|
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 |
1.47e-97 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 315.12 E-value: 1.47e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 298 VLSVSSGAAAHRHVNEINATIYLLKTKLSERENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLIQKESMDT 377
Cdd:pfam06008 1 LLSLNSLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 378 IKHASQLVEQAHDMRDKIQEINNKMLYYGEE-HELSPKEISEKLVLAQKMLEEIRRRQpFFTQRELVDEEADEAHELLSQ 456
Cdd:pfam06008 81 LGHAKELAEAIKNLIDNIKEINEKVATLGENdFALPSSDLSRMLAEAQRMLGEIRSRD-FGTQLQNAEAELKAAQDLLSR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 457 AESW-QRLHNETRTLFPVVLEQLDDYNAKLSDLQEALDQALNHVRDAEDMNRATAARQRDHEKQQERVREQMEAVNMSLN 535
Cdd:pfam06008 160 IQTWfQSPQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEETLK 239
|
250
....*....|....*....
gi 1622930177 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 |
5.63e-44 |
|
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 368703 [Multi-domain] Cd Length: 138 Bit Score: 156.49 E-value: 5.63e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 734 SRLITEEANRTTMEVQQATAPMANNLTNWSQNLQHFDSSA---------YNTAVDSARDAVRNLTEVVPQLLDQLRTVEQ 804
Cdd:pfam06009 1 SKELAREANETAKEVLEQLAPLSQNLENTSEKLSGINRSLeetnelvndANKALDDAGRSVKKLEELAPDLLDKLKPLKQ 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622930177 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 |
3.54e-40 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 146.02 E-value: 3.54e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 1492 KSQFSIRLRTRSSHGMIFYVSDQEENDFMTLFLAHGRLVYMFNVGHKKLKIRSQEKYNDGLWHDVVFIRERSSGRLVIDG 1571
Cdd:cd00110 21 RLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDGQWHSVSVERNGRSVTLSVDG 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1622930177 1572 LRVLEESLPPTEATWKIKGPIYLGGVAPGKavKNVQINSIYSFSGCLSNLQLN 1624
Cdd:cd00110 101 ERVVESGSPGGSALLNLDGPLYLGGLPEDL--KSPGLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
1494-1625 |
2.06e-36 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 134.77 E-value: 2.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 1494 QFSIRLRTRSSHGMIFYVSDQEENDFMTLFLAHGRLVYMFNVGHKKLKIRSQ-EKYNDGLWHDVVFIRERSSGRLVIDGL 1572
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDpTPLNDGQWHRVAVERNGRSVTLSVDGG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1622930177 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 1622930177 1648 GTYFStEGGYVVLDESFNIGLKFEIAFEVRPRSSSGTLVH-GHSVNGEYLNVHMKNGQVIVKVNNGirDFSTSVTPKQSL 1726
Cdd:cd00110 1 GVSFS-GSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYaGSQNGGDFLALELEDGRLVLRYDLG--SGSLVLSSKTPL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622930177 1727 CDGRWHRITVIRDSNVVQLDVDSE-VNHVVGPLNPKPIDHREPVFVGGVPESLLTPRLAPSKPFTGCIRHFVID 1799
Cdd:cd00110 78 NDGQWHSVSVERNGRSVTLSVDGErVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
1671-1801 |
3.75e-31 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 119.75 E-value: 3.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 1671 EIAFEVRPRSSSGTLVHGHSVNG-EYLNVHMKNGQVIVKVNNGIRDFSTSVTPKQsLCDGRWHRITVIRDSNVVQLDVDS 1749
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGgDYLALELRDGRLVLRYDLGSGPARLTSDPTP-LNDGQWHRVAVERNGRSVTLSVDG 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1622930177 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 |
2.49e-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: 2.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 1499 LRTRSSHGMIFYVSDQEeNDFMTLFLAHGRLVYMFNVGHKKLKIRSQEK-YNDGLWHDVVFIRERSSGRLVIDGLRVLEE 1577
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGG-SDFLALELVNGRLVLRYDLGSGPESLLSSGKnLNDGQWHSVRVERNGNTLTLSVDGQTVVSS 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1622930177 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 |
1.57e-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: 1.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 1676 VRPRSSSGTLVHGHSVNGEYLNVHMKNGQVIVKVNNGIRDFSTSVTPKqSLCDGRWHRITVIRDSNVVQLDVDSEVNH-V 1754
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDFLALELVNGRLVLRYDLGSGPESLLSSGK-NLNDGQWHSVRVERNGNTLTLSVDGQTVVsS 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1622930177 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 |
1.05e-22 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 96.33 E-value: 1.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 1049 SYFFDGSGYAAVRDitkRGKFGQVTRFDIEVRTPADNSLILLM--VNGSMFFRLEMRNGYLHVFYDFGfsSGPVHLEDtl 1126
Cdd:cd00110 1 GVSFSGSSYVRLPT---LPAPRTRLSISFSFRTTSPNGLLLYAgsQNGGDFLALELEDGRLVLRYDLG--SGSLVLSS-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 1127 kKAQINDAKYHEISIIyHNDKKMILVVDR-RHVKSMDNEKMKI--PFTDIYIGGAPPEILQSRTLRAHlpldiNFRGCMK 1203
Cdd:cd00110 74 -KTPLNDGQWHSVSVE-RNGRSVTLSVDGeRVVESGSPGGSALlnLDGPLYLGGLPEDLKSPGLPVSP-----GFVGCIR 146
|
....
gi 1622930177 1204 GFQF 1207
Cdd:cd00110 147 DLKV 150
|
|
| LamG |
smart00282 |
Laminin G domain; |
1074-1210 |
2.60e-21 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 91.63 E-value: 2.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 1074 RFDIEVRTPADNSLILLM--VNGSMFFRLEMRNGYLHVFYDFGfsSGPVHLedTLKKAQINDAKYHEISIIyHNDKKMIL 1151
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAgsKGGGDYLALELRDGRLVLRYDLG--SGPARL--TSDPTPLNDGQWHRVAVE-RNGRSVTL 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622930177 1152 VVD---RRHVKSMDNEKMKIPFTDIYIGGAPPEILQSRTLRAHlpldiNFRGCMKGFQFQKK 1210
Cdd:smart00282 76 SVDggnRVSGESPGGLTILNLDGPLYLGGLPEDLKLPPLPVTP-----GFRGCIRNLKVNGK 132
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
1237-1376 |
6.77e-20 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 88.24 E-value: 6.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 1237 AYFNGQSFIASIQKISFFDGFEGGFNFRTLQPNGLLFYYASG--SDVFSISLDNGTVVMDV----KGIKVESvDKQYNDG 1310
Cdd:cd00110 2 VSFSGSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQngGDFLALELEDGRLVLRYdlgsGSLVLSS-KTPLNDG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622930177 1311 LSHFVITSVSPTRYELIVDKSRVGSKNPTKGKIEQTQagEKKFYFGGSPISAQ------YANFTGCISNAYF 1376
Cdd:cd00110 81 QWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNL--DGPLYLGGLPEDLKspglpvSPGFVGCIRDLKV 150
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
1079-1207 |
7.33e-20 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 87.09 E-value: 7.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 1079 VRTPADNSLIL-LMVNGSMFFRLEMRNGYLHVFYDFGfsSGPVHLedTLKKAQINDAKYHEISIIYhNDKKMILVVDRRH 1157
Cdd:pfam02210 1 FRTRQPNGLLLyAGGGGSDFLALELVNGRLVLRYDLG--SGPESL--LSSGKNLNDGQWHSVRVER-NGNTLTLSVDGQT 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1622930177 1158 VKSMDNEKMKIPF---TDIYIGGAPPeilqsRTLRAHLPLDINFRGCMKGFQF 1207
Cdd:pfam02210 76 VVSSLPPGESLLLnlnGPLYLGGLPP-----LLLLPALPVRAGFVGCIRDVRV 123
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
1263-1376 |
4.57e-18 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 82.08 E-value: 4.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 1263 FRTLQPNGLLFYYASG-SDVFSISLDNGTVVMDVK----GIKVESVDKQYNDGLSHFVITSVSPTRYELIVDKSRVGSKN 1337
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGgSDFLALELVNGRLVLRYDlgsgPESLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1622930177 1338 PTKGKIEQTQagEKKFYFGG------SPISAQYANFTGCISNAYF 1376
Cdd:pfam02210 81 PPGESLLLNL--NGPLYLGGlpplllLPALPVRAGFVGCIRDVRV 123
|
|
| LamG |
smart00282 |
Laminin G domain; |
860-1013 |
5.39e-18 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 82.00 E-value: 5.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 860 SLSLYMKppvrqpelTETADQFILYLGSKNaKKEYMGLAIKNDNLVYIYNLGTKDVEIPLDSKPVSswPAYFSIVKIERV 939
Cdd:smart00282 1 SISFSFR--------TTSPNGLLLYAGSKG-GGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLN--DGQWHRVAVERN 69
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622930177 940 GKHgkVFLTVPSLSSTAEEKFIKKgefsgddSLLDLDpedTVFYVGGVPSNFKLPNSLNLPGFVGCLELATLNN 1013
Cdd:smart00282 70 GRS--VTLSVDGGNRVSGESPGGL-------TILNLD---GPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNG 131
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
835-1012 |
9.01e-18 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 82.08 E-value: 9.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 835 SMMFDGQSAVEVhsrTSMDDLKAFTSLSLYMKppvrqpelTETADQFILYLGSKNaKKEYMGLAIKNDNLVYIYNLGTKD 914
Cdd:cd00110 1 GVSFSGSSYVRL---PTLPAPRTRLSISFSFR--------TTSPNGLLLYAGSQN-GGDFLALELEDGRLVLRYDLGSGS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 915 VEIpldSKPVSSWPAYFSIVKIERVGKHgkVFLTVPSLSStaeekfikkGEFSGDDSLLDLDPEDTVfYVGGVPSNFKLP 994
Cdd:cd00110 69 LVL---SSKTPLNDGQWHSVSVERNGRS--VTLSVDGERV---------VESGSPGGSALLNLDGPL-YLGGLPEDLKSP 133
|
170
....*....|....*...
gi 1622930177 995 NSLNLPGFVGCLELATLN 1012
Cdd:cd00110 134 GLPVSPGFVGCIRDLKVN 151
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
187-238 |
8.67e-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: 8.67e-16
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1622930177 187 CDCSGNSDPNlifEDCDEVTGQCRnCLRNTTGFKCERCAPGYYGDARIAKNC 238
Cdd:cd00055 2 CDCNGHGSLS---GQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGGC 49
|
|
| LamG |
smart00282 |
Laminin G domain; |
1261-1379 |
1.23e-15 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 75.07 E-value: 1.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 1261 FNFRTLQPNGLLFYYAS--GSDVFSISLDNGTVVMDVKG----IKVESVDKQYNDGLSHFVITSVSPTRYELIVDksrvg 1334
Cdd:smart00282 4 FSFRTTSPNGLLLYAGSkgGGDYLALELRDGRLVLRYDLgsgpARLTSDPTPLNDGQWHRVAVERNGRSVTLSVD----- 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1622930177 1335 SKNPTKGKIEQTQAG---EKKFYFGGSP------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 |
5.35e-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: 5.35e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1622930177 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 ... |
132-185 |
8.36e-13 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 64.30 E-value: 8.36e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1622930177 132 CPCPlPHlANFAESCYRKNGavRCICKENYAGPNCERCAPGYYGNPlLIGSTCK 185
Cdd:cd00055 2 CDCN-GH-GSLSGQCDPGTG--QCECKPNTTGRRCDRCAPGYYGLP-SQGGGCQ 50
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
325-821 |
1.03e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 73.54 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 325 LSERENQYALRKIQINNAE--------NTMKSLLSDVEELVEKENQasrkgqliQKESMDTIKHASQLVEQAHdmRDKIQ 396
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEEKEekdlherlNGLESELAELDEEIERYEE--------QREQARETRDEADEVLEEH--EERRE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 397 EInnkmlyygEEHELSPKEISEKLVLAQKMLEEIRRRqpFFTQRELVDEEADEAHELLSQAEsWQRLHNETrtlfpvVLE 476
Cdd:PRK02224 252 EL--------ETLEAEIEDLRETIAETEREREELAEE--VRDLRERLEELEEERDDLLAEAG-LDDADAEA------VEA 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 477 QLDDYNAKLSDLQEALDQALNHVRDAEdmNRATAARQR--DHEKQQERVREQMEAVNMSLNTSADSLTTPRLTLSELDDI 554
Cdd:PRK02224 315 RREELEDRDEELRDRLEECRVAAQAHN--EEAESLREDadDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 555 IKNASGIYA----EIDGAKNELQVKLSNLSNLSHDL---------VQEAIDHAQELQQEAN------------------- 602
Cdd:PRK02224 393 IEELRERFGdapvDLGNAEDFLEELREERDELREREaeleatlrtARERVEEAEALLEAGKcpecgqpvegsphvetiee 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 603 ------ELSRKLhsSDMNGLVQKALDASNVYENIVNYVSEANETAEFALNTTDRIYDAVSGIDTQiiyhKDESENLLNQA 676
Cdd:PRK02224 473 drerveELEAEL--EDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEK----RERAEELRERA 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 677 RELQAKAESSSDEAV-----ADTSRRVGGAL-ARKSALKTRLsDAVKQL--QAAERGDAQQRLGqsRLITEEANRTTMEV 748
Cdd:PRK02224 547 AELEAEAEEKREAAAeaeeeAEEAREEVAELnSKLAELKERI-ESLERIrtLLAAIADAEDEIE--RLREKREALAELND 623
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622930177 749 QQatapmANNLTNWSQNLQHFDSSAYNTAVDSARDAVRNLTEVVPQLLDQLRTVEQKRPA-----SNVSASIQRIREL 821
Cdd:PRK02224 624 ER-----RERLAEKRERKRELEAEFDEARIEEAREDKERAEEYLEQVEEKLDELREERDDlqaeiGAVENELEELEEL 696
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
132-184 |
2.02e-12 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 63.14 E-value: 2.02e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1622930177 132 CPCPlpHLANFAESCYRKNGavRCICKENYAGPNCERCAPGYYGNPLLIGSTC 184
Cdd:pfam00053 1 CDCN--PHGSLSDTCDPETG--QCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
132-177 |
3.38e-12 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 62.71 E-value: 3.38e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1622930177 132 CPCPLPHlaNFAESCYRKNGavRCICKENYAGPNCERCAPGYYGNP 177
Cdd:smart00180 1 CDCDPGG--SASGTCDPDTG--QCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
187-231 |
4.67e-12 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 61.94 E-value: 4.67e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1622930177 187 CDCS--GNSDPnlifeDCDEVTGQCRnCLRNTTGFKCERCAPGYYGD 231
Cdd:smart00180 1 CDCDpgGSASG-----TCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD 41
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
321-647 |
4.70e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 71.63 E-value: 4.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 321 LKTKLSERENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLIQKESMDTIKHASQLVEQA--HDMRDKIQEI 398
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKqiLRERLANLER 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 399 NNKML-YYGEEHELSPKEISEKLVLAQKMLEEIRrrqpffTQRELVDEEADEAHELLSQAESwqrlHNETRTlfpvvlEQ 477
Cdd:TIGR02168 317 QLEELeAQLEELESKLDELAEELAELEEKLEELK------EELESLEAELEELEAELEELES----RLEELE------EQ 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 478 LDDYNAKLSDLQEALDQALNHVRDAED-MNRATAARQRDHEKQQERVRE----QMEAVNMSLNTSADSLTTprlTLSELD 552
Cdd:TIGR02168 381 LETLRSKVAQLELQIASLNNEIERLEArLERLEDRRERLQQEIEELLKKleeaELKELQAELEELEEELEE---LQEELE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 553 DIIKNASGIYAEIDGAKNELQVKLSNLSNLSH--DLVQEAIDHAQELQQEANELsrKLHSSDMNGLVQKALDASNV---Y 627
Cdd:TIGR02168 458 RLEEALEELREELEEAEQALDAAERELAQLQArlDSLERLQENLEGFSEGVKAL--LKNQSGLSGILGVLSELISVdegY 535
|
330 340
....*....|....*....|....*....
gi 1622930177 628 E---------NIVNYVSEANETAEFALNT 647
Cdd:TIGR02168 536 EaaieaalggRLQAVVVENLNAAKKAIAF 564
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
81-130 |
1.68e-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: 60.83 E-value: 1.68e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1622930177 81 PCDCNGN---SNECLDGSGFCvHCQRNTTGEHCEKCLDGYIGDSIRGAPrfCQ 130
Cdd:cd00055 1 PCDCNGHgslSGQCDPGTGQC-ECKPNTTGRRCDRCAPGYYGLPSQGGG--CQ 50
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
875-1013 |
1.54e-10 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 60.51 E-value: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 875 TETADQFILYLGSKnaKKEYMGLAIKNDNLVYIYNLGTKDVEIPLDSKPVS--SWpayfSIVKIERVGKHgkVFLTVPSL 952
Cdd:pfam02210 3 TRQPNGLLLYAGGG--GSDFLALELVNGRLVLRYDLGSGPESLLSSGKNLNdgQW----HSVRVERNGNT--LTLSVDGQ 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622930177 953 SSTAEEKfikkgefSGDDSLLDLDpedTVFYVGGVPSNFKLPNSLNLPGFVGCLELATLNN 1013
Cdd:pfam02210 75 TVVSSLP-------PGESLLLNLN---GPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVNG 125
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
321-743 |
2.54e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.73 E-value: 2.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 321 LKTKLSERENQYALRKIQinNAENTMKSLLSDVEELVEKENQASRKGQLIQKESMDTIKHASQLVEQAHDMRDKIQEINN 400
Cdd:COG1196 218 LKEELKELEAELLLLKLR--ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 401 KMLyyGEEHELSPKEisEKLVLAQKMLEEIRRRqpfftQRELVDEEADEAHELLSQAESWQRLHNETRTLfpvvLEQLDD 480
Cdd:COG1196 296 ELA--RLEQDIARLE--ERRRELEERLEELEEE-----LAELEEELEELEEELEELEEELEEAEEELEEA----EAELAE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 481 YNAKLSDLQEALDQALNHVRDAEDMNRATAARQRDHEKQQERVREQMEAVNMSLNTSADSLTTPRLTLSELDDIIKNASG 560
Cdd:COG1196 363 AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 561 IYAEIDGAKNELQVKLSNLSNLSHDLVQEAIDHAQELQQEANELSRKLHSSDMnglvqkALDASNVYENIVNYVSEANET 640
Cdd:COG1196 443 ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL------LLEAEADYEGFLEGVKAALLL 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 641 AEFALnttdriydaVSGIDTQIIYHKDESENLLNQARELQAKAESSSDEAVADtsRRVGGALARKSALKTRL-SDAVKQL 719
Cdd:COG1196 517 AGLRG---------LAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAA--AAIEYLKAAKAGRATFLpLDKIRAR 585
|
410 420
....*....|....*....|....
gi 1622930177 720 QAAERGDAQQRLGQSRLITEEANR 743
Cdd:COG1196 586 AALAAALARGAIGAAVDLVASDLR 609
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
82-129 |
2.50e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 54.67 E-value: 2.50e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1622930177 82 CDCNGN---SNECLDGSGFCvHCQRNTTGEHCEKCLDGYIGDSIrGAPRFC 129
Cdd:pfam00053 1 CDCNPHgslSDTCDPETGQC-LCKPGVTGRHCDRCKPGYYGLPS-DPPQGC 49
|
|
| TNFRSF16 |
cd13416 |
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 ... |
65-257 |
2.66e-09 |
|
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 neurotrophin receptor (p75NTR) or CD271; TNFRSF16 (also known as nerve growth factor receptor (NGFR) or p75 neurotrophin receptor (p75NTR or p75(NTR)), CD271, Gp80-LNGFR) is a common receptor for both neurotrophins and proneurotrophins, and plays a diverse role in many tissues, including the nervous system. It has been shown to be expressed in various types of stem cells and has been used to prospectively isolate stem cells with different degrees of potency. p75NTR owes its signaling to the recruitment of intracellular binding proteins, leading to the activation of different signaling pathways. It binds nerve growth factor (NGF) and the complex can initiate a signaling cascade which has been associated with both neuronal apoptosis and neuronal survival of discrete populations of neurons, depending on the presence or absence of intracellular signaling molecules downstream of p75NTR (e.g. NF-kB, JNK, or p75NTR intracellular death domain). p75NTR can also bind NGF in concert with the neurotrophic tyrosine kinase receptor type 1 (TrkA) protein where it is thought to modulate the formation of the high-affinity neurotrophin binding complex. On melanoma cell, p75NTR is an immunosuppressive factor, induced by interferon (IFN)-gamma, and mediates down-regulation of melanoma antigens. It can interact with the aggregated form of amyloid beta (Abeta) peptides, and plays an important role in etiopathogenesis of Alzheimer's disease by influencing protein tau hyper-phosphorylation. p75(NTR) is involved in the formation and progression of retina diseases; its expression is induced in retinal pigment epithelium (RPE) cells and its knockdown rescues RPE cell proliferation activity and inhibits RPE apoptosis induced by hypoxia. It can therefore be a potential therapeutic target for RPE hypoxia or oxidative stress diseases.
