPEEVVNT---LKEQSDNFANNLQEVSSSLKEEAKKKQGEVEEAWNEFKTKL 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2217361438 789 TEVVPQLLDQLRTVEQkrpASNVSASIQ-RIRELIAQTRSVASKIQVSM 836
Cdd:cd13769 78 SETVPELRKSLPVEEK---AQELQAKLQsGLQTLVTESQKLAKAISENS 123
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
521-764 |
2.41e-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: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 521 ERVREQMEVVNMSLSTSADSLTTPRLTLSELDDIIKnaSGIYAEIDGAKSELQVKLSNLSNLSHDLVQEAIDHAQD---L 597
Cdd:TIGR01612 500 MRMKDFKDIIDFMELYKPDEVPSKNIIGFDIDQNIK--AKLYKEIEAGLKESYELAKNWKKLIHEIKKELEEENEDsihL 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 598 QQEAN---------------------ELSRKLHS-SDMNGLVQKALDASNVYENIVNYVSEANETAEFA----LNTTDRI 651
Cdd:TIGR01612 578 EKEIKdlfdkyleiddeiiyinklklELKEKIKNiSDKNEYIKKAIDLKKIIENNNAYIDELAKISPYQvpehLKNKDKI 657
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 652 YDAVSGIDTQI--------------IYHKDESENLLNQAR--ELQAKAESSSDEAVADTSRRVGGALARKSALKTRLSDA 715
Cdd:TIGR01612 658 YSTIKSELSKIyeddidalynelssIVKENAIDNTEDKAKldDLKSKIDKEYDKIQNMETATVELHLSNIENKKNELLDI 737
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2217361438 716 VKQLQAAERGDaqqrlgqsrlITEEANRTTMEVQQATAPMANNLTNWSQ 764
Cdd:TIGR01612 738 IVEIKKHIHGE----------INKDLNKILEDFKNKEKELSNKINDYAK 776
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
666-824 |
1.39e-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: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 666 KDESENLLNQARELQAK-AESSSDEAVADTSRR--------VGGAlaRKSALKTRLSDAVKQLQAAE--RGDAQQRLGQS 734
Cdd:COG4913 294 EAELEELRAELARLEAElERLEARLDALREELDeleaqirgNGGD--RLEQLEREIERLERELEERErrRARLEALLAAL 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 735 RLiTEEANRTTMEVQQATAPMAnnLTNWSQnlqhfDSSAYNTAVNSARDAVRNLTEVVPQLLDQLRTVEQKRpaSNVSAS 814
Cdd:COG4913 372 GL-PLPASAEEFAALRAEAAAL--LEALEE-----ELEALEEALAEAEAALRDLRRELRELEAEIASLERRK--SNIPAR 441
|
170
....*....|
gi 2217361438 815 IQRIRELIAQ 824
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 ... |
298-554 |
1.35e-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: 326.68 E-value: 1.35e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 298 VLSVSSGAAAHRHVNEINATIYLLKTKLSERENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLVQKESMDT 377
Cdd:pfam06008 1 LLSLNSLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 378 INHASQLVEQAHDMRDKIQEINNKMLYYGEE-HELSPKEISEKLVLAQKMLEEIRSRQpFFTQRELVDEEADEAYELLSQ 456
Cdd:pfam06008 81 LGHAKELAEAIKNLIDNIKEINEKVATLGENdFALPSSDLSRMLAEAQRMLGEIRSRD-FGTQLQNAEAELKAAQDLLSR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 457 AESW-QRLHNETRTLFPVVLEQLDDYNAKLSDLQEALDQALNYVRDAEDMNRATAARQRDHEKQQERVREQMEVVNMSLS 535
Cdd:pfam06008 160 IQTWfQSPQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEETLK 239
|
250
....*....|....*....
gi 2217361438 536 TSADSLTTPRLTLSELDDI 554
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 ... |
734-861 |
2.27e-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: 154.95 E-value: 2.27e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 734 SRLITEEANRTTMEVQQATAPMANNLTNWSQNLQHFDSSA---------YNTAVNSARDAVRNLTEVVPQLLDQLRTVEQ 804
Cdd:pfam06009 1 SKELAREANETAKEVLEQLAPLSQNLENTSEKLSGINRSLeetnelvndANKALDDAGRSVKKLEELAPDLLDKLKPLKQ 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2217361438 805 KRPAS-NVSASIQRIRELIAQTRSVASKIQVSMMFDGQSAVEVHSRTSMDDLKAFTSL 861
Cdd:pfam06009 81 LEVNSsSLSDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTSL 138
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
1492-1624 |
2.00e-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: 2.00e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 1492 KSQFSIRLRTRSSHGMIFYVSDQEENDFMTLFLAHGRLVYMFNVGHKKLKIRSQEKYNDGLWHDVIFIRERSSGRLVIDG 1571
Cdd:cd00110 21 RLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDGQWHSVSVERNGRSVTLSVDG 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2217361438 1572 LRVLEESLPPTEATWKIKGPIYLGGVAPGKavKNVQINSIYSFSGCLSNLQLN 1624
Cdd:cd00110 101 ERVVESGSPGGSALLNLDGPLYLGGLPEDL--KSPGLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
1494-1625 |
1.00e-35 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 132.85 E-value: 1.00e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 1494 QFSIRLRTRSSHGMIFYVSDQEENDFMTLFLAHGRLVYMFNVGHKKLKIRSQ-EKYNDGLWHDVIFIRERSSGRLVIDGL 1572
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDpTPLNDGQWHRVAVERNGRSVTLSVDGG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2217361438 1573 RVLEESLPPTEATWKIKGPIYLGGVAPGKavKNVQINSIYSFSGCLSNLQLNG 1625
Cdd:smart00282 81 NRVSGESPGGLTILNLDGPLYLGGLPEDL--KLPPLPVTPGFRGCIRNLKVNG 131
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
1648-1799 |
2.83e-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: 2.83e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 1648 GTYFStEGGYVVLDESFNIGLKFEIAFEVRPRSSSGTLVH-GHSVNGEYLNVHMKNGQVIVKVNNGirDFSTSVTPKQSL 1726
Cdd:cd00110 1 GVSFS-GSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYaGSQNGGDFLALELEDGRLVLRYDLG--SGSLVLSSKTPL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217361438 1727 CDGRWHRITVIRDSNVVQLDVDSE-VNHVVGPLNPKPIDHREPVFVGGVPESLLTPRLAPSKPFTGCIRHFVID 1799
Cdd:cd00110 78 NDGQWHSVSVERNGRSVTLSVDGErVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
1671-1801 |
3.71e-31 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 119.75 E-value: 3.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 1671 EIAFEVRPRSSSGTLVHGHSVNG-EYLNVHMKNGQVIVKVNNGIRDFSTSVTPKQsLCDGRWHRITVIRDSNVVQLDVDS 1749
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGgDYLALELRDGRLVLRYDLGSGPARLTSDPTP-LNDGQWHRVAVERNGRSVTLSVDG 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2217361438 1750 EvNHVVG--PLNPKPIDHREPVFVGGVPESLLTPRLAPSKPFTGCIRHFVIDGH 1801
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 ... |
1499-1625 |
2.37e-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: 2.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 1499 LRTRSSHGMIFYVSDQEeNDFMTLFLAHGRLVYMFNVGHKKLKIRSQEK-YNDGLWHDVIFIRERSSGRLVIDGLRVLEE 1577
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGG-SDFLALELVNGRLVLRYDLGSGPESLLSSGKnLNDGQWHSVRVERNGNTLTLSVDGQTVVSS 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2217361438 1578 SLPPTEATWKIKGPIYLGGVAPGKAVKNVQINSiySFSGCLSNLQLNG 1625
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 ... |
1676-1801 |
1.66e-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: 1.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 1676 VRPRSSSGTLVHGHSVNGEYLNVHMKNGQVIVKVNNGIRDFSTSVTPKqSLCDGRWHRITVIRDSNVVQLDVDSEVNH-V 1754
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDFLALELVNGRLVLRYDLGSGPESLLSSGK-NLNDGQWHSVRVERNGNTLTLSVDGQTVVsS 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2217361438 1755 VGPLNPKPIDHREPVFVGGVPESLLTPRLAPSKPFTGCIRHFVIDGH 1801
Cdd:pfam02210 80 LPPGESLLLNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
1500-1628 |
7.33e-24 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 98.54 E-value: 7.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 1500 RTRSSHGMIFYVSDQEENDFMTLFLAHGRLVYMFNVGHKKLKIRSQEKYNDGLWHDVIFIRERSSGRLVIDGLRVLE-ES 1578
Cdd:pfam00054 2 RTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTgES 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2217361438 1579 LPPTEATWKIKGPIYLGGvAPGKAVKNVQINSIYSFSGCLSNLQLNGASI 1628
Cdd:pfam00054 82 PLGATTDLDVDGPLYVGG-LPSLGVKKRRLAISPSFDGCIRDVIVNGKPL 130
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
1049-1207 |
8.38e-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: 8.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 1049 SYFFDGSGYAvvrDITRRGKFGQVTRFDIEVRTPADNGLILLM--VNGSMFFRLEMRNGYLHVFYDFGfsGGPVHLEDtl 1126
Cdd:cd00110 1 GVSFSGSSYV---RLPTLPAPRTRLSISFSFRTTSPNGLLLYAgsQNGGDFLALELEDGRLVLRYDLG--SGSLVLSS-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 1127 kKAQINDAKYHEISIIyHNDKKMILVVDR-RHVKSMDNEKMKI--PFTDIYIGGAPPEILQSRALRAHlpldiNFRGCMK 1203
Cdd:cd00110 74 -KTPLNDGQWHSVSVE-RNGRSVTLSVDGeRVVESGSPGGSALlnLDGPLYLGGLPEDLKSPGLPVSP-----GFVGCIR 146
|
....
gi 2217361438 1204 GFQF 1207
Cdd:cd00110 147 DLKV 150
|
|
| LamG |
smart00282 |
Laminin G domain; |
1074-1210 |
2.35e-22 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 94.33 E-value: 2.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 1074 RFDIEVRTPADNGLILLM--VNGSMFFRLEMRNGYLHVFYDFGfsGGPVHLedTLKKAQINDAKYHEISIIyHNDKKMIL 1151
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAgsKGGGDYLALELRDGRLVLRYDLG--SGPARL--TSDPTPLNDGQWHRVAVE-RNGRSVTL 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217361438 1152 VVD---RRHVKSMDNEKMKIPFTDIYIGGAPPEILQSralraHLPLDINFRGCMKGFQFQKK 1210
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 ... |
1079-1207 |
1.55e-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: 1.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 1079 VRTPADNGLIL-LMVNGSMFFRLEMRNGYLHVFYDFGfsGGPVHLedTLKKAQINDAKYHEISIIYhNDKKMILVVDRRH 1157
Cdd:pfam02210 1 FRTRQPNGLLLyAGGGGSDFLALELVNGRLVLRYDLG--SGPESL--LSSGKNLNDGQWHSVRVER-NGNTLTLSVDGQT 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2217361438 1158 VKSMDNEKMKIPF---TDIYIGGAPPeilqsRALRAHLPLDINFRGCMKGFQF 1207
Cdd:pfam02210 76 VVSSLPPGESLLLnlnGPLYLGGLPP-----LLLLPALPVRAGFVGCIRDVRV 123
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
1237-1376 |
4.13e-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: 4.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 1237 AYFNGQSFIASIQKISFFDGFEGGFNFRTLQPNGLLFYYASG--SDVFSISLDNGTVIMDV----KGIKVQSvDKQYNDG 1310
Cdd:cd00110 2 VSFSGSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQngGDFLALELEDGRLVLRYdlgsGSLVLSS-KTPLNDG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217361438 1311 LSHFVISSVSPTRYELIVDKSRVGSKNPTKGKIEQTqaSEKKFYFGGSPISAQ------YANFTGCISNAYF 1376
Cdd:cd00110 81 QWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLN--LDGPLYLGGLPEDLKspglpvSPGFVGCIRDLKV 150
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
835-1012 |
1.78e-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: 1.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 835 SMMFDGQSAVEVhsrTSMDDLKAFTSLSLYMKppvkrpelTETADQFILYLGSKNaKKEYMGLAIKNDNLVYVYNLGTKD 914
Cdd:cd00110 1 GVSFSGSSYVRL---PTLPAPRTRLSISFSFR--------TTSPNGLLLYAGSQN-GGDFLALELEDGRLVLRYDLGSGS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 915 VEIpldSKPVSSWPAYFSIVKIERVGKHgkVFLTVPSLSStaeekfikkGEFSGDDSLLDLDPEDTVfYVGGVPSNFKLP 994
Cdd:cd00110 69 LVL---SSKTPLNDGQWHSVSVERNGRS--VTLSVDGERV---------VESGSPGGSALLNLDGPL-YLGGLPEDLKSP 133
|
170
....*....|....*...
