|
Name |
Accession |
Description |
Interval |
E-value |
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
30-251 |
2.55e-22 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 100.37 E-value: 2.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 30 TKELVSWMRGHESSVCSISVHASGRYAITTSSD-TAQLWDLDTFQRKRKLNIRQSvGIQKVFFLPLSNTILSCFKDNSIF 108
Cdd:COG2319 193 TGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADgTVRLWDLATGKLLRTLTGHSG-SVRSVAFSPDGRLLASGSADGTVR 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 109 AWECDTLFCKYQLPGPPEGSNILykvfAVTRDGRILAAGGKSNHLHLWCLEATGLFRIIQmpAKVRAVRHLEFLPDsfda 188
Cdd:COG2319 272 LWDLATGELLRTLTGHSGGVNSV----AFSPDGKLLASGSDDGTVRLWDLATGKLLRTLT--GHTGAVRSVAFSPD---- 341
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1248026918 189 gsNQVLGVLSQDGIMRFVNIQTCKLLFEIGTVEEGISSSVISPHGRYIASIMENGSLNVYSVQ 251
Cdd:COG2319 342 --GKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
8-251 |
4.97e-22 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 99.60 E-value: 4.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 8 AIPSLLGTIRetsmfltCMETVTKELVSWMRGHESSVCSISVHASGRYAITTSSD-TAQLWDLDTFQRKRKLNiRQSVGI 86
Cdd:COG2319 94 ASASADGTVR-------LWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADgTVRLWDLATGKLLRTLT-GHSGAV 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 87 QKVFFLPLSNTILSCFKDNSIFAWECDTLFCKYQLPGPPEGSNILykvfAVTRDGRILAAGGKSNHLHLWCLEATGLFRI 166
Cdd:COG2319 166 TSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSV----AFSPDGKLLASGSADGTVRLWDLATGKLLRT 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 167 IQMPAkvRAVRHLEFLPDSfdagsnQVLGVLSQDGIMRFVNIQTCKLLFEIGTVEEGISSSVISPHGRYIASIMENGSLN 246
Cdd:COG2319 242 LTGHS--GSVRSVAFSPDG------RLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVR 313
|
....*
gi 1248026918 247 VYSVQ 251
Cdd:COG2319 314 LWDLA 318
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
30-255 |
2.58e-21 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 97.29 E-value: 2.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 30 TKELVSWMRGHESSVCSISVHASGRYAITTSSD-TAQLWDLDTFQRKRKLNIRQSvGIQKVFFLPLSNTILSCFKDNSIF 108
Cdd:COG2319 151 TGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDgTVRLWDLATGKLLRTLTGHTG-AVRSVAFSPDGKLLASGSADGTVR 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 109 AWECDTLFCKYQLPGPPEGSNILykvfAVTRDGRILAAGGKSNHLHLWCLEATGLFRIIQMPAkvRAVRHLEFLPDSfda 188
Cdd:COG2319 230 LWDLATGKLLRTLTGHSGSVRSV----AFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHS--GGVNSVAFSPDG--- 300
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1248026918 189 gsnQVLGVLSQDGIMRFVNIQTCKLLFEIGTVEEGISSSVISPHGRYIASIMENGSLNVYSVQALTQ 255
Cdd:COG2319 301 ---KLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGEL 364
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
30-251 |
4.41e-20 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 93.82 E-value: 4.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 30 TKELVSWMRGHESSVCSISVHASGRYAITTSSD-TAQLWDLDTFQRKRKLNIRQSvGIQKVFFLPLSNTILSCFKDNSIF 108
Cdd:COG2319 67 AGALLATLLGHTAAVLSVAFSPDGRLLASASADgTVRLWDLATGLLLRTLTGHTG-AVRSVAFSPDGKTLASGSADGTVR 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 109 AWECDTLFCKYQLPGPPEGSNILykvfAVTRDGRILAAGGKSNHLHLWCLEATGLFRIIQmpAKVRAVRHLEFLPDSfda 188
Cdd:COG2319 146 LWDLATGKLLRTLTGHSGAVTSV----AFSPDGKLLASGSDDGTVRLWDLATGKLLRTLT--GHTGAVRSVAFSPDG--- 216
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1248026918 189 gsnQVLGVLSQDGIMRFVNIQTCKLLFEIGTVEEGISSSVISPHGRYIASIMENGSLNVYSVQ 251
Cdd:COG2319 217 ---KLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLA 276
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
30-249 |
9.60e-18 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 84.69 E-value: 9.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 30 TKELVSWMRGHESSVCSISVHASGRYAITTSSD-TAQLWDLDTFQRKRKLNIRQSvGIQKVFFLPLSNTILSCFKDNSIF 108
Cdd:cd00200 82 TGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDkTIKVWDVETGKCLTTLRGHTD-WVNSVAFSPDGTFVASSSQDGTIK 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 109 AWECDTLFCKYQLPGpPEGSnilykVFAVT--RDGRILAAGGKSNHLHLWclEATGLFRIIQMPAKVRAVRHLEFLPDsf 186
Cdd:cd00200 161 LWDLRTGKCVATLTG-HTGE-----VNSVAfsPDGEKLLSSSSDGTIKLW--DLSTGKCLGTLRGHENGVNSVAFSPD-- 230
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1248026918 187 dagsNQVLGVLSQDGIMRFVNIQTCKLLFEIGTVEEGISSSVISPHGRYIASIMENGSLNVYS 249
Cdd:cd00200 231 ----GYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
38-252 |
2.64e-16 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 80.46 E-value: 2.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 38 RGHESSVCSISVHASGRYAITTSSD-TAQLWDLDTFQRKRKLNIrQSVGIQKVFFLPLSNTILSCFKDNSIFAWECDTLF 116
Cdd:cd00200 6 KGHTGGVTCVAFSPDGKLLATGSGDgTIKVWDLETGELLRTLKG-HTGPVRDVAASADGTYLASGSSDKTIRLWDLETGE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 117 CKYQLPGPPEGsnilykVFAV--TRDGRILAAGGKSNHLHLWCLEATGLfrIIQMPAKVRAVRHLEFLPDsfdagsNQVL 194
Cdd:cd00200 85 CVRTLTGHTSY------VSSVafSPDGRILSSSSRDKTIKVWDVETGKC--LTTLRGHTDWVNSVAFSPD------GTFV 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1248026918 195 GVLSQDGIMRFVNIQTCKLLFEIGTVEEGISSSVISPHGRYIASIMENGSLNVYSVQA 252
Cdd:cd00200 151 ASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLST 208
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
27-205 |
6.68e-15 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 76.22 E-value: 6.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 27 ETVTKELVSWMRGHESSVCSISVHASGRYAITTSSD-TAQLWDLDTFQRKRKLNIRQSvGIQKVFFLPLSNTILSCFKDN 105
Cdd:cd00200 121 DVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDgTIKLWDLRTGKCVATLTGHTG-EVNSVAFSPDGEKLLSSSSDG 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 106 SIFAWECDTLFCKYQLPGPPEGSNILykvfAVTRDGRILAAGGKSNHLHLWCLEATGLFRIIQMPAK-VRAVRhleFLPD 184
Cdd:cd00200 200 TIKLWDLSTGKCLGTLRGHENGVNSV----AFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNsVTSLA---WSPD 272
|
170 180
....*....|....*....|.
gi 1248026918 185 SfdagsnQVLGVLSQDGIMRF 205
Cdd:cd00200 273 G------KRLASGSADGTIRI 287
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
38-251 |
6.95e-14 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 74.56 E-value: 6.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 38 RGHESSVCSISVHASGRYAITTSSDTAQLWDLDTFQRKRKLNIRQSVGIQKVFFLPLSNTILSCFKDNSIFAWECDTLFC 117
Cdd:COG2319 33 LGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 118 KYQLPGPPEGSNILykvfAVTRDGRILAAGGKSNHLHLWCLEATGLFRIIQMPAkvRAVRHLEFLPDSfdagsnQVLGVL 197
Cdd:COG2319 113 LRTLTGHTGAVRSV----AFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHS--GAVTSVAFSPDG------KLLASG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1248026918 198 SQDGIMRFVNIQTCKLLFEIGTVEEGISSSVISPHGRYIASIMENGSLNVYSVQ 251
Cdd:COG2319 181 SDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLA 234
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
603-843 |
1.25e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 75.36 E-value: 1.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 603 QTREWE-RIRNDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQELL---RRAEETRREILLQEEEKMAQQRQRLAAVKR 678
Cdd:COG1196 261 ELAELEaELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLeerRRELEERLEELEEELAELEEELEELEEELE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 679 ELEIKEIHLQDAARRRLLKLQQ--DQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRL---------YE 747
Cdd:COG1196 341 ELEEELEEAEEELEEAEAELAEaeEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEeallerlerLE 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 748 KDLTTSQEAVAKEIREDTDAHRRKAALEEHMFQKLLENSQMGGRRAQRWKEAEEKEfHLQSAKKASALSDASRKWfLRQE 827
Cdd:COG1196 421 EELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE-AALAELLEELAEAAARLL-LLLE 498
|
250
....*....|....*.
gi 1248026918 828 TSAALEHEEMPWLQRQ 843
Cdd:COG1196 499 AEADYEGFLEGVKAAL 514
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
599-856 |
4.02e-13 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 73.23 E-value: 4.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 599 IVDYQTREWERIRNDELDFL---RERQTVENMQAEVDEQRAKDEAwyqkqELLRRAEETRREILLQEEEKMAQQRQR--- 672
Cdd:pfam17380 277 IVQHQKAVSERQQQEKFEKMeqeRLRQEKEEKAREVERRRKLEEA-----EKARQAEMDRQAAIYAEQERMAMERERele 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 673 ---LAAVKRELE-------------IKEIH-LQ--------------DAARR-------RLLKLQQDQREMELRRLEDEI 714
Cdd:pfam17380 352 rirQEERKRELErirqeeiameisrMRELErLQmerqqknervrqelEAARKvkileeeRQRKIQQQKVEMEQIRAEQEE 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 715 ERKVQMRDQEiAATAKDLE-IRQLELEAQKRLyekDLTTSQEAVAKEIREDTDAHRRKAALEEHMFQKLLENSQMGGRRA 793
Cdd:pfam17380 432 ARQREVRRLE-EERAREMErVRLEEQERQQQV---ERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQA 507
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1248026918 794 QRWKEAEEKEFHLQSAKKASALSDASRKWFLRQETSAALEHEEMPWLQRQYMDSAylPQTSRL 856
Cdd:pfam17380 508 MIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKAT--EERSRL 568
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
614-836 |
1.51e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.89 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 614 ELDFLRERQtvENMQAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELEIKE---IHLQDA 690
Cdd:COG1196 233 KLRELEAEL--EELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEqdiARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 691 ARRRLLKLQQDQREME--LRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRL--YEKDLTTSQEAVAKEIREDTD 766
Cdd:COG1196 311 RRELEERLEELEEELAelEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALleAEAELAEAEEELEELAEELLE 390
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 767 AHRRKAALEEHMFQKLLENSQMGGRRAQRWKEAEEKEfhlQSAKKASALSDASRKWFLRQETSAALEHEE 836
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELE---EALAELEEEEEEEEEALEEAAEEEAELEEE 457
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
608-836 |
5.89e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.97 E-value: 5.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 608 ERIRNDELDFLRERQTVENMQAEVDEQRAK--------DEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRE 679
Cdd:COG1196 246 AELEELEAELEELEAELAELEAELEELRLEleelelelEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 680 LEIKEIHLQDAARRRLLKLQQDQREMELRRLEDEIERKVQMRD------QEIAATAKDLEIRQLELEAQKRLYEKDLTTS 753
Cdd:COG1196 326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLeaeaelAEAEEELEELAEELLEALRAAAELAAQLEEL 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 754 QEAVAKEIREDTDAHRRKAALEEHMFQKLLEnsqmggRRAQRWKEAEEKEFHLQSAKKASALSDASRKWFLRQETSAALE 833
Cdd:COG1196 406 EEAEEALLERLERLEEELEELEEALAELEEE------EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAAL 479
|
...
gi 1248026918 834 HEE 836
Cdd:COG1196 480 AEL 482
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
604-842 |
9.25e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.20 E-value: 9.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 604 TREWERIRNDELDFLRERQTVENMQAEVDEQRAKDEAwyqkqellRRAEETRREILLQEEEKMAQQRQRLAAVKRELEIK 683
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEERLEELEEELAELEE--------ELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 684 EIHLQDAARRRLLKLQQDQREMELRRLEDEIERKVQMrdQEIAATAKDLEIRQLELEAQKRLYEKDLTTSQEAVAKEIRE 763
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL--EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1248026918 764 DTDAHRRKAALEEHMfQKLLENSQMGGRRAQRWKEAEEKEFHLQSAKKASALSDASRKWFLRQETSAALEHEEMPWLQR 842
Cdd:COG1196 444 LEEAAEEEAELEEEE-EALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRG 521
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
603-780 |
1.53e-11 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 68.23 E-value: 1.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 603 QTREWERIRNDELDflrERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEE----KMAQQRQRLAAVKR 678
Cdd:pfam17380 444 RAREMERVRLEEQE---RQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEerkqAMIEEERKRKLLEK 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 679 ELEIKEIHLQDAARRRLLKLQQ-DQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEKDLTTSQEAV 757
Cdd:pfam17380 521 EMEERQKAIYEEERRREAEEERrKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAEYEATTPITTI 600
|
170 180
....*....|....*....|...