Pssm-ID: 276921 [Multi-domain] Cd Length: 159 Bit Score: 57.70 E-value: 2.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 65 EKCNAGFFRTlSGECvpCDcngnsnECLDGSGFCVHCQRNTTGehCEKCLDGYIGDSIRGAPRFCQLC-PCPlpHLANFA 143
Cdd:cd13416 1 EACPSGQYTS-SGEC--CE------QCPPGEGVARPCGDNQTV--CEPCLDGVTFSDVVSHTEPCQPCtRCP--GLMSMR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 144 ESCYRKNGAVrcickenyagpnCErCAPGYYGNPLliGSTCKKCDCsgnsdpnlifedCDEVTGQCRNC--LRNTtgfKC 221
Cdd:cd13416 68 APCTATHDTV------------CE-CAYGYYLDED--SGTCEPCTV------------CPPGQGVVQSCgpNQDT---VC 117
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1622930177 222 ERCAPGYYGDARIAKN----CAVCncggGPCDSVTGECLE 257
Cdd:cd13416 118 EACPEGTYSDEDSSTDpclpCTVC----EDGEVELRECTP 153
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
82-121 |
4.05e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 53.85 E-value: 4.05e-09
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1622930177 82 CDCNGN---SNECLDGSGFCvHCQRNTTGEHCEKCLDGYIGDS 121
Cdd:smart00180 1 CDCDPGgsaSGTCDPDTGQC-ECKPNVTGRRCDRCAPGYYGDG 42
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
415-855 |
1.08e-07 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 57.14 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 415 EISEKLVLAQKmlEEIRRRQpfftqrelvdeeadEAHELLSQA--ESWQ---RLHNETRTLFPVVLEQLDDYNAKLSDLQ 489
Cdd:NF041483 696 EAAEALAAAQE--EAARRRR--------------EAEETLGSAraEADQereRAREQSEELLASARKRVEEAQAEAQRLV 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 490 EALDQ-ALNHVRDAEDmnraTAARQRD-----HEKQQERVREQMEAVNMSlntsADSltTPRLTLSELDDIIKNAsgiYA 563
Cdd:NF041483 760 EEADRrATELVSAAEQ----TAQQVRDsvaglQEQAEEEIAGLRSAAEHA----AER--TRTEAQEEADRVRSDA---YA 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 564 EIDGA-------KNELQVKLSNLSNLSHDLVQEAIDHAQELQQEANELSRKLHSSDMNGLVQKALDASNVYenivnyvSE 636
Cdd:NF041483 827 ERERAsedanrlRREAQEETEAAKALAERTVSEAIAEAERLRSDASEYAQRVRTEASDTLASAEQDAARTR-------AD 899
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 637 ANETAefalnttDRI-YDAVSGIDTQIIYHKDESENLLNQARelqAKAESSSDEAVADTSRRVGGALARKSALKTRLSDA 715
Cdd:NF041483 900 AREDA-------NRIrSDAAAQADRLIGEATSEAERLTAEAR---AEAERLRDEARAEAERVRADAAAQAEQLIAEATGE 969
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 716 VKQL--QAAER-GDAQQRLGQSRlitEEANRTTMEvqqaTAPMANNLTNWSQN-----LQHFDSSAYNTAVDSARDAVRN 787
Cdd:NF041483 970 AERLraEAAETvGSAQQHAERIR---TEAERVKAE----AAAEAERLRTEAREeadrtLDEARKDANKRRSEAAEQADTL 1042
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622930177 788 LTEVVPQlLDQLRTVEQKRPASNVSASIQRIRELIAQTRSVASKIQVSMMFDGQSAVEvHSRTSMDDL 855
Cdd:NF041483 1043 ITEAAAE-ADQLTAKAQEEALRTTTEAEAQADTMVGAARKEAERIVAEATVEGNSLVE-KARTDADEL 1108
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
529-794 |
2.14e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.22 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 529 AVNMSLNTSADSLTTPRLTLSELDDIIKNASGIYAEIDGAKNELQVKLSNLSNLSHDL--VQEAIDhaqELQQEANELSR 606
Cdd:COG3883 3 ALALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELeaLQAEID---KLQAEIAEAEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 607 KLhsSDMNGLVQKALDASNVYENIVNYVS---EANETAEFA--LNTTDRIYDAVSGIDTQIIYHKDESENLLNQARELQA 681
Cdd:COG3883 80 EI--EERREELGERARALYRSGGSVSYLDvllGSESFSDFLdrLSALSKIADADADLLEELKADKAELEAKKAELEAKLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 682 KAESSSDEAvADTSRRVGGALARKSALKTRLSDAVKQLQAA-ERGDAQQRLGQSRLITEEANRTTMEVQQATAPMANNLT 760
Cdd:COG3883 158 ELEALKAEL-EAAKAELEAQQAEQEALLAQLSAEEAAAEAQlAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
250 260 270
....*....|....*....|....*....|....
gi 1622930177 761 NWSQNLQHFDSSAYNTAVDSARDAVRNLTEVVPQ 794
Cdd:COG3883 237 AAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAG 270
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
307-827 |
8.40e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 54.20 E-value: 8.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 307 AHRHVNEINATIYLLKTKLSERENQYALRKiqiNNAENTMKSLLSDVEELVEKENQASRKGQLiQKESMDTIKHASQLVE 386
Cdd:TIGR00618 192 LHGKAELLTLRSQLLTLCTPCMPDTYHERK---QVLEKELKHLREALQQTQQSHAYLTQKREA-QEEQLKKQQLLKQLRA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 387 QAHDMRDKIQEINNKMlyygEEHELSPKeiSEKLVLAQKMLEEIRR---------------RQPFFTQRELVDEEADEAH 451
Cdd:TIGR00618 268 RIEELRAQEAVLEETQ----ERINRARK--AAPLAAHIKAVTQIEQqaqrihtelqskmrsRAKLLMKRAAHVKQQSSIE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 452 ELLSQAESWQRLHNETRTLFPVVLEQLDDYNAKLSDLQ------------EALDQALNHVRDAEDMNRATA----ARQRD 515
Cdd:TIGR00618 342 EQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQhihtlqqqkttlTQKLQSLCKELDILQREQATIdtrtSAFRD 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 516 HEKQQERVREQMEAvnmslntSADSLTTPRLTLSELDDIIKNASGIYAEIDGAKNELQVKLSNLSNLshdLVQEAIDHAQ 595
Cdd:TIGR00618 422 LQGQLAHAKKQQEL-------QQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQI---HLQETRKKAV 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 596 ELQ--QEANELSRKLHSSDMNgLVQKALDAsnvyenivnYVSEANetaefalntTDRiydaVSGIDTQIIYHKDESENL- 672
Cdd:TIGR00618 492 VLArlLELQEEPCPLCGSCIH-PNPARQDI---------DNPGPL---------TRR----MQRGEQTYAQLETSEEDVy 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 673 ------LNQARELQAKAESSSDEAVADTSRRvggalARKSALKTRLSDAVKQLQaaERGDAQQRLGQSRLITEEANRTTM 746
Cdd:TIGR00618 549 hqltseRKQRASLKEQMQEIQQSFSILTQCD-----NRSKEDIPNLQNITVRLQ--DLTEKLSEAEDMLACEQHALLRKL 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 747 EVQQATAPMANNLTNWSQNLQ----HFDSSAYNTAVDSARDAVRNLTEVVPQLLDQLRTVEQKrpASNVSASIQRIRELI 822
Cdd:TIGR00618 622 QPEQDLQDVRLHLQQCSQELAlkltALHALQLTLTQERVREHALSIRVLPKELLASRQLALQK--MQSEKEQLTYWKEML 699
|
....*
gi 1622930177 823 AQTRS 827
Cdd:TIGR00618 700 AQCQT 704
|
|
| ApoLp-III_like |
cd13769 |
Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles ... |
710-836 |
3.94e-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: 3.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 710 TRLSDAVKQLQAAERGDAQQRLGQSRL-ITEEANRTtmeVQQATAPMANNLTNWSQNLQHFDSSAYNTAVDSARDAVRNL 788
Cdd:cd13769 1 TQLSELIQKAQEAINNLAQQVQKQLGLqNPEEVVNT---LKEQSDNFANNLQEVSSSLKEEAKKKQGEVEEAWNEFKTKL 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1622930177 789 TEVVPQLLDQLRTVEQkrpASNVSASIQ-RIRELIAQTRSVASKIQVSM 836
Cdd:cd13769 78 SETVPELRKSLPVEEK---AQELQAKLQsGLQTLVTESQKLAKAISENS 123
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
339-829 |
7.64e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 50.99 E-value: 7.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 339 INNAENTMKSLLSDVE----ELVEKENQASRKgQLIQKESMDTIKhaSQLVEQAHDMRDKIQEINNkmlyygeehELSPK 414
Cdd:pfam12128 246 LQQEFNTLESAELRLShlhfGYKSDETLIASR-QEERQETSAELN--QLLRTLDDQWKEKRDELNG---------ELSAA 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 415 EisEKLVLAQKMLEEIRRRQpfftqRELVDEEADEAHELLSQAESWQRLHNETRTLFPVVLEQLDDYNAKLSDLQEALDQ 494
Cdd:pfam12128 314 D--AAVAKDRSELEALEDQH-----GAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKE 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 495 ALNhvRDAEDMN------RATAARQR-----DHEKQQERVREQMEAVNMSLNTSADSLttpRLTLSELDDIIKNASgiya 563
Cdd:pfam12128 387 QNN--RDIAGIKdklakiREARDRQLavaedDLQALESELREQLEAGKLEFNEEEYRL---KSRLGELKLRLNQAT---- 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 564 eidgAKNELQVKLSNLsnlshdlvQEAIDHAQELQQEANELSRKLHSSD--MNGLVQKALDASNVYENIVNYVSEANETA 641
Cdd:pfam12128 458 ----ATPELLLQLENF--------DERIERAREEQEAANAEVERLQSELrqARKRRDQASEALRQASRRLEERQSALDEL 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 642 EFALnttdriyDAVSG-----IDTQIIYHKDESENLLNQARELQAKAESSSDEAVADTSRRVGGA------------LAR 704
Cdd:pfam12128 526 ELQL-------FPQAGtllhfLRKEAPDWEQSIGKVISPELLHRTDLDPEVWDGSVGGELNLYGVkldlkridvpewAAS 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 705 KSALKTRLSDAVKQLQAAERGDAQQ--RLGQSRLITEEANRttmEVQQATAPMANN------LTNWSQNLQHFDSSAYNT 776
Cdd:pfam12128 599 EEELRERLDKAEEALQSAREKQAAAeeQLVQANGELEKASR---EETFARTALKNArldlrrLFDEKQSEKDKKNKALAE 675
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1622930177 777 AVDSARDAVRNLTEVVPQLLDQLRTV--EQKRPASNVSASIQRIRELIAQTRSVA 829
Cdd:pfam12128 676 RKDSANERLNSLEAQLKQLDKKHQAWleEQKEQKREARTEKQAYWQVVEGALDAQ 730
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
291-821 |
8.50e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.11 E-value: 8.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 291 IEEGKSGVlsvssgAAAH-RHVNEINAtiyLLKTKLSERENQYALRKiQINNAENTMKSLLSDVEELVEKEnqasrkgql 369
Cdd:PRK04863 263 ITESTNYV------AADYmRHANERRV---HLEEALELRRELYTSRR-QLAAEQYRLVEMARELAELNEAE--------- 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 370 iqkesmdtikhaSQLVEQAHDMRDKIQEINNKMLYYG--EEHELSPKEISEKLVlAQKMLeeirrrqpfftqRELVDEEA 447
Cdd:PRK04863 324 ------------SDLEQDYQAASDHLNLVQTALRQQEkiERYQADLEELEERLE-EQNEV------------VEEADEQQ 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 448 DEAHELLSQAEswqrlhnetrtlfpvvlEQLDDYNAKLSDLQEALDQAlnhvrdaedmnrATAARQRDHEKQQ-ERVReq 526
Cdd:PRK04863 379 EENEARAEAAE-----------------EEVDELKSQLADYQQALDVQ------------QTRAIQYQQAVQAlERAK-- 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 527 meavnmslntsadslttprlTLSELDDIiknasgiyaEIDGAKnelqvklsnlsnlshDLVQEAIDHAQELQQEANELSR 606
Cdd:PRK04863 428 --------------------QLCGLPDL---------TADNAE---------------DWLEEFQAKEQEATEELLSLEQ 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 607 KLHSSDMnglvqkaldasnvyenivnyvseANETAEFALNTTDRIYDAVSGIDTQiiyhkDESENLLNQARELQAKAEss 686
Cdd:PRK04863 464 KLSVAQA-----------------------AHSQFEQAYQLVRKIAGEVSRSEAW-----DVARELLRRLREQRHLAE-- 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 687 sdeavadtsrRVGGALARKSALKTRLsdavKQLQAAER--GDAQQRLGQS--------RLITE-EANRTTMEVQQATA-- 753
Cdd:PRK04863 514 ----------QLQQLRMRLSELEQRL----RQQQRAERllAEFCKRLGKNlddedeleQLQEElEARLESLSESVSEAre 579
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 754 ---PMANNLTNWSQNLQHFDSSAynTAVDSARDAVRNLTEVVP--------------QLLDQLR--TVEQKRPASNVSAS 814
Cdd:PRK04863 580 rrmALRQQLEQLQARIQRLAARA--PAWLAAQDALARLREQSGeefedsqdvteymqQLLERERelTVERDELAARKQAL 657
|
....*..
gi 1622930177 815 IQRIREL 821
Cdd:PRK04863 658 DEEIERL 664
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
666-824 |
3.75e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 3.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 666 KDESENLLNQARELQAK-AESSSDEAVADTSRR--------VGGAlaRKSALKTRLSDAVKQLQAAE--RGDAQQRLGQS 734
Cdd:COG4913 294 EAELEELRAELARLEAElERLEARLDALREELDeleaqirgNGGD--RLEQLEREIERLERELEERErrRARLEALLAAL 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 735 RLiTEEANRTTMEVQQATAPMAnnLTNWSQnlqhfDSSAYNTAVDSARDAVRNLTEVVPQLLDQLRTVEQKRpaSNVSAS 814
Cdd:COG4913 372 GL-PLPASAEEFAALRAEAAAL--LEALEE-----ELEALEEALAEAEAALRDLRRELRELEAEIASLERRK--SNIPAR 441
|
170
....*....|
gi 1622930177 815 IQRIRELIAQ 824
Cdd:COG4913 442 LLALRDALAE 451
|
|
| Prefoldin_alpha_GimC |
cd23160 |
Prefoldin alpha subunit, archaeal; Archaeal alpha subunit of prefoldin (GimC), a hexameric ... |
517-608 |
5.54e-03 |
|
Prefoldin alpha subunit, archaeal; Archaeal alpha subunit of prefoldin (GimC), a hexameric molecular chaperone complex, found in both eukaryotes and archaea. Prefoldin binds and stabilizes newly synthesized polypeptides allowing them to fold correctly. The complex contains two alpha and four beta subunits, the two subunits being evolutionarily related. In archaea, there is usually only one gene for each subunit while in eukaryotes there two or more paralogous genes encoding each subunit adding heterogeneity to the structure of the hexamer. The structure of the complex consists of a double beta barrel assembly with six protruding coiled-coils.
Pssm-ID: 467476 [Multi-domain] Cd Length: 127 Bit Score: 38.62 E-value: 5.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 517 EKQQERVREQMEAVNMSLNtsadSLTTPRLTLSELDDI-------------------IKNA--------SGIYAE--IDG 567
Cdd:cd23160 13 EQQAEALQQQIELLQASIN----ELNRAKETLEELKKLkegteilvpigggsfvkakIKDTdkvlvnigAGVVVEktIDE 88
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1622930177 568 AKNELQVKLSNLSNLSHDLVQEaidhAQELQQEANELSRKL 608
Cdd:cd23160 89 AIEILEKRIKELEKALEKLQEQ----LQQIAQRLEELEAEL 125
|
|
| |
|
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 |
1.47e-97 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 315.12 E-value: 1.47e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 298 VLSVSSGAAAHRHVNEINATIYLLKTKLSERENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLIQKESMDT 377
Cdd:pfam06008 1 LLSLNSLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 378 IKHASQLVEQAHDMRDKIQEINNKMLYYGEE-HELSPKEISEKLVLAQKMLEEIRRRQpFFTQRELVDEEADEAHELLSQ 456
Cdd:pfam06008 81 LGHAKELAEAIKNLIDNIKEINEKVATLGENdFALPSSDLSRMLAEAQRMLGEIRSRD-FGTQLQNAEAELKAAQDLLSR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 457 AESW-QRLHNETRTLFPVVLEQLDDYNAKLSDLQEALDQALNHVRDAEDMNRATAARQRDHEKQQERVREQMEAVNMSLN 535
Cdd:pfam06008 160 IQTWfQSPQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEETLK 239
|
250
....*....|....*....
gi 1622930177 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 |
5.63e-44 |
|
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 368703 [Multi-domain] Cd Length: 138 Bit Score: 156.49 E-value: 5.63e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 734 SRLITEEANRTTMEVQQATAPMANNLTNWSQNLQHFDSSA---------YNTAVDSARDAVRNLTEVVPQLLDQLRTVEQ 804
Cdd:pfam06009 1 SKELAREANETAKEVLEQLAPLSQNLENTSEKLSGINRSLeetnelvndANKALDDAGRSVKKLEELAPDLLDKLKPLKQ 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622930177 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 |
3.54e-40 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 146.02 E-value: 3.54e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 1492 KSQFSIRLRTRSSHGMIFYVSDQEENDFMTLFLAHGRLVYMFNVGHKKLKIRSQEKYNDGLWHDVVFIRERSSGRLVIDG 1571
Cdd:cd00110 21 RLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDGQWHSVSVERNGRSVTLSVDG 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1622930177 1572 LRVLEESLPPTEATWKIKGPIYLGGVAPGKavKNVQINSIYSFSGCLSNLQLN 1624
Cdd:cd00110 101 ERVVESGSPGGSALLNLDGPLYLGGLPEDL--KSPGLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
1494-1625 |
2.06e-36 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 134.77 E-value: 2.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 1494 QFSIRLRTRSSHGMIFYVSDQEENDFMTLFLAHGRLVYMFNVGHKKLKIRSQ-EKYNDGLWHDVVFIRERSSGRLVIDGL 1572
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDpTPLNDGQWHRVAVERNGRSVTLSVDGG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1622930177 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 1622930177 1648 GTYFStEGGYVVLDESFNIGLKFEIAFEVRPRSSSGTLVH-GHSVNGEYLNVHMKNGQVIVKVNNGirDFSTSVTPKQSL 1726
Cdd:cd00110 1 GVSFS-GSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYaGSQNGGDFLALELEDGRLVLRYDLG--SGSLVLSSKTPL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622930177 1727 CDGRWHRITVIRDSNVVQLDVDSE-VNHVVGPLNPKPIDHREPVFVGGVPESLLTPRLAPSKPFTGCIRHFVID 1799
Cdd:cd00110 78 NDGQWHSVSVERNGRSVTLSVDGErVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
1671-1801 |
3.75e-31 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 119.75 E-value: 3.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 1671 EIAFEVRPRSSSGTLVHGHSVNG-EYLNVHMKNGQVIVKVNNGIRDFSTSVTPKQsLCDGRWHRITVIRDSNVVQLDVDS 1749
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGgDYLALELRDGRLVLRYDLGSGPARLTSDPTP-LNDGQWHRVAVERNGRSVTLSVDG 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1622930177 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 |
2.49e-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: 2.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 1499 LRTRSSHGMIFYVSDQEeNDFMTLFLAHGRLVYMFNVGHKKLKIRSQEK-YNDGLWHDVVFIRERSSGRLVIDGLRVLEE 1577
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGG-SDFLALELVNGRLVLRYDLGSGPESLLSSGKnLNDGQWHSVRVERNGNTLTLSVDGQTVVSS 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1622930177 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 |
1.57e-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: 1.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 1676 VRPRSSSGTLVHGHSVNGEYLNVHMKNGQVIVKVNNGIRDFSTSVTPKqSLCDGRWHRITVIRDSNVVQLDVDSEVNH-V 1754
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDFLALELVNGRLVLRYDLGSGPESLLSSGK-NLNDGQWHSVRVERNGNTLTLSVDGQTVVsS 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1622930177 1755 VGPLNPKPIDHREPVFVGGVPESLLTPRLAPSKPFTGCIRHFVIDGH 1801
Cdd:pfam02210 80 LPPGESLLLNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
1500-1628 |
1.48e-24 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 100.85 E-value: 1.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 1500 RTRSSHGMIFYVSDQEENDFMTLFLAHGRLVYMFNVGHKKLKIRSQEKYNDGLWHDVVFIRERSSGRLVIDGLRVLE-ES 1578
Cdd:pfam00054 2 RTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTgES 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1622930177 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 |
1.05e-22 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 96.33 E-value: 1.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 1049 SYFFDGSGYAAVRDitkRGKFGQVTRFDIEVRTPADNSLILLM--VNGSMFFRLEMRNGYLHVFYDFGfsSGPVHLEDtl 1126
Cdd:cd00110 1 GVSFSGSSYVRLPT---LPAPRTRLSISFSFRTTSPNGLLLYAgsQNGGDFLALELEDGRLVLRYDLG--SGSLVLSS-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 1127 kKAQINDAKYHEISIIyHNDKKMILVVDR-RHVKSMDNEKMKI--PFTDIYIGGAPPEILQSRTLRAHlpldiNFRGCMK 1203
Cdd:cd00110 74 -KTPLNDGQWHSVSVE-RNGRSVTLSVDGeRVVESGSPGGSALlnLDGPLYLGGLPEDLKSPGLPVSP-----GFVGCIR 146
|
....