gi 2217361438 995 TSLNLPGFVGCLELATLN 1012
Cdd:cd00110 134 GLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
860-1013 |
3.32e-18 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 82.77 E-value: 3.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 860 SLSLYMKppvkrpelTETADQFILYLGSKNaKKEYMGLAIKNDNLVYVYNLGTKDVEIPLDSKPVSswPAYFSIVKIERV 939
Cdd:smart00282 1 SISFSFR--------TTSPNGLLLYAGSKG-GGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLN--DGQWHRVAVERN 69
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217361438 940 GKHgkVFLTVPSLSSTAEEKFIKKgefsgddSLLDLDpedTVFYVGGVPSNFKLPTSLNLPGFVGCLELATLNN 1013
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 ... |
1263-1376 |
1.45e-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: 1.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 1263 FRTLQPNGLLFYYASG-SDVFSISLDNGTVIMDVK----GIKVQSVDKQYNDGLSHFVISSVSPTRYELIVDKSRVGSKN 1337
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGgSDFLALELVNGRLVLRYDlgsgPESLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2217361438 1338 PTKGkiEQTQASEKKFYFGG------SPISAQYANFTGCISNAYF 1376
Cdd:pfam02210 81 PPGE--SLLLNLNGPLYLGGlpplllLPALPVRAGFVGCIRDVRV 123
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
1676-1803 |
5.37e-16 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 76.20 E-value: 5.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 1676 VRPRSSSGTLVHGHSVN-GEYLNVHMKNGQVIVKVNNGIRdfSTSVTPKQSLCDGRWHRITVIRDSNVVQLDVDSEVNHV 1754
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTeRDFLALELRDGRLEVSYDLGSG--AAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPT 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2217361438 1755 V-GPLNPK-PIDHREPVFVGGVPESLLTPRLAP-SKPFTGCIRHFVIDGHPV 1803
Cdd:pfam00054 79 GeSPLGATtDLDVDGPLYVGGLPSLGVKKRRLAiSPSFDGCIRDVIVNGKPL 130
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
187-238 |
8.76e-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: 72.77 E-value: 8.76e-16
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2217361438 187 CDCSGNSDPNlifEDCDEVTGQCRnCLRNTTGFKCERCAPGYYGDARIAKNC 238
Cdd:cd00055 2 CDCNGHGSLS---GQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGGC 49
|
|
| LamG |
smart00282 |
Laminin G domain; |
1261-1379 |
1.13e-14 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 72.37 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 1261 FNFRTLQPNGLLFYYAS--GSDVFSISLDNGTVIMDVKG----IKVQSVDKQYNDGLSHFVISSVSPTRYELIVDksrvg 1334
Cdd:smart00282 4 FSFRTTSPNGLLLYAGSkgGGDYLALELRDGRLVLRYDLgsgpARLTSDPTPLNDGQWHRVAVERNGRSVTLSVD----- 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2217361438 1335 SKNPTKGKIEQTQA---SEKKFYFGGSP------ISAQYANFTGCISNAYFTRV 1379
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 |
5.57e-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: 5.57e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2217361438 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 ... |
279-723 |
7.44e-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: 7.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 279 DLTDDLRLAALSIEEGKsgVLSVSSGAAAHRHVNEINATIYLL----KTKLSERENQYALRKIQINNAENTMKSLLSDVE 354
Cdd:pfam05483 187 DLNNNIEKMILAFEELR--VQAENARLEMHFKLKEDHEKIQHLeeeyKKEINDKEKQVSLLLIQITEKENKMKDLTFLLE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 355 ELVEKENQASRKGQLvQKESMdtinhaSQLVEQAHDMRDKIQEINNKMlyygEEHELSPKEISEKLVLAQKMLEEIRSrq 434
Cdd:pfam05483 265 ESRDKANQLEEKTKL-QDENL------KELIEKKDHLTKELEDIKMSL----QRSMSTQKALEEDLQIATKTICQLTE-- 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 435 pfftQRELVDEEADEAY------------------ELLSQAEswQRLHNETRTLFPVVLEqlddYNAKLSDLQEALDQAL 496
Cdd:pfam05483 332 ----EKEAQMEELNKAKaahsfvvtefeattcsleELLRTEQ--QRLEKNEDQLKIITME----LQKKSSELEEMTKFKN 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 497 NYVRDAEDMNRATAARQR--DHEKQQERVREQMEVVNMSLSTsadSLTTPRLTLSELD---DIIKNASGIYA-EIDGAKS 570
Cdd:pfam05483 402 NKEVELEELKKILAEDEKllDEKKQFEKIAEELKGKEQELIF---LLQAREKEIHDLEiqlTAIKTSEEHYLkEVEDLKT 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 571 ELQ-VKLSNLSNLSH---------DLVQEAID-------HAQDLQQEANELSRKLhsSDMNGLVQKALDASNVYENIVNY 633
Cdd:pfam05483 479 ELEkEKLKNIELTAHcdklllenkELTQEASDmtlelkkHQEDIINCKKQEERML--KQIENLEEKEMNLRDELESVREE 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 634 VSEANETAEFALnttDRIYDAVSGIDTQIIYHKDESENLLNQARELQAKAEsssdeavaDTSRRVGGALARKSALKTRLS 713
Cdd:pfam05483 557 FIQKGDEVKCKL---DKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIE--------NKNKNIEELHQENKALKKKGS 625
|
490
....*....|
gi 2217361438 714 DAVKQLQAAE 723
Cdd:pfam05483 626 AENKQLNAYE 635
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
131-185 |
1.14e-12 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 63.91 E-value: 1.14e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2217361438 131 PCPCPlPHlANFAESCYRKNGavRCICNENYAGPNCERCAPGYYGNPlLIGSTCK 185
Cdd:cd00055 1 PCDCN-GH-GSLSGQCDPGTG--QCECKPNTTGRRCDRCAPGYYGLP-SQGGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
187-231 |
4.76e-12 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 61.94 E-value: 4.76e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2217361438 187 CDCS--GNSDPnlifeDCDEVTGQCRnCLRNTTGFKCERCAPGYYGD 231
Cdd:smart00180 1 CDCDpgGSASG-----TCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD 41
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
347-821 |
9.47e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 70.45 E-value: 9.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 347 KSLLSDVEELVEKENQASRKGQL-----VQKESMDTINHASQLVEQAHDMRDKIQEINnkmlyygEEHELSPKEI----S 417
Cdd:PRK02224 186 RGSLDQLKAQIEEKEEKDLHERLnglesELAELDEEIERYEEQREQARETRDEADEVL-------EEHEERREELetleA 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 418 EKLVLAQKMLEEIRSRQPF----FTQRELVDEEADEAYELLSQAEsWQRLHNETrtlfpvVLEQLDDYNAKLSDLQEALD 493
Cdd:PRK02224 259 EIEDLRETIAETEREREELaeevRDLRERLEELEEERDDLLAEAG-LDDADAEA------VEARREELEDRDEELRDRLE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 494 QALNYVRDAEdmNRATAARQR--DHEKQQERVREQMEVVNMSLSTSADSLTTPRLTLSELDDIIKNASGIYA----EIDG 567
Cdd:PRK02224 332 ECRVAAQAHN--EEAESLREDadDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGdapvDLGN 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 568 AKSELQVKLSNLSNLSHDL---------VQEAIDHAQDLQQEAN-------------------------ELSRKLhsSDM 613
Cdd:PRK02224 410 AEDFLEELREERDELREREaeleatlrtARERVEEAEALLEAGKcpecgqpvegsphvetieedrerveELEAEL--EDL 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 614 NGLVQKALDASNVYENIVNYVSEANETAEFALNTTDRIYDAVSGIDTQiiyhKDESENLLNQARELQAKAESSSDEAV-- 691
Cdd:PRK02224 488 EEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEK----RERAEELRERAAELEAEAEEKREAAAea 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 692 ---ADTSRRVGGAL-ARKSALKTRLsDAVKQL--QAAERGDAQQRLGqsRLITEEANRTTMEVQQatapmANNLTNWSQN 765
Cdd:PRK02224 564 eeeAEEAREEVAELnSKLAELKERI-ESLERIrtLLAAIADAEDEIE--RLREKREALAELNDER-----RERLAEKRER 635
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217361438 766 LQHFDSSAYNTAVNSARDAVRNLTEVVPQLLDQLRTVEQKRPA-----SNVSASIQRIREL 821
Cdd:PRK02224 636 KRELEAEFDEARIEEAREDKERAEEYLEQVEEKLDELREERDDlqaeiGAVENELEELEEL 696
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
1079-1203 |
9.62e-12 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 63.88 E-value: 9.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 1079 VRTPADNGLILLM--VNGSMFFRLEMRNGYLHVFYDFGfsGGPVHLEdtlKKAQINDAKYHEISIIYhNDKKMILVVDRR 1156
Cdd:pfam00054 1 FRTTEPSGLLLYNgtQTERDFLALELRDGRLEVSYDLG--SGAAVVR---SGDKLNDGKWHSVELER-NGRSGTLSVDGE 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2217361438 1157 HVKSMDNEK---MKIPF-TDIYIGGAPPEILqsraLRAHLPLDINFRGCMK 1203
Cdd:pfam00054 75 ARPTGESPLgatTDLDVdGPLYVGGLPSLGV----KKRRLAISPSFDGCIR 121
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
302-833 |
1.52e-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: 1.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 302 SSGAAAHRHVNEINATIYLLKTKLSERENQYALRKIQINNA--------ENTMKSLLSDVE----ELVEKENQASRKGQL 369
Cdd:pfam15921 217 SLGSAISKILRELDTEISYLKGRIFPVEDQLEALKSESQNKielllqqhQDRIEQLISEHEveitGLTEKASSARSQANS 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 370 VQKEsMDTI-----NHASQLVEQAHDMRDKIQEINNKMLYYGEEHELSPKEISEKLVLAQKMLEEIRSRQPFFTQR---- 440
Cdd:pfam15921 297 IQSQ-LEIIqeqarNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQEsgnl 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 441 ---------ELVDEEADEAYELLSQAESWQRLHNETRTLfPVVLEQLDDYNAKLSDLqEALDQALNYVRDAEdMNRATAA 511
Cdd:pfam15921 376 ddqlqkllaDLHKREKELSLEKEQNKRLWDRDTGNSITI-DHLRRELDDRNMEVQRL-EALLKAMKSECQGQ-MERQMAA 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 512 RQRDHEKQQE----------------RVREQMEVVNMSLSTSADSLTTPRLTLSELDDIIKNASgiyAEIDGAKSELQVK 575
Cdd:pfam15921 453 IQGKNESLEKvssltaqlestkemlrKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATN---AEITKLRSRVDLK 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 576 LSNLSNLSHDLvqeaiDHAQDLQQEANELSRKLHSSD--MNGLVQKaldasnvYENIVNYVSEANETAefalnttdriyd 653
Cdd:pfam15921 530 LQELQHLKNEG-----DHLRNVQTECEALKLQMAEKDkvIEILRQQ-------IENMTQLVGQHGRTA------------ 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 654 avsgidTQIIYHKDESENLLNQAR-ELQakaESSSDEAVADTSRRvggalarksALKTRLSD----AVKQLQAaergdAQ 728
Cdd:pfam15921 586 ------GAMQVEKAQLEKEINDRRlELQ---EFKILKDKKDAKIR---------ELEARVSDleleKVKLVNA-----GS 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 729 QRLGQSRLITEEANRTTMEVQQATAPMaNNLTNWSQNLQ-HF--DSSAYNTAVNSARDAVRNLTEVVPQLLDQLRTVE-Q 804
Cdd:pfam15921 643 ERLRAVKDIKQERDQLLNEVKTSRNEL-NSLSEDYEVLKrNFrnKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEgS 721
|
570 580 590
....*....|....*....|....*....|
gi 2217361438 805 KRPASNVSASIQR-IRELIAQTRSVASKIQ 833
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 |
1.72e-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: 60.44 E-value: 1.72e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2217361438 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 ... |
321-647 |
2.19e-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: 2.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 321 LKTKLSERENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLVQKESMDTINHASQLVEQAHDMRDKIQEINN 400
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLER 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 401 KMLYYGEEHELSPKEISEKLVLAQKMLEEIRSRQPFFT-QRELVDEEADEAYELLSQAESWQRLHNETRTLFPVVLEQLD 479
Cdd:TIGR02168 317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELEsLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 480 DYNAKLSDLQEALDQalnyvrdAEDMNRATAARQRDHEKQQERVreQMEVVNMSLSTSADSLTTprlTLSELDDIIKNAS 559
Cdd:TIGR02168 397 SLNNEIERLEARLER-------LEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEE---LQEELERLEEALE 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 560 GIYAEIDGAKSELQVKLSNLSNLSH--DLVQEAIDHAQDLQQEANELsrKLHSSDMNGLVQKALDASNV---YE------ 628
Cdd:TIGR02168 465 ELREELEEAEQALDAAERELAQLQArlDSLERLQENLEGFSEGVKAL--LKNQSGLSGILGVLSELISVdegYEaaieaa 542
|
330 340
....*....|....*....|..