gi 1248026918 758 AKEIREDTDAHrRKAALEEHMFQ 780
Cdd:pfam17380 601 KPIYRPRISEY-QPPDVESHMIR 622
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
602-836 |
1.33e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.34 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 602 YQT-REWERIRNDELdFLRERQTVENMQAEVDEQRAkdeawyQKQELLRRAEETRREIllqeEEKMAQQRQRLAAVKREL 680
Cdd:COG1196 215 YRElKEELKELEAEL-LLLKLRELEAELEELEAELE------ELEAELEELEAELAEL----EAELEELRLELEELELEL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 681 EIKEIHLQdAARRRLLKLQQDQR--EMELRRLEDEIERKvQMRDQEIAATAKDLEIRQLELEAQKRLYEKDLTTSQEAVA 758
Cdd:COG1196 284 EEAQAEEY-ELLAELARLEQDIArlEERRRELEERLEEL-EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1248026918 759 KEIREDTDAHRRKAALEEHMFQKLLENSqmggRRAQRWKEAEEKEFHLQSAKKASALSDASRKWFLRQETSAALEHEE 836
Cdd:COG1196 362 EAEEALLEAEAELAEAEEELEELAEELL----EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE 435
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
628-837 |
1.60e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.88 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 628 QAEV---------DEQRAKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELEIKEIHLQdAARRRLLKL 698
Cdd:COG1196 208 QAEKaeryrelkeELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELE-ELELELEEA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 699 QQDQRE--MELRRLEDEIERKVQMRdqeiaataKDLEIRQLELEAQKRLYEKDLTTSQEAVAKEIREDTDAHRRKAALEE 776
Cdd:COG1196 287 QAEEYEllAELARLEQDIARLEERR--------RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA 358
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1248026918 777 HMFQKLLENSQMGGRRAQRWKEAEEKEFHLQSAKKASALSDASRKWFLRQETSAALEHEEM 837
Cdd:COG1196 359 ELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL 419
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
606-787 |
2.59e-09 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 60.74 E-value: 2.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 606 EWERIRNDELDFLRERQ----TVENMQAEVD--EQRAKDEAWYQKQellRRAEETRReillQEEEKMAQQRQRLAAVKRE 679
Cdd:pfam15709 349 EVERKRREQEEQRRLQQeqleRAEKMREELEleQQRRFEEIRLRKQ---RLEEERQR----QEEEERKQRLQLQAAQERA 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 680 leikeiHLQDAA-RRRLLKLQQDQREMELRRLEDEIERKVQMRDQeIAATAKDL-EIRQLE-LEAQKRLYEKDLTTSQEA 756
Cdd:pfam15709 422 ------RQQQEEfRRKLQELQRKKQQEEAERAEAEKQRQKELEMQ-LAEEQKRLmEMAEEErLEYQRQKQEAEEKARLEA 494
|
170 180 190
....*....|....*....|....*....|.
gi 1248026918 757 VAKEIREDTDAhrrKAALEEHMFQKLLENSQ 787
Cdd:pfam15709 495 EERRQKEEEAA---RLALEEAMKQAQEQARQ 522
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
606-803 |
2.85e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 61.31 E-value: 2.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 606 EWERIRNDELDFLRE--RQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREilLQEEEKMAQQrqrlaaVKRELEIK 683
Cdd:PTZ00121 1657 EENKIKAAEEAKKAEedKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKK--EAEEKKKAEE------LKKAEEEN 1728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 684 EIHLQDAARrrllKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQ-------LELEAQKRLYEKDLTT---- 752
Cdd:PTZ00121 1729 KIKAEEAKK----EAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKeavieeeLDEEDEKRRMEVDKKIkdif 1804
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1248026918 753 -------------------SQEAVAKEIREDTDAH---RRKA-ALEEHMFQKLLENSQMGGRRAQRWKEAEEKE 803
Cdd:PTZ00121 1805 dnfaniieggkegnlvindSKEMEDSAIKEVADSKnmqLEEAdAFEKHKFNKNNENGEDGNKEADFNKEKDLKE 1878
|
|
| RabGAP-TBC |
pfam00566 |
Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are ... |
376-520 |
3.06e-09 |
|
Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are GTPase activator proteins of yeast Ypt6 and Ypt7, implies that these domains are GTPase activator proteins of Rab-like small GTPases.
Pssm-ID: 459855 Cd Length: 178 Bit Score: 57.26 E-value: 3.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 376 SLQKKYPIKSRKLLRVLQRTLSALAHWsaiFSDTPY---LPLLAFPFVkLFQNNQLICFEVVATLIINwcQHWFEYFPN- 451
Cdd:pfam00566 19 TFPHSFFFDNGPGQNSLRRILKAYSIY---NPDVGYcqgMNFIAAPLL-LVYLDEEDAFWCFVSLLEN--YLLRDFYTPd 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1248026918 452 -PPINILSMI-ENVLAFHDKELLQHFIDRDITSQVYAWPLLETLFSEVLTREEWLRLFDNIFSNHPSFLLM 520
Cdd:pfam00566 93 fPGLKRDLYVfEELLKKKLPKLYKHLKELGLDPDLFASQWFLTLFAREFPLSTVLRIWDYFFLEGEKFVLF 163
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
608-821 |
1.46e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.00 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 608 ERIRNDELdflreRQTVENMQAEVDEQRAKDEAwYQKQELLRRAEETRR--EILLQEEEKMAQQRQRLAAVKRELEIKei 685
Cdd:PTZ00121 1481 EAKKADEA-----KKKAEEAKKKADEAKKAAEA-KKKADEAKKAEEAKKadEAKKAEEAKKADEAKKAEEKKKADELK-- 1552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 686 hlqdaaRRRLLKLQQDQREMELRRLEDEiERKVQMRDQEIAATAKDLEIrqlelEAQKRLYEKDLTTSQEAVAKEIREDT 765
Cdd:PTZ00121 1553 ------KAEELKKAEEKKKAEEAKKAEE-DKNMALRKAEEAKKAEEARI-----EEVMKLYEEEKKMKAEEAKKAEEAKI 1620
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1248026918 766 DAHR-RKAALEEHMFQKLLENSQMGGRRAQRWKEAEEkEFHLQSAKKASALSDASRK 821
Cdd:PTZ00121 1621 KAEElKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEE-ENKIKAAEEAKKAEEDKKK 1676
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
648-836 |
1.75e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.41 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 648 LRRAEE--TRREILLQEeekMAQQRQRLA----------AVKRELEIKEIHLQdAARRRLLKLQQDQREMELRRLEDEIE 715
Cdd:COG1196 181 LEATEEnlERLEDILGE---LERQLEPLErqaekaeryrELKEELKELEAELL-LLKLRELEAELEELEAELEELEAELE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 716 R-KVQMRDQEIAATAKDLEIRQLELE---AQKRLYE--KDLTTSQEAVAKEIREDTDAHRRKAALEEhmfQKLLENSQMG 789
Cdd:COG1196 257 ElEAELAELEAELEELRLELEELELEleeAQAEEYEllAELARLEQDIARLEERRRELEERLEELEE---ELAELEEELE 333
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1248026918 790 GRRAQRwKEAEEKEFHLQSAKKASALSDASRKWFLRQETSAALEHEE 836
Cdd:COG1196 334 ELEEEL-EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
613-821 |
1.78e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.61 E-value: 1.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 613 DELDFLRERQTVENMQAEvdEQRAKDEAwYQKQELLRRAEETRR--EILLQEEEKMAQQRQRLAAVKReleikeihLQDA 690
Cdd:PTZ00121 1095 EAFGKAEEAKKTETGKAE--EARKAEEA-KKKAEDARKAEEARKaeDARKAEEARKAEDAKRVEIARK--------AEDA 1163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 691 ARRRLLKLQQDQREMELRRLEDEIERKVQMRDQE----IAATAKDLEIRQLE----------LEAQKRLYEKDLTTSQEA 756
Cdd:PTZ00121 1164 RKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEdarkAEAARKAEEERKAEearkaedakkAEAVKKAEEAKKDAEEAK 1243
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1248026918 757 VAKEIREDTDAHRRKAALEEHMFQKLLENSQMGGRRAQRWKEAEEKefhlqsaKKASALSDASRK 821
Cdd:PTZ00121 1244 KAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEK-------KKADEAKKAEEK 1301
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
605-811 |
2.27e-08 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 57.83 E-value: 2.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 605 REWERIRNdELDFLR-------ERQ-TVENMQAEVDEQRAKDEAwyQKQELLRRAEETR-REILLQEEEKMAQQRQrlaa 675
Cdd:pfam17380 389 QKNERVRQ-ELEAARkvkileeERQrKIQQQKVEMEQIRAEQEE--ARQREVRRLEEERaREMERVRLEEQERQQQ---- 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 676 vkreleiKEIHLQDAARRRLLKLQQDQREMELRRLEDE----IERKVQMRDQEIaatakdleirqLELEAQKRLYEKDLT 751
Cdd:pfam17380 462 -------VERLRQQEEERKRKKLELEKEKRDRKRAEEQrrkiLEKELEERKQAM-----------IEEERKRKLLEKEME 523
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 752 TSQEAVAKEiredtdaHRRKAALEEHMFQKLLENSQmggRRAQRWKEAEEKEFHLQSAKK 811
Cdd:pfam17380 524 ERQKAIYEE-------ERRREAEEERRKQQEMEERR---RIQEQMRKATEERSRLEAMER 573
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
605-835 |
2.67e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.23 E-value: 2.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 605 REWERIRNDELDFLRERQtvENMQAEvdeQRAKDEAWYQKQELLRRAEETRREILlQEEEKMAQQRQRLAAVKRELEIKE 684
Cdd:PTZ00121 1587 KKAEEARIEEVMKLYEEE--KKMKAE---EAKKAEEAKIKAEELKKAEEEKKKVE-QLKKKEAEEKKKAEELKKAEEENK 1660
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 685 IHLQDAARrrllKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKDLE-IRQLELEAQKRlyekdlttsqeavAKEIRE 763
Cdd:PTZ00121 1661 IKAAEEAK----KAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEeLKKKEAEEKKK-------------AEELKK 1723
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1248026918 764 DTDAHRRKAaleehmfQKLLENSQMGGRRAQRWKEAEEKEFHLQSAKKasalSDASRKWFLRQETSAALEHE 835
Cdd:PTZ00121 1724 AEEENKIKA-------EEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKK----EEEKKAEEIRKEKEAVIEEE 1784
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
605-815 |
3.27e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.84 E-value: 3.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 605 REWERIRNDELdflreRQTVENMQAevDEQRAKDEAwyQKQELLRRAEETRR--EILLQEEEKMAQQRQRLAAVKRELEI 682
Cdd:PTZ00121 1505 AAEAKKKADEA-----KKAEEAKKA--DEAKKAEEA--KKADEAKKAEEKKKadELKKAEELKKAEEKKKAEEAKKAEED 1575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 683 KEIHLQDAARRRllKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEKDLTTSQEAVAKEIR 762
Cdd:PTZ00121 1576 KNMALRKAEEAK--KAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELK 1653
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1248026918 763 EDTDAHRRKAAleehmfqKLLENSQMGGRRAQRWKEAEEKEfhlqsAKKASAL 815
Cdd:PTZ00121 1654 KAEEENKIKAA-------EEAKKAEEDKKKAEEAKKAEEDE-----KKAAEAL 1694
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
628-836 |
5.43e-08 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 56.59 E-value: 5.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 628 QAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELE--IKEIHLQDAARRRLLKLQQDQREM 705
Cdd:COG3064 1 AQEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEeeAREAKAEAEQRAAELAAEAAKKLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 706 ELRRLEDEIERKVQMRDQEIAATA-KDLEIRQLELEAQKRLYEKdlttSQEAVAKEIREDTDAHRRKAALEEHMFQKLLE 784
Cdd:COG3064 81 EAEKAAAEAEKKAAAEKAKAAKEAeAAAAAEKAAAAAEKEKAEE----AKRKAEEEAKRKAEEERKAAEAEAAAKAEAEA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1248026918 785 NSQMGGRRAQRWKEAEEKEFHLQSAKKASALSDASRKWFLRQETSAALEHEE 836
Cdd:COG3064 157 ARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAA 208
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
601-776 |
5.47e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.85 E-value: 5.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 601 DYQTREWERIRNDELDFLRERQTVENMQaevdeqrakdeawyQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKREL 680
Cdd:COG4913 260 LAERYAAARERLAELEYLRAALRLWFAQ--------------RRLELLEAELEELRAELARLEAELERLEARLDALREEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 681 EIKEIHLQDAARRRLLKLQQdqremELRRLEDEIERKVQMRDQ----------EIAATAKDLEIRQLELEAQKRLYEKDL 750
Cdd:COG4913 326 DELEAQIRGNGGDRLEQLER-----EIERLERELEERERRRARleallaalglPLPASAEEFAALRAEAAALLEALEEEL 400
|
170 180
....*....|....*....|....*.