gi 1622930177 1204 GFQF 1207
Cdd:cd00110 147 DLKV 150
|
|
| LamG |
smart00282 |
Laminin G domain; |
1074-1210 |
2.60e-21 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 91.63 E-value: 2.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 1074 RFDIEVRTPADNSLILLM--VNGSMFFRLEMRNGYLHVFYDFGfsSGPVHLedTLKKAQINDAKYHEISIIyHNDKKMIL 1151
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAgsKGGGDYLALELRDGRLVLRYDLG--SGPARL--TSDPTPLNDGQWHRVAVE-RNGRSVTL 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622930177 1152 VVD---RRHVKSMDNEKMKIPFTDIYIGGAPPEILQSRTLRAHlpldiNFRGCMKGFQFQKK 1210
Cdd:smart00282 76 SVDggnRVSGESPGGLTILNLDGPLYLGGLPEDLKLPPLPVTP-----GFRGCIRNLKVNGK 132
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
1237-1376 |
6.77e-20 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 88.24 E-value: 6.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 1237 AYFNGQSFIASIQKISFFDGFEGGFNFRTLQPNGLLFYYASG--SDVFSISLDNGTVVMDV----KGIKVESvDKQYNDG 1310
Cdd:cd00110 2 VSFSGSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQngGDFLALELEDGRLVLRYdlgsGSLVLSS-KTPLNDG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622930177 1311 LSHFVITSVSPTRYELIVDKSRVGSKNPTKGKIEQTQagEKKFYFGGSPISAQ------YANFTGCISNAYF 1376
Cdd:cd00110 81 QWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNL--DGPLYLGGLPEDLKspglpvSPGFVGCIRDLKV 150
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
1079-1207 |
7.33e-20 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 87.09 E-value: 7.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 1079 VRTPADNSLIL-LMVNGSMFFRLEMRNGYLHVFYDFGfsSGPVHLedTLKKAQINDAKYHEISIIYhNDKKMILVVDRRH 1157
Cdd:pfam02210 1 FRTRQPNGLLLyAGGGGSDFLALELVNGRLVLRYDLG--SGPESL--LSSGKNLNDGQWHSVRVER-NGNTLTLSVDGQT 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1622930177 1158 VKSMDNEKMKIPF---TDIYIGGAPPeilqsRTLRAHLPLDINFRGCMKGFQF 1207
Cdd:pfam02210 76 VVSSLPPGESLLLnlnGPLYLGGLPP-----LLLLPALPVRAGFVGCIRDVRV 123
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
1263-1376 |
4.57e-18 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 82.08 E-value: 4.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 1263 FRTLQPNGLLFYYASG-SDVFSISLDNGTVVMDVK----GIKVESVDKQYNDGLSHFVITSVSPTRYELIVDKSRVGSKN 1337
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGgSDFLALELVNGRLVLRYDlgsgPESLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1622930177 1338 PTKGKIEQTQagEKKFYFGG------SPISAQYANFTGCISNAYF 1376
Cdd:pfam02210 81 PPGESLLLNL--NGPLYLGGlpplllLPALPVRAGFVGCIRDVRV 123
|
|
| LamG |
smart00282 |
Laminin G domain; |
860-1013 |
5.39e-18 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 82.00 E-value: 5.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 860 SLSLYMKppvrqpelTETADQFILYLGSKNaKKEYMGLAIKNDNLVYIYNLGTKDVEIPLDSKPVSswPAYFSIVKIERV 939
Cdd:smart00282 1 SISFSFR--------TTSPNGLLLYAGSKG-GGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLN--DGQWHRVAVERN 69
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622930177 940 GKHgkVFLTVPSLSSTAEEKFIKKgefsgddSLLDLDpedTVFYVGGVPSNFKLPNSLNLPGFVGCLELATLNN 1013
Cdd:smart00282 70 GRS--VTLSVDGGNRVSGESPGGL-------TILNLD---GPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNG 131
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
835-1012 |
9.01e-18 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 82.08 E-value: 9.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 835 SMMFDGQSAVEVhsrTSMDDLKAFTSLSLYMKppvrqpelTETADQFILYLGSKNaKKEYMGLAIKNDNLVYIYNLGTKD 914
Cdd:cd00110 1 GVSFSGSSYVRL---PTLPAPRTRLSISFSFR--------TTSPNGLLLYAGSQN-GGDFLALELEDGRLVLRYDLGSGS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 915 VEIpldSKPVSSWPAYFSIVKIERVGKHgkVFLTVPSLSStaeekfikkGEFSGDDSLLDLDPEDTVfYVGGVPSNFKLP 994
Cdd:cd00110 69 LVL---SSKTPLNDGQWHSVSVERNGRS--VTLSVDGERV---------VESGSPGGSALLNLDGPL-YLGGLPEDLKSP 133
|
170
....*....|....*...
gi 1622930177 995 NSLNLPGFVGCLELATLN 1012
Cdd:cd00110 134 GLPVSPGFVGCIRDLKVN 151
|
|
| 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 1622930177 1676 VRPRSSSGTLVHGHSVN-GEYLNVHMKNGQVIVKVNNGIRdfSTSVTPKQSLCDGRWHRITVIRDSNVVQLDVDSEVNHV 1754
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTeRDFLALELRDGRLEVSYDLGSG--AAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPT 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1622930177 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 |
8.67e-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: 8.67e-16
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1622930177 187 CDCSGNSDPNlifEDCDEVTGQCRnCLRNTTGFKCERCAPGYYGDARIAKNC 238
Cdd:cd00055 2 CDCNGHGSLS---GQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGGC 49
|
|
| LamG |
smart00282 |
Laminin G domain; |
1261-1379 |
1.23e-15 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 75.07 E-value: 1.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 1261 FNFRTLQPNGLLFYYAS--GSDVFSISLDNGTVVMDVKG----IKVESVDKQYNDGLSHFVITSVSPTRYELIVDksrvg 1334
Cdd:smart00282 4 FSFRTTSPNGLLLYAGSkgGGDYLALELRDGRLVLRYDLgsgpARLTSDPTPLNDGQWHRVAVERNGRSVTLSVD----- 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1622930177 1335 SKNPTKGKIEQTQAG---EKKFYFGGSP------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 |
5.35e-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: 5.35e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1622930177 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 |
1.31e-13 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 76.30 E-value: 1.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 279 DLTDDLRLAALSIEEGKsgVLSVSSGAAAHRHVNEINATIYLL----KTKLSERENQYALRKIQINNAENTMKSLLSDVE 354
Cdd:pfam05483 187 DLNNNIEKMILAFEELR--VQAENARLEMHFKLKEDHEKIQHLeeeyKKEINDKEKQVSLLLIQITEKENKMKDLTFLLE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 355 ELVEKENQASRKGQLiQKESMdtikhaSQLVEQAHDMRDKIQEINNKMlyygEEHELSPKEISEKLVLAQKMLEEIRRRQ 434
Cdd:pfam05483 265 ESRDKANQLEEKTKL-QDENL------KELIEKKDHLTKELEDIKMSL----QRSMSTQKALEEDLQIATKTICQLTEEK 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 435 PffTQRELVDeEADEAH---------------ELLSQAEswQRLHNETRTLFPVVLEqlddYNAKLSDLQEALDQALNHV 499
Cdd:pfam05483 334 E--AQMEELN-KAKAAHsfvvtefeattcsleELLRTEQ--QRLEKNEDQLKIITME----LQKKSSELEEMTKFKNNKE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 500 RDAEDMNRATAARQR--DHEKQQERVREQMEAVNMSLntsADSLTTPRLTLSELD---DIIKNASGIYA-EIDGAKNELQ 573
Cdd:pfam05483 405 VELEELKKILAEDEKllDEKKQFEKIAEELKGKEQEL---IFLLQAREKEIHDLEiqlTAIKTSEEHYLkEVEDLKTELE 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 574 -VKLSNLSNLSH---------DLVQEAIDHAQEL--QQE---ANELSRKLHSSDMNGLVQKALDASNVYENIVNYVSEAN 638
Cdd:pfam05483 482 kEKLKNIELTAHcdklllenkELTQEASDMTLELkkHQEdiiNCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKG 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 639 ETAEFALnttDRIYDAVSGIDTQIIYHKDESENLLNQARELQAKAEsssdeavaDTSRRVGGALARKSALKTRLSDAVKQ 718
Cdd:pfam05483 562 DEVKCKL---DKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIE--------NKNKNIEELHQENKALKKKGSAENKQ 630
|
....*
gi 1622930177 719 LQAAE 723
Cdd:pfam05483 631 LNAYE 635
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
132-185 |
8.36e-13 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 64.30 E-value: 8.36e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1622930177 132 CPCPlPHlANFAESCYRKNGavRCICKENYAGPNCERCAPGYYGNPlLIGSTCK 185
Cdd:cd00055 2 CDCN-GH-GSLSGQCDPGTG--QCECKPNTTGRRCDRCAPGYYGLP-SQGGGCQ 50
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
325-821 |
1.03e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 73.54 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 325 LSERENQYALRKIQINNAE--------NTMKSLLSDVEELVEKENQasrkgqliQKESMDTIKHASQLVEQAHdmRDKIQ 396
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEEKEekdlherlNGLESELAELDEEIERYEE--------QREQARETRDEADEVLEEH--EERRE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 397 EInnkmlyygEEHELSPKEISEKLVLAQKMLEEIRRRqpFFTQRELVDEEADEAHELLSQAEsWQRLHNETrtlfpvVLE 476
Cdd:PRK02224 252 EL--------ETLEAEIEDLRETIAETEREREELAEE--VRDLRERLEELEEERDDLLAEAG-LDDADAEA------VEA 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 477 QLDDYNAKLSDLQEALDQALNHVRDAEdmNRATAARQR--DHEKQQERVREQMEAVNMSLNTSADSLTTPRLTLSELDDI 554
Cdd:PRK02224 315 RREELEDRDEELRDRLEECRVAAQAHN--EEAESLREDadDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 555 IKNASGIYA----EIDGAKNELQVKLSNLSNLSHDL---------VQEAIDHAQELQQEAN------------------- 602
Cdd:PRK02224 393 IEELRERFGdapvDLGNAEDFLEELREERDELREREaeleatlrtARERVEEAEALLEAGKcpecgqpvegsphvetiee 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 603 ------ELSRKLhsSDMNGLVQKALDASNVYENIVNYVSEANETAEFALNTTDRIYDAVSGIDTQiiyhKDESENLLNQA 676
Cdd:PRK02224 473 drerveELEAEL--EDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEK----RERAEELRERA 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 677 RELQAKAESSSDEAV-----ADTSRRVGGAL-ARKSALKTRLsDAVKQL--QAAERGDAQQRLGqsRLITEEANRTTMEV 748
Cdd:PRK02224 547 AELEAEAEEKREAAAeaeeeAEEAREEVAELnSKLAELKERI-ESLERIrtLLAAIADAEDEIE--RLREKREALAELND 623
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622930177 749 QQatapmANNLTNWSQNLQHFDSSAYNTAVDSARDAVRNLTEVVPQLLDQLRTVEQKRPA-----SNVSASIQRIREL 821
Cdd:PRK02224 624 ER-----RERLAEKRERKRELEAEFDEARIEEAREDKERAEEYLEQVEEKLDELREERDDlqaeiGAVENELEELEEL 696
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
132-184 |
2.02e-12 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 63.14 E-value: 2.02e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1622930177 132 CPCPlpHLANFAESCYRKNGavRCICKENYAGPNCERCAPGYYGNPLLIGSTC 184
Cdd:pfam00053 1 CDCN--PHGSLSDTCDPETG--QCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
132-177 |
3.38e-12 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 62.71 E-value: 3.38e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1622930177 132 CPCPLPHlaNFAESCYRKNGavRCICKENYAGPNCERCAPGYYGNP 177
Cdd:smart00180 1 CDCDPGG--SASGTCDPDTG--QCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
187-231 |
4.67e-12 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 61.94 E-value: 4.67e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1622930177 187 CDCS--GNSDPnlifeDCDEVTGQCRnCLRNTTGFKCERCAPGYYGD 231
Cdd:smart00180 1 CDCDpgGSASG-----TCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD 41
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
321-647 |
4.70e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 71.63 E-value: 4.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 321 LKTKLSERENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLIQKESMDTIKHASQLVEQA--HDMRDKIQEI 398
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKqiLRERLANLER 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 399 NNKML-YYGEEHELSPKEISEKLVLAQKMLEEIRrrqpffTQRELVDEEADEAHELLSQAESwqrlHNETRTlfpvvlEQ 477
Cdd:TIGR02168 317 QLEELeAQLEELESKLDELAEELAELEEKLEELK------EELESLEAELEELEAELEELES----RLEELE------EQ 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 478 LDDYNAKLSDLQEALDQALNHVRDAED-MNRATAARQRDHEKQQERVRE----QMEAVNMSLNTSADSLTTprlTLSELD 552
Cdd:TIGR02168 381 LETLRSKVAQLELQIASLNNEIERLEArLERLEDRRERLQQEIEELLKKleeaELKELQAELEELEEELEE---LQEELE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 553 DIIKNASGIYAEIDGAKNELQVKLSNLSNLSH--DLVQEAIDHAQELQQEANELsrKLHSSDMNGLVQKALDASNV---Y 627
Cdd:TIGR02168 458 RLEEALEELREELEEAEQALDAAERELAQLQArlDSLERLQENLEGFSEGVKAL--LKNQSGLSGILGVLSELISVdegY 535
|
330 340
....*....|....*....|....*....
gi 1622930177 628 E---------NIVNYVSEANETAEFALNT 647
Cdd:TIGR02168 536 EaaieaalggRLQAVVVENLNAAKKAIAF 564
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
81-130 |
1.68e-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: 60.83 E-value: 1.68e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1622930177 81 PCDCNGN---SNECLDGSGFCvHCQRNTTGEHCEKCLDGYIGDSIRGAPrfCQ 130
Cdd:cd00055 1 PCDCNGHgslSGQCDPGTGQC-ECKPNTTGRRCDRCAPGYYGLPSQGGG--CQ 50
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
1079-1203 |
2.37e-11 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 63.10 E-value: 2.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 1079 VRTPADNSLILLM--VNGSMFFRLEMRNGYLHVFYDFGfsSGPVHLEdtlKKAQINDAKYHEISIIYhNDKKMILVVDRR 1156
Cdd:pfam00054 1 FRTTEPSGLLLYNgtQTERDFLALELRDGRLEVSYDLG--SGAAVVR---SGDKLNDGKWHSVELER-NGRSGTLSVDGE 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1622930177 1157 HVKSMDNEK---MKIPF-TDIYIGGAPPEIlqsrTLRAHLPLDINFRGCMK 1203
Cdd:pfam00054 75 ARPTGESPLgatTDLDVdGPLYVGGLPSLG----VKKRRLAISPSFDGCIR 121
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
875-1013 |
1.54e-10 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 60.51 E-value: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 875 TETADQFILYLGSKnaKKEYMGLAIKNDNLVYIYNLGTKDVEIPLDSKPVS--SWpayfSIVKIERVGKHgkVFLTVPSL 952
Cdd:pfam02210 3 TRQPNGLLLYAGGG--GSDFLALELVNGRLVLRYDLGSGPESLLSSGKNLNdgQW----HSVRVERNGNT--LTLSVDGQ 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622930177 953 SSTAEEKfikkgefSGDDSLLDLDpedTVFYVGGVPSNFKLPNSLNLPGFVGCLELATLNN 1013
Cdd:pfam02210 75 TVVSSLP-------PGESLLLNLN---GPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVNG 125
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
321-743 |
2.54e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.73 E-value: 2.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 321 LKTKLSERENQYALRKIQinNAENTMKSLLSDVEELVEKENQASRKGQLIQKESMDTIKHASQLVEQAHDMRDKIQEINN 400
Cdd:COG1196 218 LKEELKELEAELLLLKLR--ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 401 KMLyyGEEHELSPKEisEKLVLAQKMLEEIRRRqpfftQRELVDEEADEAHELLSQAESWQRLHNETRTLfpvvLEQLDD 480
Cdd:COG1196 296 ELA--RLEQDIARLE--ERRRELEERLEELEEE-----LAELEEELEELEEELEELEEELEEAEEELEEA----EAELAE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 481 YNAKLSDLQEALDQALNHVRDAEDMNRATAARQRDHEKQQERVREQMEAVNMSLNTSADSLTTPRLTLSELDDIIKNASG 560
Cdd:COG1196 363 AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 561 IYAEIDGAKNELQVKLSNLSNLSHDLVQEAIDHAQELQQEANELSRKLHSSDMnglvqkALDASNVYENIVNYVSEANET 640
Cdd:COG1196 443 ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL------LLEAEADYEGFLEGVKAALLL 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 641 AEFALnttdriydaVSGIDTQIIYHKDESENLLNQARELQAKAESSSDEAVADtsRRVGGALARKSALKTRL-SDAVKQL 719
Cdd:COG1196 517 AGLRG---------LAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAA--AAIEYLKAAKAGRATFLpLDKIRAR 585
|
410 420
....*....|....*....|....