gi 2217361438 629 ---NIVNYVSEANETAEFALNT 647
Cdd:TIGR02168 543 lggRLQAVVVENLNAAKKAIAF 564
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
81-130 |
3.23e-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: 3.23e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2217361438 81 PCDCNGN---SNECLDGSGYCvHCQRNTTGEHCEKCLDGYIGDSIRGAPqfCQ 130
Cdd:cd00055 1 PCDCNGHgslSGQCDPGTGQC-ECKPNTTGRRCDRCAPGYYGLPSQGGG--CQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
132-177 |
4.17e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 59.25 E-value: 4.17e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2217361438 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 ... |
875-1013 |
8.80e-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: 8.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 875 TETADQFILYLGSKnaKKEYMGLAIKNDNLVYVYNLGTKDVEIPLDSKPVS--SWpayfSIVKIERVGKHgkVFLTVPSL 952
Cdd:pfam02210 3 TRQPNGLLLYAGGG--GSDFLALELVNGRLVLRYDLGSGPESLLSSGKNLNdgQW----HSVRVERNGNT--LTLSVDGQ 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217361438 953 SSTAEEKfikkgefSGDDSLLDLDpedTVFYVGGVPSNFKLPTSLNLPGFVGCLELATLNN 1013
Cdd:pfam02210 75 TVVSSLP-------PGESLLLNLN---GPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVNG 125
|
|
| TNFRSF16 |
cd13416 |
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 ... |
65-257 |
2.80e-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: 60.78 E-value: 2.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 65 EKCNAGFFhTLSGECvpCDcngnsnECLDGSGYCVHCQRNTTGehCEKCLDGYIGDSIRGAPQFCQPC-PCplPHLANFA 143
Cdd:cd13416 1 EACPSGQY-TSSGEC--CE------QCPPGEGVARPCGDNQTV--CEPCLDGVTFSDVVSHTEPCQPCtRC--PGLMSMR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 144 ESCYRKNGAVrcicnenyagpnCErCAPGYYGNPLliGSTCKKCDCsgnsdpnlifedCDEVTGQCRNC--LRNTtgfKC 221
Cdd:cd13416 68 APCTATHDTV------------CE-CAYGYYLDED--SGTCEPCTV------------CPPGQGVVQSCgpNQDT---VC 117
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2217361438 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 |
6.47e-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: 6.47e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2217361438 82 CDCNGN---SNECLDGSGYCvHCQRNTTGEHCEKCLDGYIGDSIrGAPQFC 129
Cdd:pfam00053 1 CDCNPHgslSDTCDPETGQC-LCKPGVTGRHCDRCKPGYYGLPS-DPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
82-121 |
4.70e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 53.47 E-value: 4.70e-09
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2217361438 82 CDCNGN---SNECLDGSGYCvHCQRNTTGEHCEKCLDGYIGDS 121
Cdd:smart00180 1 CDCDPGgsaSGTCDPDTGQC-ECKPNVTGRRCDRCAPGYYGDG 42
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
319-731 |
2.43e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.01 E-value: 2.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 319 YLLKTKLseRENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLVQKESmdtinhasQLVEQAHDMRDKIQEI 398
Cdd:COG4717 45 AMLLERL--EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELE--------ELEEELEELEAELEEL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 399 NNKMLYYgeEHELSPKEISEKLVLAQKMLEEIRSRQPFFTQRELVDEEADEAYE-LLSQAESWQR-LHNETRTLFPVVLE 476
Cdd:COG4717 115 REELEKL--EKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEeLEAELAELQEeLEELLEQLSLATEE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 477 QLDDYNAKLSDLQEALDQALNYVRDAEDmNRATAARQRD-------HEKQQERVREQMEVVN-----MSLSTSADSLTTP 544
Cdd:COG4717 193 ELQDLAEELEELQQRLAELEEELEEAQE-ELEELEEELEqleneleAAALEERLKEARLLLLiaaalLALLGLGGSLLSL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 545 RLTL----------------------SELDDIIKNASGIYAEIDGAKSELQVKLSNL---SNLSHDLVQEAIDHAQDLQQ 599
Cdd:COG4717 272 ILTIagvlflvlgllallflllarekASLGKEAEELQALPALEELEEEELEELLAALglpPDLSPEELLELLDRIEELQE 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 600 ---EANELSRKLHSSDMNGLVQKALDASNV-----YENIVNYVSEANETAEfalnttdriydAVSGIDTQIIYHKDESEN 671
Cdd:COG4717 352 llrEAEELEEELQLEELEQEIAALLAEAGVedeeeLRAALEQAEEYQELKE-----------ELEELEEQLEELLGELEE 420
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217361438 672 LLNQARELQAKAE-SSSDEAVADTSRRVGGALARKSALKTRLSDAVKQLQAAERGDAQQRL 731
Cdd:COG4717 421 LLEALDEEELEEElEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEEL 481
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
321-743 |
2.67e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.18 E-value: 2.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 321 LKTKLSERENQYALRKIQinNAENTMKSLLSDVEELVEKENQASRKGQLVQKESMDTINHASQLVEQAHDMRDKIQEINN 400
Cdd:COG1196 218 LKEELKELEAELLLLKLR--ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 401 KMLyyGEEHELSPKEisEKLVLAQKMLEEIRSRqpfftQRELVDEEADEAYELLSQAESWQRLHNETRTLfpvvLEQLDD 480
Cdd:COG1196 296 ELA--RLEQDIARLE--ERRRELEERLEELEEE-----LAELEEELEELEEELEELEEELEEAEEELEEA----EAELAE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 481 YNAKLSDLQEALDQALNYVRDAEDMNRATAARQRDHEKQQERVREQMEVVNMSLSTSADSLTTPRLTLSELDDIIKNASG 560
Cdd:COG1196 363 AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 561 IYAEIDGAKSELQVKLSNLSNLSHDLVQEAIDHAQDLQQEANELSRKLHSSDMnglvqkALDASNVYENIVNYVSEANET 640
Cdd:COG1196 443 ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL------LLEAEADYEGFLEGVKAALLL 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 641 AEFALnttdriydaVSGIDTQIIYHKDESENLLNQARELQAKAESSSDEAVADtsRRVGGALARKSALKTRL-SDAVKQL 719
Cdd:COG1196 517 AGLRG---------LAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAA--AAIEYLKAAKAGRATFLpLDKIRAR 585
|
410 420
....*....|....*....|....
gi 2217361438 720 QAAERGDAQQRLGQSRLITEEANR 743
Cdd:COG1196 586 AALAAALARGAIGAAVDLVASDLR 609
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
311-610 |
2.82e-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: 59.30 E-value: 2.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 311 VNEINATIYLLKTKLSERENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLVQKESMDTINHASQLVEQAHD 390
Cdd:TIGR02168 693 IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE 772
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 391 MRDKIQEINNKMlyygEEHELSPKEISEKLVLAQKMLEEIRSRqpFFTQRELVDEEADEAYELLSQAESWQRLHNETRTL 470
Cdd:TIGR02168 773 AEEELAEAEAEI----EELEAQIEQLKEELKALREALDELRAE--LTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 471 FPVVLEQLDDYNAKLSDLQEALDQAlnyvrdAEDMNRATAARQRdHEKQQERVREQMEVVNMSLSTSADSLTTPRLTLSE 550
Cdd:TIGR02168 847 IEELSEDIESLAAEIEELEELIEEL------ESELEALLNERAS-LEEALALLRSELEELSEELRELESKRSELRRELEE 919
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 551 LDDIIKNASgiyAEIDGAKSELQVKLSNLSNLSHDLVQEAIDHAQDLQQEANELSRKLHS 610
Cdd:TIGR02168 920 LREKLAQLE---LRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKR 976
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
327-749 |
3.31e-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: 3.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 327 ERENQYALRKIqINNAENTMKSLLSDVEELVEKENQASRKGQLVQKESMDTINhasQL-VEQAHD--MRDKIQEInnkml 403
Cdd:pfam10174 224 DPAKTKALQTV-IEMKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIK---QMeVYKSHSkfMKNKIDQL----- 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 404 yygeEHELSPKEiSEKLVLaQKMLEEIRSRQPFFTQRELVDEEADEAYEllsqaeswQR---LHNETRTLfPVVLEQ--- 477
Cdd:pfam10174 295 ----KQELSKKE-SELLAL-QTKLETLTNQNSDCKQHIEVLKESLTAKE--------QRaaiLQTEVDAL-RLRLEEkes 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 478 -LDDYNAKLSDLQEALDQALNYVRDAEDM----NRATAARQ----------RDHEKQQERVREQMEVVNMSLSTSADSLT 542
Cdd:pfam10174 360 fLNKKTKQLQDLTEEKSTLAGEIRDLKDMldvkERKINVLQkkienlqeqlRDKDKQLAGLKERVKSLQTDSSNTDTALT 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 543 TPRLTLSELDDIIKNASGIYA--------EIDGAKSELQVKLSNLSNLSHDL------VQEAIDHAQDLQQEANELSRKL 608
Cdd:pfam10174 440 TLEEALSEKERIIERLKEQREredrerleELESLKKENKDLKEKVSALQPELtekessLIDLKEHASSLASSGLKKDSKL 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 609 HSSDMNglVQKALDASNVYENIVNYVSEANETAEFALNTTDRIydavSGIDTQIIYHKDES-------ENLLNQARELQA 681
Cdd:pfam10174 520 KSLEIA--VEQKKEECSKLENQLKKAHNAEEAVRTNPEINDRI----RLLEQEVARYKEESgkaqaevERLLGILREVEN 593
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217361438 682 KaESSSDEAVADTSRRVggalARKSALKTRLSDAVKQLQAAERGDAQQRLGQSRLITEEANRTTMEVQ 749
Cdd:pfam10174 594 E-KNDKDKKIAELESLT----LRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQ 656
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
311-751 |
4.67e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.41 E-value: 4.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 311 VNEINATIYLLKTKLSERENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLVQKESMDTINHASQLVEQAHD 390
Cdd:COG1196 283 LEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 391 MRDKIQEINNKMLyyGEEHELSpKEISEKLVLAQKMLEEIRSRQpffTQRELVDEEADEAYELLSQAESWQRLHNETRTL 470
Cdd:COG1196 363 AEEALLEAEAELA--EAEEELE-ELAEELLEALRAAAELAAQLE---ELEEAEEALLERLERLEEELEELEEALAELEEE 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 471 FPVVLEQLDDYNAKLSDLQEALDQALNYVRDAE------DMNRATAARQRDHEKQQERVREQMEVVNMSLSTSADSLTTP 544
Cdd:COG1196 437 EEEEEEALEEAAEEEAELEEEEEALLELLAELLeeaallEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLL 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 545 RLTLSELDDIIKNASGIYAEIDGAKSELQVKLSNLSNLSHDLVQEAIDHAQD-----------LQQEANELSRKLHSSDM 613
Cdd:COG1196 517 AGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAakagratflplDKIRARAALAAALARGA 596
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 614 NGLVQKALDASNVYENIVNYV-----------SEANETAEFALNTTDRIYDAVSGIDTQIIYHKDESENLLNQARELQAK 682
Cdd:COG1196 597 IGAAVDLVASDLREADARYYVlgdtllgrtlvAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLE 676
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217361438 683 AESSSDEAVADTSRRVGGALARKSALKTRLSDAVKQLQAAERGDAQQRLGQSRLITEEANRTTMEVQQA 751
Cdd:COG1196 677 AEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEE 745
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
318-745 |
2.02e-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: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 318 IYLLKTKLSERENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLVQKESMDTINHASQLVEQAHDMRDKIQE 397
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 398 INNKMLYYGEEHElspkEISEKLVLAQKMLEEIRsrqpffTQRELVDEEADEAYELLSQAEswQRLHNETRTLFPVVLEQ 477