gi 1248026918 751 TTSQEAVAKEIREDTDAHRRKAALEE 776
Cdd:COG4913 401 EALEEALAEAEAALRDLRRELRELEA 426
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
650-836 |
7.32e-08 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 56.11 E-value: 7.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 650 RAEETRREILLQEEEKMAQQRQRL---AAVKRELEIKEIHLQDAARRRLlklQQDQREMElRRLEDEIERKVQMRDQEIA 726
Cdd:pfam15709 315 RSEEDPSKALLEKREQEKASRDRLraeRAEMRRLEVERKRREQEEQRRL---QQEQLERA-EKMREELELEQQRRFEEIR 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 727 ATAKDLE---IRQLELEAQKRLyekdlttsQEAVAKE-IREDTDAHRRKaaLEEHMFQKLLENSQMGGRRAQRWKEAEEK 802
Cdd:pfam15709 391 LRKQRLEeerQRQEEEERKQRL--------QLQAAQErARQQQEEFRRK--LQELQRKKQQEEAERAEAEKQRQKELEMQ 460
|
170 180 190
....*....|....*....|....*....|....*...
gi 1248026918 803 EFHLQsaKKASALSDASRKWFLRQ----ETSAALEHEE 836
Cdd:pfam15709 461 LAEEQ--KRLMEMAEEERLEYQRQkqeaEEKARLEAEE 496
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
608-802 |
2.11e-07 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 53.77 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 608 ERIRNDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRL---------AAVKR 678
Cdd:pfam13868 138 EQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERdelraklyqEEQER 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 679 ELEIKEIHLQDAARRRLLKLQQDQREM---ELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEKdlttSQE 755
Cdd:pfam13868 218 KERQKEREEAEKKARQRQELQQAREEQielKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLE----HRR 293
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1248026918 756 AVAKEIREdtdAHRRKAALEEHMFQKLLENSQMGGRRAQRWKEAEEK 802
Cdd:pfam13868 294 ELEKQIEE---REEQRAAEREEELEEGERLREEEAERRERIEEERQK 337
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
614-813 |
3.42e-07 |
|
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: 54.29 E-value: 3.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 614 ELDFLRER-QTVENMQAEVDEQRAKDEawyQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELEIKEIHLQD--- 689
Cdd:TIGR02168 303 QKQILRERlANLERQLEELEAQLEELE---SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEElee 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 690 -----AARRRLLKLQQDQREMELRRLEDEIERKVQMRDQEIAatakdlEIRQLEleaqKRLYEKDLTTSQEAVAKEIRED 764
Cdd:TIGR02168 380 qletlRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQ------EIEELL----KKLEEAELKELQAELEELEEEL 449
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1248026918 765 TDAHRRKAALEEhmfqkLLENSQMGGRRAQRWKEAEEKEFHLQSAKKAS 813
Cdd:TIGR02168 450 EELQEELERLEE-----ALEELREELEEAEQALDAAERELAQLQARLDS 493
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
597-747 |
3.62e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 53.63 E-value: 3.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 597 KFIVDYQTREWERIRNDEL-----DFLRERQTVENmqaEVDEQRAKdeawYQKQEL-LRRAEET---RREILLQEEEKMA 667
Cdd:PRK12704 41 KRILEEAKKEAEAIKKEALleakeEIHKLRNEFEK---ELRERRNE----LQKLEKrLLQKEENldrKLELLEKREEELE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 668 QQRQRLAAVKRELEIKEIHLQDAARRRLLKLQQ-------DQREMELRRLEDEIErkvqmrdQEIAATAKDLEiRQLELE 740
Cdd:PRK12704 114 KKEKELEQKQQELEKKEEELEELIEEQLQELERisgltaeEAKEILLEKVEEEAR-------HEAAVLIKEIE-EEAKEE 185
|
....*..
gi 1248026918 741 AQKRLYE 747
Cdd:PRK12704 186 ADKKAKE 192
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
611-836 |
4.85e-07 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 53.12 E-value: 4.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 611 RNDELDFLRERQTVENMQAEvdEQRAKDEawyQKQELLRRaeETRREILLQEEEKMAQQRQRLAAVKRELE------IKE 684
Cdd:pfam15558 16 RHKEEQRMRELQQQAALAWE--ELRRRDQ---KRQETLER--ERRLLLQQSQEQWQAEKEQRKARLGREERrradrrEKQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 685 IHLQDAARRRLLKLQQDQRE--MELRRLEDEIERKVQ-------------MRDQEIAATAKDLEI----RQL-ELEAQKR 744
Cdd:pfam15558 89 VIEKESRWREQAEDQENQRQekLERARQEAEQRKQCQeqrlkekeeelqaLREQNSLQLQERLEEachkRQLkEREEQKK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 745 LYEKDLttsQEAVAKEIREDTDAHRRKAalEEHMFQKLLENS---------QMGGRRAQRWKE-AEEKEFHLQSAKKASA 814
Cdd:pfam15558 169 VQENNL---SELLNHQARKVLVDCQAKA--EELLRRLSLEQSlqrsqenyeQLVEERHRELREkAQKEEEQFQRAKWRAE 243
|
250 260
....*....|....*....|....*
gi 1248026918 815 LSDASRKWFLR---QETSAALEHEE 836
Cdd:pfam15558 244 EKEEERQEHKEalaELADRKIQQAR 268
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
603-812 |
5.47e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.99 E-value: 5.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 603 QTREWERIRNDEldflRERQTVENMQAEvDEQRA----KDEAWYQKQELLRRAEETR--REILLQEEEKMAQQRQRLAAV 676
Cdd:PTZ00121 1198 DARKAEAARKAE----EERKAEEARKAE-DAKKAeavkKAEEAKKDAEEAKKAEEERnnEEIRKFEEARMAHFARRQAAI 1272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 677 KRELEIKEIHLQDAARRRllKLQQDQREMELRRLeDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEKdlttSQEA 756
Cdd:PTZ00121 1273 KAEEARKADELKKAEEKK--KADEAKKAEEKKKA-DEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEA----KKAA 1345
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1248026918 757 VAKEIREDTDAHRRKAALEEHMFQKLlENSQMGGRRAQRWKEAEEKEFHLQSAKKA 812
Cdd:PTZ00121 1346 EAAKAEAEAAADEAEAAEEKAEAAEK-KKEEAKKKADAAKKKAEEKKKADEAKKKA 1400
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
598-822 |
6.92e-07 |
|
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: 53.44 E-value: 6.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 598 FIVDYQTREWE-RIRNDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRR-EILLQEEEKMAQQRQRLAA 675
Cdd:pfam02463 168 KRKKKEALKKLiEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLyLDYLKLNEERIDLLQELLR 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 676 VKRELEIKEIHLQDAARRRLLKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRlyEKDLTTSQE 755
Cdd:pfam02463 248 DEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKL--KESEKEKKK 325
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1248026918 756 AVAKEIREDTDAHRRKAALEEHMFQKLLENSQMGGRRAQRWKEAEEKEFHLQSAKKASA--LSDASRKW 822
Cdd:pfam02463 326 AEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESErlSSAAKLKE 394
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
603-743 |
7.42e-07 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 52.65 E-value: 7.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 603 QTREWE--RIRNDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKREL 680
Cdd:pfam15709 382 QQRRFEeiRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQL 461
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1248026918 681 EIKEIHLQD-AARRRLLKLQQDQREMELRRLEDEIERKvqmRDQEIAATAKDLEIRQLELEAQK 743
Cdd:pfam15709 462 AEEQKRLMEmAEEERLEYQRQKQEAEEKARLEAEERRQ---KEEEAARLALEEAMKQAQEQARQ 522
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
605-837 |
8.25e-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: 53.15 E-value: 8.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 605 REWERIRNdELDFLRERqtVENMQAEVDE--------QRAKDEAwYQKQELLRRAEETRREILLQEEEKMAQQRQR---- 672
Cdd:TIGR02169 170 RKKEKALE-ELEEVEEN--IERLDLIIDEkrqqlerlRREREKA-ERYQALLKEKREYEGYELLKEKEALERQKEAierq 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 673 LAAVKRELEIKEIHLQDAARRrllklqQDQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEKDLTT 752
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKR------LEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELED 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 753 SQEAVAKEIREDTDAHRRKAALEEHMFQKLLENSQMGGRRAQRWKEAEEKEFHLQSAKKASALsdasrkwfLRQETSAAL 832
Cdd:TIGR02169 320 AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAE--------TRDELKDYR 391
|
....*
gi 1248026918 833 EHEEM 837
Cdd:TIGR02169 392 EKLEK 396
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
636-761 |
9.75e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 52.47 E-value: 9.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 636 AKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLaavKRELEIKEIHLQDAARRRLlklqqdQREMELRRLEDEIE 715
Cdd:PRK12704 36 AEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEF---EKELRERRNELQKLEKRLL------QKEENLDRKLELLE 106
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1248026918 716 RkvqmRDQEIAATAKDLEIRQLELEAQKRLYEKdLTTSQEAVAKEI 761
Cdd:PRK12704 107 K----REEELEKKEKELEQKQQELEKKEEELEE-LIEEQLQELERI 147
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
618-782 |
1.20e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.63 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 618 LRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELEIKEIHLQDAARRRLLK 697
Cdd:COG1196 680 ELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEP 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 698 LQQDQREMELRRLEDEIER--KVQMR-DQEIAATAKDLEirqlELEAQKrlyeKDLTTSQEAVAKEIRE-DTDAHRR-KA 772
Cdd:COG1196 760 PDLEELERELERLEREIEAlgPVNLLaIEEYEELEERYD----FLSEQR----EDLEEARETLEEAIEEiDRETRERfLE 831
|
170
....*....|....*.
gi 1248026918 773 ALEE------HMFQKL 782
Cdd:COG1196 832 TFDAvnenfqELFPRL 847
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
606-843 |
2.09e-06 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 51.00 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 606 EWERIRNDELDFLR-ERQT---VENMQAEVDEQRAKDEAwyQKQELLRRAEEtrreillQEEEKMAQQRQRLAAVKR--E 679
Cdd:TIGR02794 51 QANRIQQQKKPAAKkEQERqkkLEQQAEEAEKQRAAEQA--RQKELEQRAAA-------EKAAKQAEQAAKQAEEKQkqA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 680 LEIKEIHLQDAArrrllklqqdqremelRRLEDEIERKVQmrdQEIAATAKDLEIRQLELEAQKRLYEKDLTTSQEAVAK 759
Cdd:TIGR02794 122 EEAKAKQAAEAK----------------AKAEAEAERKAK---EEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 760 EiredtDAhRRKAALEEHMFQKLlensqmgGRRAQRWKEAEEKefhLQSAKKASALSDASRK-WFLRQETSAALEHEEMP 838
Cdd:TIGR02794 183 A-----EA-EAKAKAEEAKAKAE-------AAKAKAAAEAAAK---AEAEAAAAAAAEAERKaDEAELGDIFGLASGSNA 246
|
....*
gi 1248026918 839 WLQRQ 843
Cdd:TIGR02794 247 EKQGG 251
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
606-770 |
2.12e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.07 E-value: 2.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 606 EWERIRNDELDFLRE-RQTVENMQAEVDEQ--------RAKDEAWYQKQELLRRAEETRR--EILLQEEE---KMAQQRQ 671
Cdd:PTZ00121 1616 EEAKIKAEELKKAEEeKKKVEQLKKKEAEEkkkaeelkKAEEENKIKAAEEAKKAEEDKKkaEEAKKAEEdekKAAEALK 1695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 672 RLAAVKRELEikEIHLQDAARRRllKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKDLE-----IRQLELEAQKRLY 746
Cdd:PTZ00121 1696 KEAEEAKKAE--ELKKKEAEEKK--KAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEeekkkIAHLKKEEEKKAE 1771
|
170 180
....*....|....*....|....
gi 1248026918 747 EkdLTTSQEAVAKEIREDTDAHRR 770
Cdd:PTZ00121 1772 E--IRKEKEAVIEEELDEEDEKRR 1793
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
603-788 |
3.16e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.92 E-value: 3.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 603 QTREWERIRNDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREiLLQEEEKMAQQRQRLAAVKRelei 682
Cdd:COG4717 86 KEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAE-LAELPERLEELEERLEELRE---- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 683 keihlqdaarrrlLKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEKDLTTSQEAVaKEIR 762
Cdd:COG4717 161 -------------LEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEEL-EELE 226
|
170 180
....*....|....*....|....*.
gi 1248026918 763 EDTDAHRRKAALEEhMFQKLLENSQM 788
Cdd:COG4717 227 EELEQLENELEAAA-LEERLKEARLL 251
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
607-803 |
3.41e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 50.30 E-value: 3.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 607 WERIRNDELDFLRERQT-VENMQAEVDEQRAKDEAWYQKQ-----ELLRRAEETRREILLQEEEKMAQQRQRLAAVKREL 680
Cdd:pfam13868 107 VERIQEEDQAEAEEKLEkQRQLREEIDEFNEEQAEWKELEkeeerEEDERILEYLKEKAEREEEREAEREEIEEEKEREI 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 681 ---------EIKEIHLQDAARRRLL------KLQQDQREMELRRLEDEIERKvQMRDQEIAATAkdlEIRQLELEAQKRL 745
Cdd:pfam13868 187 arlraqqekAQDEKAERDELRAKLYqeeqerKERQKEREEAEKKARQRQELQ-QAREEQIELKE---RRLAEEAEREEEE 262
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1248026918 746 YEKDLTTSQEAVAKEIREdtdAHRRKAALEEHmfQKLLENsQMGGRRAQRWKEAEEKE 803
Cdd:pfam13868 263 FERMLRKQAEDEEIEQEE---AEKRRMKRLEH--RRELEK-QIEEREEQRAAEREEEL 314
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
621-776 |
4.18e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.21 E-value: 4.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 621 RQTVENMQAEVDE-QRAKDEAWYQKQELLRRAEETRREILlQEEEKMAQQRQRLAAVKRELEIKEI------------HL 687
Cdd:COG3883 36 QAELDALQAELEElNEEYNELQAELEALQAEIDKLQAEIA-EAEAEIEERREELGERARALYRSGGsvsyldvllgseSF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 688 QDAARRRLL--KLQQDQREM--ELRRLEDEIERKvqmrDQEIAATAKDLEIRQLELEAQKRLYEKDLTTSQEAVAKEIRE 763
Cdd:COG3883 115 SDFLDRLSAlsKIADADADLleELKADKAELEAK----KAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAE 190
|
170
....*....|...