gi 1622930177 720 QAAERGDAQQRLGQSRLITEEANR 743
Cdd:COG1196 586 AALAAALARGAIGAAVDLVASDLR 609
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
302-833 |
3.11e-10 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 65.52 E-value: 3.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 302 SSGAAAHRHVNEINATIYLLKTKLSERENQYALRKIQINNA--------ENTMKSLLSDVE----ELVEKENQASRKGQL 369
Cdd:pfam15921 217 SLGSAISKILRELDTEISYLKGRIFPVEDQLEALKSESQNKielllqqhQDRIEQLISEHEveitGLTEKASSARSQANS 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 370 IQKEsMDTIKHA-----SQLVEQAHDMRDKIQEINNKMLYYGEEHELSPKEISEKLVLAQKMLEEIRRRQPFFTQRE--- 441
Cdd:pfam15921 297 IQSQ-LEIIQEQarnqnSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESgnl 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 442 -------LVDEEADEAHELLSQAES---WQRLHNETRTLfPVVLEQLDDYNAKLSDLqEALDQALNHVRDAEdMNRATAA 511
Cdd:pfam15921 376 ddqlqklLADLHKREKELSLEKEQNkrlWDRDTGNSITI-DHLRRELDDRNMEVQRL-EALLKAMKSECQGQ-MERQMAA 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 512 RQRDHEKQQE----------------RVREQMEAVNMSLNTSADSLTTPRLTLSELDDIIKNASgiyAEIDGAKNELQVK 575
Cdd:pfam15921 453 IQGKNESLEKvssltaqlestkemlrKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATN---AEITKLRSRVDLK 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 576 LSNLSNLSHDLvqeaiDHAQELQQEANELSRKLHSSD--MNGLVQKaldasnvYENIVNYVSEANETAefalnttdriyd 653
Cdd:pfam15921 530 LQELQHLKNEG-----DHLRNVQTECEALKLQMAEKDkvIEILRQQ-------IENMTQLVGQHGRTA------------ 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 654 avsgidTQIIYHKDESENLLNQAR-ELQakaESSSDEAVADTSRRvggalarksALKTRLSD----AVKQLQAaergdAQ 728
Cdd:pfam15921 586 ------GAMQVEKAQLEKEINDRRlELQ---EFKILKDKKDAKIR---------ELEARVSDleleKVKLVNA-----GS 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 729 QRLGQSRLITEEANRTTMEVQQATAPMaNNLTNWSQNLQ-HF--DSSAYNTAVDSARDAVRNLTEVVPQLLDQLRTVE-Q 804
Cdd:pfam15921 643 ERLRAVKDIKQERDQLLNEVKTSRNEL-NSLSEDYEVLKrNFrnKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEgS 721
|
570 580 590
....*....|....*....|....*....|
gi 1622930177 805 KRPASNVSASIQR-IRELIAQTRSVASKIQ 833
Cdd:pfam15921 722 DGHAMKVAMGMQKqITAKRGQIDALQSKIQ 751
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
311-610 |
6.64e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 64.31 E-value: 6.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 311 VNEINATIYLLKTKLSERENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLIQKESMDTIKHASQLVEQAHD 390
Cdd:TIGR02168 693 IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE 772
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 391 MRDKIQEINNKMlyygEEHELSPKEISEKLVLAQKMLEEIRRRqpFFTQRELVDEEADEAHELLSQAESWQRLHNETRTL 470
Cdd:TIGR02168 773 AEEELAEAEAEI----EELEAQIEQLKEELKALREALDELRAE--LTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 471 FPVVLEQLDDYNAKLSDLQEALDQAlnhvrdAEDMNRATAARQRdHEKQQERVREQMEAVNMSLNTSADSLTTPRLTLSE 550
Cdd:TIGR02168 847 IEELSEDIESLAAEIEELEELIEEL------ESELEALLNERAS-LEEALALLRSELEELSEELRELESKRSELRRELEE 919
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 551 LDDIIKNASgiyAEIDGAKNELQVKLSNLSNLSHDLVQEAIDHAQELQQEANELSRKLHS 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 |
1.07e-09 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 63.69 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 327 ERENQYALRKIqINNAENTMKSLLSDVEELVEKENQASRKGQLIQKESMDTIKhasQL-VEQAHD--MRDKIQEInnkml 403
Cdd:pfam10174 224 DPAKTKALQTV-IEMKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIK---QMeVYKSHSkfMKNKIDQL----- 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 404 yygeEHELSPKEiSEKLVLaQKMLEEIRRRQPFFTQRELVDEEADEAHEllsqaeswQR---LHNETRTLfPVVLEQ--- 477
Cdd:pfam10174 295 ----KQELSKKE-SELLAL-QTKLETLTNQNSDCKQHIEVLKESLTAKE--------QRaaiLQTEVDAL-RLRLEEkes 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 478 -LDDYNAKLSDLQEALDQALNHVRDAEDM----NRATAARQ----------RDHEKQQERVREQMEAVNMSLNTSADSLT 542
Cdd:pfam10174 360 fLNKKTKQLQDLTEEKSTLAGEIRDLKDMldvkERKINVLQkkienlqeqlRDKDKQLAGLKERVKSLQTDSSNTDTALT 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 543 TPRLTLSELDDIIKNASGIYA--------EIDGAKNELQVKLSNLSNLSHDL------VQEAIDHAQELQQEANELSRKL 608
Cdd:pfam10174 440 TLEEALSEKERIIERLKEQREredrerleELESLKKENKDLKEKVSALQPELtekessLIDLKEHASSLASSGLKKDSKL 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 609 HSSDMNglVQKALDASNVYENIVNYVSEANETAEFALNTTDRIydavSGIDTQIIYHKDES-------ENLLNQARELQA 681
Cdd:pfam10174 520 KSLEIA--VEQKKEECSKLENQLKKAHNAEEAVRTNPEINDRI----RLLEQEVARYKEESgkaqaevERLLGILREVEN 593
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622930177 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 |
1.83e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.03 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 311 VNEINATIYLLKTKLSERENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLIQKESMDTIKHASQLVEQAHD 390
Cdd:COG1196 283 LEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 391 MRDKIQEINNKMLyyGEEHELSpKEISEKLVLAQKMLEEIRRRQpffTQRELVDEEADEAHELLSQAESWQRLHNETRTL 470
Cdd:COG1196 363 AEEALLEAEAELA--EAEEELE-ELAEELLEALRAAAELAAQLE---ELEEAEEALLERLERLEEELEELEEALAELEEE 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 471 FPVVLEQLDDYNAKLSDLQEALDQALNHVRDAE------DMNRATAARQRDHEKQQERVREQMEAVNMSLNTSADSLTTP 544
Cdd:COG1196 437 EEEEEEALEEAAEEEAELEEEEEALLELLAELLeeaallEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLL 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 545 RLTLSELDDIIKNASGIYAEIDGAKNELQVKLSNLSNLSHDLVQEAIDHAQE-----------LQQEANELSRKLHSSDM 613
Cdd:COG1196 517 AGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAakagratflplDKIRARAALAAALARGA 596
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 614 NGLVQKALDASNVYENIVNYV-----------SEANETAEFALNTTDRIYDAVSGIDTQIIYHKDESENLLNQARELQAK 682
Cdd:COG1196 597 IGAAVDLVASDLREADARYYVlgdtllgrtlvAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLE 676
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622930177 683 AESSSDEAVADTSRRVGGALARKSALKTRLSDAVKQLQAAERGDAQQRLGQSRLITEEANRTTMEVQQA 751
Cdd:COG1196 677 AEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEE 745
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
82-129 |
2.50e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 54.67 E-value: 2.50e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1622930177 82 CDCNGN---SNECLDGSGFCvHCQRNTTGEHCEKCLDGYIGDSIrGAPRFC 129
Cdd:pfam00053 1 CDCNPHgslSDTCDPETGQC-LCKPGVTGRHCDRCKPGYYGLPS-DPPQGC 49
|
|
| TNFRSF16 |
cd13416 |
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 ... |
65-257 |
2.66e-09 |
|
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 neurotrophin receptor (p75NTR) or CD271; TNFRSF16 (also known as nerve growth factor receptor (NGFR) or p75 neurotrophin receptor (p75NTR or p75(NTR)), CD271, Gp80-LNGFR) is a common receptor for both neurotrophins and proneurotrophins, and plays a diverse role in many tissues, including the nervous system. It has been shown to be expressed in various types of stem cells and has been used to prospectively isolate stem cells with different degrees of potency. p75NTR owes its signaling to the recruitment of intracellular binding proteins, leading to the activation of different signaling pathways. It binds nerve growth factor (NGF) and the complex can initiate a signaling cascade which has been associated with both neuronal apoptosis and neuronal survival of discrete populations of neurons, depending on the presence or absence of intracellular signaling molecules downstream of p75NTR (e.g. NF-kB, JNK, or p75NTR intracellular death domain). p75NTR can also bind NGF in concert with the neurotrophic tyrosine kinase receptor type 1 (TrkA) protein where it is thought to modulate the formation of the high-affinity neurotrophin binding complex. On melanoma cell, p75NTR is an immunosuppressive factor, induced by interferon (IFN)-gamma, and mediates down-regulation of melanoma antigens. It can interact with the aggregated form of amyloid beta (Abeta) peptides, and plays an important role in etiopathogenesis of Alzheimer's disease by influencing protein tau hyper-phosphorylation. p75(NTR) is involved in the formation and progression of retina diseases; its expression is induced in retinal pigment epithelium (RPE) cells and its knockdown rescues RPE cell proliferation activity and inhibits RPE apoptosis induced by hypoxia. It can therefore be a potential therapeutic target for RPE hypoxia or oxidative stress diseases.
Pssm-ID: 276921 [Multi-domain] Cd Length: 159 Bit Score: 57.70 E-value: 2.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 65 EKCNAGFFRTlSGECvpCDcngnsnECLDGSGFCVHCQRNTTGehCEKCLDGYIGDSIRGAPRFCQLC-PCPlpHLANFA 143
Cdd:cd13416 1 EACPSGQYTS-SGEC--CE------QCPPGEGVARPCGDNQTV--CEPCLDGVTFSDVVSHTEPCQPCtRCP--GLMSMR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 144 ESCYRKNGAVrcickenyagpnCErCAPGYYGNPLliGSTCKKCDCsgnsdpnlifedCDEVTGQCRNC--LRNTtgfKC 221
Cdd:cd13416 68 APCTATHDTV------------CE-CAYGYYLDED--SGTCEPCTV------------CPPGQGVVQSCgpNQDT---VC 117
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1622930177 222 ERCAPGYYGDARIAKN----CAVCncggGPCDSVTGECLE 257
Cdd:cd13416 118 EACPEGTYSDEDSSTDpclpCTVC----EDGEVELRECTP 153
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
82-121 |
4.05e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 53.85 E-value: 4.05e-09
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1622930177 82 CDCNGN---SNECLDGSGFCvHCQRNTTGEHCEKCLDGYIGDS 121
Cdd:smart00180 1 CDCDPGgsaSGTCDPDTGQC-ECKPNVTGRRCDRCAPGYYGDG 42
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
318-745 |
4.71e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.49 E-value: 4.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 318 IYLLKTKLSERENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLIQKESMDTIKHASQLVEQAHDMRDKIQE 397
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 398 INNKMLYYGEEHElspkEISEKLVLAQKMLEEIrrrqpfftQRELVDEEADEAHELLSQAESWQRLHNETRTLFPVVLEQ 477
Cdd:COG1196 314 LEERLEELEEELA----ELEEELEELEEELEEL--------EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 478 LDDYNAKLSDLQEALDQAlNHVRDAEDMNRATAARQRDHEKQQERVREQMEAVNMSLNTSADSLTTPRLTLSELDDIIKN 557
Cdd:COG1196 382 EELAEELLEALRAAAELA-AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 558 ASGIYAEIDGAKNELQVKLSNLSNLSHDLVQ--EAIDHAQELQQEANELSRKLHSSDMNGLVQKALDAsnvyENIVNYVS 635
Cdd:COG1196 461 LLELLAELLEEAALLEAALAELLEELAEAAArlLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAV----LIGVEAAY 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 636 EANETAEFALNTTDRIYDAVSGIDTQIIYHKDESEN-----LLNQARELQAKAESSSDEAVADTSRRVGGALARKSALKT 710
Cdd:COG1196 537 EAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGratflPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYY 616
|
410 420 430
....*....|....*....|....*....|....*
gi 1622930177 711 RLSDAVkQLQAAERGDAQQRLGQSRLITEEANRTT 745
Cdd:COG1196 617 VLGDTL-LGRTLVAARLEAALRRAVTLAGRLREVT 650
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
312-528 |
1.60e-08 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 58.00 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 312 NEINATIYLLKTKLSERENQYAlrkiQINNAENTMKSLLSDVEEL----------VEKENQ----ASRKGQLIQ--KESM 375
Cdd:COG1340 81 DELNEKLNELREELDELRKELA----ELNKAGGSIDKLRKEIERLewrqqtevlsPEEEKElvekIKELEKELEkaKKAL 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 376 DTIKHASQLVEQAHDMRDKIQEINNKMlyygeehelspKEISEKlvlAQKMLEEIrrrQPFFTQRELVDEEADEAHELLS 455
Cdd:COG1340 157 EKNEKLKELRAELKELRKEAEEIHKKI-----------KELAEE---AQELHEEM---IELYKEADELRKEADELHKEIV 219
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622930177 456 QA-ESWQRLHnetrtlfpvvlEQLDDYNAKLSDLQEALDQALNHVRDAEdmnrataaRQRDHEKQQERVREQME 528
Cdd:COG1340 220 EAqEKADELH-----------EEIIELQKELRELRKELKKLRKKQRALK--------REKEKEELEEKAEEIFE 274
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
319-731 |
1.70e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.40 E-value: 1.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 319 YLLKTKLseRENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLIQKESmdtikhasQLVEQAHDMRDKIQEI 398
Cdd:COG4717 45 AMLLERL--EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELE--------ELEEELEELEAELEEL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 399 NNKMLYYGEEHELSP-----KEISEKLVLAQKMLEEIRRRQPFFTQRElvdEEADEAHELLSQAEswQRLHNETRTLFPV 473
Cdd:COG4717 115 REELEKLEKLLQLLPlyqelEALEAELAELPERLEELEERLEELRELE---EELEELEAELAELQ--EELEELLEQLSLA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 474 VLEQLDDYNAKLSDLQEALDQALNHVRDAEDmNRATAARQRD-------HEKQQERVREQM-----EAVNMSLNTSADSL 541
Cdd:COG4717 190 TEEELQDLAEELEELQQRLAELEEELEEAQE-ELEELEEELEqleneleAAALEERLKEARlllliAAALLALLGLGGSL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 542 TTPRLTL----------------------SELDDIIKNASGIYAEIDGAKNELQVKLSNL---SNLSHDLVQEAIDHAQE 596
Cdd:COG4717 269 LSLILTIagvlflvlgllallflllarekASLGKEAEELQALPALEELEEEELEELLAALglpPDLSPEELLELLDRIEE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 597 LQQ---EANELSRKLHSSDMNGLVQKALDASNV-----YENIVNYVSEANETAEfalnttdriydAVSGIDTQIIYHKDE 668
Cdd:COG4717 349 LQEllrEAEELEEELQLEELEQEIAALLAEAGVedeeeLRAALEQAEEYQELKE-----------ELEELEEQLEELLGE 417
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622930177 669 SENLLNQARELQAKAE-SSSDEAVADTSRRVGGALARKSALKTRLSDAVKQLQAAERGDAQQRL 731
Cdd:COG4717 418 LEELLEALDEEELEEElEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEEL 481
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
425-831 |
2.00e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.57 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 425 KMLEEI--------RRRQpffTQRELvdEEADE--------AHELLSQ----------AESWQRLHNETRtlfpvVLE-- 476
Cdd:COG1196 159 AIIEEAagiskykeRKEE---AERKL--EATEEnlerlediLGELERQleplerqaekAERYRELKEELK-----ELEae 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 477 ----QLDDYNAKLSDLQEALDQALNHVRDAEdmnrataARQRDHEKQQERVREQMEAVNMSLNTSADSLttpRLTLSELd 552
Cdd:COG1196 229 llllKLRELEAELEELEAELEELEAELEELE-------AELAELEAELEELRLELEELELELEEAQAEE---YELLAEL- 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 553 diiknasgiyAEIDGAKNELQVKLSNLSNLSHDLVQEAIDHAQELQQEANELSRKLHSSDMngLVQKALDASNVYENIVN 632
Cdd:COG1196 298 ----------ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE--AEEELEEAEAELAEAEE 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 633 YVSEANETAEFALNTTDRIYDAVSGIDTQIIYHKDESENLLNQARELQAKAESSSDEAVADTSRRVGGALARKSALKTRL 712
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 713 SDAVKQLQAAERGDAQQR----LGQSRLITEEANRTTMEVQQATAPMANNLTNWSQNLQHFDSSAyntavdsARDAVRNL 788
Cdd:COG1196 446 EAAEEEAELEEEEEALLEllaeLLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGV-------KAALLLAG 518
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1622930177 789 TEVVPQLLDQLRTVEQKRPASNVSASIQRIRELIAQTRSVASK 831
Cdd:COG1196 519 LRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAA 561
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
424-885 |
4.15e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.24 E-value: 4.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 424 QKMLEEIRRRQPffTQRELVDEEADEAHELLSQAESWQRLHNETRtlfpvvlEQLDDYNAKLSDLQEALDQALNHVRDAE 503
Cdd:COG4717 52 EKEADELFKPQG--RKPELNLKELKELEEELKEAEEKEEEYAELQ-------EELEELEEELEELEAELEELREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 504 DMNRAtaarqRDHEKQQERVREQMEavnmSLNTSADSLTTPRLTLSELDDIIKNASgiyAEIDGAKNELQVKLSNLSNLS 583
Cdd:COG4717 123 KLLQL-----LPLYQELEALEAELA----ELPERLEELEERLEELRELEEELEELE---AELAELQEELEELLEQLSLAT 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 584 HDLVQEAIDHAQELQQEANELSRKL---------HSSDMNGLVQKALDAsNVYENIVNY-------------VSEANETA 641
Cdd:COG4717 191 EEELQDLAEELEELQQRLAELEEELeeaqeeleeLEEELEQLENELEAA-ALEERLKEArlllliaaallalLGLGGSLL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 642 EFALNTTDRIYDAVSGIDTQIIYHKDESENLLNQARELQAKAESSS--DEAVADTSRRVGGALARKSALKTRLSDAVKQL 719
Cdd:COG4717 270 SLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEEleEEELEELLAALGLPPDLSPEELLELLDRIEEL 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 720 QAA--ERGDAQQRLGQSRLITE------------------------EANRTTMEVQQATAPMANNLTNWSQNLQHFDSSA 773
Cdd:COG4717 350 QELlrEAEELEEELQLEELEQEiaallaeagvedeeelraaleqaeEYQELKEELEELEEQLEELLGELEELLEALDEEE 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 774 YNTAVDSARDAVRNLTEVVPQLLDQLRTVEQK----RPASNVSASIQRIRELIAQTRSVASKIQVSMMfdGQSAVEVHSR 849
Cdd:COG4717 430 LEEELEELEEELEELEEELEELREELAELEAEleqlEEDGELAELLQELEELKAELRELAEEWAALKL--ALELLEEARE 507
|
490 500 510
....*....|....*....|....*....|....*.
gi 1622930177 850 TSMDDlkaftslslymkppvRQPELTETADQFILYL 885
Cdd:COG4717 508 EYREE---------------RLPPVLERASEYFSRL 528
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
415-855 |
1.08e-07 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 57.14 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 415 EISEKLVLAQKmlEEIRRRQpfftqrelvdeeadEAHELLSQA--ESWQ---RLHNETRTLFPVVLEQLDDYNAKLSDLQ 489
Cdd:NF041483 696 EAAEALAAAQE--EAARRRR--------------EAEETLGSAraEADQereRAREQSEELLASARKRVEEAQAEAQRLV 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 490 EALDQ-ALNHVRDAEDmnraTAARQRD-----HEKQQERVREQMEAVNMSlntsADSltTPRLTLSELDDIIKNAsgiYA 563
Cdd:NF041483 760 EEADRrATELVSAAEQ----TAQQVRDsvaglQEQAEEEIAGLRSAAEHA----AER--TRTEAQEEADRVRSDA---YA 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 564 EIDGA-------KNELQVKLSNLSNLSHDLVQEAIDHAQELQQEANELSRKLHSSDMNGLVQKALDASNVYenivnyvSE 636
Cdd:NF041483 827 ERERAsedanrlRREAQEETEAAKALAERTVSEAIAEAERLRSDASEYAQRVRTEASDTLASAEQDAARTR-------AD 899
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 637 ANETAefalnttDRI-YDAVSGIDTQIIYHKDESENLLNQARelqAKAESSSDEAVADTSRRVGGALARKSALKTRLSDA 715
Cdd:NF041483 900 AREDA-------NRIrSDAAAQADRLIGEATSEAERLTAEAR---AEAERLRDEARAEAERVRADAAAQAEQLIAEATGE 969
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 716 VKQL--QAAER-GDAQQRLGQSRlitEEANRTTMEvqqaTAPMANNLTNWSQN-----LQHFDSSAYNTAVDSARDAVRN 787
Cdd:NF041483 970 AERLraEAAETvGSAQQHAERIR---TEAERVKAE----AAAEAERLRTEAREeadrtLDEARKDANKRRSEAAEQADTL 1042
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622930177 788 LTEVVPQlLDQLRTVEQKRPASNVSASIQRIRELIAQTRSVASKIQVSMMFDGQSAVEvHSRTSMDDL 855
Cdd:NF041483 1043 ITEAAAE-ADQLTAKAQEEALRTTTEAEAQADTMVGAARKEAERIVAEATVEGNSLVE-KARTDADEL 1108
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
321-600 |
2.03e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 56.23 E-value: 2.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 321 LKTKLSERENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLIQKEsmdtikhASQLVEQAHDMRDKIQEINN 400
Cdd:TIGR02169 679 LRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQE-------EEKLKERLEELEEDLSSLEQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 401 KMLYYGEEHELSPKEIS---EKLVLAQKMLEEIRRR---QPFFTQRELVDEEADEAHELLSQAESWQRLHNEtRTLFPVV 474
Cdd:TIGR02169 752 EIENVKSELKELEARIEeleEDLHKLEEALNDLEARlshSRIPEIQAELSKLEEEVSRIEARLREIEQKLNR-LTLEKEY 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 475 LE----------------------QLDDYNAKLSDLQEALDQALNHVRDAEDmnrataaRQRDHEKQQERVREQMEAVNM 532
Cdd:TIGR02169 831 LEkeiqelqeqridlkeqiksiekEIENLNGKKEELEEELEELEAALRDLES-------RLGDLKKERDELEAQLRELER 903
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622930177 533 SLNTSADSLTTPRLTLSELDDIIKNASGIYAEIDGAKNELQVKLSNLsnLSHDLVQEAIdhaQELQQE 600
Cdd:TIGR02169 904 KIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEE--LSLEDVQAEL---QRVEEE 966
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
529-794 |
2.14e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.22 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 529 AVNMSLNTSADSLTTPRLTLSELDDIIKNASGIYAEIDGAKNELQVKLSNLSNLSHDL--VQEAIDhaqELQQEANELSR 606
Cdd:COG3883 3 ALALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELeaLQAEID---KLQAEIAEAEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 607 KLhsSDMNGLVQKALDASNVYENIVNYVS---EANETAEFA--LNTTDRIYDAVSGIDTQIIYHKDESENLLNQARELQA 681
Cdd:COG3883 80 EI--EERREELGERARALYRSGGSVSYLDvllGSESFSDFLdrLSALSKIADADADLLEELKADKAELEAKKAELEAKLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 682 KAESSSDEAvADTSRRVGGALARKSALKTRLSDAVKQLQAA-ERGDAQQRLGQSRLITEEANRTTMEVQQATAPMANNLT 760
Cdd:COG3883 158 ELEALKAEL-EAAKAELEAQQAEQEALLAQLSAEEAAAEAQlAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
250 260 270
....*....|....*....|....*....|....