Cdd:COG1196 314 LEERLEELEEELA----ELEEELEELEEELEELE------EELEEAEEELEEAEAELAEAE--EALLEAEAELAEAEEEL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 478 LDDYNAKLSDLQEALDQAlNYVRDAEDMNRATAARQRDHEKQQERVREQMEVVNMSLSTSADSLTTPRLTLSELDDIIKN 557
Cdd:COG1196 382 EELAEELLEALRAAAELA-AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 558 ASGIYAEIDGAKSELQVKLSNLSNLSHDLVQ--EAIDHAQDLQQEANELSRKLHSSDMNGLVQKALDAsnvyENIVNYVS 635
Cdd:COG1196 461 LLELLAELLEEAALLEAALAELLEELAEAAArlLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAV----LIGVEAAY 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 636 EANETAEFALNTTDRIYDAVSGIDTQIIYHKDESEN-----LLNQARELQAKAESSSDEAVADTSRRVGGALARKSALKT 710
Cdd:COG1196 537 EAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGratflPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYY 616
|
410 420 430
....*....|....*....|....*....|....*
gi 2217361438 711 RLSDAVkQLQAAERGDAQQRLGQSRLITEEANRTT 745
Cdd:COG1196 617 VLGDTL-LGRTLVAARLEAALRRAVTLAGRLREVT 650
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
298-753 |
2.41e-07 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 55.68 E-value: 2.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 298 VLSVSSGAAAHRHVNEINATIYLLKTklsERENQYALRKIQ--INNAENTMKS-LLSDVEELVEKENQAsrkgqlvQKES 374
Cdd:COG5278 19 LLLLVLGVLSYLSLNRLREASEWVEH---TYEVLRALEELLsaLLDAETGQRGyLLTGDESFLEPYEEA-------RAEI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 375 MDTINHASQLVEQAHDMRDKIQEINNKMLYYGEEHELS-------PKEISEKLVLA---QKMLEEIRSRQpfFTQRELVD 444
Cdd:COG5278 89 DELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVialrragGLEAALALVRSgegKALMDEIRARL--LLLALALA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 445 EEADEAYELLSQAESWQRLHNETRTLFPVVLEQLDDYNAKLSDLQEALDQALNYVRDAEDMNRATAARQRDHEKQQERVR 524
Cdd:COG5278 167 ALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 525 EQMEVVNMSLSTSADSLTTPRLTLSELDDIIKNAsgiyAEIDGAKSELQVKLSNLSNLSHDLVQEAIDHAQDLQQEANEL 604
Cdd:COG5278 247 AALLLALLAALALAALLAAALLALAALLLALAAA----AALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 605 SRKLHSSDMNGLVQKALDASNVYENIVNYVSEANETAEFALNTTDRIYDAVSGIDTQIIYHKDESENLLNQARELQAKAE 684
Cdd:COG5278 323 AALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAA 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217361438 685 SSSDEAVADTSRRVGGALARKSALKTRLSDAVKQLQAAERGDAQQRLGQSRLITEEANRTTMEVQQATA 753
Cdd:COG5278 403 AAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAV 471
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
374-851 |
2.45e-07 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 55.68 E-value: 2.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 374 SMDTINHASQLVEQAHDMRDKIQEINNKM----------LYYGEEHELspkeiseklvlaqkmleeirsrQPFFTQRELV 443
Cdd:COG5278 31 SLNRLREASEWVEHTYEVLRALEELLSALldaetgqrgyLLTGDESFL----------------------EPYEEARAEI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 444 DEEADEAYELLSQAESWQRLhnetrtlfpvvLEQLDD-YNAKLSDLQEAL--------DQALNYVRDAEDMNRATAARQR 514
Cdd:COG5278 89 DELLAELRSLTADNPEQQAR-----------LDELEAlIDQWLAELEQVIalrragglEAALALVRSGEGKALMDEIRAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 515 DHEKQQERVREQMEVVNMSLSTSADSLTTPRLTLSELDDIIKNASGIYAEIDGAKSELQVKLSNLSNLSHDLVQEAIDHA 594
Cdd:COG5278 158 LLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 595 QDLQQEANELSRKLHSSDMNGLVQKALDASNVYENIVNYVSEANETAEFALNTTDRIYDAVSGIDTQIIYHKDESENLLN 674
Cdd:COG5278 238 LALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 675 QARELQAKAESSSDEAVADTSRRVGGALARKSALKTRLSDAVKQLQAAERGDAQQRLGQSRLITEEANRTTMEVQQATAP 754
Cdd:COG5278 318 AAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 755 MANNLTNWSQNLQHFDSSAYNTAVNSARDAVRNLTEVVPQLLDQLRTVEQKRPASNVSASIQRIRELIAQTRSVASKIQV 834
Cdd:COG5278 398 AAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAAL 477
|
490
....*....|....*..
gi 2217361438 835 SMMFDGQSAVEVHSRTS 851
Cdd:COG5278 478 AAAAAALAEAEAAAALA 494
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
529-757 |
2.62e-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: 2.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 529 VVNMSLSTSADslTTPRLTLSELDDIIKNASGIYAEIDGAKSELQVKLSNLSNLSHDL--VQEAIDhaqDLQQEANELSR 606
Cdd:COG3883 5 ALAAPTPAFAD--PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELeaLQAEID---KLQAEIAEAEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 607 KLhsSDMNGLVQKALDASNVYENIVNYVS---EANETAEFA--LNTTDRIYDAVSGIDTQIIYHKDESENLLNQARELQA 681
Cdd:COG3883 80 EI--EERREELGERARALYRSGGSVSYLDvllGSESFSDFLdrLSALSKIADADADLLEELKADKAELEAKKAELEAKLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 682 KAESSSDEAvADTSRRVGGALARKSALKTRLSDAVKQLQA------AERGDAQQRLGQSRLITEEANRTTMEVQQATAPM 755
Cdd:COG3883 158 ELEALKAEL-EAAKAELEAQQAEQEALLAQLSAEEAAAEAqlaeleAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
..
gi 2217361438 756 AN 757
Cdd:COG3883 237 AA 238
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
312-528 |
2.83e-07 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 54.15 E-value: 2.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 312 NEINATIYLLKTKLSERENQYAlrkiQINNAENTMKSLLSDVEEL----------VEKENQ----ASRKGQLVQ--KESM 375
Cdd:COG1340 81 DELNEKLNELREELDELRKELA----ELNKAGGSIDKLRKEIERLewrqqtevlsPEEEKElvekIKELEKELEkaKKAL 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 376 DTINHASQLVEQAHDMRDKIQEINNKMlyygeehelspKEISEKlvlAQKMLEEIRSRqpfFTQRELVDEEADEAYELLS 455
Cdd:COG1340 157 EKNEKLKELRAELKELRKEAEEIHKKI-----------KELAEE---AQELHEEMIEL---YKEADELRKEADELHKEIV 219
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217361438 456 QA-ESWQRLHnetrtlfpvvlEQLDDYNAKLSDLQEALDQALNYVRDAEdmnrataaRQRDHEKQQERVREQME 528
Cdd:COG1340 220 EAqEKADELH-----------EEIIELQKELRELRKELKKLRKKQRALK--------REKEKEELEEKAEEIFE 274
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
418-833 |
4.08e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.16 E-value: 4.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 418 EKLVLAQKMLEEIRSRQPfftqrELVDEEADEAYELLSQAESWQRLHNETRtlfpvvlEQLDDYNAKLSDLQEALDQALN 497
Cdd:COG4717 49 ERLEKEADELFKPQGRKP-----ELNLKELKELEEELKEAEEKEEEYAELQ-------EELEELEEELEELEAELEELRE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 498 YVRDAEDMNRAtaarqRDHEKQQERVREQMEvvnmSLSTSADSLTTPRLTLSELDDIIKNASgiyAEIDGAKSELQVKLS 577
Cdd:COG4717 117 ELEKLEKLLQL-----LPLYQELEALEAELA----ELPERLEELEERLEELRELEEELEELE---AELAELQEELEELLE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 578 NLSNLSHDLVQEAIDHAQDLQQEANELSRKL---------HSSDMNGLVQKALDAsNVYENIVNY-------------VS 635
Cdd:COG4717 185 QLSLATEEELQDLAEELEELQQRLAELEEELeeaqeeleeLEEELEQLENELEAA-ALEERLKEArlllliaaallalLG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 636 EANETAEFALNTTDRIYDAVSGIDTQIIYHKDESENLLNQARELQAKAESSS--DEAVADTSRRVGGALARKSALKTRLS 713
Cdd:COG4717 264 LGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEEleEEELEELLAALGLPPDLSPEELLELL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 714 DAVKQLQAA--ERGDAQQRLGQSRLITE------------------------EANRTTMEVQQATAPMANNLTNWSQNLQ 767
Cdd:COG4717 344 DRIEELQELlrEAEELEEELQLEELEQEiaallaeagvedeeelraaleqaeEYQELKEELEELEEQLEELLGELEELLE 423
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217361438 768 HFDSSAYNTAVNSARDAVRNLTEVVPQLLDQLRTVEQKRpaSNVSASiQRIRELIAQTRSVASKIQ 833
Cdd:COG4717 424 ALDEEELEEELEELEEELEELEEELEELREELAELEAEL--EQLEED-GELAELLQELEELKAELR 486
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
321-677 |
5.39e-07 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 54.46 E-value: 5.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 321 LKTKLSERENQY--ALRKI--QINNAEntmkSLLSDVEELVEKEN-QASRKGQLVQKESMDTINH-----ASQLVEQAHD 390
Cdd:PRK04778 152 LRKSLLANRFSFgpALDELekQLENLE----EEFSQFVELTESGDyVEAREILDQLEEELAALEQimeeiPELLKELQTE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 391 MRDKIQEINN---KML---YYGEEHELSP--KEISEKLVLAQKMLEEI---RSRQpfftQRELVDEEADEAYELLsQAES 459
Cdd:PRK04778 228 LPDQLQELKAgyrELVeegYHLDHLDIEKeiQDLKEQIDENLALLEELdldEAEE----KNEEIQERIDQLYDIL-EREV 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 460 wqRLHNETRTLFPVVLEQLDDYNAKLSDLQEALDQ-ALNYVRDAEDMnrataARQRDHEKQQERVREQMEVVnmslstsA 538
Cdd:PRK04778 303 --KARKYVEKNSDTLPDFLEHAKEQNKELKEEIDRvKQSYTLNESEL-----ESVRQLEKQLESLEKQYDEI-------T 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 539 DSLTTPRLTLSELDDIIKNASGIYAEIDgaksELQVKLSN-LSNLSHDlVQEAIDHAQDLQQEANELSRKLHSSDMNGLV 617
Cdd:PRK04778 369 ERIAEQEIAYSELQEELEEILKQLEEIE----KEQEKLSEmLQGLRKD-ELEAREKLERYRNKLHEIKRYLEKSNLPGLP 443
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217361438 618 QKALDAsnvYENIVNYVSEANEtaefALNTT----DRIYDAVSGIDTQIIYHKDESENLLNQAR 677
Cdd:PRK04778 444 EDYLEM---FFEVSDEIEALAE----ELEEKpinmEAVNRLLEEATEDVETLEEETEELVENAT 500
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
354-855 |
7.63e-07 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 54.45 E-value: 7.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 354 EELVEKENQASRKgqlvQKESMDTINHASQLVEQahdmrdkiqeinnkmlyygeEHELSPKEISEKLVLAQKMLEEIRSR 433
Cdd:NF041483 699 EALAAAQEEAARR----RREAEETLGSARAEADQ--------------------ERERAREQSEELLASARKRVEEAQAE 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 434 qpffTQReLVdEEADE-AYELLSQAESwqrlhnetrtlfpvVLEQLDDynaKLSDLQEALDQALNYVRDAEDMnraTAAR 512
Cdd:NF041483 755 ----AQR-LV-EEADRrATELVSAAEQ--------------TAQQVRD---SVAGLQEQAEEEIAGLRSAAEH---AAER 808
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 513 QRDhEKQQE--RVReqmevvnmslstsADSLTTpRLTLSEldDIIKNASGIYAEIDGAKSelqvklsnlsnLSHDLVQEA 590
Cdd:NF041483 809 TRT-EAQEEadRVR-------------SDAYAE-RERASE--DANRLRREAQEETEAAKA-----------LAERTVSEA 860
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 591 IDHAQDLQQEANELSRKLHSSDMNGLVQKALDASNVYenivnyvSEANETAefalnttDRI-YDAVSGIDTQIIYHKDES 669
Cdd:NF041483 861 IAEAERLRSDASEYAQRVRTEASDTLASAEQDAARTR-------ADAREDA-------NRIrSDAAAQADRLIGEATSEA 926
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 670 ENLLNQARelqAKAESSSDEAVADTSRRVGGALARKSALKTRLSDAVKQL--QAAER-GDAQQRLGQSRlitEEANRTTM 746
Cdd:NF041483 927 ERLTAEAR---AEAERLRDEARAEAERVRADAAAQAEQLIAEATGEAERLraEAAETvGSAQQHAERIR---TEAERVKA 1000
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 747 EvqqaTAPMANNLTNWSQN-----LQHFDSSAYNTAVNSARDAVRNLTEVVPQlLDQLRTVEQKRPASNVSASIQRIREL 821
Cdd:NF041483 1001 E----AAAEAERLRTEAREeadrtLDEARKDANKRRSEAAEQADTLITEAAAE-ADQLTAKAQEEALRTTTEAEAQADTM 1075
|
490 500 510
....*....|....*....|....*....|....