gi 1248026918 764 DTDAHRRKAALEE 776
Cdd:COG3883 191 EAAAEAQLAELEA 203
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
603-815 |
4.46e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 4.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 603 QTREWERIRNDELdfLRERQTVENMQA--EVDEQRAKDEAwyQKQELLRRAEETRReilLQEEEKMAQQRQRLAAVKREL 680
Cdd:PTZ00121 1180 AARKAEEVRKAEE--LRKAEDARKAEAarKAEEERKAEEA--RKAEDAKKAEAVKK---AEEAKKDAEEAKKAEEERNNE 1252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 681 EIKEIhlqDAARRRLLKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKdlEIRQLElEAQKRLYEKDLTTSQEAVAKE 760
Cdd:PTZ00121 1253 EIRKF---EEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAE--EKKKAD-EAKKKAEEAKKADEAKKKAEE 1326
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 761 IREDTDAHRRKAalEE-----HMFQKLLENSQMGGRRAQRWKEAEEKEFHlQSAKKASAL 815
Cdd:PTZ00121 1327 AKKKADAAKKKA--EEakkaaEAAKAEAEAAADEAEAAEEKAEAAEKKKE-EAKKKADAA 1383
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
608-811 |
5.55e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.52 E-value: 5.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 608 ERIRNDELDFLRERQTVENMQaEVDEQRAKDEawyQKQELLRRAEETRreillQEEEKMAQQRQRLAAVKRELEIKEIHL 687
Cdd:PTZ00121 1544 EKKKADELKKAEELKKAEEKK-KAEEAKKAEE---DKNMALRKAEEAK-----KAEEARIEEVMKLYEEEKKMKAEEAKK 1614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 688 QDAARrrlLKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEKDLTTSQEA--VAKEIREDT 765
Cdd:PTZ00121 1615 AEEAK---IKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAkkAEEDEKKAA 1691
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1248026918 766 DAHRRKAAlEEHMFQKLLENSQMGGRRAQRWKEAEE-KEFHLQSAKK 811
Cdd:PTZ00121 1692 EALKKEAE-EAKKAEELKKKEAEEKKKAEELKKAEEeNKIKAEEAKK 1737
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
622-812 |
6.83e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.34 E-value: 6.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 622 QTVENMQAEVDEQRAKDEAwyqkQELLRRAEETR--------REILLQEEEKMAQQRQRLAAVKRELEIK-EIHLQDAAr 692
Cdd:PRK04863 480 QLVRKIAGEVSRSEAWDVA----RELLRRLREQRhlaeqlqqLRMRLSELEQRLRQQQRAERLLAEFCKRlGKNLDDED- 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 693 rrLLKLQQDQREMELRRLEDE----IERKVQMRDQEIAATAkdlEIRQLELEAQKRLyekdltTSQEAVAK--EIREDTD 766
Cdd:PRK04863 555 --ELEQLQEELEARLESLSESvseaRERRMALRQQLEQLQA---RIQRLAARAPAWL------AAQDALARlrEQSGEEF 623
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1248026918 767 AHRrkAALEEHMfQKLLEnsqmggrraqRWKEAEEKEFHLQSAKKA 812
Cdd:PRK04863 624 EDS--QDVTEYM-QQLLE----------RERELTVERDELAARKQA 656
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
629-776 |
7.37e-06 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 49.49 E-value: 7.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 629 AEVDEQRAKDEAwyqkqELLRRAEETRREILLQEEEKMAQQrqrlaavKRELEIKEIHLQDAARRRllKLQQDQREMELR 708
Cdd:COG2268 195 AEIIRDARIAEA-----EAERETEIAIAQANREAEEAELEQ-------EREIETARIAEAEAELAK--KKAEERREAETA 260
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1248026918 709 RLEDEIERKVQmrdQEIAATAKDLEIRQLELEAQKRLYEKDLTTSQEAVAKEIREDTDAHRRKAALEE 776
Cdd:COG2268 261 RAEAEAAYEIA---EANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEA 325
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
611-859 |
7.38e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.06 E-value: 7.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 611 RNDELDFLRERqtVENMQAEVDEQRAKDEAWYQKQE--------LLRRAEETRREI---------LLQEEEKMAQQRQRL 673
Cdd:TIGR02168 675 RRREIEELEEK--IEELEEKIAELEKALAELRKELEeleeeleqLRKELEELSRQIsalrkdlarLEAEVEQLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 674 aavkrELEIKEIhlqdAARRRLLKLQQDQREMELRRLEDEIErKVQMRDQEIAATAKDLEIRQLELEAQKRLYEKDLTTS 753
Cdd:TIGR02168 753 -----SKELTEL----EAEIEELEERLEEAEEELAEAEAEIE-ELEAQIEQLKEELKALREALDELRAELTLLNEEAANL 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 754 QEAVAKEIREDTDAHRRKAALEEHMFQKLLENSQMGGRRAQRWKEAEEKEFHLQSAKKASALSDASRKWFLRQETSAALE 833
Cdd:TIGR02168 823 RERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEE 902
|
250 260
....*....|....*....|....*.
gi 1248026918 834 HEEMPwLQRQYMDSAYLPQTSRLHDV 859
Cdd:TIGR02168 903 LRELE-SKRSELRRELEELREKLAQL 927
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
627-835 |
1.47e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 47.99 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 627 MQAEVDEQRA-----KDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELeikEIHLQDAARRRLLKLQQD 701
Cdd:pfam13868 20 CNKERDAQIAekkriKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQEL---EEQIEEREQKRQEEYEEK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 702 QREMEL-----RRLEDEIERKVQMRDQEIAATAKDL--------EIRQLELEAQKRL------YEKDLTTSQEAVAKEIR 762
Cdd:pfam13868 97 LQEREQmdeivERIQEEDQAEAEEKLEKQRQLREEIdefneeqaEWKELEKEEEREEderileYLKEKAEREEEREAERE 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1248026918 763 EDTDAH-RRKAALEEHMFQKLLENSQMGGRRAQRWKEAEEKEFHLQsakkasALSDASRKWFLRQETSAALEHE 835
Cdd:pfam13868 177 EIEEEKeREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQK------EREEAEKKARQRQELQQAREEQ 244
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
604-837 |
1.56e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 48.26 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 604 TREWERIRNDELDFLR---ERQTVENMQAEvdEQRAKDEAWYQK-----------QELLRRAEETRREILLQEEEKMAQQ 669
Cdd:PRK09510 61 VEQYNRQQQQQKSAKRaeeQRKKKEQQQAE--ELQQKQAAEQERlkqlekerlaaQEQKKQAEEAAKQAALKQKQAEEAA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 670 RQRLAAVKRELEIKEIHLQDAArrrllklqqdqremelRRLEDEIERKvqmrdqEIAATAKdleirQLELEAQKRLYEKd 749
Cdd:PRK09510 139 AKAAAAAKAKAEAEAKRAAAAA----------------KKAAAEAKKK------AEAEAAK-----KAAAEAKKKAEAE- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 750 lttSQEAVAKEIREDTDAHRRKAALEEhmfqkllensqmggrrAQRWKEAEEKEFHLQSAKKASALSDASRKWFLRQETS 829
Cdd:PRK09510 191 ---AAAKAAAEAKKKAEAEAKKKAAAE----------------AKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAA 251
|
....*...
gi 1248026918 830 AALEHEEM 837
Cdd:PRK09510 252 AAKAAAEV 259
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
619-773 |
1.69e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 619 RERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREiLLQEEEKMAQQRQRLAAVKRELE--------IKEIHLQ-D 689
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQERREALQRLAE-YSWDEIDVASAEREIAELEAELErldassddLAALEEQlE 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 690 AARRRLLKLQQDQREM--ELRRLEDEIERKVQMRD--QEIAATAKDLEIRQLELEAQKRLYEkdltTSQEAVAKEIREDT 765
Cdd:COG4913 696 ELEAELEELEEELDELkgEIGRLEKELEQAEEELDelQDRLEAAEDLARLELRALLEERFAA----ALGDAVERELRENL 771
|
....*...
gi 1248026918 766 DAHRRKAA 773
Cdd:COG4913 772 EERIDALR 779
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
619-747 |
1.73e-05 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 45.80 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 619 RERQTVENMQAEVDEQRAKDEAWYQ-KQELLRRAEETRREillQEEE--KMAQQRQRLAAVKRELEIKEIHLQDAARRRL 695
Cdd:pfam05672 19 KRRQAREQREREEQERLEKEEEERLrKEELRRRAEEERAR---REEEarRLEEERRREEEERQRKAEEEAEEREQREQEE 95
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1248026918 696 LKLQQDQREMELRRLEDEIERKVQMRDQEIaatakdLEIRQLELEAQKRLYE 747
Cdd:pfam05672 96 QERLQKQKEEAEAKAREEAERQRQEREKIM------QQEEQERLERKKRIEE 141
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
608-837 |
2.06e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.60 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 608 ERIRNDELdflreRQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREILLQ---EEEKMAQQRQRLAAVKRELEIKE 684
Cdd:PTZ00121 1389 EKKKADEA-----KKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKkkaEEAKKADEAKKKAEEAKKAEEAK 1463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 685 IHLQDAARRRLLKLQQDQREM--ELRRLEDEIERKVQMRDQEIAATAKDLEIRQLElEAQK----RLYEKDLTTSQEAVA 758
Cdd:PTZ00121 1464 KKAEEAKKADEAKKKAEEAKKadEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAE-EAKKadeaKKAEEAKKADEAKKA 1542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 759 KEIREDTDAHR----RKAALEEHMFQ--KLLENSQMGGRRAQRWKEAEEKEfhLQSAKKASALSDASRKWFLRQETSAAL 832
Cdd:PTZ00121 1543 EEKKKADELKKaeelKKAEEKKKAEEakKAEEDKNMALRKAEEAKKAEEAR--IEEVMKLYEEEKKMKAEEAKKAEEAKI 1620
|
....*
gi 1248026918 833 EHEEM 837
Cdd:PTZ00121 1621 KAEEL 1625
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
614-764 |
2.81e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.46 E-value: 2.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 614 ELDFLRERQtvENMQAEVDEQRAKDEAWYQKQELLRRA-EETRREI------LLQEEEKMAQQRQRLAAVK--RELEI-- 682
Cdd:COG1579 18 ELDRLEHRL--KELPAELAELEDELAALEARLEAAKTElEDLEKEIkrleleIEEVEARIKKYEEQLGNVRnnKEYEAlq 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 683 KEIHLqdaarrrlLKLQQDQREMELRRLEDEIERKVQMRDQ---EIAATAKDLEIRQLELEAQKRLYEKD---LTTSQEA 756
Cdd:COG1579 96 KEIES--------LKRRISDLEDEILELMERIEELEEELAEleaELAELEAELEEKKAELDEELAELEAEleeLEAEREE 167
|
....*...
gi 1248026918 757 VAKEIRED 764
Cdd:COG1579 168 LAAKIPPE 175
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
606-723 |
2.90e-05 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 45.03 E-value: 2.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 606 EWERIRNDELdflRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEEKMA-QQRQRLAAVKRELEike 684
Cdd:pfam05672 39 EEERLRKEEL---RRRAEEERARREEEARRLEEERRREEEERQRKAEEEAEEREQREQEEQErLQKQKEEAEAKARE--- 112
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1248026918 685 ihlqDAARRRLLKLQQDQREMELR-----RLEdEIERKVQMRDQ 723
Cdd:pfam05672 113 ----EAERQRQEREKIMQQEEQERlerkkRIE-EIMKRTRKSDQ 151
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
612-784 |
3.01e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 3.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 612 NDELDFLRERQTVENMQAEVDEQ----RAKDEAWYQKQELLRRAEETRREIllqeeekmAQQRQRLAAVKRELeikeihl 687
Cdd:COG4913 637 EAELDALQERREALQRLAEYSWDeidvASAEREIAELEAELERLDASSDDL--------AALEEQLEELEAEL------- 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 688 qDAARRRLLKLQQDQR--EMELRRLEDEIERKvqmrdQEIAATAKDLEIRQLELEAQKRLYEKDLTTSQEAVAKEIREDT 765
Cdd:COG4913 702 -EELEEELDELKGEIGrlEKELEQAEEELDEL-----QDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERI 775
|
170
....*....|....*....