gi 1622930177 761 NWSQNLQHFDSSAYNTAVDSARDAVRNLTEVVPQ 794
Cdd:COG3883 237 AAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAG 270
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
438-907 |
2.56e-07 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 55.68 E-value: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 438 TQRELVDEEADEAHELLSQAESWQR------------LHNETRTLFPVVLEQLDDYNA-------KLSDLQEALDQ---A 495
Cdd:COG5278 43 EHTYEVLRALEELLSALLDAETGQRgylltgdesflePYEEARAEIDELLAELRSLTAdnpeqqaRLDELEALIDQwlaE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 496 LNHVRDAEDMNRATAARQRDHEKQQERVREQMEAVNMSLNTSADSLTTPRLTLSELDDIIKNASGIYAEIDGAKNELQVK 575
Cdd:COG5278 123 LEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 576 LSNLSNLSHDLVQEAIDHAQELQQEANELSRKLHSSDMNGLVQKALDAsnvyenIVNYVSEANETAEFALNTTDRIYDAV 655
Cdd:COG5278 203 LLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALL------LALLAALALAALLAAALLALAALLLA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 656 SGIDTQIIYHKDESENLLNQARELQAKAESSSDEAVADTSRRVGGALARKSALKTRLSDAVKQLQAAERGDAQQRLGQSR 735
Cdd:COG5278 277 LAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAA 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 736 LITEEANRTTMEVQQATAPMANNLTNWSQNLQHFDSSAYNTAVDSARDAVRNLTEVVPQLLDQLRTVEQKRPASNVSASI 815
Cdd:COG5278 357 AAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAE 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 816 QRIRELIAQTRSVASKIQVSMMFDGQSAVEVHSRTSMDDLKAFTSLSLYMKPPVRQPELTETADQFILYLGSKNAKKEYM 895
Cdd:COG5278 437 EEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAA 516
|
490
....*....|..
gi 1622930177 896 GLAIKNDNLVYI 907
Cdd:COG5278 517 LAAALAAALASA 528
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
310-790 |
8.04e-07 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 54.09 E-value: 8.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 310 HVNEINATIYLLKTKLSERenqyALRKI--QINNAENTMKSLLSDVEELVEKEnqasrkgqliqKESMDTIKHAsqlveq 387
Cdd:pfam06160 68 LLFEAEELNDKYRFKKAKK----ALDEIeeLLDDIEEDIKQILEELDELLESE-----------EKNREEVEEL------ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 388 ahdmRDKIQEINNKMLYYGeeHELSPKEisEKLvlaQKMLEEIrrrQPFFTQRELVDEEAD--EAHELLSQaeswqrLHN 465
Cdd:pfam06160 127 ----KDKYRELRKTLLANR--FSYGPAI--DEL---EKQLAEI---EEEFSQFEELTESGDylEAREVLEK------LEE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 466 ETRTL------FPVVLEQL-DDYNAKLSDLQEALDQ------ALNHVRDAEDMNRATAARQRD----HEKQQERVREQME 528
Cdd:pfam06160 187 ETDALeelmedIPPLYEELkTELPDQLEELKEGYREmeeegyALEHLNVDKEIQQLEEQLEENlallENLELDEAEEALE 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 529 AVNMSLNTSADSLTTprltlsELD---DIIKNASGIYAEIDGAK---NELQVKLSNLsNLSHDLVQEAIDHAQELQQEAN 602
Cdd:pfam06160 267 EIEERIDQLYDLLEK------EVDakkYVEKNLPEIEDYLEHAEeqnKELKEELERV-QQSYTLNENELERVRGLEKQLE 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 603 ELSRKLHSsdmngLVQKALDASNVYENIVNYVSEanetaefalnttdrIYDAVSGIDTQIIYHKDESENLLNQarELQAK 682
Cdd:pfam06160 340 ELEKRYDE-----IVERLEEKEVAYSELQEELEE--------------ILEQLEEIEEEQEEFKESLQSLRKD--ELEAR 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 683 AESSS-DEAVADTSRRVggalaRKSAL-------KTRLSDAVKQLQaaergDAQQRLGQSRLITEEANRTTMEVQQAtap 754
Cdd:pfam06160 399 EKLDEfKLELREIKRLV-----EKSNLpglpesyLDYFFDVSDEIE-----DLADELNEVPLNMDEVNRLLDEAQDD--- 465
|
490 500 510
....*....|....*....|....*....|....*.
gi 1622930177 755 mannltnwsqnLQHFDSSAYNTaVDSARdavrnLTE 790
Cdd:pfam06160 466 -----------VDTLYEKTEEL-IDNAT-----LAE 484
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
307-827 |
8.40e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 54.20 E-value: 8.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 307 AHRHVNEINATIYLLKTKLSERENQYALRKiqiNNAENTMKSLLSDVEELVEKENQASRKGQLiQKESMDTIKHASQLVE 386
Cdd:TIGR00618 192 LHGKAELLTLRSQLLTLCTPCMPDTYHERK---QVLEKELKHLREALQQTQQSHAYLTQKREA-QEEQLKKQQLLKQLRA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 387 QAHDMRDKIQEINNKMlyygEEHELSPKeiSEKLVLAQKMLEEIRR---------------RQPFFTQRELVDEEADEAH 451
Cdd:TIGR00618 268 RIEELRAQEAVLEETQ----ERINRARK--AAPLAAHIKAVTQIEQqaqrihtelqskmrsRAKLLMKRAAHVKQQSSIE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 452 ELLSQAESWQRLHNETRTLFPVVLEQLDDYNAKLSDLQ------------EALDQALNHVRDAEDMNRATA----ARQRD 515
Cdd:TIGR00618 342 EQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQhihtlqqqkttlTQKLQSLCKELDILQREQATIdtrtSAFRD 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 516 HEKQQERVREQMEAvnmslntSADSLTTPRLTLSELDDIIKNASGIYAEIDGAKNELQVKLSNLSNLshdLVQEAIDHAQ 595
Cdd:TIGR00618 422 LQGQLAHAKKQQEL-------QQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQI---HLQETRKKAV 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 596 ELQ--QEANELSRKLHSSDMNgLVQKALDAsnvyenivnYVSEANetaefalntTDRiydaVSGIDTQIIYHKDESENL- 672
Cdd:TIGR00618 492 VLArlLELQEEPCPLCGSCIH-PNPARQDI---------DNPGPL---------TRR----MQRGEQTYAQLETSEEDVy 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 673 ------LNQARELQAKAESSSDEAVADTSRRvggalARKSALKTRLSDAVKQLQaaERGDAQQRLGQSRLITEEANRTTM 746
Cdd:TIGR00618 549 hqltseRKQRASLKEQMQEIQQSFSILTQCD-----NRSKEDIPNLQNITVRLQ--DLTEKLSEAEDMLACEQHALLRKL 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 747 EVQQATAPMANNLTNWSQNLQ----HFDSSAYNTAVDSARDAVRNLTEVVPQLLDQLRTVEQKrpASNVSASIQRIRELI 822
Cdd:TIGR00618 622 QPEQDLQDVRLHLQQCSQELAlkltALHALQLTLTQERVREHALSIRVLPKELLASRQLALQK--MQSEKEQLTYWKEML 699
|
....*
gi 1622930177 823 AQTRS 827
Cdd:TIGR00618 700 AQCQT 704
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
415-767 |
1.30e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.60 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 415 EISEKLVLAQKMLEEIRRR--QPFFTQRELVDEEADEAHELLSQAESWQRLHNETRTLFPVVLEQLDDYNAKLSDLQEAL 492
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKtgILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 493 DQALNHVRDAEDMNRATAARQRDHEKQQERVREQMEAVNmslntsadslttprltlSELDDIIKNASGIYAEIDGAKNEL 572
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQ-----------------KERQDLEQQRKQLEAQIAELQSEI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 573 QVKLSNLSNLSHDLvQEAIDHAQELQQEANELSRKLHSSDMNGLVQKAldasnvyENIVNYVSEANETAEFALNTTDRIY 652
Cdd:COG4372 146 AEREEELKELEEQL-ESLQEELAALEQELQALSEAEAEQALDELLKEA-------NRNAEKEEELAEAEKLIESLPRELA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 653 DAVSGIDTQIIYHKDESENLLNQARELQAKAESSSDEAVADTSRRVGGALARKSALKTRLSDAVKQLQAAERGDAQQRLG 732
Cdd:COG4372 218 EELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKL 297
|
330 340 350
....*....|....*....|....*....|....*
gi 1622930177 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 |
2.39e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 52.72 E-value: 2.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 313 EINATIYLLKTKLSERENQYALRKIQINNAENTMKSL---LSDVEELVEKENQASRKGQ--LIQKESM-DTIK-HASQLV 385
Cdd:TIGR04523 430 RLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLetqLKVLSRSINKIKQNLEQKQkeLKSKEKElKKLNeEKKELE 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 386 EQAHDMRDKIQEINNKMlyygEEHELSPKEISEKLVLAQKMLEEIRrrqpFFTQRELVDEEADEAHELLSQaeswqrLHN 465
Cdd:TIGR04523 510 EKVKDLTKKISSLKEKI----EKLESEKKEKESKISDLEDELNKDD----FELKKENLEKEIDEKNKEIEE------LKQ 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 466 ETRTLfpvvleqlddyNAKLSDLQEALDQalnhvrdaedmnrataarqrdHEKQQERVREQMEAVNMSLNTSADSLTTPR 545
Cdd:TIGR04523 576 TQKSL-----------KKKQEEKQELIDQ---------------------KEKEKKDLIKEIEEKEKKISSLEKELEKAK 623
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 546 LTLSELDDIIKNasgiyaeIDGAKNELQVKLSNLsnlsHDLVQEAIDHAQELQQEANELSRKLhsSDMNGLVQKALDASN 625
Cdd:TIGR04523 624 KENEKLSSIIKN-------IKSKKNKLKQEVKQI----KETIKEIRNKWPEIIKKIKESKTKI--DDIIELMKDWLKELS 690
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1622930177 626 VYENivNYVSEANETAEfaLNTTDRIYDAVSGIDTQIIYHKDESENLLN 674
Cdd:TIGR04523 691 LHYK--KYITRMIRIKD--LPKLEEKYKEIEKELKKLDEFSKELENIIK 735
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
320-608 |
2.83e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.84 E-value: 2.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 320 LLKTKLSERENQYALRKiqinNAENTMKsllsdVEELVEKENQASRKGQLIQKESMDTIKHASQLVEQAHDMRDKIQEIN 399
Cdd:PTZ00121 1680 AKKAEEDEKKAAEALKK----EAEEAKK-----AEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAK 1750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 400 nkmlyygeehelspKEISEKLVLAQKMLEEIRRRQPFFTQRELV-DEEADEAHEllSQAESWQRLHNETRTLFPVVLEQL 478
Cdd:PTZ00121 1751 --------------KDEEEKKKIAHLKKEEEKKAEEIRKEKEAViEEELDEEDE--KRRMEVDKKIKDIFDNFANIIEGG 1814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 479 DDYNAKLSDLQEALDQALNHVRDAEDMNRATAARQRDHEKQQERVREQMEAVNMSLNTSADSLTTPRLTLSELDDIIKna 558
Cdd:PTZ00121 1815 KEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEK-- 1892
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1622930177 559 sgiyaeIDGAKNELQVKLSNLSNLSHDLVQEAIDHAQELQQEANELSRKL 608
Cdd:PTZ00121 1893 ------IDKDDIEREIPNNNMAGKNNDIIDDKLDKDEYIKRDAEETREEI 1936
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
321-611 |
3.26e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 52.38 E-value: 3.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 321 LKTKLSEREnQYALrkiqinnaentMKSLLSDVEELVEKENQASRkgqlIQKESMDTIKHASQLVEQAHDMRDKIQEINN 400
Cdd:TIGR02169 216 LLKEKREYE-GYEL-----------LKEKEALERQKEAIERQLAS----LEEELEKLTEEISELEKRLEEIEQLLEELNK 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 401 KMLYYGEEHELspkEISEKLVLAQKMLEEIRRRQPfFTQRELVDEEADEA------HELLSQAESWQRLHNETRTlfpvv 474
Cdd:TIGR02169 280 KIKDLGEEEQL---RVKEKIGELEAEIASLERSIA-EKERELEDAEERLAkleaeiDKLLAEIEELEREIEEERK----- 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 475 leQLDDYNAKLSDLQEALDQALNHVRDAEDMNRATAARQRDHEKQQERVREQMEAVNMSLNTSADSLTTPRLTLSELDDI 554
Cdd:TIGR02169 351 --RRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAA 428
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622930177 555 IKNASGIYAEIDGAKNELQVKLS----NLSNLSHDLVQEAIDHAQeLQQEANELSRKLHSS 611
Cdd:TIGR02169 429 IAGIEAKINELEEEKEDKALEIKkqewKLEQLAADLSKYEQELYD-LKEEYDRVEKELSKL 488
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
309-580 |
3.32e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 52.38 E-value: 3.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 309 RHVNEINATIYLLKTKLSERENQYALRKIQINNAENTMKSLLSDvEELVEKENQASRKGQLIQKEsmDTIKHASQLVEQA 388
Cdd:TIGR02169 244 RQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEE-EQLRVKEKIGELEAEIASLE--RSIAEKERELEDA 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 389 HDMRDKIQEINNKMLyygEEHELSPKEISEKLVLAQKMLEEIrrrqpfftqrelvDEEADEAHELLSQAESWQRLHNETR 468
Cdd:TIGR02169 321 EERLAKLEAEIDKLL---AEIEELEREIEEERKRRDKLTEEY-------------AELKEELEDLRAELEEVDKEFAETR 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 469 TLFPVVLEQLDDYNAKLSDLQEALDQALNHVRDAEdmnrataARQRDHEKQQERVREQMEAVNMSLNTSADSLTTPRLTL 548
Cdd:TIGR02169 385 DELKDYREKLEKLKREINELKRELDRLQEELQRLS-------EELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKL 457
|
250 260 270
....*....|....*....|....*....|..
gi 1622930177 549 SELDDIIKNASGIYAEIDGAKNELQVKLSNLS 580
Cdd:TIGR02169 458 EQLAADLSKYEQELYDLKEEYDRVEKELSKLQ 489
|
|
| ApoLp-III_like |
cd13769 |
Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles ... |
710-836 |
3.94e-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: 3.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 710 TRLSDAVKQLQAAERGDAQQRLGQSRL-ITEEANRTtmeVQQATAPMANNLTNWSQNLQHFDSSAYNTAVDSARDAVRNL 788
Cdd:cd13769 1 TQLSELIQKAQEAINNLAQQVQKQLGLqNPEEVVNT---LKEQSDNFANNLQEVSSSLKEEAKKKQGEVEEAWNEFKTKL 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1622930177 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 |
4.07e-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: 4.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 339 INNAENTMKSL-----LSDVEELVEKeNQASRKGQLIQKESMDTI-KHASQLVEQAHDMRDKIQE----INNKMlyygee 408
Cdd:cd00176 16 LSEKEELLSSTdygddLESVEALLKK-HEALEAELAAHEERVEALnELGEQLIEEGHPDAEEIQErleeLNQRW------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 409 helspKEISEKLVLAQKMLEEIRRRQPFFTQrelVDEEADEAHELLSQAESWQRLHNETRtlfpvVLEQLDdynaKLSDL 488
Cdd:cd00176 89 -----EELRELAEERRQRLEEALDLQQFFRD---ADDLEQWLEEKEAALASEDLGKDLES-----VEELLK----KHKEL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1622930177 489 QEALDQALNHVRDAEDMNRATAARQrdHEKQQERVREQMEAVN 531
Cdd:cd00176 152 EEELEAHEPRLKSLNELAEELLEEG--HPDADEEIEEKLEELN 192
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
321-678 |
4.12e-06 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 52.36 E-value: 4.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 321 LKTKLS--ERENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLIQKESMDTIKHASQLVEQAHDMRDKIQEI 398
Cdd:TIGR01612 2049 IKEKIDnyEKEKEKFGIDFDVKAMEEKFDNDIKDIEKFENNYKHSEKDNHDFSEEKDNIIQSKKKLKELTEAFNTEIKII 2128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 399 NNKMLyygEEHELSPKeiseklvlaqkmLEEIRRRQPFFTQRELVDEeadeaheLLSQAESWQRLHNETRTLFPVVLEQL 478
Cdd:TIGR01612 2129 EDKII---EKNDLIDK------------LIEMRKECLLFSYATLVET-------LKSKVINHSEFITSAAKFSKDFFEFI 2186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 479 DDYNAKLSDLQEALDQALNHVRDAEDMNRATAARQRDHEKQQERVREQMEAVNM--------SLNTSADSLTTPRLTL-- 548
Cdd:TIGR01612 2187 EDISDSLNDDIDALQIKYNLNQTKKHMISILADATKDHNNLIEKEKEATKIINNltelftidFNNADADILHNNKIQIiy 2266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 549 --SELDDIIKNASGIYAEIDGAKnelqvklsnLSNLSHdLVQEAIDHAQE----LQQEANELSRKLHssDMNGLVQKALD 622
Cdd:TIGR01612 2267 fnSELHKSIESIKKLYKKINAFK---------LLNISH-INEKYFDISKEfdniIQLQKHKLTENLN--DLKEIDQYISD 2334
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622930177 623 ASNVYENIVNyvseanETAEFALNTTDRIYDAVSGIDTQIiyhkDESENLLNQARE 678
Cdd:TIGR01612 2335 KKNIFLHALN------ENTNFNFNALKEIYDDIINRENKA----DEIENINNKENE 2380
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
1263-1376 |
5.01e-06 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 47.70 E-value: 5.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 1263 FRTLQPNGLLFYYAS--GSDVFSISLDNGTVVMDVKG----IKVESVDKqYNDGLSHFVITSVSPTRYELIVDK-SRVGS 1335
Cdd:pfam00054 1 FRTTEPSGLLLYNGTqtERDFLALELRDGRLEVSYDLgsgaAVVRSGDK-LNDGKWHSVELERNGRSGTLSVDGeARPTG 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1622930177 1336 KNPTKGKieQTQAGEKKFYFGGSPISAQYA-------NFTGCISNAYF 1376
Cdd:pfam00054 80 ESPLGAT--TDLDVDGPLYVGGLPSLGVKKrrlaispSFDGCIRDVIV 125
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
321-677 |
7.05e-06 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 50.99 E-value: 7.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 321 LKTKLSERENQY--ALRKI--QINNAEntmkSLLSDVEELVEKEN--QASR-----KGQLIQ-KESMDTIKhaSQLVEQA 388
Cdd:PRK04778 152 LRKSLLANRFSFgpALDELekQLENLE----EEFSQFVELTESGDyvEAREildqlEEELAAlEQIMEEIP--ELLKELQ 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 389 HDMRDKIQEINN---KML---YYGEEHELSP--KEISEKLVLAQKMLEEIrrrqpfftqrelvdeEADEAHELLSQAESw 460
Cdd:PRK04778 226 TELPDQLQELKAgyrELVeegYHLDHLDIEKeiQDLKEQIDENLALLEEL---------------DLDEAEEKNEEIQE- 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 461 qRL-------------HNETRTLFPVVLEQLDDYNAKLSDLQEALDQ-----ALNHvRDAEdmnrataaRQRDHEKQQER 522
Cdd:PRK04778 290 -RIdqlydilerevkaRKYVEKNSDTLPDFLEHAKEQNKELKEEIDRvkqsyTLNE-SELE--------SVRQLEKQLES 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 523 VREQMEAVnmslntsADSLTTPRLTLSELDDIIKNASGIYAEIdgakNELQVKLSN-LSNLSHDlVQEAIDHAQELQQEA 601
Cdd:PRK04778 360 LEKQYDEI-------TERIAEQEIAYSELQEELEEILKQLEEI----EKEQEKLSEmLQGLRKD-ELEAREKLERYRNKL 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 602 NELSRKLHSSDMNGLVQKALDAsnvYENIVNYVSEANEtaefALNTT----DRIYDAVSGIDTQIIYHKDESENLLNQAR 677
Cdd:PRK04778 428 HEIKRYLEKSNLPGLPEDYLEM---FFEVSDEIEALAE----ELEEKpinmEAVNRLLEEATEDVETLEEETEELVENAT 500
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
339-829 |
7.64e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 50.99 E-value: 7.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 339 INNAENTMKSLLSDVE----ELVEKENQASRKgQLIQKESMDTIKhaSQLVEQAHDMRDKIQEINNkmlyygeehELSPK 414
Cdd:pfam12128 246 LQQEFNTLESAELRLShlhfGYKSDETLIASR-QEERQETSAELN--QLLRTLDDQWKEKRDELNG---------ELSAA 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 415 EisEKLVLAQKMLEEIRRRQpfftqRELVDEEADEAHELLSQAESWQRLHNETRTLFPVVLEQLDDYNAKLSDLQEALDQ 494
Cdd:pfam12128 314 D--AAVAKDRSELEALEDQH-----GAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKE 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 495 ALNhvRDAEDMN------RATAARQR-----DHEKQQERVREQMEAVNMSLNTSADSLttpRLTLSELDDIIKNASgiya 563
Cdd:pfam12128 387 QNN--RDIAGIKdklakiREARDRQLavaedDLQALESELREQLEAGKLEFNEEEYRL---KSRLGELKLRLNQAT---- 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 564 eidgAKNELQVKLSNLsnlshdlvQEAIDHAQELQQEANELSRKLHSSD--MNGLVQKALDASNVYENIVNYVSEANETA 641
Cdd:pfam12128 458 ----ATPELLLQLENF--------DERIERAREEQEAANAEVERLQSELrqARKRRDQASEALRQASRRLEERQSALDEL 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 642 EFALnttdriyDAVSG-----IDTQIIYHKDESENLLNQARELQAKAESSSDEAVADTSRRVGGA------------LAR 704
Cdd:pfam12128 526 ELQL-------FPQAGtllhfLRKEAPDWEQSIGKVISPELLHRTDLDPEVWDGSVGGELNLYGVkldlkridvpewAAS 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 705 KSALKTRLSDAVKQLQAAERGDAQQ--RLGQSRLITEEANRttmEVQQATAPMANN------LTNWSQNLQHFDSSAYNT 776
Cdd:pfam12128 599 EEELRERLDKAEEALQSAREKQAAAeeQLVQANGELEKASR---EETFARTALKNArldlrrLFDEKQSEKDKKNKALAE 675
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1622930177 777 AVDSARDAVRNLTEVVPQLLDQLRTV--EQKRPASNVSASIQRIRELIAQTRSVA 829
Cdd:pfam12128 676 RKDSANERLNSLEAQLKQLDKKHQAWleEQKEQKREARTEKQAYWQVVEGALDAQ 730
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
291-821 |
8.50e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.11 E-value: 8.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 291 IEEGKSGVlsvssgAAAH-RHVNEINAtiyLLKTKLSERENQYALRKiQINNAENTMKSLLSDVEELVEKEnqasrkgql 369
Cdd:PRK04863 263 ITESTNYV------AADYmRHANERRV---HLEEALELRRELYTSRR-QLAAEQYRLVEMARELAELNEAE--------- 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 370 iqkesmdtikhaSQLVEQAHDMRDKIQEINNKMLYYG--EEHELSPKEISEKLVlAQKMLeeirrrqpfftqRELVDEEA 447
Cdd:PRK04863 324 ------------SDLEQDYQAASDHLNLVQTALRQQEkiERYQADLEELEERLE-EQNEV------------VEEADEQQ 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 448 DEAHELLSQAEswqrlhnetrtlfpvvlEQLDDYNAKLSDLQEALDQAlnhvrdaedmnrATAARQRDHEKQQ-ERVReq 526
Cdd:PRK04863 379 EENEARAEAAE-----------------EEVDELKSQLADYQQALDVQ------------QTRAIQYQQAVQAlERAK-- 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 527 meavnmslntsadslttprlTLSELDDIiknasgiyaEIDGAKnelqvklsnlsnlshDLVQEAIDHAQELQQEANELSR 606
Cdd:PRK04863 428 --------------------QLCGLPDL---------TADNAE---------------DWLEEFQAKEQEATEELLSLEQ 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 607 KLHSSDMnglvqkaldasnvyenivnyvseANETAEFALNTTDRIYDAVSGIDTQiiyhkDESENLLNQARELQAKAEss 686
Cdd:PRK04863 464 KLSVAQA-----------------------AHSQFEQAYQLVRKIAGEVSRSEAW-----DVARELLRRLREQRHLAE-- 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 687 sdeavadtsrRVGGALARKSALKTRLsdavKQLQAAER--GDAQQRLGQS--------RLITE-EANRTTMEVQQATA-- 753
Cdd:PRK04863 514 ----------QLQQLRMRLSELEQRL----RQQQRAERllAEFCKRLGKNlddedeleQLQEElEARLESLSESVSEAre 579
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 754 ---PMANNLTNWSQNLQHFDSSAynTAVDSARDAVRNLTEVVP--------------QLLDQLR--TVEQKRPASNVSAS 814
Cdd:PRK04863 580 rrmALRQQLEQLQARIQRLAARA--PAWLAAQDALARLREQSGeefedsqdvteymqQLLERERelTVERDELAARKQAL 657
|
....*..