gi 2217361438 822 IAQTRSVASKIQVSMMFDGQSAVEvHSRTSMDDL 855
Cdd:NF041483 1076 VGAARKEAERIVAEATVEGNSLVE-KARTDADEL 1108
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
415-767 |
1.26e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.98 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 415 EISEKLVLAQKMLEEIRSR--QPFFTQRELVDEEADEAYELLSQAESWQRLHNETRtlfpvvlEQLDDYNAKLSDLQEAL 492
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKtgILIAALSEQLRKALFELDKLQEELEQLREELEQAR-------EELEQLEEELEQARSEL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 493 DQALNYVRDAEDMNRATAARQRDHEKQQERVREQMEvvnmSLSTSADSLttprltLSELDDIIKNASGIYAEIDGAKSEL 572
Cdd:COG4372 76 EQLEEELEELNEQLQAAQAELAQAQEELESLQEEAE----ELQEELEEL------QKERQDLEQQRKQLEAQIAELQSEI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 573 QVKLSNLSNLSHDLvQEAIDHAQDLQQEANELSRKLHSSDMNGLVQKAldasnvyENIVNYVSEANETAEFALNTTDRIY 652
Cdd:COG4372 146 AEREEELKELEEQL-ESLQEELAALEQELQALSEAEAEQALDELLKEA-------NRNAEKEEELAEAEKLIESLPRELA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 653 DAVSGIDTQIIYHKDESENLLNQARELQAKAESSSDEAVADTSRRVGGALARKSALKTRLSDAVKQLQAAERGDAQQRLG 732
Cdd:COG4372 218 EELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKL 297
|
330 340 350
....*....|....*....|....*....|....*
gi 2217361438 733 QSRLITEEANRTTMEVQQATAPMANNLTNWSQNLQ 767
Cdd:COG4372 298 LALLLNLAALSLIGALEDALLAALLELAKKLELAL 332
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
313-674 |
1.33e-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: 53.49 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 313 EINATIYLLKTKLSERENQYALRKIQINNAENTMKSL---LSDVEELVEKENQASRKGQ--LVQKESM-DTIN-HASQLV 385
Cdd:TIGR04523 430 RLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLetqLKVLSRSINKIKQNLEQKQkeLKSKEKElKKLNeEKKELE 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 386 EQAHDMRDKIQEINNKMlyygEEHELSPKEISEKLVLAQKMLEEIRSRqpffTQRELVDEEADEAYELLSQaeswqrLHN 465
Cdd:TIGR04523 510 EKVKDLTKKISSLKEKI----EKLESEKKEKESKISDLEDELNKDDFE----LKKENLEKEIDEKNKEIEE------LKQ 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 466 ETRTLfpvvleqlddyNAKLSDLQEALDQalnyvrdaedmnrataarqrdHEKQQERVREQMEVVNMSLSTSADSLTTPR 545
Cdd:TIGR04523 576 TQKSL-----------KKKQEEKQELIDQ---------------------KEKEKKDLIKEIEEKEKKISSLEKELEKAK 623
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 546 LTLSELDDIIKNasgiyaeIDGAKSELQVKLSNLsnlsHDLVQEAIDHAQDLQQEANELSRKLhsSDMNGLVQKALDASN 625
Cdd:TIGR04523 624 KENEKLSSIIKN-------IKSKKNKLKQEVKQI----KETIKEIRNKWPEIIKKIKESKTKI--DDIIELMKDWLKELS 690
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2217361438 626 VYENivNYVSEANETAEfaLNTTDRIYDAVSGIDTQIIYHKDESENLLN 674
Cdd:TIGR04523 691 LHYK--KYITRMIRIKD--LPKLEEKYKEIEKELKKLDEFSKELENIIK 735
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
338-611 |
2.03e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 51.45 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 338 QINNAENTMKSLLSDVEELVEKENQASRKGQLVQKESMDTINHASQLVEQAHDMRDKIQEINNKMlyygEEHELSPKEIS 417
Cdd:COG1340 9 SLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKV----KELKEERDELN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 418 EKLVLAQKMLEEIRSRQPfftQRELVDEEADEAYELLSQAEsWQRlhnETRTLFP----VVLEQLDDYNAKLSDLQEALD 493
Cdd:COG1340 85 EKLNELREELDELRKELA---ELNKAGGSIDKLRKEIERLE-WRQ---QTEVLSPeeekELVEKIKELEKELEKAKKALE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 494 QALNYVrdaEDMNRATAARqrdheKQQERVREQMEvvnmSLSTSADSLTTprltlsELDDIIKNASGIYAEIDGAKSELq 573
Cdd:COG1340 158 KNEKLK---ELRAELKELR-----KEAEEIHKKIK----ELAEEAQELHE------EMIELYKEADELRKEADELHKEI- 218
|
250 260 270
....*....|....*....|....*....|....*...
gi 2217361438 574 VKLSNLSNLSHDLVQEAIDHAQDLQQEANELSRKLHSS 611
Cdd:COG1340 219 VEAQEKADELHEEIIELQKELRELRKELKKLRKKQRAL 256
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
456-831 |
2.25e-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: 2.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 456 QAESWQRLHNETRTLfpvvleQLDDYNAKLSDLQEALDQALNYVRDAEDMNRATAARQRDHEKQQERVREQMEVVNMSLS 535
Cdd:COG1196 211 KAERYRELKEELKEL------EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 536 TSADSLttpRLTLSELddiiknasgiyAEIDGAKSELQVKLSNLSNLSHDLVQEAIDHAQDLQQEANELSRKLHSSDMng 615
Cdd:COG1196 285 EAQAEE---YELLAEL-----------ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE-- 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 616 LVQKALDASNVYENIVNYVSEANETAEFALNTTDRIYDAVSGIDTQIIYHKDESENLLNQARELQAKAESSSDEAVADTS 695
Cdd:COG1196 349 AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 696 RRVGGALARKSALKTRLSDAVKQLQAAERGDAQQR----LGQSRLITEEANRTTMEVQQATAPMANNLTNWSQNLQHFDS 771
Cdd:COG1196 429 ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEllaeLLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 772 SAYNTAVNSARDAvrnltevVPQLLDQLRTVEQKRPASNVSASIQRIRELIAQTRSVASK 831
Cdd:COG1196 509 GVKAALLLAGLRG-------LAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAA 561
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
309-573 |
2.78e-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: 52.76 E-value: 2.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 309 RHVNEINATIYLLKTKLSERENQYAlrkiQINNAENTMKSLLSDVEELVEKENQAsrkgQLVQKESMDTIN-HASQLVEQ 387
Cdd:TIGR02169 702 NRLDELSQELSDASRKIGEIEKEIE----QLEQEEEKLKERLEELEEDLSSLEQE----IENVKSELKELEaRIEELEED 773
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 388 AHDMRDKIQEInnkmlyygeEHELSPKEISEKLVLAQKmLEEIRSRQPFFTQ---RELVDEEADEAY------ELLSQAE 458
Cdd:TIGR02169 774 LHKLEEALNDL---------EARLSHSRIPEIQAELSK-LEEEVSRIEARLReieQKLNRLTLEKEYlekeiqELQEQRI 843
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 459 SWQRLHNETRtlfpvvlEQLDDYNAKLSDLQEALDQALNYVRDAEDmnrataaRQRDHEKQQERVREQMEVVNMSLSTSA 538
Cdd:TIGR02169 844 DLKEQIKSIE-------KEIENLNGKKEELEEELEELEAALRDLES-------RLGDLKKERDELEAQLRELERKIEELE 909
|
250 260 270
....*....|....*....|....*....|....*
gi 2217361438 539 DSLTTPRLTLSELDDIIKNASGIYAEIDGAKSELQ 573
Cdd:TIGR02169 910 AQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDE 944
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
314-574 |
3.80e-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: 52.36 E-value: 3.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 314 INATIYLLKTKLSERENQYAlrkiQINNAENTMKSLLSDV---EELVEKENQASRK-GQLVQK-ESMDTINHASQLVEQA 388
Cdd:TIGR00606 756 VNRDIQRLKNDIEEQETLLG----TIMPEEESAKVCLTDVtimERFQMELKDVERKiAQQAAKlQGSDLDRTVQQVNQEK 831
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 389 HDMRDKIQEINNKmlyyGEEHELSPKEISEKLVLAQKMLEEIRS-----------RQPFFTQRELVDEEADEAYELLSQA 457
Cdd:TIGR00606 832 QEKQHELDTVVSK----IELNRKLIQDQQEQIQHLKSKTNELKSeklqigtnlqrRQQFEEQLVELSTEVQSLIREIKDA 907
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 458 --------ESWQRLHNETRTLFPVVLEQLDDYNAKLSDLQEALDQAL-------NYVRDAED---MNRAT-----AARQR 514
Cdd:TIGR00606 908 keqdspleTFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHgymkdieNKIQDGKDdylKQKETelntvNAQLE 987
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217361438 515 DHEKQQERVREQMEVVNMSLSTS--ADSLTTPRLTLSELDDIIKNASGIYAEIDGAKSELQV 574
Cdd:TIGR00606 988 ECEKHQEKINEDMRLMRQDIDTQkiQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQV 1049
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
440-821 |
4.05e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 52.27 E-value: 4.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 440 RELVDEEAD---EAYELLSQAESWQRLHNETRtlfpvvlEQLDDYNAKLSDLQEALDQA---LNYVRDAEDMNRATAARQ 513
Cdd:PRK04863 282 RVHLEEALElrrELYTSRRQLAAEQYRLVEMA-------RELAELNEAESDLEQDYQAAsdhLNLVQTALRQQEKIERYQ 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 514 RDHEKQQERVREQMEVVNMSLSTSADSLTTPRLTLSELD-------------DIIKNASGIYAE----IDGAKSELQVKL 576
Cdd:PRK04863 355 ADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDelksqladyqqalDVQQTRAIQYQQavqaLERAKQLCGLPD 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 577 SNLSNLShDLVQEAIDHAQDLQQEANELSRKLHSSDMnglvqkaldasnvyenivnyvseANETAEFALNTTDRIYDAVS 656
Cdd:PRK04863 435 LTADNAE-DWLEEFQAKEQEATEELLSLEQKLSVAQA-----------------------AHSQFEQAYQLVRKIAGEVS 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 657 GIDTQiiyhkDESENLLNQARELQAKAEsssdeavadtsrRVGGALARKSALKTRLsdavKQLQAAER--GDAQQRLGQS 734
Cdd:PRK04863 491 RSEAW-----DVARELLRRLREQRHLAE------------QLQQLRMRLSELEQRL----RQQQRAERllAEFCKRLGKN 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 735 --------RLITE-EANRTTMEVQQATA-----PMANNLTNWSQNLQHFDSSA-----YNTAVNSARDAV-------RNL 788
Cdd:PRK04863 550 lddedeleQLQEElEARLESLSESVSEArerrmALRQQLEQLQARIQRLAARApawlaAQDALARLREQSgeefedsQDV 629
|
410 420 430
....*....|....*....|....*....|....*
gi 2217361438 789 TEVVPQLLDQLR--TVEQKRPASNVSASIQRIREL 821
Cdd:PRK04863 630 TEYMQQLLERERelTVERDELAARKQALDEEIERL 664
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
313-718 |
4.15e-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: 4.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 313 EINATIYLLKTKLSERENQYALRKIQINNAENTMKSLLSDVEEL---VEKENQASRKGQLVQKESMDTINHASQLVEQAH 389
Cdd:TIGR00618 553 SERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLqdlTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRL 632
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 390 DMRDKIQEINNKMLY-YGEEHELSPKEISEKLVLA---QKMLEEIRSRQPFFTQRELVDEEADEayELLSQAESWQR-LH 464
Cdd:TIGR00618 633 HLQQCSQELALKLTAlHALQLTLTQERVREHALSIrvlPKELLASRQLALQKMQSEKEQLTYWK--EMLAQCQTLLReLE 710
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 465 NETRTLFPVVLEQLDDYNAKLSDLQ---EALDQALNYVR-------------DAEDMNRATAARQRDHEKQQerVREQME 528
Cdd:TIGR00618 711 THIEEYDREFNEIENASSSLGSDLAareDALNQSLKELMhqartvlkarteaHFNNNEEVTAALQTGAELSH--LAAEIQ 788
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 529 VVNMSLSTSADSLttpRLTLSEL------DDIIKNASGIyaEIDGAKSELQVKLSNLSNLSHDLVQEAIDHAQDLQQEAn 602
Cdd:TIGR00618 789 FFNRLREEDTHLL---KTLEAEIgqeipsDEDILNLQCE--TLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLA- 862