gi 1248026918 766 DAHRRKAALEEHMFQKLLE 784
Cdd:COG4913 776 DALRARLNRAEEELERAMR 794
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
608-807 |
3.47e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 46.84 E-value: 3.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 608 ERIRNDELDFLRERQTVENMQAEVDEQRAKDEAWYQ-KQEL-----------LRRAEETRREILL--------QEEEKMA 667
Cdd:pfam13868 38 EKEEERRLDEMMEEERERALEEEEEKEEERKEERKRyRQELeeqieereqkrQEEYEEKLQEREQmdeiveriQEEDQAE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 668 QQRQRLAAVKRELEIKEIHLQDAARRRLLKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYE 747
Cdd:pfam13868 118 AEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQ 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 748 KDLTTSQEAVAKEIREDTDAHRRKAALEEhMFQKLLENSQMggrRAQRWKEAEEKEFHLQ 807
Cdd:pfam13868 198 DEKAERDELRAKLYQEEQERKERQKEREE-AEKKARQRQEL---QQAREEQIELKERRLA 253
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
628-765 |
3.56e-05 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 45.65 E-value: 3.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 628 QAEVDEQRAKDEAwyqKQEllrrAEETRREILLQEEEKMAQQRQRLaavkrELEIKEihlqdaaRRRLLKLQQD---QRE 704
Cdd:pfam12072 31 SAEELAKRIIEEA---KKE----AETKKKEALLEAKEEIHKLRAEA-----ERELKE-------RRNELQRQERrllQKE 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1248026918 705 MEL-RRLE--DEIERKVQMRDQEIAATAKDLEIRQLELEA-----QKRLYEKDLTTSQEA-------VAKEIREDT 765
Cdd:pfam12072 92 ETLdRKDEslEKKEESLEKKEKELEAQQQQLEEKEEELEElieeqRQELERISGLTSEEAkeilldeVEEELRHEA 167
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
601-776 |
3.65e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 3.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 601 DYQTREWERIRnDELDFLRErqtvenmqAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKREL 680
Cdd:COG4717 315 ELEEEELEELL-AALGLPPD--------LSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEE 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 681 EIKEIHLQDAARRRLLKlQQDQREMELRRLEDEIERKVQMRDQEiaatakDLEIRQLELEAQKRLYEKDLTTSQEAVA-- 758
Cdd:COG4717 386 ELRAALEQAEEYQELKE-ELEELEEQLEELLGELEELLEALDEE------ELEEELEELEEELEELEEELEELREELAel 458
|
170 180
....*....|....*....|..
gi 1248026918 759 ----KEIREDTDAHRRKAALEE 776
Cdd:COG4717 459 eaelEQLEEDGELAELLQELEE 480
|
|
| COG5210 |
COG5210 |
GTPase-activating protein [General function prediction only]; |
457-573 |
3.74e-05 |
|
GTPase-activating protein [General function prediction only];
Pssm-ID: 227535 [Multi-domain] Cd Length: 496 Bit Score: 47.49 E-value: 3.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 457 LSMIENVLAFHDKELLQHFIDRDITSQVYAWPLLETLFSEVLTREEWLRLFDNIFSNHPSFLLMTVVAYSTCSRAPLLNC 536
Cdd:COG5210 350 LKVLDDLVEELDPELYEHLLREGVVLLMFAFRWFLTLFVREFPLEYALRIWDCLFLEGSSMLFQLALAILKLLRDKLLKL 429
|
90 100 110
....*....|....*....|....*....|....*..
gi 1248026918 537 TLKNDFEYFFHHRNNLDINVVIREVYHLMETTPADIH 573
Cdd:COG5210 430 DSDELLDLLLKQLFLHSGKEAWSSILKFRHGTDRDIL 466
|
|
| Fibrinogen_BP |
pfam08017 |
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family ... |
619-802 |
3.82e-05 |
|
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family includes the fibrinogen receptor, FbsA, which mediates platelet aggregation.
Pssm-ID: 311808 [Multi-domain] Cd Length: 393 Bit Score: 47.17 E-value: 3.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 619 RERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEetrREILLQEEEKMAQQRQRLAAVKRELEIKEIHLQDAARRRLLK- 697
Cdd:pfam08017 130 RQRDAENRSQGNVLERRQRDAENRSQGNVLERRQ---RDAENRSQGNVLERRQRDAENKSQGNVLERRQRDAENRSQGNv 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 698 LQQDQREMELRRLEDEIERKvqMRDQEIAATAKDLEIRQLELEAQkrlyekdlttSQEAVAKEIREDTDAHRRKAALEEH 777
Cdd:pfam08017 207 LERRQRDAENRSQGNVLERR--QRDAENRSQGNVLERRQRDAENK----------SQGNVLERRQRDAENRSQGNVLERR 274
|
170 180
....*....|....*....|....*
gi 1248026918 778 mfQKLLENSQMGGRRAQRWKEAEEK 802
Cdd:pfam08017 275 --QRDAENRSQGNVLERRQRDAENK 297
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
634-801 |
4.88e-05 |
|
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 198 and 469 amino acids in length. There are two completely conserved L residues that may be functionally important.
Pssm-ID: 405647 [Multi-domain] Cd Length: 206 Bit Score: 45.53 E-value: 4.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 634 QRAKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLaaVKRELEIKEIHLQDAARRRLLKLQQDQrEMELRRLEDE 713
Cdd:pfam14988 17 QKKIEKLWNQYVQECEEIERRRQELASRYTQQTAELQTQL--LQKEKEQASLKKELQALRPFAKLKESQ-EREIQDLEEE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 714 IErKVQmrdQEIAATAKDLEIRQLELEA--QKRLYEKDLTTSQEAVAKEIREDTDAHRRKA--ALEEHM----------- 778
Cdd:pfam14988 94 KE-KVR---AETAEKDREAHLQFLKEKAllEKQLQELRILELGERATRELKRKAQALKLAAkqALSEFCrsikrenrqlq 169
|
170 180 190
....*....|....*....|....*....|..
gi 1248026918 779 ---------FQKLLENSQMGGRRAQRWKEAEE 801
Cdd:pfam14988 170 kellqliqeTQALEAIKSKLENRKQRLKEEQW 201
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
622-801 |
4.93e-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: 47.25 E-value: 4.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 622 QTVENMQAEVDeqraKDEAWYQKQELLRRAEETRreillqeeeKMAQQRQRLAAVKRELEiKEIHLQDAARRRL------ 695
Cdd:COG3096 479 ELVCKIAGEVE----RSQAWQTARELLRRYRSQQ---------ALAQRLQQLRAQLAELE-QRLRQQQNAERLLeefcqr 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 696 ----------LKLQQDQREMELRRLEDE----IERKVQMRDQEIAATAKDLEIRQLE---LEAQKRLyEKDLTTSQEAVA 758
Cdd:COG3096 545 igqqldaaeeLEELLAELEAQLEELEEQaaeaVEQRSELRQQLEQLRARIKELAARApawLAAQDAL-ERLREQSGEALA 623
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1248026918 759 KeiREDTDAHRRKAALEEHMFQklLENSQMGGRRAQRWKEAEE 801
Cdd:COG3096 624 D--SQEVTAAMQQLLEREREAT--VERDELAARKQALESQIER 662
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
30-68 |
6.10e-05 |
|
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.
Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 41.14 E-value: 6.10e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1248026918 30 TKELVSWMRGHESSVCSISVHASGRYAITTSSD-TAQLWD 68
Cdd:smart00320 1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDgTIKLWD 40
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
628-762 |
6.27e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 46.63 E-value: 6.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 628 QAEVDEQRAKDEAWYQKQELLRRAEET-------RREILLQEEEKMAQQRQRLAAVKRELEIKEIHLqdAARRRLLKLQQ 700
Cdd:PRK12705 41 EAQKEAEEKLEAALLEAKELLLRERNQqrqearrEREELQREEERLVQKEEQLDARAEKLDNLENQL--EEREKALSARE 118
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1248026918 701 DQREMELRRLEDEIERKVQMRDQEiaatAKDLEIRQL--ELEAQK-RLYEKDLTTSQEAVAKEIR 762
Cdd:PRK12705 119 LELEELEKQLDNELYRVAGLTPEQ----ARKLLLKLLdaELEEEKaQRVKKIEEEADLEAERKAQ 179
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
599-812 |
6.81e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.98 E-value: 6.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 599 IVDYQTREWERIRN--DELDFL-RERQTVENMQAEVD---EQRAKDEAWYQKQ--ELLRRAEETRREILLQEEEKMAQQR 670
Cdd:TIGR02169 728 LEQEEEKLKERLEEleEDLSSLeQEIENVKSELKELEariEELEEDLHKLEEAlnDLEARLSHSRIPEIQAELSKLEEEV 807
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 671 QRLAAVKRELEIKEihlqdaaRRRLLKLQQDQREM-ELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEaQKRLYEKD 749
Cdd:TIGR02169 808 SRIEARLREIEQKL-------NRLTLEKEYLEKEIqELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELE-ELEAALRD 879
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1248026918 750 LTTSQEAVAKEiREDTDAHRRKA--ALEEHMFQKLLENSQMGGRRAQRwKEAEEKEFHLQSAKKA 812
Cdd:TIGR02169 880 LESRLGDLKKE-RDELEAQLRELerKIEELEAQIEKKRKRLSELKAKL-EALEEELSEIEDPKGE 942
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
605-773 |
9.62e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.47 E-value: 9.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 605 REWERIRNDELDFLRERQTVEN-----MQAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRE 679
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAqleelEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 680 LEIKEIHLQDAARRRLLKLQQDQREMELRRLEDEIERKVQMRDQ----------------------EIAATAKDLEIRQL 737
Cdd:COG1196 459 EALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADyegflegvkaalllaglrglagAVAVLIGVEAAYEA 538
|
170 180 190
....*....|....*....|....*....|....*.
gi 1248026918 738 ELEAQKRLYEKDLTTSQEAVAKEIREDTDAHRRKAA 773
Cdd:COG1196 539 ALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRA 574
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
604-847 |
1.20e-04 |
|
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: 45.94 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 604 TREWERIRNdeLDFLRERQtvENMQAEVDEQRAKDEAWYQKQELLRRAEETRREILlqeEEKMAQQRQRLAAVKRELEIK 683
Cdd:pfam01576 169 AEEEEKAKS--LSKLKNKH--EAMISDLEERLKKEEKGRQELEKAKRKLEGESTDL---QEQIAELQAQIAELRAQLAKK 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 684 EIHLQDAARR------RLLKLQQDQREME--LRRLEDEIERKVQMRDQeIAATAKDLEirqLELEAQKRLYEKDLTTS-- 753
Cdd:pfam01576 242 EEELQAALARleeetaQKNNALKKIRELEaqISELQEDLESERAARNK-AEKQRRDLG---EELEALKTELEDTLDTTaa 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 754 -QEAVAKEIREDTDAhrrKAALEEhmfQKLLENSQMGGRRAQRWKEAEEKEFHLQSAKKASALSDASRKWFlrqETSAAL 832
Cdd:pfam01576 318 qQELRSKREQEVTEL---KKALEE---ETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQAL---ESENAE 388
|
250
....*....|....*
gi 1248026918 833 EHEEMPWLQRQYMDS 847
Cdd:pfam01576 389 LQAELRTLQQAKQDS 403
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
603-820 |
1.26e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 45.80 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 603 QTREWERIRNDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQE---LLRRAEETRREILLQEEE--KMAQQRQRLAAVK 677
Cdd:COG3064 11 EAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEeeaREAKAEAEQRAAELAAEAakKLAEAEKAAAEAE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 678 RELEIKEIHLQDAARRRlLKLQQDQREMELRRLEdEIERKVQmRDQEIAATAKDLEIRQLELEAQKRLYEKDLTTSQEAV 757
Cdd:COG3064 91 KKAAAEKAKAAKEAEAA-AAAEKAAAAAEKEKAE-EAKRKAE-EEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1248026918 758 AKEIREDTDAHRRKAALEEHMFQKLLENSQMGGRRAQRWKEAEEKEFHLQSAKKASALSDASR 820
Cdd:COG3064 168 AAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASR 230
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
608-840 |
1.33e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.28 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 608 ERIRNDELDFLRERQTVENMQAEVDEQRAKDEAwyQKQELLRRAEETRREiLLQEEEKMAQQRQRLAAVKRELEIKEIHL 687
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALF--ELDKLQEELEQLREE-LEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 688 QDAaRRRLLKLQQDQREM--ELRRLEDEIERKVQMRdQEIAATAKDLEIRQLELEAQKRLYEKDLTtSQEAVAKEIREDT 765
Cdd:COG4372 83 EEL-NEQLQAAQAELAQAqeELESLQEEAEELQEEL-EELQKERQDLEQQRKQLEAQIAELQSEIA-EREEELKELEEQL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1248026918 766 dahrrkAALEEHMFQKLLENSQMGGRRAQRWKEAEEKEFHLQSAKKASALSDASRKWFLRQETSAALEHEEMPWL 840
Cdd:COG4372 160 ------ESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLE 228
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
642-821 |
1.50e-04 |
|
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: 45.82 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 642 YQKQELlrraEETRREILLQEEeKMAQQRQRLAAVKRELEIKEIHLQDAARRRLLKLQQ-DQREMELRRLEDEIERKVQM 720
Cdd:TIGR02168 674 ERRREI----EELEEKIEELEE-KIAELEKALAELRKELEELEEELEQLRKELEELSRQiSALRKDLARLEAEVEQLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 721 RDQeiaatakdLEIRQLELEAQKRLYEKDLTTSQEAVAKEIREdtdahrrKAALEEHMFQKLLENSQmgGRRAQRWKEAE 800
Cdd:TIGR02168 749 IAQ--------LSKELTELEAEIEELEERLEEAEEELAEAEAE-------IEELEAQIEQLKEELKA--LREALDELRAE 811
|
170 180
....*....|....*....|.
gi 1248026918 801 EKEFHLQSAKKASALSDASRK 821
Cdd:TIGR02168 812 LTLLNEEAANLRERLESLERR 832
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
608-822 |
1.55e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.14 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 608 ERIRNDELDFLRERQTVENMQAEVDEQRAKDEAwyQKQELLRRAEETRREILlQEEEKMAQQRQRLAAVKRELEIKEIH- 686
Cdd:COG4942 44 AALKKEEKALLKQLAALERRIAALARRIRALEQ--ELAALEAELAELEKEIA-ELRAELEAQKEELAELLRALYRLGRQp 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 687 ----------LQDAARR-RLLKLQQDQREMELRRLEDEIERKVQMRdQEIAATAKDLEIRQLELEAQKRLYEKdLTTSQE 755
Cdd:COG4942 121 plalllspedFLDAVRRlQYLKYLAPARREQAEELRADLAELAALR-AELEAERAELEALLAELEEERAALEA-LKAERQ 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1248026918 756 AVAKEIREDTDAHRRKAAleehmfqKLLENSQmggRRAQRWKEAEEKEFHLQSAKKASALSDASRKW 822
Cdd:COG4942 199 KLLARLEKELAELAAELA-------ELQQEAE---ELEALIARLEAEAAAAAERTPAAGFAALKGKL 255
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
618-785 |
1.70e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 45.34 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 618 LRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEE---TRREIL------------LQEEEKMAQQRQRLAAVKRELEI 682
Cdd:TIGR00618 327 LMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEvatSIREIScqqhtltqhihtLQQQKTTLTQKLQSLCKELDILQ 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 683 KEIHLQDAARRRLLKLQQDqremeLRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEK-DLTTSQEAVAKEI 761
Cdd:TIGR00618 407 REQATIDTRTSAFRDLQGQ-----LAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSlKEREQQLQTKEQI 481
|
170 180
....*....|....*....|....
gi 1248026918 762 redTDAHRRKAALEEHMFQKLLEN 785
Cdd:TIGR00618 482 ---HLQETRKKAVVLARLLELQEE 502
|
|
| Fibrinogen_BP |
pfam08017 |
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family ... |
628-802 |
1.72e-04 |
|
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family includes the fibrinogen receptor, FbsA, which mediates platelet aggregation.