gi 1622930177 815 IQRIREL 821
Cdd:PRK04863 658 DEEIERL 664
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
321-574 |
1.27e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 50.43 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 321 LKTKLSERENQYA--LRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLIQKESMDTikhasqlVEQAHDMRDKIQEI 398
Cdd:TIGR00606 797 FQMELKDVERKIAqqAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQ-------QEQIQHLKSKTNEL 869
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 399 NNKMLYYGEehelspkEISEKLVLAQKMLEEIRRRQpfftqrELVDEEADEAHELLSQAESWQRLHNETRTLFPVVLEQL 478
Cdd:TIGR00606 870 KSEKLQIGT-------NLQRRQQFEEQLVELSTEVQ------SLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSN 936
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 479 DDYNAKLSDLQEALDQALNHVRDAED----------MNRAT-----AARQRDHEKQQERVREQMEAVNMSLNTS--ADSL 541
Cdd:TIGR00606 937 KKAQDKVNDIKEKVKNIHGYMKDIENkiqdgkddylKQKETelntvNAQLEECEKHQEKINEDMRLMRQDIDTQkiQERW 1016
|
250 260 270
....*....|....*....|....*....|...
gi 1622930177 542 TTPRLTLSELDDIIKNASGIYAEIDGAKNELQV 574
Cdd:TIGR00606 1017 LQDNLTLRKRENELKEVEEELKQHLKEMGQMQV 1049
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
284-665 |
1.42e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.52 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 284 LRLAALSIEEGKSGVLSVSSGAAAHRHVNEINATIYLLKTKLSERENQYALRKIQINNAENTMKSLLSDVEELvEKENQA 363
Cdd:COG4372 13 LSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL-NEQLQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 364 SRKGQLIQKESMDTIKhasqlvEQAHDMRDKIQEINnkmlyygeehelspKEISEKLVLAQKMLEEIRRRQPFFTQRElv 443
Cdd:COG4372 92 AQAELAQAQEELESLQ------EEAEELQEELEELQ--------------KERQDLEQQRKQLEAQIAELQSEIAERE-- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 444 deeaDEAHELLSQAESWQRLhnetrtlfpvvLEQLDDYNAKLSD--LQEALDQALNHVRDAEDMNRATAARQRDHEKQQE 521
Cdd:COG4372 150 ----EELKELEEQLESLQEE-----------LAALEQELQALSEaeAEQALDELLKEANRNAEKEEELAEAEKLIESLPR 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 522 RVREQMEAVNMSLNTSADSLTTPRLTLSELDDIIKNASGIYAEIDGAKNELQVKLSNLSNLSHDLVQEAIDHAQELQQEA 601
Cdd:COG4372 215 ELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALE 294
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622930177 602 NELSRKLHSSDMNGLVQKALDASNVYENIVNYVSEANETAEFALNTTDRIYDAVSGIDTQIIYH 665
Cdd:COG4372 295 LKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLEL 358
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
474-707 |
1.54e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.44 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 474 VLEQLDDYNAKLSDLQEALDQALNHVRDAE----DMNRATAARQRDHEKQQERVREQMEAVNMSLNT--------SADSL 541
Cdd:COG3883 35 AQAELDALQAELEELNEEYNELQAELEALQaeidKLQAEIAEAEAEIEERREELGERARALYRSGGSvsyldvllGSESF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 542 TT--PRLTLseLDDIIKNASGIYAEIDGAKNELQVKLSNLSnlshDLVQEAIDHAQELQQEANELSRKLhsSDMNGLVQK 619
Cdd:COG3883 115 SDflDRLSA--LSKIADADADLLEELKADKAELEAKKAELE----AKLAELEALKAELEAAKAELEAQQ--AEQEALLAQ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 620 ALDASNVYENIVNYVSEANETAEFALNTTDRIYDAVSGIDTQIIYHKDESENLLNQARELQAKAESSSDEAVADTSRRVG 699
Cdd:COG3883 187 LSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAG 266
|
....*...
gi 1622930177 700 GALARKSA 707
Cdd:COG3883 267 AAAGAAGA 274
|
|
| VSP |
pfam03302 |
Giardia variant-specific surface protein; |
67-273 |
1.69e-05 |
|
Giardia variant-specific surface protein;
Pssm-ID: 146106 [Multi-domain] Cd Length: 397 Bit Score: 49.20 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 67 CNAGFFRTlSGECVPCD-----CNGNS----NECLDG-----------------------SGFCVHCQRNTTG-EHCEKC 113
Cdd:pfam03302 96 CNDGFYKS-GDACSPCHescktCSGGTasdcTECLTGkalrygndgtkgtcgegcttgtgAGACKTCGLTIDGtSYCSEC 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 114 -------LDGYIGDSIRGAPRFCQLCPCPLPHLANFAESCYRKNGAV--------RCICKENYAGPNCERCAPGYYGNPL 178
Cdd:pfam03302 175 ateteypQNGVCTSTAARATATCKASSVANGMCSSCANGYFRMNGGCyettkfpgKSVCEEANSGGTCQKEAPGYKLNNG 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 179 LIGSTCKKCD-CSGNSDPNLIFED-------CDEVTGQCRNCLRNTTgfKCERCAPGYYGDARIAKNCAVCNCGGGpcds 250
Cdd:pfam03302 255 DLVTCSPGCKtCTSNTVCTTCMDGyvktsdsCTKCDSSCETCTGATT--TCKTCATGYYKSGTGCVSCTSSESDNG---- 328
|
250 260
....*....|....*....|....*
gi 1622930177 251 VTG--ECLEegLEPPTGtDCSTISC 273
Cdd:pfam03302 329 ITGvkGCLN--CAPPSN-NKGSVLC 350
|
|
| PLU-1 |
pfam08429 |
PLU-1-like protein; Sequences in this family bear similarity to the central region of PLU-1. ... |
321-604 |
2.47e-05 |
|
PLU-1-like protein; Sequences in this family bear similarity to the central region of PLU-1. This is a nuclear protein that may have a role in DNA-binding and transcription, and is closely associated with the malignant phenotype of breast cancer. This region is found in various other Jumonji/ARID domain-containing proteins (see pfam02373, pfam01388).
Pssm-ID: 462475 [Multi-domain] Cd Length: 336 Bit Score: 48.36 E-value: 2.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 321 LKTKLSERENqyalRKIQINNAENTMKSLLSDVEELVEKENQ-------ASRKGQLIQKE---SMDTIKHASQLVEQAHD 390
Cdd:pfam08429 21 LRALLNEAEK----IKFPLPELLQDLRAFVQRANKWVEEAQQllsrkqqTRRKNEAEEDErerEKRTVEELRKLLEEADN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 391 MRDKIQEInnkmlyygeeHELspKEISEKLV----LAQKMLEEirrrqpfftqrELVDEEADEAHELLSQAESwqrlhne 466
Cdd:pfam08429 97 LPFDCPEI----------EQL--KELLEEIEefqkRAREALSE-----------EPPSLSIEELEELLEEGKS------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 467 trtlFPVVLEQLDDynaklsdLQEALDQA--LNHVRDAEDMNRAT-------------AARQRDHEKQQERVREQMEAVN 531
Cdd:pfam08429 147 ----FNVDLPELEE-------LEKVLEQLkwLEEVRETSRKKSLTledvrelieegveLGIPPPYEDLMAELQELLTAGE 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622930177 532 MSLNTSADSLTTPRLTLSELDDIIKNASGIyaeidgaknelQVKLSNLSNLshdlvQEAIDHAQELQQEANEL 604
Cdd:pfam08429 216 RWEEKAKELLSRERVSLAQLEALSKEAQEI-----------PVSLPNLAAL-----DEILKKAREWQRQIEAL 272
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
440-826 |
3.95e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 48.80 E-value: 3.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 440 RELVDEEADEAHELLSQAESW---QRLHNETRtlfpvvlEQLDDYNAKLSDLQEALDQA---LNHVRDAEDMNRATAARQ 513
Cdd:COG3096 281 RELSERALELRRELFGARRQLaeeQYRLVEMA-------RELEELSARESDLEQDYQAAsdhLNLVQTALRQQEKIERYQ 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 514 RDHEKQQERVREQMEAVnmslNTSADSLTTPRLTLSELDDIIKNASGIYAEIDGAKNELQVK----------------LS 577
Cdd:COG3096 354 EDLEELTERLEEQEEVV----EEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRaiqyqqavqalekaraLC 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 578 NLSNLS----HDLVQEAIDHAQELQQEANELSRKLHSSDM-NGLVQKALDAsnvYENIVNYV--SEANETAEFALnTTDR 650
Cdd:COG3096 430 GLPDLTpenaEDYLAAFRAKEQQATEEVLELEQKLSVADAaRRQFEKAYEL---VCKIAGEVerSQAWQTARELL-RRYR 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 651 IYDAVSGIDTQIIYHKDESENLLNQarelQAKAESSSDEavadTSRRVGGALARKSALKTRLSDAVKQLQ--AAERGDAQ 728
Cdd:COG3096 506 SQQALAQRLQQLRAQLAELEQRLRQ----QQNAERLLEE----FCQRIGQQLDAAEELEELLAELEAQLEelEEQAAEAV 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 729 QRLGQSRLiTEEANRTTMEVQQATAPM-------ANNLTNwsQNLQHFDSSAyntAVDSARDavrnltevvpQLLDQLRT 801
Cdd:COG3096 578 EQRSELRQ-QLEQLRARIKELAARAPAwlaaqdaLERLRE--QSGEALADSQ---EVTAAMQ----------QLLERERE 641
|
410 420
....*....|....*....|....*
gi 1622930177 802 VEQKRpasnvSASIQRIRELIAQTR 826
Cdd:COG3096 642 ATVER-----DELAARKQALESQIE 661
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
321-831 |
4.05e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 48.63 E-value: 4.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 321 LKTKLSERENqyalRKIQINNAENTMKSLLSDVEELVEKENQASRKGQL--------IQKESMDTIKHASQ---LVEQAH 389
Cdd:pfam01576 80 LESRLEEEEE----RSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLekvtteakIKKLEEDILLLEDQnskLSKERK 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 390 DMRDKIQEINNKMlyyGEEHELSpKEISeKLVLAQKML---EEIRRRQPFFTQREL------VDEEADEAHE----LLSQ 456
Cdd:pfam01576 156 LLEERISEFTSNL---AEEEEKA-KSLS-KLKNKHEAMisdLEERLKKEEKGRQELekakrkLEGESTDLQEqiaeLQAQ 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 457 AE----SWQRLHNETRTLfpvvLEQLDDYNAKLSDLQEALDQALNHVRDA-EDMNRATAARQRdHEKQQERVREQMEAVN 531
Cdd:pfam01576 231 IAelraQLAKKEEELQAA----LARLEEETAQKNNALKKIRELEAQISELqEDLESERAARNK-AEKQRRDLGEELEALK 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 532 MSLNTSADS------LTTPRLT------------------------------LSELDDIIKNASGIYAEIDGAK------ 569
Cdd:pfam01576 306 TELEDTLDTtaaqqeLRSKREQevtelkkaleeetrsheaqlqemrqkhtqaLEELTEQLEQAKRNKANLEKAKqalese 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 570 -NELQVKLSNLSNLSHDLVQ---EAIDHAQELQQEANELSRklHSSDMNGLVQKaldASNVYENIVNYVSEANETAEfal 645
Cdd:pfam01576 386 nAELQAELRTLQQAKQDSEHkrkKLEGQLQELQARLSESER--QRAELAEKLSK---LQSELESVSSLLNEAEGKNI--- 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 646 nttdRIYDAVSGIDTQIiyhkDESENLLNQarELQAKAESSSdeavadtsrRVGGALARKSALKTRLSDAVKQLQAAER- 724
Cdd:pfam01576 458 ----KLSKDVSSLESQL----QDTQELLQE--ETRQKLNLST---------RLRQLEDERNSLQEQLEEEEEAKRNVERq 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 725 -GDAQQRLGQSRLITEEANRTTMEVQQATAPMANNLTNWSQNLQHfDSSAYNTaVDSARDAVRnltevvpQLLDQLrTVE 803
Cdd:pfam01576 519 lSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEE-KAAAYDK-LEKTKNRLQ-------QELDDL-LVD 588
|
570 580 590
....*....|....*....|....*....|.
gi 1622930177 804 QKRPASNVSASIQRIR---ELIAQTRSVASK 831
Cdd:pfam01576 589 LDHQRQLVSNLEKKQKkfdQMLAEEKAISAR 619
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
521-764 |
4.09e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 48.89 E-value: 4.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 521 ERVREQMEAVNMSLNTSADSLTTPRLTLSELDDIIKnaSGIYAEIDGAKNELQVKLSNLSNLSHDL---VQEAIDHAQEL 597
Cdd:TIGR01612 500 MRMKDFKDIIDFMELYKPDEVPSKNIIGFDIDQNIK--AKLYKEIEAGLKESYELAKNWKKLIHEIkkeLEEENEDSIHL 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 598 QQEAN---------------------ELSRKLHS-SDMNGLVQKALDASNVYENIVNYVSEANETAEFA----LNTTDRI 651
Cdd:TIGR01612 578 EKEIKdlfdkyleiddeiiyinklklELKEKIKNiSDKNEYIKKAIDLKKIIENNNAYIDELAKISPYQvpehLKNKDKI 657
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 652 YDAVSGIDTQI--------------IYHKDESENLLNQAR--ELQAKAESSSDEAVADTSRRVGGALARKSALKTRLSDA 715
Cdd:TIGR01612 658 YSTIKSELSKIyeddidalynelssIVKENAIDNTEDKAKldDLKSKIDKEYDKIQNMETATVELHLSNIENKKNELLDI 737
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1622930177 716 VKQLQAAERGDaqqrlgqsrlITEEANRTTMEVQQATAPMANNLTNWSQ 764
Cdd:TIGR01612 738 IVEIKKHIHGE----------INKDLNKILEDFKNKEKELSNKINDYAK 776
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
882-1013 |
9.27e-05 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 43.84 E-value: 9.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 882 ILYLGSKNaKKEYMGLAIKNDNLVYIYNLGTKDVEIPldSKPVSSwPAYFSIVKIERVGKHGkvFLTV---PSLSSTAEe 958
Cdd:pfam00054 10 LLYNGTQT-ERDFLALELRDGRLEVSYDLGSGAAVVR--SGDKLN-DGKWHSVELERNGRSG--TLSVdgeARPTGESP- 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622930177 959 kfikkgefSGDDSLLDLDpedTVFYVGGVPSNFKLPNSL-NLPGFVGCLELATLNN 1013
Cdd:pfam00054 83 --------LGATTDLDVD---GPLYVGGLPSLGVKKRRLaISPSFDGCIRDVIVNG 127
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
354-607 |
1.31e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 46.61 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 354 EELVEKENQASRKGQLIQKEsMDTIKHASQLVEQAHDM-RDKIQEINNKMLYYGEEHELSpKEIsEKLVLAQKMLEEIRR 432
Cdd:COG0497 154 EELLEEYREAYRAWRALKKE-LEELRADEAERARELDLlRFQLEELEAAALQPGEEEELE-EER-RRLSNAEKLREALQE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 433 rqpfftQRELVDEEADEAHELLSQAESWqrlhnetrtlfpvvLEQLDDYNAKLSDLQEALDQALNHVRDAEDMNRATAAR 512
Cdd:COG0497 231 ------ALEALSGGEGGALDLLGQALRA--------------LERLAEYDPSLAELAERLESALIELEEAASELRRYLDS 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 513 QRDHEKQQERVREQMEAVNmslntsadslttpRLTL---SELDDIIKnasgiYAEidgaknELQVKLSNLSNLSHDL--V 587
Cdd:COG0497 291 LEFDPERLEEVEERLALLR-------------RLARkygVTVEELLA-----YAE------ELRAELAELENSDERLeeL 346
|
250 260
....*....|....*....|.