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 603 ELSRKlhSSDMNGLVQKAldasNVYENIVNYVsEANETAEFALNTTdriYDAVsgIDTQIIYH-------KDESENllnq 675
Cdd:TIGR00618 863 QLTQE--QAKIIQLSDKL----NGINQIKIQF-DGDALIKFLHEIT---LYAN--VRLANQSEgrfhgryADSHVN---- 926
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2217361438 676 ARELQAKAE---SSSDEAVADTSRRVGGALARKS-ALKTRLSDAVKQ 718
Cdd:TIGR00618 927 ARKYQGLALlvaDAYTGSVRPSATLSGGETFLASlSLALALADLLST 973
|
|
| ApoLp-III_like |
cd13769 |
Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles ... |
710-836 |
4.17e-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: 4.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 710 TRLSDAVKQLQAAERGDAQQRLGQSRL-ITEEANRTtmeVQQATAPMANNLTNWSQNLQHFDSSAYNTAVNSARDAVRNL 788
Cdd:cd13769 1 TQLSELIQKAQEAINNLAQQVQKQLGLqNPEEVVNT---LKEQSDNFANNLQEVSSSLKEEAKKKQGEVEEAWNEFKTKL 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2217361438 789 TEVVPQLLDQLRTVEQkrpASNVSASIQ-RIRELIAQTRSVASKIQVSM 836
Cdd:cd13769 78 SETVPELRKSLPVEEK---AQELQAKLQsGLQTLVTESQKLAKAISENS 123
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
339-531 |
4.26e-06 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 49.75 E-value: 4.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 339 INNAENTMKSL-----LSDVEELVEKeNQASRKGQLVQKESMDTIN-HASQLVEQAHDMRDKIQE----INNKMlyygee 408
Cdd:cd00176 16 LSEKEELLSSTdygddLESVEALLKK-HEALEAELAAHEERVEALNeLGEQLIEEGHPDAEEIQErleeLNQRW------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 409 helspKEISEKLVLAQKMLEEIRSRQPFFTQrelVDEEADEAYELLSQAESWQRLHNETRtlfpvVLEQLDdynaKLSDL 488
Cdd:cd00176 89 -----EELRELAEERRQRLEEALDLQQFFRD---ADDLEQWLEEKEAALASEDLGKDLES-----VEELLK----KHKEL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2217361438 489 QEALDQALNYVRDAEDMNRATAARQrdHEKQQERVREQMEVVN 531
Cdd:cd00176 152 EEELEAHEPRLKSLNELAEELLEEG--HPDADEEIEEKLEELN 192
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
309-579 |
6.97e-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: 6.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 309 RHVNEINATIYLLKTKLSERENQYALRKIQINNAENTMKSLLSDvEELVEKENQASRKGQLVQKEsmDTINHASQLVEQA 388
Cdd:TIGR02169 244 RQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEE-EQLRVKEKIGELEAEIASLE--RSIAEKERELEDA 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 389 HDMRDKIQEINNKMLyygEEHELSPKEISEKLVLAQKMLEEIRSRQpfftqrelvdeeaDEAYELLSQAESWQRLHNETR 468
Cdd:TIGR02169 321 EERLAKLEAEIDKLL---AEIEELEREIEEERKRRDKLTEEYAELK-------------EELEDLRAELEEVDKEFAETR 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 469 TLFPVVLEQLDDYNAKLSDLQEALDQALNYVRDAEdmnrataARQRDHEKQQERVREQ-------MEVVNMSLSTSADSL 541
Cdd:TIGR02169 385 DELKDYREKLEKLKREINELKRELDRLQEELQRLS-------EELADLNAAIAGIEAKineleeeKEDKALEIKKQEWKL 457
|
250 260 270
....*....|....*....|....*....|....*...
gi 2217361438 542 TTPRLTLSELDDIIKNASGIYAEIDGAKSELQVKLSNL 579
Cdd:TIGR02169 458 EQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEA 495
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
1263-1376 |
9.65e-06 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 46.93 E-value: 9.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 1263 FRTLQPNGLLFYYAS--GSDVFSISLDNG--TVIMDV-KGIKVQSVDKQYNDGLSHFVISSVSPTRYELIVDK-SRVGSK 1336
Cdd:pfam00054 1 FRTTEPSGLLLYNGTqtERDFLALELRDGrlEVSYDLgSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGeARPTGE 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2217361438 1337 NPTKGKieQTQASEKKFYFGGSPISAQYA-------NFTGCISNAYF 1376
Cdd:pfam00054 81 SPLGAT--TDLDVDGPLYVGGLPSLGVKKrrlaispSFDGCIRDVIV 125
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
320-608 |
9.92e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 9.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 320 LLKTKLSERENQYALRKiqinNAENTMKsllsdVEELVEKENQASRKGQLVQKESMDTINHASQLVEQAHDMRDKIQEIN 399
Cdd:PTZ00121 1680 AKKAEEDEKKAAEALKK----EAEEAKK-----AEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAK 1750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 400 NkmlyygEEHElsPKEISEKLVLAQKMLEEIRSRQPFFTQRELVDEEADEAYELlsqaeswQRLHNETRTLFPVVLEQLD 479
Cdd:PTZ00121 1751 K------DEEE--KKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEV-------DKKIKDIFDNFANIIEGGK 1815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 480 DYNAKLSDLQEALDQALNYVRDAEDMNRATAARQRDHEKQQERVREQMEVVNMSLSTSADSLTTPRLTLSELDDIIKnas 559
Cdd:PTZ00121 1816 EGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEK--- 1892
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2217361438 560 giyaeIDGAKSELQVKLSNLSNLSHDLVQEAIDHAQDLQQEANELSRKL 608
Cdd:PTZ00121 1893 -----IDKDDIEREIPNNNMAGKNNDIIDDKLDKDEYIKRDAEETREEI 1936
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
321-678 |
2.29e-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: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 321 LKTKLS--ERENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLVQKESMDTINHASQLVEQAHDMRDKIQEI 398
Cdd:TIGR01612 2049 IKEKIDnyEKEKEKFGIDFDVKAMEEKFDNDIKDIEKFENNYKHSEKDNHDFSEEKDNIIQSKKKLKELTEAFNTEIKII 2128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 399 NNKMLyygEEHELSPKeiseklvlaqkmLEEIRSRQPFFTQRELVDEeadeayeLLSQAESWQRLHNETRTLFPVVLEQL 478
Cdd:TIGR01612 2129 EDKII---EKNDLIDK------------LIEMRKECLLFSYATLVET-------LKSKVINHSEFITSAAKFSKDFFEFI 2186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 479 DDYNAKLSDLQEALDQALNYVRDAEDMNRATAARQRDHEKQQERVREQMEVVNM--------SLSTSADSLTTPRLTL-- 548
Cdd:TIGR01612 2187 EDISDSLNDDIDALQIKYNLNQTKKHMISILADATKDHNNLIEKEKEATKIINNltelftidFNNADADILHNNKIQIiy 2266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 549 --SELDDIIKNASGIYAEIDGakselqVKLSNLSNLSHDLVQEAIDHAQDLQQEANELSRKLHssDMNGLVQKALDASNV 626
Cdd:TIGR01612 2267 fnSELHKSIESIKKLYKKINA------FKLLNISHINEKYFDISKEFDNIIQLQKHKLTENLN--DLKEIDQYISDKKNI 2338
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2217361438 627 YENIVNyvseanETAEFALNTTDRIYDAVSGIDTQIiyhkDESENLLNQARE 678
Cdd:TIGR01612 2339 FLHALN------ENTNFNFNALKEIYDDIINRENKA----DEIENINNKENE 2380
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
521-764 |
2.41e-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: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 521 ERVREQMEVVNMSLSTSADSLTTPRLTLSELDDIIKnaSGIYAEIDGAKSELQVKLSNLSNLSHDLVQEAIDHAQD---L 597
Cdd:TIGR01612 500 MRMKDFKDIIDFMELYKPDEVPSKNIIGFDIDQNIK--AKLYKEIEAGLKESYELAKNWKKLIHEIKKELEEENEDsihL 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 598 QQEAN---------------------ELSRKLHS-SDMNGLVQKALDASNVYENIVNYVSEANETAEFA----LNTTDRI 651
Cdd:TIGR01612 578 EKEIKdlfdkyleiddeiiyinklklELKEKIKNiSDKNEYIKKAIDLKKIIENNNAYIDELAKISPYQvpehLKNKDKI 657
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 652 YDAVSGIDTQI--------------IYHKDESENLLNQAR--ELQAKAESSSDEAVADTSRRVGGALARKSALKTRLSDA 715
Cdd:TIGR01612 658 YSTIKSELSKIyeddidalynelssIVKENAIDNTEDKAKldDLKSKIDKEYDKIQNMETATVELHLSNIENKKNELLDI 737
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2217361438 716 VKQLQAAERGDaqqrlgqsrlITEEANRTTMEVQQATAPMANNLTNWSQ 764
Cdd:TIGR01612 738 IVEIKKHIHGE----------INKDLNKILEDFKNKEKELSNKINDYAK 776
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
321-611 |
3.06e-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: 49.30 E-value: 3.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 321 LKTKLSEREnQYALRKiQINNAENTMKSLLSDVEELvEKEnQASRKGQLvqkesmdtinhaSQLVEQAHDMRDKIQEINN 400
Cdd:TIGR02169 216 LLKEKREYE-GYELLK-EKEALERQKEAIERQLASL-EEE-LEKLTEEI------------SELEKRLEEIEQLLEELNK 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 401 KMLYYGEEHELSPKE---------------ISEKLVLAQKMLEEirsRQPFFTQRELVDEEADeayELLSQAESWQRlhn 465
Cdd:TIGR02169 280 KIKDLGEEEQLRVKEkigeleaeiaslersIAEKERELEDAEER---LAKLEAEIDKLLAEIE---ELEREIEEERK--- 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 466 ETRTLFPVVLEQLDDYNAKLSDLQEAldqalnyvrDAEdmNRATAARQRDHEKQQERVREQMEVVNMSLSTSADSLTTPR 545
Cdd:TIGR02169 351 RRDKLTEEYAELKEELEDLRAELEEV---------DKE--FAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLS 419
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 546 LTLSELDDIIKNASGIYAEIDGAKSELQVKLS----NLSNLSHDLVQEAIDHaQDLQQEANELSRKLHSS 611
Cdd:TIGR02169 420 EELADLNAAIAGIEAKINELEEEKEDKALEIKkqewKLEQLAADLSKYEQEL-YDLKEEYDRVEKELSKL 488
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
310-766 |
3.47e-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: 48.70 E-value: 3.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 310 HVNEINATIYLLKTKLSERenqyALRKI--QINNAENTMKSLLSDVEELVEKEnqasrkgqlvqKESMDTINHAsqlveq 387
Cdd:pfam06160 68 LLFEAEELNDKYRFKKAKK----ALDEIeeLLDDIEEDIKQILEELDELLESE-----------EKNREEVEEL------ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 388 ahdmRDKIQEINNKMLYYGeeHELSPKEisEKLvlaQKMLEEIRSRqpfFTQRELVDEEAD--EAYELLSQaeswqrLHN 465
Cdd:pfam06160 127 ----KDKYRELRKTLLANR--FSYGPAI--DEL---EKQLAEIEEE---FSQFEELTESGDylEAREVLEK------LEE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 466 ETRTL------FPVVLEQL-DDYNAKLSDLQEALDQAL--NYVRD----AEDMNRATAARQRD----HEKQQERVREQME 528
Cdd:pfam06160 187 ETDALeelmedIPPLYEELkTELPDQLEELKEGYREMEeeGYALEhlnvDKEIQQLEEQLEENlallENLELDEAEEALE 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 529 VVNMSLSTSADSLTTprltlsELD---DIIKNASGIYAEIDGAKS---ELQVKLSNLsNLSHDLVQEAIDHAQDLQQEAN 602
Cdd:pfam06160 267 EIEERIDQLYDLLEK------EVDakkYVEKNLPEIEDYLEHAEEqnkELKEELERV-QQSYTLNENELERVRGLEKQLE 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 603 ELSRKLHSsdmngLVQKALDASNVYENIVNYVSEanetaefalnttdrIYDAVSGIDTQIIYHKDESENLLNQarELQAK 682
Cdd:pfam06160 340 ELEKRYDE-----IVERLEEKEVAYSELQEELEE--------------ILEQLEEIEEEQEEFKESLQSLRKD--ELEAR 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 683 AESSS-DEAVADTSRRVggalaRKSAL-------KTRLSDAVKQLQaaergDAQQRLGQSRLITEEANRttmEVQQATAP 754
Cdd:pfam06160 399 EKLDEfKLELREIKRLV-----EKSNLpglpesyLDYFFDVSDEIE-----DLADELNEVPLNMDEVNR---LLDEAQDD 465
|
490
....*....|..