Pssm-ID: 311808 [Multi-domain] Cd Length: 393 Bit Score: 44.86 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 628 QAEVDEQRAKDEAWYQKQELLRRAEetrREILLQEEEKMAQQRQRLAAVKRELEIKEIHLQDAARRRLLK-LQQDQREME 706
Cdd:pfam08017 27 QGNVLERRQRDAENRSQGNVLERRQ---RDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNvLERRQRDAE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 707 LRRLEDEIERKvqMRDQEIAATAKDLEIRQLELEAQkrlyekdlttSQEAVAKEIREDTDAHRRKAALEEHmfQKLLENS 786
Cdd:pfam08017 104 NRSQGNVLERR--QRDAENKSQGNVLERRQRDAENR----------SQGNVLERRQRDAENRSQGNVLERR--QRDAENR 169
|
170
....*....|....*.
gi 1248026918 787 QMGGRRAQRWKEAEEK 802
Cdd:pfam08017 170 SQGNVLERRQRDAENK 185
|
|
| TBC |
smart00164 |
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and ... |
416-524 |
1.74e-04 |
|
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and Gyp7, thereby giving rise to the notion that it performs a GTP-activator activity on Rab-like GTPases.
Pssm-ID: 214540 [Multi-domain] Cd Length: 216 Bit Score: 43.83 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 416 AFP-FVKLFQNNQLIcFEVVATLIINWCQHWFEYFpnppinilsmienvLAFHDKELLQHFIDRDITSQVYAWPLLETLF 494
Cdd:smart00164 112 AFWcLVKLMERYGPN-FYLPDMSGLQLDLLQLDRL--------------VKEYDPDLYKHLKDLGITPSLYALRWFLTLF 176
|
90 100 110
....*....|....*....|....*....|
gi 1248026918 495 SEVLTREEWLRLFDNIFSNHPSFLLMTVVA 524
Cdd:smart00164 177 ARELPLEIVLRIWDVLFAEGSDFLFRVALA 206
|
|
| EVC2_like |
pfam12297 |
Ellis van Creveld protein 2 like protein; This family of proteins is found in eukaryotes. ... |
604-788 |
1.84e-04 |
|
Ellis van Creveld protein 2 like protein; This family of proteins is found in eukaryotes. Proteins in this family are typically between 571 and 1310 amino acids in length. There are two conserved sequence motifs: LPA and ELH. EVC2 is implicated in Ellis van Creveld chondrodysplastic dwarfism in humans. Mutations in this protein can give rise to this congenital condition. LIMBIN is a protein which shares around 80% sequence homology with EVC2 and it is implicated in a similar condition in bovine chondrodysplastic dwarfism.
Pssm-ID: 463525 [Multi-domain] Cd Length: 428 Bit Score: 45.07 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 604 TREWERIRNDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQELLRR-----AEETRREILLQEEEKMAQQRQRLaAVKR 678
Cdd:pfam12297 223 AAECNLETREKMEAQHQREMAEKEEAEELLKHADEQEALECSSLLDKlhkleQEHLQRSLLLRQEEDFAKAQRQL-AVFQ 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 679 ELEIKEI---HLQDAARRRLLKLQQDQREM-ELRRLEDEIERkvqMRDQEIAATAKDLEIR--QLE-----LEAQKRLYE 747
Cdd:pfam12297 302 RVELHKIfftQLKEATRKGELKPEAAKRLLqDYSKIQEQIEE---LMDFFQANQRYHLSERfaQREylvqsLQSLETRVS 378
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1248026918 748 KDLTTSQEAVAKEIREdtdaHRRKAALEEHMFQKLLENSQM 788
Cdd:pfam12297 379 GLLNTAATQLTSLIQK----MERAGYLDEEQMEMLLERAQK 415
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
632-856 |
1.98e-04 |
|
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: 45.21 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 632 DEQRAKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELEIKEIHLQDAarRRLLKlqqdQREMELRRLE 711
Cdd:pfam12128 586 DLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFA--RTALK----NARLDLRRLF 659
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 712 DEiERKVQMRDQEIAATAKDLEIRQL-ELEAQKRLYEKDLTTSQEAVAKEIREDTDA--HRRKAALEEHMFQKLLENSQM 788
Cdd:pfam12128 660 DE-KQSEKDKKNKALAERKDSANERLnSLEAQLKQLDKKHQAWLEEQKEQKREARTEkqAYWQVVEGALDAQLALLKAAI 738
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1248026918 789 GGRRAQRWKE--AEEKEFHLQSAKKA------SALSDASRKWFLRQETSAALEHEEMPWlqRQYMDSAYLPQTSRL 856
Cdd:pfam12128 739 AARRSGAKAElkALETWYKRDLASLGvdpdviAKLKREIRTLERKIERIAVRRQEVLRY--FDWYQETWLQRRPRL 812
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
650-801 |
2.06e-04 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 42.72 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 650 RAEETRReiLLQEEEKMA-QQRQRLAAVKRELEIKEIHLQDAARRRLLKLQQDQREmELRRLEDeiERKVQMRDQEIAAT 728
Cdd:pfam05672 8 DAEEAAR--ILAEKRRQArEQREREEQERLEKEEEERLRKEELRRRAEEERARREE-EARRLEE--ERRREEEERQRKAE 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1248026918 729 AKDLEIRQLELEAQKRLYEKdlttSQEAVAKEiREdtDAHRRKAALEEHMFQKLLEnsqmggrRAQRWKEAEE 801
Cdd:pfam05672 83 EEAEEREQREQEEQERLQKQ----KEEAEAKA-RE--EAERQRQEREKIMQQEEQE-------RLERKKRIEE 141
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
611-811 |
2.07e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 611 RNDELDFLRERqtVENMQAEVDEQRAKDEAwyQKQELLRRAEETRReiLLQEEEKMAQQRQRLAAVKRELE--IKEIHLQ 688
Cdd:COG4372 71 ARSELEQLEEE--LEELNEQLQAAQAELAQ--AQEELESLQEEAEE--LQEELEELQKERQDLEQQRKQLEaqIAELQSE 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 689 DAARRRLLKlqqdQREMELRRLEDEIERkVQMRDQEIAATAKDLEIRQLELEAQKRLYEKDLTTSQEAVAKEIREDTDAH 768
Cdd:COG4372 145 IAEREEELK----ELEEQLESLQEELAA-LEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEE 219
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1248026918 769 RRKAALEEHMFQKLLENSQMGGRRAQRWKEAEEKEFHLQSAKK 811
Cdd:COG4372 220 LLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEE 262
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
603-775 |
2.62e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.06 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 603 QTREWERIRND---ELDFLR-ERQTVENMQAEVDEQRAK-----DEAWYQKQELLRRAEETRREI--LLQEEEKMAQQRQ 671
Cdd:TIGR02169 813 RLREIEQKLNRltlEKEYLEkEIQELQEQRIDLKEQIKSiekeiENLNGKKEELEEELEELEAALrdLESRLGDLKKERD 892
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 672 RLAAVKRELEIK--EIHLQDAARRRLLKLQQDQREM---ELRRLEDEI------------ERKVQMRDQEIAATAKDLE- 733
Cdd:TIGR02169 893 ELEAQLRELERKieELEAQIEKKRKRLSELKAKLEAleeELSEIEDPKgedeeipeeelsLEDVQAELQRVEEEIRALEp 972
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1248026918 734 -----IRQLElEAQKRLyeKDLTTSQEAVAKEIR------EDTDAHRRKAALE 775
Cdd:TIGR02169 973 vnmlaIQEYE-EVLKRL--DELKEKRAKLEEERKaileriEEYEKKKREVFME 1022
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
612-755 |
2.77e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 44.47 E-value: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 612 NDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAavKRELEIKEIHLQDAA 691
Cdd:pfam02029 211 NGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEQKLEELRRRRQEKESEEFEKLRQKQQ--EAELELEELKKKREE 288
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1248026918 692 RRRLLKLQQDQREME--LRRLEDEIERKvQMRDqeiaatakDLEIRQLElEAQKRLYEKDLTTSQE 755
Cdd:pfam02029 289 RRKLLEEEEQRRKQEeaERKLREEEEKR-RMKE--------EIERRRAE-AAEKRQKLPEDSSSEG 344
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
617-725 |
2.82e-04 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 43.82 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 617 FLRERQTVENM-----QAEVDEQRAKdEAWYQKQELLRRAEETRREILLQEEEKMAQQRQR----LAAVKRELEIKEIHL 687
Cdd:pfam02841 181 FLQSKEAVEEAilqtdQALTAKEKAI-EAERAKAEAAEAEQELLREKQKEEEQMMEAQERSyqehVKQLIEKMEAEREQL 259
|
90 100 110
....*....|....*....|....*....|....*...
gi 1248026918 688 QDAARRRLLKLQQDQREMelrrLEDEIERKVQMRDQEI 725
Cdd:pfam02841 260 LAEQERMLEHKLQEQEEL----LKEGFKTEAESLQKEI 293
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
612-756 |
2.88e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 612 NDELDFLRER-QTVENMQAEVDEQRAKDEAWYQK-QELLRRAEETRREI------------LLQEEEKMAQQRQRL---- 673
Cdd:COG3206 211 SEEAKLLLQQlSELESQLAEARAELAEAEARLAAlRAQLGSGPDALPELlqspviqqlraqLAELEAELAELSARYtpnh 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 674 ---AAVKRELEIKEIHLQDAARRRLLKLQQD-----QREMELRRLEDEIERKVQmrdqEIAATAKDLEIRQLELEAQKRL 745
Cdd:COG3206 291 pdvIALRAQIAALRAQLQQEAQRILASLEAElealqAREASLQAQLAQLEARLA----ELPELEAELRRLEREVEVAREL 366
|
170
....*....|.
gi 1248026918 746 YEKDLTTSQEA 756
Cdd:COG3206 367 YESLLQRLEEA 377
|
|
| Pinin_SDK_memA |
pfam04696 |
pinin/SDK/memA/ protein conserved region; Members of this family have very varied ... |
634-724 |
3.07e-04 |
|
pinin/SDK/memA/ protein conserved region; Members of this family have very varied localizations within the eukaryotic cell. pinin is known to localize at the desmosomes and is implicated in anchoring intermediate filaments to the desmosomal plaque. SDK2/3 is a dynamically localized nuclear protein thought to be involved in modulation of alternative pre-mRNA splicing. memA is a tumour marker preferentially expressed in human melanoma cell lines. A common feature of the members of this family is that they may all participate in regulating protein-protein interactions.