gi 1622930177 588 QEAIDHA-QELQQEANELSRK 607
Cdd:COG0497 347 EAELAEAeAELLEAAEKLSAA 367
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
344-607 |
1.32e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.06 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 344 NTMKSLLSDVEELVEKENQASRK-GQLIQKESmdtikhasQLVEQAHDMRDKIQEINNKMlyygeehelspKEISEKlvl 422
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEiEELKEKRD--------ELNEELKELAEKRDELNAQV-----------KELREE--- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 423 AQKMleeirrrqpfftqRELVDEEADEAHELLSQAESWQrlhNETRTLFpvvlEQLDDYNAKLSDLQ------EALDQAL 496
Cdd:COG1340 59 AQEL-------------REKRDELNEKVKELKEERDELN---EKLNELR----EELDELRKELAELNkaggsiDKLRKEI 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 497 NHVRDAEDmnraTAARQRDHEKQ----QERVREQMEAVNMSLNTSadslttprltlSELDDIIKNASGIYAEIDGAKNEL 572
Cdd:COG1340 119 ERLEWRQQ----TEVLSPEEEKElvekIKELEKELEKAKKALEKN-----------EKLKELRAELKELRKEAEEIHKKI 183
|
250 260 270
....*....|....*....|....*....|....*
gi 1622930177 573 QvKLSNLSNLSHDLVQEAIDHAQELQQEANELSRK 607
Cdd:COG1340 184 K-ELAEEAQELHEEMIELYKEADELRKEADELHKE 217
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
311-833 |
1.37e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.82 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 311 VNEINATIYLLKTKLSERENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLIqKESMDTIKHASQLVEQAHD 390
Cdd:PRK01156 199 LENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEI-KTAESDLSMELEKNNYYKE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 391 MRDKIQEINNKMLYYGEEHELSPKEISEKLVLAQKMLEEIrrrqpfftqrelvDEEADEAHELLSQAESWQRLHNEtrtl 470
Cdd:PRK01156 278 LEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNI-------------DAEINKYHAIIKKLSVLQKDYND---- 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 471 FPVVLEQLDDYNAKLSDLQEALDQALNHVRDAEDMNRataaRQRDHEKQQERVREQMEAVNMSLNTSADSLTTPRLTL-S 549
Cdd:PRK01156 341 YIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKK----KIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEInV 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 550 ELDDIIKNASGIYAEIDGAKNELQVKLSNLSNL-----------------SHDLVQEAIDHAQELQQEANELSRKLHSSD 612
Cdd:PRK01156 417 KLQDISSKVSSLNQRIRALRENLDELSRNMEMLngqsvcpvcgttlgeekSNHIINHYNEKKSRLEEKIREIEIEVKDID 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 613 MNGLVQKALDASNVYENIVNYVSEANETAEFALNTTDrIYDAVSgidtQIIYHKDESENLLNQAR-----ELQAKAESSS 687
Cdd:PRK01156 497 EKIVDLKKRKEYLESEEINKSINEYNKIESARADLED-IKIKIN----ELKDKHDKYEEIKNRYKslkleDLDSKRTSWL 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 688 DEAVADTSRRVGGALARKSALKTRLSDAVKQLQAAERG--DAQQRLGQS-RLITEEANRTTMEVQQATAPMAnNLTNWSQ 764
Cdd:PRK01156 572 NALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGfpDDKSYIDKSiREIENEANNLNNKYNEIQENKI-LIEKLRG 650
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622930177 765 NLQHFDSSAynTAVDSARDAVRNLTEVVPQLLDQLRTVEQKRPASNVSASiqRIRELIAQTRSVASKIQ 833
Cdd:PRK01156 651 KIDNYKKQI--AEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRA--RLESTIEILRTRINELS 715
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
476-687 |
1.56e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.55 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 476 EQLDDYNAKLSDLQEALD--QALNHVRDAEDMNRATAARQRDHEKQQERVREQMEAVNMSLNTSADSLTTPRLTLSELdd 553
Cdd:COG3206 182 EQLPELRKELEEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL-- 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 554 iikNASGIYAEIDGAKNELQVKLSNLSNL---SHDLVQEAIDHAQELQQE-ANELSRKLHS--SDMNGLVQKALDASNVY 627
Cdd:COG3206 260 ---LQSPVIQQLRAQLAELEAELAELSARytpNHPDVIALRAQIAALRAQlQQEAQRILASleAELEALQAREASLQAQL 336
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 628 ENIVNYVSEANETaEFALNTTDRIYDAvsgidTQIIYhkdesENLLNQARELQAKAESSS 687
Cdd:COG3206 337 AQLEARLAELPEL-EAELRRLEREVEV-----ARELY-----ESLLQRLEEARLAEALTV 385
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
313-575 |
2.65e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.21 E-value: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 313 EINATIYLLKTKLSERENQYALRKIQINNAE-NTMKSLLSDVEELVE----KENQASRKGQLIQKESMDTIKHASQLVEQ 387
Cdd:TIGR02169 769 ELEEDLHKLEEALNDLEARLSHSRIPEIQAElSKLEEEVSRIEARLReieqKLNRLTLEKEYLEKEIQELQEQRIDLKEQ 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 388 AHDMRDKIQEIN---NKMLYYGEEHELSPKEISEKLV-------LAQKMLEEIRRRQpfftqRELvDEEADEAHELLSQ- 456
Cdd:TIGR02169 849 IKSIEKEIENLNgkkEELEEELEELEAALRDLESRLGdlkkerdELEAQLRELERKI-----EEL-EAQIEKKRKRLSEl 922
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 457 AESWQRLHNETRTLFPVVLEQLDDYNAKLS--DLQEALDQALNHVRDAEDMN-RA------TAARQRDHEKQQERVREQM 527
Cdd:TIGR02169 923 KAKLEALEEELSEIEDPKGEDEEIPEEELSleDVQAELQRVEEEIRALEPVNmLAiqeyeeVLKRLDELKEKRAKLEEER 1002
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1622930177 528 EAVnmsLNTSADSLTTPRLTLSE-LDDIIKNASGIYAEIDGAKNELQVK 575
Cdd:TIGR02169 1003 KAI---LERIEEYEKKKREVFMEaFEAINENFNEIFAELSGGTGELILE 1048
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
476-679 |
3.09e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.39 E-value: 3.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 476 EQLDDYNAKLSDLQEALDQALNHVRDAEDMNRATAarqRDHEKQQERVREQMEAVNMSLNTSADSLTTPRLTLSELDDII 555
Cdd:PHA02562 195 QQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEA---KTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKI 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 556 KNASGI---YAE----------IDGAKNELQVKLSNLSNLSH--DLVQEAIDHAQELQQEANELSRKLHssDMNGlvqka 620
Cdd:PHA02562 272 EQFQKVikmYEKggvcptctqqISEGPDRITKIKDKLKELQHslEKLDTAIDELEEIMDEFNEQSKKLL--ELKN----- 344
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622930177 621 lDASNVYENIVNYVSEAnetaefalnttDRIYDAVSGIDTQIIYHKDESENLLNQAREL 679
Cdd:PHA02562 345 -KISTNKQSLITLVDKA-----------KKVKAAIEELQAEFVDNAEELAKLQDELDKI 391
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
368-608 |
3.12e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 368 QLIQKESMDTIKHASQLVEQAHDMRDKIQEINNKMLYYGEEHELSPKEISEKLvlaqKMLEEIRRRQpffTQRELVDEEA 447
Cdd:COG4717 291 LLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELL----DRIEELQELL---REAEELEEEL 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 448 DEAHELLSQAESWQRLHNETRTLFPVVLEQLDDYNAKLSDLQEALDQALNHVRDAEDMNRATaarqrdhekQQERVREQM 527
Cdd:COG4717 364 QLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEAL---------DEEELEEEL 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 528 EAVNMSLNTSADSLTTPRLTLSELDDIIKNA--SGIYAEIDGAKNELQVKLSNLS------NLSHDLVQEAIDHAQE--- 596
Cdd:COG4717 435 EELEEELEELEEELEELREELAELEAELEQLeeDGELAELLQELEELKAELRELAeewaalKLALELLEEAREEYREerl 514
|
250
....*....|....
gi 1622930177 597 --LQQEANELSRKL 608
Cdd:COG4717 515 ppVLERASEYFSRL 528
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
306-767 |
3.28e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 45.73 E-value: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 306 AAHRHVNEINATIYLLKTKLSERENQYA-LRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLIQKESMDTIKhASQL 384
Cdd:pfam02463 227 LYLDYLKLNEERIDLLQELLRDEQEEIEsSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSE-LLKL 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 385 VEQAHDMRDKIQEinnkmlyygeeHELSPKEISEKLVLAQK--------MLEEIRRRQPF-----FTQRELVDEEADEAH 451
Cdd:pfam02463 306 ERRKVDDEEKLKE-----------SEKEKKKAEKELKKEKEeieelekeLKELEIKREAEeeeeeELEKLQEKLEQLEEE 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 452 ELLSQAESWQRLHNETRTLFPVVLEQLDDYNAKLSDLQEAldqalnhvRDAEDMNRATAARQRDHEKQQERVREQMEAvn 531
Cdd:pfam02463 375 LLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELA--------RQLEDLLKEEKKEELEILEEEEESIELKQG-- 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 532 mSLNTSADSLTTPRLTLSELDDIIKNASGIYAEIDGAKNELQVKLsnlsnLSHDLVQEAIDHAQELQQEANELSRKLHSS 611
Cdd:pfam02463 445 -KLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLEL-----LLSRQKLEERSQKESKARSGLKVLLALIKD 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 612 DMNGLVQKALDASNVYENIVNYVSEANETAEFALNTTDRI--------YDAVSGIDTQIIYHKDESENLLNQARELQ--- 680
Cdd:pfam02463 519 GVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADeveerqklVRALTELPLGARKLRLLIPKLKLPLKSIAvle 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 681 -------AKAESSSDEAVADTSRRVGGALARKSALKTRLSDAVKQLQaaERGDAQQRLGQSRLITEEANRTTMEVQQATA 753
Cdd:pfam02463 599 idpilnlAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKE--SGLRKGVSLEEGLAEKSEVKASLSELTKELL 676
|
490
....*....|....
gi 1622930177 754 PMANNLTNWSQNLQ 767
Cdd:pfam02463 677 EIQELQEKAESELA 690
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
666-824 |
3.75e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 3.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 666 KDESENLLNQARELQAK-AESSSDEAVADTSRR--------VGGAlaRKSALKTRLSDAVKQLQAAE--RGDAQQRLGQS 734
Cdd:COG4913 294 EAELEELRAELARLEAElERLEARLDALREELDeleaqirgNGGD--RLEQLEREIERLERELEERErrRARLEALLAAL 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 735 RLiTEEANRTTMEVQQATAPMAnnLTNWSQnlqhfDSSAYNTAVDSARDAVRNLTEVVPQLLDQLRTVEQKRpaSNVSAS 814
Cdd:COG4913 372 GL-PLPASAEEFAALRAEAAAL--LEALEE-----ELEALEEALAEAEAALRDLRRELRELEAEIASLERRK--SNIPAR 441
|
170
....*....|
gi 1622930177 815 IQRIRELIAQ 824
Cdd:COG4913 442 LLALRDALAE 451
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
414-610 |
3.98e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 3.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 414 KEISEKLVLAQKMLEEIRRrqpfftQRELVDEEADEAHELLSQAES---WQRLHNETRTLfPVVLEQLDDYNAKLSDLQE 490
Cdd:COG4913 620 AELEEELAEAEERLEALEA------ELDALQERREALQRLAEYSWDeidVASAEREIAEL-EAELERLDASSDDLAALEE 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 491 ALDQALNHVRDAEDMNRATAARQRDHEKQQERVREQMEAVNMSLNT-SADSLTTPRLTLSELddiiknasgiYAEIDGAK 569
Cdd:COG4913 693 QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAaEDLARLELRALLEER----------FAAALGDA 762
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1622930177 570 NELQVKlsnlSNLSHDLVQEaidhAQELQQEANELSRKLHS 610
Cdd:COG4913 763 VERELR----ENLEERIDAL----RARLNRAEEELERAMRA 795
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
323-550 |
4.01e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 4.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 323 TKLSERENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLIQKEsMDT----IKHASQLVEQAhdmRDKIQEI 398
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAE-IDKlqaeIAEAEAEIEER---REELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 399 NNKMlyYGEEHELSPKEIseklVLAQKMLEEirrrqpFFTQRELVDEEADEAHELLSQAESWQRLHNETRTLfpvVLEQL 478
Cdd:COG3883 92 ARAL--YRSGGSVSYLDV----LLGSESFSD------FLDRLSALSKIADADADLLEELKADKAELEAKKAE---LEAKL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622930177 479 DDYNAKLSDLQEALDQALNHVRDAEDMNRATAARQRDHEKQQERVREQMEAVNMSLNTSADSLTTPRLTLSE 550
Cdd:COG3883 157 AELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
508-814 |
4.92e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 4.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 508 ATAARQRDHEKQQERVREQMEAVNMSLNTSADSLTTPRLTLSELDDIIKNASGIYAEIDGAKNELQVKLsnlsnlshdlv 587
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL----------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 588 qeaidhaQELQQEANELSRKLHSsdmnglvQKALDASNVYeniVNYVSEANETAEFALNTTDriydaVSGIDTQIIYHKD 667
Cdd:COG4942 86 -------AELEKEIAELRAELEA-------QKEELAELLR---ALYRLGRQPPLALLLSPED-----FLDAVRRLQYLKY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 668 ESENLLNQARELQAKaesssdeavadtsrrvggaLARKSALKTRLSDAVKQLQAAErgdAQQRLGQSRLITEEANRTTME 747
Cdd:COG4942 144 LAPARREQAEELRAD-------------------LAELAALRAELEAERAELEALL---AELEEERAALEALKAERQKLL 201
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622930177 748 VQQATapmannltnwsqnlqhfDSSAYNTAVDSARDAVRNLTEVVPQLLDQLRTVEQKRPASNVSAS 814
Cdd:COG4942 202 ARLEK-----------------ELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
343-682 |
5.14e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.33 E-value: 5.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 343 ENTMKSLLSDVEELVEKENQASRKGQLIQKesmdTIKHASQLV------------EQA-HDMRDKIQEINNKMlyygEEH 409
Cdd:PRK04863 785 EKRIEQLRAEREELAERYATLSFDVQKLQR----LHQAFSRFIgshlavafeadpEAElRQLNRRRVELERAL----ADH 856
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 410 ELSPKEISEKLVLAQKMLEEIRRRQPFFT--QRELVDEEADEAHELLSQAESWQR-LHNETRTLfpvvlEQLDDYNAKLS 486
Cdd:PRK04863 857 ESQEQQQRSQLEQAKEGLSALNRLLPRLNllADETLADRVEEIREQLDEAEEAKRfVQQHGNAL-----AQLEPIVSVLQ 931
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 487 DLQEALDQAlnhvrdaedmnrataarQRDH---EKQQERVREQMEAVnmslntsaDSLTTPRLTLSelddiIKNASGIYA 563
Cdd:PRK04863 932 SDPEQFEQL-----------------KQDYqqaQQTQRDAKQQAFAL--------TEVVQRRAHFS-----YEDAAEMLA 981
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 564 EIDGAKNELQVKLSNLSNLSHDLVQEAIDHAQELQQeANELSRKLHSSdMNGLVQKALDASNVYENI-VNYVSEANETAE 642
Cdd:PRK04863 982 KNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQ-YNQVLASLKSS-YDAKRQMLQELKQELQDLgVPADSGAEERAR 1059
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1622930177 643 falNTTDRIYDAVSG-------IDTQIIYHKDESENLLNQARELQAK 682
Cdd:PRK04863 1060 ---ARRDELHARLSAnrsrrnqLEKQLTFCEAEMDNLTKKLRKLERD 1103
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
312-678 |
5.46e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.89 E-value: 5.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 312 NEINATIYLLKTKLSerenqyalrkiqinNAENTMKSLLSDVEELveKENQASRKGQ---------LIQKESMDTIKHAS 382
Cdd:PRK01156 412 NEINVKLQDISSKVS--------------SLNQRIRALRENLDEL--SRNMEMLNGQsvcpvcgttLGEEKSNHIINHYN 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 383 qlvEQAHDMRDKIQEINNKMlyygeehelspKEISEKLVLAQKMLE-----EIRRRQPFFTQ-----RELVDEEADEAhE 452
Cdd:PRK01156 476 ---EKKSRLEEKIREIEIEV-----------KDIDEKIVDLKKRKEyleseEINKSINEYNKiesarADLEDIKIKIN-E 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 453 LLSQAESWQRLHNETRTLFPVVLEQ-LDDYNAKLS--------DLQEALDQALNHVRDAED-MNRATAARQRDHEKQQER 522
Cdd:PRK01156 541 LKDKHDKYEEIKNRYKSLKLEDLDSkRTSWLNALAvislidieTNRSRSNEIKKQLNDLESrLQEIEIGFPDDKSYIDKS 620
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 523 VREQMEAVNmSLNTSADSLTTPRLTLSELDDIIKNASGIYAEIDG---AKNELQVKLSNlSNLSHDLVQEAIDHAQELQQ 599
Cdd:PRK01156 621 IREIENEAN-NLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSiipDLKEITSRIND-IEDNLKKSRKALDDAKANRA 698
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622930177 600 EANELSRKLHSsDMNGLVQKALDasnvyeniVNYVSEANETAEFALNTTDRIYDAVSGIDTQIIYHKDESENLLNQARE 678
Cdd:PRK01156 699 RLESTIEILRT-RINELSDRIND--------INETLESMKKIKKAIGDLKRLREAFDKSGVPAMIRKSASQAMTSLTRK 768
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
311-609 |
5.52e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 5.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 311 VNEINATIYLLKTKLSERENQYALRKIQINNAENTMKSLLSDVEELVEKENQASRKGQLIQKESMDTIKHASQLVEQAHD 390
Cdd:COG4372 82 LEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLES 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 391 MRDKIQEINNkmlyygEEHELSPKEISEKLvlaQKMLEEIRRRQPFFTQRELVDEEADEAHELLSQAESwQRLHNETRTL 470
Cdd:COG4372 162 LQEELAALEQ------ELQALSEAEAEQAL---DELLKEANRNAEKEEELAEAEKLIESLPRELAEELL-EAKDSLEAKL 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 471 FPVVLEQLDDYNAKLSDLQEALDQALNHVRDAEDMNRATAARQRDHEKQQERVREQMEAVNmslNTSADSLTTPRLTLSE 550
Cdd:COG4372 232 GLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAA---LELKLLALLLNLAALS 308
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622930177 551 LDDIIKNASGIYAEIDGAKNELQVKLSNLSNLSHDLVQEAIDHAQELQQEANELSRKLH 609
Cdd:COG4372 309 LIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGV 367
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
305-603 |
7.51e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 7.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 305 AAAHRHVNEINATIYLLKTKLSERENQYALRKIQINNAENTMKSLLSDVEELVEKEnqasrkgqliqKESMDTIKHASQL 384
Cdd:PRK02224 373 EEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRERE-----------AELEATLRTARER 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 385 VEQAHDMRD--KIQEInnkmlyyGEEHELSP--KEISEKLVLAQKM---LEEIRrrqpffTQRELVDEEADEAHELLSQA 457
Cdd:PRK02224 442 VEEAEALLEagKCPEC-------GQPVEGSPhvETIEEDRERVEELeaeLEDLE------EEVEEVEERLERAEDLVEAE 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 458 ESWQRLHNETRTLFPVVLEQLDDYNAKLSDLQEALDQALNHVRDAEDmNRATAARQRDhekQQERVREQMEAVN---MSL 534
Cdd:PRK02224 509 DRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEE-KREAAAEAEE---EAEEAREEVAELNsklAEL 584
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622930177 535 NTSADSLTTPRLTLSELDDIIKNASGI------YAEI-DGAKNELQVKLSNLSNLSHDLVQEAIDHAQELQQEANE 603
Cdd:PRK02224 585 KERIESLERIRTLLAAIADAEDEIERLrekreaLAELnDERRERLAEKRERKRELEAEFDEARIEEAREDKERAEE 660
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
424-684 |
9.64e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.36 E-value: 9.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 424 QKMLEEIRRrqpfftQRELVDEEADEA----HELLSQAESW--QR--LHNETRTL---FPVVLEQLDDYNAKLSDLQEAL 492
Cdd:COG1340 7 SSSLEELEE------KIEELREEIEELkekrDELNEELKELaeKRdeLNAQVKELreeAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 493 D---QALNHVRDAEDMNRATAARQRDHEKQQERVREQMEAVNMSLNTSAdslttprLTLSELDDIIKNASGIYAEIDGAK 569
Cdd:COG1340 81 DelnEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEV-------LSPEEEKELVEKIKELEKELEKAK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 570 --NELQVKLSNLSNLS----------HDLVQEAIDHAQELQQEANELSRKLhssdmNGLVQKALDAsnvYENIVNYVSEA 637
Cdd:COG1340 154 kaLEKNEKLKELRAELkelrkeaeeiHKKIKELAEEAQELHEEMIELYKEA-----DELRKEADEL---HKEIVEAQEKA 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1622930177 638 NET-AEFalnttDRIYDAVSGIDTQIIYHKDESENLL--NQARELQAKAE 684
Cdd:COG1340 226 DELhEEI-----IELQKELRELRKELKKLRKKQRALKreKEKEELEEKAE 270
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
476-607 |
1.03e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.60 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 476 EQLDDYNAKLSDLQEALDQALNHVRDAEDMNRATAARQRDHEKQQERVR--EQMEAVNMSLntsaDSLttpRLTLSELDD 553
Cdd:COG1579 38 DELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnKEYEALQKEI----ESL---KRRISDLED 110
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622930177 554 IIKNasgIYAEIDGAKNELQVKLSNLSNLSHDL--VQEAIDHA-QELQQEANELSRK 607
Cdd:COG1579 111 EILE---LMERIEELEEELAELEAELAELEAELeeKKAELDEElAELEAELEELEAE 164
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
532-751 |
1.05e-03 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 42.78 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 532 MSLNTSADSLTTPRLTLSELDDIIKNASgiyaEIDGAKNELQVKLSNLSNLSHDLVQEaidhAQELQQEANELSRK--LH 609
Cdd:pfam06008 2 LSLNSLTGALPAPYKINYNLENLTKQLQ----EYLSPENAHKIQIEILEKELSSLAQE----TEELQKKATQTLAKaqQV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 610 SSDMNGLVQKALDASNVYENIVNYVSEANETAEfALNTTDriyDAVSGidTQIIYHKDESENLLNQARELQAKAESSSDE 689
Cdd:pfam06008 74 NAESERTLGHAKELAEAIKNLIDNIKEINEKVA-TLGEND---FALPS--SDLSRMLAEAQRMLGEIRSRDFGTQLQNAE 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622930177 690 AVADTSRRVggaLAR---------------KSALKTRLSDAVKQLQaaergDAQQRLGQSRLITEEANRTTMEVQQA 751
Cdd:pfam06008 148 AELKAAQDL---LSRiqtwfqspqeenkalANALRDSLAEYEAKLS-----DLRELLREAAAKTRDANRLNLANQAN 216
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
346-608 |
1.83e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 346 MKSLLSDVEELVEKENQASRKGQLIQKEsmdtIKHASQLVEQaHDMRDKIQEINNKMLYYGEEhELSPK-----EISEKL 420
Cdd:PRK03918 461 LKRIEKELKEIEEKERKLRKELRELEKV----LKKESELIKL-KELAEQLKELEEKLKKYNLE-ELEKKaeeyeKLKEKL 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 421 VLAQK----MLEEIRRRQPFFTQRELVDEEADEAHELLSQaeswqrLHNETRTLFpvvLEQLDDYNAKLSDLQEALDQAL 496
Cdd:PRK03918 535 IKLKGeiksLKKELEKLEELKKKLAELEKKLDELEEELAE------LLKELEELG---FESVEELEERLKELEPFYNEYL 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 497 NhVRDAEDmnrataaRQRDHEKQQERVREqmeavnmslntsadslttprltlsELDDIIKNASGIYAEIDGAKNELQVKL 576
Cdd:PRK03918 606 E-LKDAEK-------ELEREEKELKKLEE------------------------ELDKAFEELAETEKRLEELRKELEELE 653
|
250 260 270
....*....|....*....|....*....|..
gi 1622930177 577 SNLSNLSHdlvqeaidhaQELQQEANELSRKL 608
Cdd:PRK03918 654 KKYSEEEY----------EELREEYLELSREL 675
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
373-606 |
1.83e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 373 ESMDTIKHASQLVEQAHDMRDKIQ------EINNKMLYYGEEHElspKEISEKLVLAQKmLEEIRRRQPFFTQRelVDEE 446
Cdd:COG4717 341 ELLDRIEELQELLREAEELEEELQleeleqEIAALLAEAGVEDE---EELRAALEQAEE-YQELKEELEELEEQ--LEEL 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 447 ADEAHELLSQA--ESWQRLHNETRtlfpvvlEQLDDYNAKLSDLQEALDQALNHVRDAEDMNRATAARQrdhekQQERVR 524
Cdd:COG4717 415 LGELEELLEALdeEELEEELEELE-------EELEELEEELEELREELAELEAELEQLEEDGELAELLQ-----ELEELK 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 525 EQMEAV---NMSLNTSADSLTTPRLTLSE--LDDIIKNASGIYAEI-DGAKNELQVklsnlsNLSHDLVqeaIDHAQELQ 598
Cdd:COG4717 483 AELRELaeeWAALKLALELLEEAREEYREerLPPVLERASEYFSRLtDGRYRLIRI------DEDLSLK---VDTEDGRT 553
|
....*...
gi 1622930177 599 QEANELSR 606
Cdd:COG4717 554 RPVEELSR 561
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
366-682 |
2.74e-03 |
|
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.