gi 2217361438 755 MaNNLTNWSQNL 766
Cdd:pfam06160 466 V-DTLYEKTEEL 476
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
313-579 |
4.80e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 4.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 313 EINATIYLLKTKLSERENQyalrKIQINNAENTMKSLLSDVEELVEKENQASRKGQLVQKEsmdtinhasqlVEQAHDMR 392
Cdd:PRK03918 173 EIKRRIERLEKFIKRTENI----EELIKEKEKELEEVLREINEISSELPELREELEKLEKE-----------VKELEELK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 393 DKIQEINNKMlyygEEHELSPKEISEKLVLAQKMLEEIRSRqpfftQRELvDEEADEAYELLSQAESWQRL---HNETRT 469
Cdd:PRK03918 238 EEIEELEKEL----ESLEGSKRKLEEKIRELEERIEELKKE-----IEEL-EEKVKELKELKEKAEEYIKLsefYEEYLD 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 470 LFPVVLEQLDDYNAKLSDLQEALDQALNYVRDAEDMNRATAARQRDHEKQQERVREQMEVvnMSLSTSADSLTTpRLTLS 549
Cdd:PRK03918 308 ELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEA--KAKKEELERLKK-RLTGL 384
|
250 260 270
....*....|....*....|....*....|
gi 2217361438 550 ELDDIIKNasgiYAEIDGAKSELQVKLSNL 579
Cdd:PRK03918 385 TPEKLEKE----LEELEKAKEEIEEEISKI 410
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
882-1013 |
8.34e-05 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 44.23 E-value: 8.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 882 ILYLGSKNaKKEYMGLAIKNDNLVYVYNLGTKDVEIPldSKPVSSwPAYFSIVKIERVGKHGkvFLTV---PSLSSTAEe 958
Cdd:pfam00054 10 LLYNGTQT-ERDFLALELRDGRLEVSYDLGSGAAVVR--SGDKLN-DGKWHSVELERNGRSG--TLSVdgeARPTGESP- 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2217361438 959 kfikkgefSGDDSLLDLDpedTVFYVGGVPSNFKLPTSL-NLPGFVGCLELATLNN 1013
Cdd:pfam00054 83 --------LGATTDLDVD---GPLYVGGLPSLGVKKRRLaISPSFDGCIRDVIVNG 127
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
284-665 |
1.13e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.43 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 284 LRLAALSIEEGKSGVLSVSSGAAAHRHVNEINATIYLLKTKLSERENQYALRKIQINNAENTMKSLLSDVEELvEKENQA 363
Cdd:COG4372 13 LSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL-NEQLQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 364 SRKGQLVQKESMDTINhasqlvEQAHDMRDKIQEINnkmlyygeehelspKEISEKLVLAQKMLEEIRSRQPFFTQRElv 443
Cdd:COG4372 92 AQAELAQAQEELESLQ------EEAEELQEELEELQ--------------KERQDLEQQRKQLEAQIAELQSEIAERE-- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 444 deeaDEAYELLSQAESWQRLhnetrtlfpvvLEQLDDYNAKLSD--LQEALDQALNYVRDAEDMNRATAARQRDHEKQQE 521
Cdd:COG4372 150 ----EELKELEEQLESLQEE-----------LAALEQELQALSEaeAEQALDELLKEANRNAEKEEELAEAEKLIESLPR 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 522 RVREQMEVVNMSLSTSADSLTTPRLTLSELDDIIKNASGIYAEIDGAKSELQVKLSNLSNLSHDLVQEAIDHAQDLQQEA 601
Cdd:COG4372 215 ELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALE 294
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217361438 602 NELSRKLHSSDMNGLVQKALDASNVYENIVNYVSEANETAEFALNTTDRIYDAVSGIDTQIIYH 665
Cdd:COG4372 295 LKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLEL 358
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
311-725 |
3.93e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 45.28 E-value: 3.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 311 VNEINATIYLLKTKLSERENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRkgqlvqkesmdtinhasqLVEQAHD 390
Cdd:PRK01156 199 LENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNR------------------YESEIKT 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 391 MRDKIQEINNKMLYYGEEHELSPKEISEKLVLAQKMLEE-IRSRQPFFTQREL---VDEEADEAYELLSQAESWQRLHNE 466
Cdd:PRK01156 261 AESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDyFKYKNDIENKKQIlsnIDAEINKYHAIIKKLSVLQKDYND 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 467 trtlFPVVLEQLDDYNAKLSDLQEALDQALNYVRDAEDMNRataaRQRDHEKQQERVREQMEVVNMSLSTSADSLTTPRL 546
Cdd:PRK01156 341 ----YIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKK----KIEEYSKNIERMSAFISEILKIQEIDPDAIKKELN 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 547 TL-SELDDIIKNASGIYAEIDGAKSELQVKLSNLSNL-----------------SHDLVQEAIDHAQDLQQEANELSRKL 608
Cdd:PRK01156 413 EInVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLngqsvcpvcgttlgeekSNHIINHYNEKKSRLEEKIREIEIEV 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 609 HSSDMNGLVQKALDASNVYENIVNYVSEANETAEFALNTTDrIYDAVSgidtQIIYHKDESENLLNQAR-----ELQAKA 683
Cdd:PRK01156 493 KDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLED-IKIKIN----ELKDKHDKYEEIKNRYKslkleDLDSKR 567
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2217361438 684 ESSSDEAVADTSRRVGGALARKSALKTRLSDAVKQLQAAERG 725
Cdd:PRK01156 568 TSWLNALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIG 609
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
313-575 |
3.97e-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: 3.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 313 EINATIYLLKTKLSERENQYALRKIQINNAE-NTMKSLLSDVEELVE----KENQASRKGQLVQKESMDTINHASQLVEQ 387
Cdd:TIGR02169 769 ELEEDLHKLEEALNDLEARLSHSRIPEIQAElSKLEEEVSRIEARLReieqKLNRLTLEKEYLEKEIQELQEQRIDLKEQ 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 388 AHDMRDKIQEIN---NKMLYYGEEHELSPKEISEKLVLAQKMLEEIRS--RQPFFTQRELvDEEADEAYELLSQ-AESWQ 461
Cdd:TIGR02169 849 IKSIEKEIENLNgkkEELEEELEELEAALRDLESRLGDLKKERDELEAqlRELERKIEEL-EAQIEKKRKRLSElKAKLE 927
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 462 RLHNETRTLFPVVLEQLDDYNAKLS--DLQEALDQALNYVRDAEDMN-RA------TAARQRDHEKQQERVREQMEvvnm 532
Cdd:TIGR02169 928 ALEEELSEIEDPKGEDEEIPEEELSleDVQAELQRVEEEIRALEPVNmLAiqeyeeVLKRLDELKEKRAKLEEERK---- 1003
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2217361438 533 SLSTSADSLTTPR--LTLSELDDIIKNASGIYAEIDGAKSELQVK 575
Cdd:TIGR02169 1004 AILERIEEYEKKKreVFMEAFEAINENFNEIFAELSGGTGELILE 1048
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
311-609 |
4.45e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 4.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 311 VNEINATIYLLKTKLSERENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLVQKESMDTINHASQLVEQAHD 390
Cdd:COG4372 82 LEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLES 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 391 MRDKIQEINNkmlyygEEHELSPKEISEKLvlaQKMLEEIRSRQPFFTQRELVDEEADEAYELLSQAESwQRLHNETRTL 470
Cdd:COG4372 162 LQEELAALEQ------ELQALSEAEAEQAL---DELLKEANRNAEKEEELAEAEKLIESLPRELAEELL-EAKDSLEAKL 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 471 FPVVLEQLDDYNAKLSDLQEALDQALNYVRDAEDMNRATAARQRDHEKQQERVREQMEVVNMSLSTSAdslTTPRLTLSE 550
Cdd:COG4372 232 GLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLA---LLLNLAALS 308
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2217361438 551 LDDIIKNASGIYAEIDGAKSELQVKLSNLSNLSHDLVQEAIDHAQDLQQEANELSRKLH 609
Cdd:COG4372 309 LIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGV 367
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
366-682 |
8.13e-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: 43.92 E-value: 8.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 366 KGQLVQKESMDTINHASQLVEQAHDMRDKIQEINnkmlyygeehelspKEISEKLVLAQKMLEEIRSRqpfftqRELVDE 445
Cdd:pfam04108 4 SAQDLCRWANELLTDARSLLEELVVLLAKIAFLR--------------RGLSVQLANLEKVREGLEKV------LNELKK 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 446 EADEAYELLSQA-ESWQR-LHNETRTLFPVVLEQLDDYNAKLSDL--QEALDQALNYVRdaedmnrataarqrdheKQQE 521
Cdd:pfam04108 64 DFKQLLKDLDAAlERLEEtLDKLRNTPVEPALPPGEEKQKTLLDFidEDSVEILRDALK-----------------ELID 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 522 RVREQMEvvnmSLSTSADSLTTprlTLSELDDIIKNASGIYAEIDGAKSELQvklsNLSNLSHDLVQ--EAIDHAQDLQQ 599
Cdd:pfam04108 127 ELQAAQE----SLDSDLKRFDD---DLRDLQKELESLSSPSESISLIPTLLK----ELESLEEEMASllESLTNHYDQCV 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 600 EANELSRKLHSSDMNGLVQKALDASNVYENIVNYVSEANETAEFALNTTDRIYDAvsgidtqiiyhKDESENLLNQAREL 679
Cdd:pfam04108 196 TAVKLTEGGRAEMLEVLENDARELDDVVPELQDRLDEMENNYERLQKLLEQKNSL-----------IDELLSALQLIAEI 264
|
...