Pssm-ID: 461396 [Multi-domain] Cd Length: 130 Bit Score: 41.51 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 634 QRAKDEAWYQKQELLRRAEETRREillqeEEKMAQQRQRLAAVKREleikeihlqdaaRRRLLKLQQDQREMELRRLEDE 713
Cdd:pfam04696 19 QKFKKEESKQKEKEERRAEIEKRL-----EEKAKQEKEELEERKRE------------EREELFEERRAEQIELRALEEK 81
|
90
....*....|.
gi 1248026918 714 IERKVQMRDQE 724
Cdd:pfam04696 82 LELKELMETWH 92
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
608-812 |
3.11e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 3.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 608 ERIRNDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREillQEEEKMAQQrqrlaAVKRELEIKEIHL 687
Cdd:PTZ00121 1288 EKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKK---AEEAKKAAE-----AAKAEAEAAADEA 1359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 688 QDAARRrllKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEKDLTTSQEAVAKEIREDTDA 767
Cdd:PTZ00121 1360 EAAEEK---AEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEA 1436
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1248026918 768 hRRKAalEEhmfqkllensqmgGRRAQRWKE-AEEKEFHLQSAKKA 812
Cdd:PTZ00121 1437 -KKKA--EE-------------AKKADEAKKkAEEAKKAEEAKKKA 1466
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
659-754 |
3.16e-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: 43.98 E-value: 3.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 659 LLQEEEKMAQQRQRLAAVKRELEIKEIHLQDAARRRLLKLQQ----DQREMELRRLEDEIERKVQMRDQEIAATAKDLEI 734
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQlaalERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100
....*....|....*....|
gi 1248026918 735 RQLELEAQKRLYEKDLTTSQ 754
Cdd:COG4942 95 LRAELEAQKEELAELLRALY 114
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
608-750 |
3.36e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.37 E-value: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 608 ERIRNDELDFLRERQTVENMQAEVDEQRAKDEawyQKQELLRRAEEtrREILLQEEEKMAQQRQRLAavKRELEIKEIHl 687
Cdd:COG1579 48 EAAKTELEDLEKEIKRLELEIEEVEARIKKYE---EQLGNVRNNKE--YEALQKEIESLKRRISDLE--DEILELMERI- 119
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1248026918 688 qDAARRRLLKLQQdqremELRRLEDEIERKVQMRDQEIAATAKDLEirqlELEAQKRLYEKDL 750
Cdd:COG1579 120 -EELEEELAELEA-----ELAELEAELEEKKAELDEELAELEAELE----ELEAEREELAAKI 172
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
615-787 |
3.66e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.24 E-value: 3.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 615 LDFLRERqtVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREI---------LLQEEEKMAQQRQRLAAVKRELEIKEI 685
Cdd:COG3206 177 LEFLEEQ--LPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLqqlselesqLAEARAELAEAEARLAALRAQLGSGPD 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 686 HLQDAA--------RRRLLKLQQDQREM---------ELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEK 748
Cdd:COG3206 255 ALPELLqspviqqlRAQLAELEAELAELsarytpnhpDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQA 334
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1248026918 749 DLTTSQEAVAK--EIREDTDAHRRKAALEEHMFQKLLENSQ 787
Cdd:COG3206 335 QLAQLEARLAElpELEAELRRLEREVEVARELYESLLQRLE 375
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
608-815 |
4.14e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 4.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 608 ERIRNDELDFLRER-QTVENMQAEVDEQRAKDEAWYQKQELLRRAEEtRREILLQEEEKMAQQRQRLAAVKRELEIKEIH 686
Cdd:COG4717 49 ERLEKEADELFKPQgRKPELNLKELKELEEELKEAEEKEEEYAELQE-ELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 687 LQDAARRRLLKLQQDQREMELRRLEDEIERKVQMRDQeiaatakdleIRQLELEAQK------RLYEKDLTTSQEAVAKE 760
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEERLEELRELEEE----------LEELEAELAElqeeleELLEQLSLATEEELQDL 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1248026918 761 IREDTDAHRRKAALEEHmfqkLLENSQMGGRRAQRWKEAEEKEFHLQSAKKASAL 815
Cdd:COG4717 198 AEELEELQQRLAELEEE----LEEAQEELEELEEELEQLENELEAAALEERLKEA 248
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
632-809 |
4.15e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.16 E-value: 4.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 632 DEQRAKDEAWYQKQELLRRAE---------------------ETRREILLQEEEKMAQQRQRLAAVKRELEIKEIHLQDA 690
Cdd:COG1196 555 DDEVAAAAIEYLKAAKAGRATflpldkiraraalaaalargaIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEA 634
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 691 ARRRLLKLQQDQREMELRRlEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEKDLTTSQEAVAKEIREDTDAHRR 770
Cdd:COG1196 635 ALRRAVTLAGRLREVTLEG-EGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAE 713
|
170 180 190
....*....|....*....|....*....|....*....
gi 1248026918 771 KAALEEHMFQKLLENSQMGGRRAQRWKEAEEKEFHLQSA 809
Cdd:COG1196 714 EERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEA 752
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
693-812 |
4.30e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.99 E-value: 4.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 693 RRLLKLQQ-DQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLE---LEAQKRLYEKDLTTSQEAVA---------- 758
Cdd:COG1579 7 RALLDLQElDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTEledLEKEIKRLELEIEEVEARIKkyeeqlgnvr 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 759 --KEI----REDTDAHRRKAALEEHMFQKLLENSQMGGRRAQRWKEAEEKEFHLQSAKKA 812
Cdd:COG1579 87 nnKEYealqKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAE 146
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
611-843 |
4.92e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 43.87 E-value: 4.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 611 RNDELDFLRE-RQTVENMQAEVDEQRAKDEAwyQKQELLRRAEETRREI---LLQEEEKMAQQRQRLAAVKRELEI-KEI 685
Cdd:COG3064 43 RLAELEAKRQaEEEAREAKAEAEQRAAELAA--EAAKKLAEAEKAAAEAekkAAAEKAKAAKEAEAAAAAEKAAAAaEKE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 686 HLQDAARR--RLLKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEKDLTTSQEAVAKEIRE 763
Cdd:COG3064 121 KAEEAKRKaeEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAA 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 764 DTDAHRRKAALEEHMFQKLLENSQMGGRRAQRWKEAEEKEFHLQSAKKASALSDASRKWFLRQETSAALEHEEMPWLQRQ 843
Cdd:COG3064 201 AALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVV 280
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
30-71 |
5.08e-04 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 43.36 E-value: 5.08e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1248026918 30 TKELVSWMRGHESSVCSISVHASGRYAITTSSD-TAQLWDLDT 71
Cdd:COG2319 361 TGELLRTLTGHTGAVTSVAFSPDGRTLASGSADgTVRLWDLAT 403
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
606-811 |
5.23e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 43.73 E-value: 5.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 606 EWERIRND----------ELDFLRERQTvENMQAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEE------------ 663
Cdd:pfam07888 70 QWERQRRElesrvaelkeELRQSREKHE-ELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEdiktltqrvler 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 664 -----------EKMAQQRQRLAAVKRELEIKEIHLQDAARRRLLKLQ-----QDQREMELRRLEDEIERKVQMRDQeiaA 727
Cdd:pfam07888 149 etelermkeraKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQelrnsLAQRDTQVLQLQDTITTLTQKLTT---A 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 728 TAKDLEIRQleLEAQKRLYEKDLTTSQEAVA--KEIREDTDAHRRKAALEEHmfQKLLENSQMGGRRAQ---RWKE---- 798
Cdd:pfam07888 226 HRKEAENEA--LLEELRSLQERLNASERKVEglGEELSSMAAQRDRTQAELH--QARLQAAQLTLQLADaslALREgrar 301
|
250
....*....|....
gi 1248026918 799 -AEEKEFHLQSAKK 811
Cdd:pfam07888 302 wAQERETLQQSAEA 315
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
603-811 |
5.81e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 5.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 603 QTREWERIRNDEldflrERQTVENMQAEVDEQRAKDE----AWYQKQELLRRAEETRREILLQEEEK-MAQQRQRLAAVK 677
Cdd:PTZ00121 1216 EARKAEDAKKAE-----AVKKAEEAKKDAEEAKKAEEernnEEIRKFEEARMAHFARRQAAIKAEEArKADELKKAEEKK 1290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 678 RELEIKEIHLQDAARRRLLKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEKDLTTSQEAV 757
Cdd:PTZ00121 1291 KADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAE 1370
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1248026918 758 AK--EIREDTDAHRRKAAlEEHMFQKLLENSQMGGRRAQRWKEAEEKEFHLQSAKK 811
Cdd:PTZ00121 1371 KKkeEAKKKADAAKKKAE-EKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKK 1425
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
599-744 |
6.02e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.77 E-value: 6.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 599 IVDYQTREWERIRNDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEEKmAQQRQRLAAVKR 678
Cdd:COG1196 623 LGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLA-EEELELEEALLA 701
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1248026918 679 ELEIKEIHLQDAARRRLLKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKR 744
Cdd:COG1196 702 EEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELER 767
|
|
| DUF4200 |
pfam13863 |
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ... |
655-748 |
6.11e-04 |
|
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.
Pssm-ID: 464003 [Multi-domain] Cd Length: 119 Bit Score: 40.24 E-value: 6.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 655 RREI-LLQEE-----EKMAQQRQRLAAVKRELEIKEIHLQDAARR--RLLKLQQDQREMELRRLEDEIERKVQmRDQEIA 726
Cdd:pfam13863 5 KREMfLVQLAldakrEEIERLEELLKQREEELEKKEQELKEDLIKfdKFLKENDAKRRRALKKAEEETKLKKE-KEKEIK 83
|
90 100
....*....|....*....|..
gi 1248026918 727 ATAKDLEIRQLELEAQKRLYEK 748
Cdd:pfam13863 84 KLTAQIEELKSEISKLEEKLEE 105
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
612-836 |
6.43e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.49 E-value: 6.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 612 NDELDFLRER-QTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREILlqeEEKMAQQRQRLAAVKRELEIKEIHLQDA 690
Cdd:PRK02224 341 NEEAESLREDaDDLEERAEELREEAAELESELEEAREAVEDRREEIEEL---EEEIEELRERFGDAPVDLGNAEDFLEEL 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 691 ARRR-LLKLQQDQREMELRRLEDEIERKVQMR-------------DQEIAATAKD-------LEIRQLELEAQKRLYEKD 749
Cdd:PRK02224 418 REERdELREREAELEATLRTARERVEEAEALLeagkcpecgqpveGSPHVETIEEdrerveeLEAELEDLEEEVEEVEER 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 750 LTTSQEAVAKEIREDTDAHRRKAALEehmfqkllensqmggRRAQRWKEAEEKEFHLQSAKK-ASALSDASRKWflrqET 828
Cdd:PRK02224 498 LERAEDLVEAEDRIERLEERREDLEE---------------LIAERRETIEEKRERAEELRErAAELEAEAEEK----RE 558
|
....*...
gi 1248026918 829 SAALEHEE 836
Cdd:PRK02224 559 AAAEAEEE 566
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
667-821 |
6.52e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 42.91 E-value: 6.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 667 AQQRQRLAAVKRELEIKEIHLQDAARRRLLKLQQDQR--EMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKR 744
Cdd:TIGR02794 49 AQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAaeQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQ 128
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1248026918 745 lyEKDLTTSQEAVAkEIREDTDAhRRKAALEehmfqKLLEnsqmggRRAQRWKEAEEKEFHLQSAKKASALSDASRK 821
Cdd:TIGR02794 129 --AAEAKAKAEAEA-ERKAKEEA-AKQAEEE-----AKAK------AAAEAKKKAEEAKKKAEAEAKAKAEAEAKAK 190
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
611-744 |
6.64e-04 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 43.48 E-value: 6.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 611 RNDELDFLRER-----QTVENMQAEVDE-----QRAKDEAWYQKQELLRRAEETRR-----EILLQEEEKMAQ-QR---- 670
Cdd:pfam05667 333 REEELEELQEQledleSSIQELEKEIKKlessiKQVEEELEELKEQNEELEKQYKVkkktlDLLPDAEENIAKlQAlvda 412
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1248026918 671 --QRLAAVKRELEIKEIHLQDAARRrlLKLQQDQREMELRRLEDEIER-KVQMRDQEIAATAKDLEIRQLELEAQKR 744
Cdd:pfam05667 413 saQRLVELAGQWEKHRVPLIEEYRA--LKEAKSNKEDESQRKLEEIKElREKIKEVAEEAKQKEELYKQLVAEYERL 487
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
604-820 |
7.39e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 43.66 E-value: 7.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 604 TREWERIRNDELdflrERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREI------LLQEEEKMAQQRQ------ 671
Cdd:NF041483 501 TAESERVRTEAI----ERATTLRRQAEETLERTRAEAERLRAEAEEQAEEVRAAAeraareLREETERAIAARQaeaaee 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 672 ----------RLAAVKREL----------------EIKEIHLQDAARRRLLklqQDQREMELRRLEDEIERKVQMRDQEI 725
Cdd:NF041483 577 ltrlhteaeeRLTAAEEALadaraeaerirreaaeETERLRTEAAERIRTL---QAQAEQEAERLRTEAAADASAARAEG 653
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 726 AATAKDL------EIRQLELEAQKrlyEKDLTTSQEAVAKEiREDTDAHRRKAALEEHMFQKLLENSQ-MGGRRA----Q 794
Cdd:NF041483 654 ENVAVRLrseaaaEAERLKSEAQE---SADRVRAEAAAAAE-RVGTEAAEALAAAQEEAARRRREAEEtLGSARAeadqE 729
|
250 260
....*....|....*....|....*...