Pssm-ID: 427715 [Multi-domain] Cd Length: 360 Bit Score: 41.99 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 366 KGQLIQKESMDTIKHASQLVEQAHDMRDKIQEINnkmlyygeehelspKEISEKLVLAQKMLEEIRRRqpfftQRELVDE 445
Cdd:pfam04108 4 SAQDLCRWANELLTDARSLLEELVVLLAKIAFLR--------------RGLSVQLANLEKVREGLEKV-----LNELKKD 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 446 EADEAHELLSQAESWQR-LHNETRTLFPVVLEQLDDYNAKLSDL--QEALDQALNHVRdaedmnrataarqrdheKQQER 522
Cdd:pfam04108 65 FKQLLKDLDAALERLEEtLDKLRNTPVEPALPPGEEKQKTLLDFidEDSVEILRDALK-----------------ELIDE 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 523 VREQMEAVNMSLNTSADSLTTPRLTLSELDDIIKNASGIYaeidgaknelqVKLSNLSNLSHDLVQ--EAIDHAQELQQE 600
Cdd:pfam04108 128 LQAAQESLDSDLKRFDDDLRDLQKELESLSSPSESISLIP-----------TLLKELESLEEEMASllESLTNHYDQCVT 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 601 ANELSRKLHSSDMNGLVQKALDASNVYENIVNYVSEANETAEFALNTTDRIYDAvsgidtqiiyhKDESENLLNQARELQ 680
Cdd:pfam04108 197 AVKLTEGGRAEMLEVLENDARELDDVVPELQDRLDEMENNYERLQKLLEQKNSL-----------IDELLSALQLIAEIQ 265
|
..
gi 1622930177 681 AK 682
Cdd:pfam04108 266 SR 267
|
|
| DivIVA |
pfam05103 |
DivIVA protein; The Bacillus subtilis divIVA1 mutation causes misplacement of the septum ... |
383-467 |
2.75e-03 |
|
DivIVA protein; The Bacillus subtilis divIVA1 mutation causes misplacement of the septum during cell division, resulting in the formation of small, circular, anucleate mini-cells. Inactivation of divIVA produces a mini-cell phenotype, whereas overproduction of DivIVA results in a filamentation phenotype. These proteins appear to contain coiled-coils.
Pssm-ID: 428304 [Multi-domain] Cd Length: 131 Bit Score: 39.86 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 383 QLVEQAHDMRDKIQEINNKMLYYGEEHElspkEISEKLVLAQKMLEEIRRRQPffTQRELVDEEA-DEAHELLSQAES-W 460
Cdd:pfam05103 36 ALIRENAELKEKIEELEEKLAHYKNLEE----TLQNTLILAQETAEEVKANAQ--KEAELIIKEAeAKAERIVDDANNeV 109
|
....*..
gi 1622930177 461 QRLHNET 467
Cdd:pfam05103 110 KKINDEI 116
|
|
| TNFRSF4 |
cd13406 |
Tumor necrosis factor receptor superfamily member 4 (TNFRSF4), also known as CD134 or OXO40; ... |
166-273 |
4.13e-03 |
|
Tumor necrosis factor receptor superfamily member 4 (TNFRSF4), also known as CD134 or OXO40; TNFRSF4 (also known as OX40, ACT35, CD134, IMD16, TXGP1L) activates NF-kappaB through its interaction with adaptor proteins TRAF2 and TRAF5. It also promotes the expression of apoptosis inhibitors BCL2 and BCL2lL1/BCL2-XL, and thus suppresses apoptosis. It is primarily expressed on activated CD4+ and CD8+ T cells, where it is transiently expressed and upregulated on the most recently antigen-activated T cells within inflammatory lesions. This makes it an attractive target to modulate immune responses, i.e. TNFRSF4 (OX40) blocking agents to inhibit adverse inflammation or agonists to enhance immune responses. An artificially created biologic fusion protein, OX40-immunoglobulin (OX40-Ig), prevents OX40 from reaching the T-cell receptors, thus reducing the T-cell response. Some single nucleotide polymorphisms (SNPs) of its natural ligand OX40 ligand (OX40L, CD252), which is also found on activated T cells, have been associated with systemic lupus erythematosus.
Pssm-ID: 276911 [Multi-domain] Cd Length: 142 Bit Score: 39.69 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 166 CERCAPGYYgnplligstcKKCDCSGNSDPnlifedcdevtgqcrnclrnttgfKCERCAPGYYGDARIAKNCAVCNcgg 245
Cdd:cd13406 15 CHECPPGEG----------MESRCTGTQDT------------------------VCSPCEPGFYNEAVNYEPCKPCT--- 57
|
90 100
....*....|....*....|....*...
gi 1622930177 246 gPCDSVTGECLEEGLEPPTGTDCSTISC 273
Cdd:cd13406 58 -QCNQRSGSEEKQKCTKTSDTVCRCRPG 84
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
414-608 |
4.29e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.93 E-value: 4.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 414 KEISEKLVLAQKMLEEIRRRQPFFTqrelVDEEADEAHELLSQAESwQRlhNETRTlfpvvleQLDDYNAKLSDLQEALD 493
Cdd:COG3206 185 PELRKELEEAEAALEEFRQKNGLVD----LSEEAKLLLQQLSELES-QL--AEARA-------ELAEAEARLAALRAQLG 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 494 QALNHVRDAEDMNRATAARQRDHEKQQERVReqmeavnMSLNTSADSlttPRLT-----LSELDDIIKN-ASGIYAEIDG 567
Cdd:COG3206 251 SGPDALPELLQSPVIQQLRAQLAELEAELAE-------LSARYTPNH---PDVIalraqIAALRAQLQQeAQRILASLEA 320
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1622930177 568 AKNELQVKLSNLSNLSHDLvQEAIDHAQELQQEANELSRKL 608
Cdd:COG3206 321 ELEALQAREASLQAQLAQL-EARLAELPELEAELRRLEREV 360
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
321-685 |
4.43e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.93 E-value: 4.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 321 LKTKLSERENQYALRKIQINNAENTMKSLLSDVEEL------VEKENQaSRKGQLIQKES-MDTIKHASQ-LVEQAHDMR 392
Cdd:TIGR04523 312 LKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLkkeltnSESENS-EKQRELEEKQNeIEKLKKENQsYKQEIKNLE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 393 DKIQEINNKMLYYGEEHELSPKEISEKLVLAQKMLEEIRRrqpfftQRELVDEEADEAHELLSQAESWQRLHNETRTLFP 472
Cdd:TIGR04523 391 SQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIER------LKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRE 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 473 VVLEQLDDYNAKLSDLQEALDQALNHVRDAEDMNRATAARQRDHEKQQERVREQMEavnmSLNTSADSLTTprlTLSELD 552
Cdd:TIGR04523 465 SLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKIS----SLKEKIEKLES---EKKEKE 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 553 DiiknasgiyaEIDGAKNELqvkLSNLSNLSHDLVQEAIDhaqELQQEANELSrklhssdmngLVQKALDASN--VYENI 630
Cdd:TIGR04523 538 S----------KISDLEDEL---NKDDFELKKENLEKEID---EKNKEIEELK----------QTQKSLKKKQeeKQELI 591
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622930177 631 VNYVSEANE-TAEFALNTTdriydAVSGIDTQIIYHKDESENLLNQARELQAKAES 685
Cdd:TIGR04523 592 DQKEKEKKDlIKEIEEKEK-----KISSLEKELEKAKKENEKLSSIIKNIKSKKNK 642
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
324-458 |
4.46e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.05 E-value: 4.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 324 KLSERENQYALRKiQINNAENTMKSLLSDVEELVEKENQASRK----GQLIQK--ESMDTI-KHASQLVEQAHDMRDKIQ 396
Cdd:COG1340 141 KIKELEKELEKAK-KALEKNEKLKELRAELKELRKEAEEIHKKikelAEEAQElhEEMIELyKEADELRKEADELHKEIV 219
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622930177 397 EINNKMlyyGEEHEL------SPKEISEKLVLAQKMLEEIRRRQpfftQRELVDEEADEAHELLSQAE 458
Cdd:COG1340 220 EAQEKA---DELHEEiielqkELRELRKELKKLRKKQRALKREK----EKEELEEKAEEIFEKLKKGE 280
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
476-734 |
4.75e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.29 E-value: 4.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 476 EQLDDYNAKLSDLQEALDQalnhvrdaedmnraTAARQRDHEKQQERVREQMEAVNMSLNTSADSLTTPRLTLSELDDII 555
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAE--------------LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 556 KNASgiyAEIDGAKNELQVKLSNLSNLshdlvqeaIDHAQELQQeANELSRKLHSSDMNGLVQKAldasnvyeNIVNYVS 635
Cdd:COG4942 86 AELE---KEIAELRAELEAQKEELAEL--------LRALYRLGR-QPPLALLLSPEDFLDAVRRL--------QYLKYLA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 636 EANETAEFALNTTdriYDAVSGIDTQIIYHKDESENLLNQARELQA---KAESSSDEAVADTSRRVGGALARKSALK--- 709
Cdd:COG4942 146 PARREQAEELRAD---LAELAALRAELEAERAELEALLAELEEERAaleALKAERQKLLARLEKELAELAAELAELQqea 222
|
250 260
....*....|....*....|....*
gi 1622930177 710 TRLSDAVKQLQAAERGDAQQRLGQS 734
Cdd:COG4942 223 EELEALIARLEAEAAAAAERTPAAG 247
|
|
| Rcc_KIF21A |
cd22263 |
regulatory coiled-coil domain found in kinesin-like protein KIF21A; KIF21A, also called ... |
335-402 |
5.01e-03 |
|
regulatory coiled-coil domain found in kinesin-like protein KIF21A; KIF21A, also called kinesin-like protein KIF2 or renal carcinoma antigen NY-REN-62, is a microtubule-binding motor protein involved in neuronal axonal transport. It works as a microtubule stabilizer that regulates axonal morphology, suppressing cortical microtubule dynamics in neurons. Mutations in KIF21A cause congenital fibrosis of the extraocular muscles type 1 (CFEOM1). In vitro, it has a plus-end directed motor activity. This model corresponds to the regulatory coiled-coil domain of KIF21A, which folds into an intramolecular antiparallel coiled-coil monomer in solution, but crystallizes into a dimeric domain-swapped antiparallel coiled-coil.
Pssm-ID: 410204 [Multi-domain] Cd Length: 82 Bit Score: 37.60 E-value: 5.01e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622930177 335 RKIQINNAENTMKSLLSDVEELVEKENQASRKGQLIQKESMDTIKHASQLVEQAHDMRDKIQEINNKM 402
Cdd:cd22263 1 QRMTISNMEADMNRLLKQREELTKRREKLSKKREKIIKENGEGDKNVHNINEEMESLTANIDYINDSI 68
|
|
| Laminin_G_3 |
pfam13385 |
Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin ... |
1497-1619 |
5.19e-03 |
|
Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin A-like lectin/glucanases superfamily.
Pssm-ID: 463865 [Multi-domain] Cd Length: 151 Bit Score: 39.29 E-value: 5.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 1497 IRLRTRSSHGMIFYVSDQEeNDFMTLFLAHGRLVYMFNVGHKKLK-IRSQEKYNDGLWHDVVFIRERSSGRLVIDGLRVL 1575
Cdd:pfam13385 25 VKPDSLPGWARAIISSSGG-GGYSLGLDGDGRLRFAVNGGNGGWDtVTSGASVPLGQWTHVAVTYDGGTLRLYVNGVLVG 103
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1622930177 1576 EESLPPTeATWKIKGPIYLGGVAPGKAVKNVQINSIYSFSGCLS 1619
Cdd:pfam13385 104 SSTLTGG-PPPGTGGPLYIGRSPGGDDYFNGLIDEVRIYDRALS 146
|
|
| Prefoldin_alpha_GimC |
cd23160 |
Prefoldin alpha subunit, archaeal; Archaeal alpha subunit of prefoldin (GimC), a hexameric ... |
517-608 |
5.54e-03 |
|
Prefoldin alpha subunit, archaeal; Archaeal alpha subunit of prefoldin (GimC), a hexameric molecular chaperone complex, found in both eukaryotes and archaea. Prefoldin binds and stabilizes newly synthesized polypeptides allowing them to fold correctly. The complex contains two alpha and four beta subunits, the two subunits being evolutionarily related. In archaea, there is usually only one gene for each subunit while in eukaryotes there two or more paralogous genes encoding each subunit adding heterogeneity to the structure of the hexamer. The structure of the complex consists of a double beta barrel assembly with six protruding coiled-coils.
Pssm-ID: 467476 [Multi-domain] Cd Length: 127 Bit Score: 38.62 E-value: 5.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 517 EKQQERVREQMEAVNMSLNtsadSLTTPRLTLSELDDI-------------------IKNA--------SGIYAE--IDG 567
Cdd:cd23160 13 EQQAEALQQQIELLQASIN----ELNRAKETLEELKKLkegteilvpigggsfvkakIKDTdkvlvnigAGVVVEktIDE 88
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1622930177 568 AKNELQVKLSNLSNLSHDLVQEaidhAQELQQEANELSRKL 608
Cdd:cd23160 89 AIEILEKRIKELEKALEKLQEQ----LQQIAQRLEELEAEL 125
|
|
| DivIVA |
COG3599 |
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle ... |
383-470 |
5.96e-03 |
|
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442818 [Multi-domain] Cd Length: 125 Bit Score: 38.68 E-value: 5.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 383 QLVEQAHDMRDKIQEINNKMLYYGEEHElspkEISEKLVLAQKMLEEIRR--RQpfftQRELVDEEAD-EAHELLSQAES 459
Cdd:COG3599 38 RLIRENKELKEKLEELEEELEEYRELEE----TLQKTLVVAQETAEEVKEnaEK----EAELIIKEAElEAEKIIEEAQE 109
|
90
....*....|..
gi 1622930177 460 -WQRLHNETRTL 470
Cdd:COG3599 110 kARKIVREIEEL 121
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
309-724 |
6.39e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 6.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 309 RHVNEIN--ATIYLlktKLSERENQYALRKIQINNAENTMKSLLSDVEELVEK-ENQASRKGQLIQKESmDTIKHASQLV 385
Cdd:PRK03918 283 KELKELKekAEEYI---KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKElEEKEERLEELKKKLK-ELEKRLEELE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 386 EQAHDMRDKIQEINNKMLYYGEEHELSPKEISEKLVLAQKMLEEIRRRQPFFTQR--ELVDEEAD--EAHELLSQAES-- 459
Cdd:PRK03918 359 ERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARigELKKEIKElkKAIEELKKAKGkc 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 460 ---WQRLHNETRtlfpvvLEQLDDYNAKLSDLQEALDQALNHVRDAED---------MNRATAARQRDHEKQQERVREQM 527
Cdd:PRK03918 439 pvcGRELTEEHR------KELLEEYTAELKRIEKELKEIEEKERKLRKelrelekvlKKESELIKLKELAEQLKELEEKL 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 528 EAVNMS-LNTSADSLttpRLTLSELDDIIKNASGIYAEID------GAKNELQVKLSN----LSNLSHDLVQEAIDHAQE 596
Cdd:PRK03918 513 KKYNLEeLEKKAEEY---EKLKEKLIKLKGEIKSLKKELEkleelkKKLAELEKKLDEleeeLAELLKELEELGFESVEE 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 597 LQQEANELsRKLHSSDMnglvqKALDASNVYENIVNYVSEANETAEFALNTTDRIYDAVSGIDTQI-----IYHKDESEN 671
Cdd:PRK03918 590 LEERLKEL-EPFYNEYL-----ELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELeelekKYSEEEYEE 663
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1622930177 672 LLNQARELqakaesssdeavadtSRRVGGALARKSALKTRLSDAVKQLQAAER 724
Cdd:PRK03918 664 LREEYLEL---------------SRELAGLRAELEELEKRREEIKKTLEKLKE 701
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
476-733 |
6.73e-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: 6.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 476 EQLDDYNAKLSDLQEALDQALNHVRDAEDMNRATAARQRDHEKQQER---------VREQMEAVNMSLntsaDSLTTPRL 546
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYswdeidvasAEREIAELEAEL----ERLDASSD 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 547 TLSELDDIIKNASGIYAEIDGAKNELQVKLSNLSNlSHDLVQEAIDHAQELQQEANELSRKLHSSDMNGLVQKALDasnv 626
Cdd:COG4913 686 DLAALEEQLEELEAELEELEEELDELKGEIGRLEK-ELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALG---- 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 627 yENIVNYVSEanetaefalnttdRIYDAVSGIDTQIIYHKDESENLLNQ--------ARELQAKAESSSD-EAVADTSRR 697
Cdd:COG4913 761 -DAVERELRE-------------NLEERIDALRARLNRAEEELERAMRAfnrewpaeTADLDADLESLPEyLALLDRLEE 826
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1622930177 698 VGgaLAR-----KSALKTRLSDAVKQLQAA---ERGDAQQRLGQ 733
Cdd:COG4913 827 DG--LPEyeerfKELLNENSIEFVADLLSKlrrAIREIKERIDP 868
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
371-603 |
7.68e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.44 E-value: 7.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 371 QKESMDTIKHASQLVEQAHDMRDKIQEINNKMLYYGEEHELSPKEISEklvlAQKMLEEIRrrqpfftqrELVDEEADEA 450
Cdd:PRK11281 51 QKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQ----AQAELEALK---------DDNDEETRET 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 451 HELLSQAESWQRLhNETRTLFPVVLEQLDDYNAKLSDLQEALDQALNHVrdaedmnraTAARQRdhekqqervreqMEAV 530
Cdd:PRK11281 118 LSTLSLRQLESRL-AQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAAL---------YANSQR------------LQQI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622930177 531 NMSLNTSADSLTTPRLTLSELddiiknasgIYAEID--GAKNELQVK-------LSNLSNLSHDLVQEAIDHAQE----L 597
Cdd:PRK11281 176 RNLLKGGKVGGKALRPSQRVL---------LQAEQAllNAQNDLQRKslegntqLQDLLQKQRDYLTARIQRLEHqlqlL 246
|
....*.
gi 1622930177 598 QQEANE 603
Cdd:PRK11281 247 QEAINS 252
|
|
| |