gi 2217361438 680 QAK 682
Cdd:pfam04108 265 QSR 267
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
476-679 |
9.60e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.85 E-value: 9.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 476 EQLDDYNAKLSDLQEALDQALNYVRDAEDMNRATAarqRDHEKQQERVREQMEVVNMSLSTSADSLTTPRLTLSELDDII 555
Cdd:PHA02562 195 QQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEA---KTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKI 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 556 KNASGI----------------YAEIDGAKSELQVKLSNLsNLSHDLVQEAIDHAQDLQQEANELSRKLHssDMNGlvqk 619
Cdd:PHA02562 272 EQFQKVikmyekggvcptctqqISEGPDRITKIKDKLKEL-QHSLEKLDTAIDELEEIMDEFNEQSKKLL--ELKN---- 344
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 620 alDASNVYENIVNYVSEAnetaefalnttDRIYDAVSGIDTQIIYHKDESENLLNQAREL 679
Cdd:PHA02562 345 --KISTNKQSLITLVDKA-----------KKVKAAIEELQAEFVDNAEELAKLQDELDKI 391
|
|
| VSP |
pfam03302 |
Giardia variant-specific surface protein; |
87-212 |
1.00e-03 |
|
Giardia variant-specific surface protein;
Pssm-ID: 146106 [Multi-domain] Cd Length: 397 Bit Score: 43.80 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 87 NSNECLDGSGYCVHCQRNTTgehCEKCLDGYIGDSirgapQFCQPCpcplphlanfAESCYRKNGAVRcicnenyagpNC 166
Cdd:pfam03302 252 NNGDLVTCSPGCKTCTSNTV---CTTCMDGYVKTS-----DSCTKC----------DSSCETCTGATT----------TC 303
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2217361438 167 ERCAPGYYGNplliGSTCKKCDCSgNSDPNLIfedcdEVTGqCRNC 212
Cdd:pfam03302 304 KTCATGYYKS----GTGCVSCTSS-ESDNGIT-----GVKG-CLNC 338
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
666-824 |
1.39e-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: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 666 KDESENLLNQARELQAK-AESSSDEAVADTSRR--------VGGAlaRKSALKTRLSDAVKQLQAAE--RGDAQQRLGQS 734
Cdd:COG4913 294 EAELEELRAELARLEAElERLEARLDALREELDeleaqirgNGGD--RLEQLEREIERLERELEERErrRARLEALLAAL 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 735 RLiTEEANRTTMEVQQATAPMAnnLTNWSQnlqhfDSSAYNTAVNSARDAVRNLTEVVPQLLDQLRTVEQKRpaSNVSAS 814
Cdd:COG4913 372 GL-PLPASAEEFAALRAEAAAL--LEALEE-----ELEALEEALAEAEAALRDLRRELRELEAEIASLERRK--SNIPAR 441
|
170
....*....|
gi 2217361438 815 IQRIRELIAQ 824
Cdd:COG4913 442 LLALRDALAE 451
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
323-550 |
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 2217361438 323 TKLSERENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLVQKEsMDT----INHASQLVEQAhdmRDKIQEI 398
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAE-IDKlqaeIAEAEAEIEER---REELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 399 NNKMlyYGEEHELSPKEIseklVLAQKMLEEirsrqpFFTQRELVDEEADEAYELLSQAESWQRLHNETRTLfpvVLEQL 478
Cdd:COG3883 92 ARAL--YRSGGSVSYLDV----LLGSESFSD------FLDRLSALSKIADADADLLEELKADKAELEAKKAE---LEAKL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217361438 479 DDYNAKLSDLQEALDQALNYVRDAEDMNRATAARQRDHEKQQERVREQMEVVNMSLSTSADSLTTPRLTLSE 550
Cdd:COG3883 157 AELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
405-608 |
1.77e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 405 YGEEHELSPKEISEKLvlaqKMLEEIRSRQpffTQRELVDEEADEAYELLSQAESWQRLHNETRTLFPVVLEQLDDYN-- 482
Cdd:COG4717 328 LGLPPDLSPEELLELL----DRIEELQELL---REAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQel 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 483 -AKLSDLQEALDQALNYVRDAEDMNrataarqrdhekQQERVREQMEVVNMSLSTSADSLTTPRLTLSELDDIIKNA--S 559
Cdd:COG4717 401 kEELEELEEQLEELLGELEELLEAL------------DEEELEEELEELEEELEELEEELEELREELAELEAELEQLeeD 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 560 GIYAEIDGAKSELQVKLSNLS------NLSHDLVQEAIDHAQD-----LQQEANELSRKL 608
Cdd:COG4717 469 GELAELLQELEELKAELRELAeewaalKLALELLEEAREEYREerlppVLERASEYFSRL 528
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
476-687 |
2.14e-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: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 476 EQLDDYNAKLSDLQEALD--QALNYVRDAEDMNRATAARQRDHEKQQERVREQMEVVNMSLSTSADSLTTPRLTLSELdd 553
Cdd:COG3206 182 EQLPELRKELEEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL-- 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 554 iikNASGIYAEIDGAKSELQVKLSNLSNL---SHDLVQEAIDHAQDLQQE-ANELSRKLHS--SDMNGLVQKALDASNVY 627
Cdd:COG3206 260 ---LQSPVIQQLRAQLAELEAELAELSARytpNHPDVIALRAQIAALRAQlQQEAQRILASleAELEALQAREASLQAQL 336
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 628 ENIVNYVSEANETaEFALNTTDRIYDAvsgidTQIIYhkdesENLLNQARELQAKAESSS 687
Cdd:COG3206 337 AQLEARLAELPEL-EAELRRLEREVEV-----ARELY-----ESLLQRLEEARLAEALTV 385
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
324-458 |
2.90e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.82 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 324 KLSERENQYALRKiQINNAENTMKSLLSDVEELVEKENQASRK-GQLVQK-----ESMDTI-NHASQLVEQAHDMRDKIQ 396
Cdd:COG1340 141 KIKELEKELEKAK-KALEKNEKLKELRAELKELRKEAEEIHKKiKELAEEaqelhEEMIELyKEADELRKEADELHKEIV 219
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217361438 397 EINNKMlyyGEEHEL------SPKEISEKLVLAQKMLEEIRSRQpfftQRELVDEEADEAYELLSQAE 458
Cdd:COG1340 220 EAQEKA---DELHEEiielqkELRELRKELKKLRKKQRALKREK----EKEELEEKAEEIFEKLKKGE 280
|
|
| DivIVA |
pfam05103 |
DivIVA protein; The Bacillus subtilis divIVA1 mutation causes misplacement of the septum ... |
383-467 |
5.03e-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: 5.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 383 QLVEQAHDMRDKIQEINNKMLYYGEEHElspkEISEKLVLAQKMLEEIRSRQPffTQRELVDEEA-DEAYELLSQAES-W 460
Cdd:pfam05103 36 ALIRENAELKEKIEELEEKLAHYKNLEE----TLQNTLILAQETAEEVKANAQ--KEAELIIKEAeAKAERIVDDANNeV 109
|
....*..
gi 2217361438 461 QRLHNET 467
Cdd:pfam05103 110 KKINDEI 116
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
346-607 |
5.98e-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: 5.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 346 MKSLlSDVEELVekenqasRKGQLVQKESMDTINHASQLVEQAHDMRDKIQEINNKMlyygeehelspkeiseklvlaqK 425
Cdd:COG4913 203 FKPI-GDLDDFV-------REYMLEEPDTFEAADALVEHFDDLERAHEALEDAREQI----------------------E 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 426 MLEEIRSRQpffTQRELVDEEADEAYELLSQAESWQR------LHNETRTLfpvvLEQLDDYNAKLSDLQEALDQALNYV 499
Cdd:COG4913 253 LLEPIRELA---ERYAAARERLAELEYLRAALRLWFAqrrlelLEAELEEL----RAELARLEAELERLEARLDALREEL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 500 RDAE----------------DMNRATAARQRdHEKQQERVREQMEVVNMSLSTSADslttprltlsELDDIIKNASGIYA 563
Cdd:COG4913 326 DELEaqirgnggdrleqlerEIERLERELEE-RERRRARLEALLAALGLPLPASAE----------EFAALRAEAAALLE 394
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2217361438 564 EIDGAKSELQVKLSNLSNLSHDLVQEaidhAQDLQQEANELSRK 607
Cdd:COG4913 395 ALEEELEALEEALAEAEAALRDLRRE----LRELEAEIASLERR 434
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
414-693 |
6.50e-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: 6.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 414 KEISEKLVLAQKMLEEIRsrqpffTQRELVDEEADEAYELLSQAES---WQRLHNETRTLfPVVLEQLDDYNAKLSDLQE 490
Cdd:COG4913 620 AELEEELAEAEERLEALE------AELDALQERREALQRLAEYSWDeidVASAEREIAEL-EAELERLDASSDDLAALEE 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 491 ALDQALNYVRDAEDMNRATAARQRDHEKQQERVREQMEVVNMSLST-SADSLTTPRLTLSE-LDDIIKNASG------IY 562
Cdd:COG4913 693 QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAaEDLARLELRALLEErFAAALGDAVErelrenLE 772
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 563 AEIDGAKSELQVKLSNLSNLSHDLVQEAIDHAQDLQ------QEANELSRKLHSSDMNGLVQKALDA--SNVYENIVNYV 634
Cdd:COG4913 773 ERIDALRARLNRAEEELERAMRAFNREWPAETADLDadleslPEYLALLDRLEEDGLPEYEERFKELlnENSIEFVADLL 852
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2217361438 635 SEANETAEFALNTTDRIYDAVSGIDtqiiYHKDesenllnqaRELQAKAESSSDEAVAD 693
Cdd:COG4913 853 SKLRRAIREIKERIDPLNDSLKRIP----FGPG---------RYLRLEARPRPDPEVRE 898
|
|
| TNFRSF6_teleost |
cd13423 |
Tumor necrosis factor receptor superfamily member 6 (TNFRSF6) in teleosts; also known as fas ... |
157-249 |
7.88e-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: 37.79 E-value: 7.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 157 CNENYAGPNCERCAPGYYGNPLLIGSTCKKCD-CSGNSdpNLIFED-CdeVTGQCRNClrnttgfkceRCAPGYYGDARi 234
Cdd:cd13423 27 CTNNGTDGECEACEDGTYNSHPNSLDSCEPCTsCDPNA--NLEVEErC--TPSSDTVC----------RCKEGHYCDKG- 91
|
90
....*....|....*
gi 2217361438 235 aKNCAVCNcgggPCD 249
Cdd:cd13423 92 -EECKVCY----PCD 101
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
476-607 |
8.38e-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: 8.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361438 476 EQLDDYNAKLSDLQEALDQALNYVRDAEDMNRATAARQRDHEKQQERVREQMEVVNMSlstsaDSLTTPRLTLSELDDII 555
Cdd:COG1579 38 DELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEALQ-----KEIESLKRRISDLEDEI 112
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2217361438 556 KNasgIYAEIDGAKSELQVKLSNLSNLSHDL--VQEAIDHA-QDLQQEANELSRK 607
Cdd:COG1579 113 LE---LMERIEELEEELAELEAELAELEAELeeKKAELDEElAELEAELEELEAE 164
|
|
| |