gi 1248026918 795 RWKEAEEKEFHLQSAKK--ASALSDASR 820
Cdd:NF041483 730 RERAREQSEELLASARKrvEEAQAEAQR 757
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
608-747 |
8.50e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 42.60 E-value: 8.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 608 ERIRN--DELDFLRERQTVENMQAEvDEQRAKDEAwYQKQELLRRAEETRREILLQEEEKMAQQRQR-----LAAVKREL 680
Cdd:pfam13868 194 EKAQDekAERDELRAKLYQEEQERK-ERQKEREEA-EKKARQRQELQQAREEQIELKERRLAEEAEReeeefERMLRKQA 271
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 681 EIKEIHLQDAARRRL--LKLQQD-QREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYE 747
Cdd:pfam13868 272 EDEEIEQEEAEKRRMkrLEHRRElEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKKLKE 341
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
608-810 |
8.74e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 8.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 608 ERIRNDELDF---LRERQTVENMQAEVDEQRAKDEAWYQKQELLR-RAEETRREILLQE------EEKMAQQRQRLAAVK 677
Cdd:PRK03918 193 ELIKEKEKELeevLREINEISSELPELREELEKLEKEVKELEELKeEIEELEKELESLEgskrklEEKIRELEERIEELK 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 678 REL--------EIKEIHLQDAARRRLLKLQQDQREmELRRLEDEIER------KVQMRDQEIAATAKDL-EIRQLELEAQ 742
Cdd:PRK03918 273 KEIeeleekvkELKELKEKAEEYIKLSEFYEEYLD-ELREIEKRLSRleeeinGIEERIKELEEKEERLeELKKKLKELE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 743 KRL--YEKDLTTSQEAVAKE------------------IREDTDAHRRKAALEEHMFQKLLENSQMGGRRAQRWKEAEEk 802
Cdd:PRK03918 352 KRLeeLEERHELYEEAKAKKeelerlkkrltgltpeklEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEE- 430
|
....*...
gi 1248026918 803 efhLQSAK 810
Cdd:PRK03918 431 ---LKKAK 435
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
31-68 |
8.89e-04 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 37.71 E-value: 8.89e-04
10 20 30
....*....|....*....|....*....|....*....
gi 1248026918 31 KELVSWMRGHESSVCSISVHASGRYAITTSSD-TAQLWD 68
Cdd:pfam00400 1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDgTVKVWD 39
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
612-749 |
8.95e-04 |
|
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: 43.29 E-value: 8.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 612 NDELDFlrerQTVENMQAEVDEQ-----------RAKDEAWYQKQELLRRAEETRREILL--QEEEKMAQQRQRLAAVKR 678
Cdd:pfam12128 190 SKEGKF----RDVKSMIVAILEDdgvvppksrlnRQQVEHWIRDIQAIAGIMKIRPEFTKlqQEFNTLESAELRLSHLHF 265
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1248026918 679 EleIKEIHLQDAARRRLLKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEA---QKRLYEKD 749
Cdd:pfam12128 266 G--YKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEAledQHGAFLDA 337
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
613-835 |
9.51e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 9.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 613 DELDFLR-ERQTVENMQAEVDEQR-----AKDEAwyqkQELLRRAEETRREILLQEEEkMAQQRQRLAAVKREleikeih 686
Cdd:PRK02224 206 ERLNGLEsELAELDEEIERYEEQReqareTRDEA----DEVLEEHEERREELETLEAE-IEDLRETIAETERE------- 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 687 lQDAARRRLlklqQDQREmELRRLEDEIERKVQMRDQEiAATAKDLEIRQLELEAQKRLYEKDLTTSQEAvAKEIREDTD 766
Cdd:PRK02224 274 -REELAEEV----RDLRE-RLEELEEERDDLLAEAGLD-DADAEAVEARREELEDRDEELRDRLEECRVA-AQAHNEEAE 345
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1248026918 767 AHRRKAA-LEEhmfqkllensqmggrRAQRWKE-AEEKEFHLQSAKkaSALSDasrkwflRQETSAALEHE 835
Cdd:PRK02224 346 SLREDADdLEE---------------RAEELREeAAELESELEEAR--EAVED-------RREEIEELEEE 392
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
619-837 |
9.53e-04 |
|
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: 43.12 E-value: 9.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 619 RERQTVENMQAEVDEQRAKdEAWYQKQELLRRAEETRReiLLQEEEKMAQQRQRLAAVKRELEIK--EIHLQDA-ARRRL 695
Cdd:TIGR02168 207 RQAEKAERYKELKAELREL-ELALLVLRLEELREELEE--LQEELKEAEEELEELTAELQELEEKleELRLEVSeLEEEI 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 696 LKLQQDQREM--ELRRLEDEIERKVQmRDQEIAATAKDLEIRQLELEAQKRLYEKDLTTSQE--AVAKEIREDTdahrrK 771
Cdd:TIGR02168 284 EELQKELYALanEISRLEQQKQILRE-RLANLERQLEELEAQLEELESKLDELAEELAELEEklEELKEELESL-----E 357
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1248026918 772 AALEEhmFQKLLENSqmggrrAQRWKEAEEkefHLQSAKKASALsdasrkwFLRQETSAALEHEEM 837
Cdd:TIGR02168 358 AELEE--LEAELEEL------ESRLEELEE---QLETLRSKVAQ-------LELQIASLNNEIERL 405
|
|
| Nop53 |
pfam07767 |
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ... |
629-748 |
9.69e-04 |
|
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ribosomal biogenesis. They are specifically involved in the processing beyond the 27S stage of 25S rRNA maturation. This family contains sequences that bear similarity to the glioma tumour suppressor candidate region gene 2 protein (p60). This protein has been found to interact with herpes simplex type 1 regulatory proteins.
Pssm-ID: 462259 [Multi-domain] Cd Length: 353 Bit Score: 42.28 E-value: 9.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 629 AEVDEQRAKDEAwyQKQELLRRAEETRREILLQEEEKMAQQrQRLAAVKRELEIKEihlqdAARRRLLKLQQDQremeLR 708
Cdd:pfam07767 205 VEAEKKRLKEEE--KLERVLEKIAESAATAEAREEKRKTKA-QRNKEKRRKEEERE-----AKEEKALKKKLAQ----LE 272
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1248026918 709 RLEdEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEK 748
Cdd:pfam07767 273 RLK-EIAKEIAEKEKEREEKAEARKREKRKKKKEEKKLRP 311
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
617-794 |
1.01e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 42.77 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 617 FLRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREillqeeekMAQQRQRLAAVKRELEIKEihlqdaarRRLL 696
Cdd:PRK12705 24 LLKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRE--------RNQQRQEARREREELQREE--------ERLV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 697 KL--QQDQREMELRRLEDEIERkvqmRDQEIAATAKDLEIRQLELEAqkRLYEKDLTTSQEAVAKEIRE-DTDAHRRKAA 773
Cdd:PRK12705 88 QKeeQLDARAEKLDNLENQLEE----REKALSARELELEELEKQLDN--ELYRVAGLTPEQARKLLLKLlDAELEEEKAQ 161
|
170 180
....*....|....*....|.
gi 1248026918 774 LEEHMFQKLLENSQmggRRAQ 794
Cdd:PRK12705 162 RVKKIEEEADLEAE---RKAQ 179
|
|
| DegS |
pfam05384 |
Sensor protein DegS; This is small family of Bacillus DegS proteins. The DegS-DegU ... |
623-718 |
1.30e-03 |
|
Sensor protein DegS; This is small family of Bacillus DegS proteins. The DegS-DegU two-component regulatory system of Bacillus subtilis controls various processes that characterize the transition from the exponential to the stationary growth phase, including the induction of extracellular degradative enzymes, expression of late competence genes and down-regulation of the sigma D regulon. The family also contains one sequence Swiss:Q8R9D3 from Thermoanaerobacter tengcongensis which are described as sensory transduction histidine kinases.
Pssm-ID: 428449 [Multi-domain] Cd Length: 159 Bit Score: 40.16 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 623 TVENMQAEVDE--QRAKDEAWYQKQELlrraEETRREIL--------LQEEEKMAqqRQRLAAVKR------ELEIKEIH 686
Cdd:pfam05384 10 TIENSKEEIFEiaENARQEYERLKQEL----EELKEEVSetikevdkLEKKERRA--RQRLMEVSRdfnrysEEDIKEAY 83
|
90 100 110
....*....|....*....|....*....|...
gi 1248026918 687 LQ-DAARRRLLKLQQdqREMELRRLEDEIERKV 718
Cdd:pfam05384 84 EEaKDLQVELALLRE--REKQLRERRDELERRL 114
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
652-831 |
1.32e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 42.16 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 652 EETRREILLQEEEKMAQQRQRLAAVKRELEIKEIHlQDAARRRLLKLQQDQREMELRrLEdEIERKVQMRDqeiaatakd 731
Cdd:pfam02029 223 TKRRQGGLSQSQEREEEAEVFLEAEQKLEELRRRR-QEKESEEFEKLRQKQQEAELE-LE-ELKKKREERR--------- 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 732 leiRQLELEAQKRlyekdlttSQEAVAKEIREDTDAHRRKAALE-------EHMfQKLLENSQMGGR--------RAQRW 796
Cdd:pfam02029 291 ---KLLEEEEQRR--------KQEEAERKLREEEEKRRMKEEIErrraeaaEKR-QKLPEDSSSEGKkpfkcfspKGSSL 358
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1248026918 797 KEAEEKEFHLQSAKKASALSDASRKWF-------LRQETSAA 831
Cdd:pfam02029 359 KITERAEFLNKSLQKSSSVKKTHPPAVvskidsrLEQYTSAI 400
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
622-763 |
1.44e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.15 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 622 QTVENMQAEVDEQRAKDEAwyQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELEiKEIHLQDAARRRL---LKL 698
Cdd:COG2433 376 LSIEEALEELIEKELPEEE--PEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELE-AELEEKDERIERLereLSE 452
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1248026918 699 QQDQREMELRRledeiERKVQMRDQEIAATAKDLE-----IRQLE--LEAQKRLYEKDLttSQEAVA-KEIRE 763
Cdd:COG2433 453 ARSEERREIRK-----DREISRLDREIERLERELEeererIEELKrkLERLKELWKLEH--SGELVPvKVVEK 518
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
618-814 |
1.57e-03 |
|
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: 42.63 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 618 LRERQTVENMQAEVDEQRAKdeawyqkqelLRRAEETRREilLQEEEKMAQQRQRLAavkrELEIKEIHLQDAARRRLLK 697
Cdd:COG3096 343 LRQQEKIERYQEDLEELTER----------LEEQEEVVEE--AAEQLAEAEARLEAA----EEEVDSLKSQLADYQQALD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 698 LQQD---QREMELRRLE--------DEI------ERKVQMRDQEIAATAKDLEIRQ-LEL-EAQKRLYEKDL-------- 750
Cdd:COG3096 407 VQQTraiQYQQAVQALEkaralcglPDLtpenaeDYLAAFRAKEQQATEEVLELEQkLSVaDAARRQFEKAYelvckiag 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1248026918 751 -TTSQEA--VAKEIREDTDAHRRKAALEEHMFQKLLENSQmggrRAQRWKEAEE--KEFHLQSAKKASA 814
Cdd:COG3096 487 eVERSQAwqTARELLRRYRSQQALAQRLQQLRAQLAELEQ----RLRQQQNAERllEEFCQRIGQQLDA 551
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
629-848 |
1.85e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 42.12 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 629 AEVDEQRAKDEAWYQKQELLRRAEETrreillQEEEKMAQQRQRLAAVKRELEIKeihlqdaarrrllklqqDQREMELR 708
Cdd:NF041483 500 ATAESERVRTEAIERATTLRRQAEET------LERTRAEAERLRAEAEEQAEEVR-----------------AAAERAAR 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 709 RLEDEIERKVQMRDQEIAAtakdlEIRQLELEAQKRlyekdLTTSQEAVAkEIREDTDAHRRKAALEEhmfQKLLENSQM 788
Cdd:NF041483 557 ELREETERAIAARQAEAAE-----ELTRLHTEAEER-----LTAAEEALA-DARAEAERIRREAAEET---ERLRTEAAE 622
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 789 GGRRAQRWKEAEEKEFHLQSAKKASALSDASRKWFLRQETSAALEHEEmpwLQRQYMDSA 848
Cdd:NF041483 623 RIRTLQAQAEQEAERLRTEAAADASAARAEGENVAVRLRSEAAAEAER---LKSEAQESA 679
|
|
| G_path_suppress |
pfam15991 |
G-protein pathway suppressor; This family of proteins inhibits G-protein- and ... |
619-705 |
1.99e-03 |
|
G-protein pathway suppressor; This family of proteins inhibits G-protein- and mitogen-activated protein kinase-mediated signal transduction.
Pssm-ID: 464961 [Multi-domain] Cd Length: 272 Bit Score: 41.06 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 619 RERQTVEnMQAEVDEQRAKDEAWYQKQELLRRAEETRREIlLQEEEKMAQQRQRlaavKREL--EIKEIHLQDAARRRLL 696
Cdd:pfam15991 22 RERKKQE-QEAKMEEERLRREREEREKEDRMTLEETKEQI-LKLEKKLADLKEE----KHQLflQLKKVLHEDETRKRQL 95
|
....*....
gi 1248026918 697 KLQQDQREM 705
Cdd:pfam15991 96 KEQSELFAL 104
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
626-841 |
2.30e-03 |
|
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: 41.70 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 626 NMQA-----EVDEQrAKDEAwyqkqellrrAEETRREILLQ----EEEKMAQQRQRLAAVkreleikeihlqdAARRRLl 696
Cdd:pfam01576 721 NMQAlkaqfERDLQ-ARDEQ----------GEEKRRQLVKQvrelEAELEDERKQRAQAV-------------AAKKKL- 775
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 697 klqqdqrEMELRRLEDEIerkvqmrdqEIAATAKDLEIRQL-ELEAQKRLYEKDLTTSQEAVAKEIREDTDAHRRKAALE 775
Cdd:pfam01576 776 -------ELDLKELEAQI---------DAANKGREEAVKQLkKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLE 839
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1248026918 776 EHMFQklLENSQMGGRRAQRWKEAEEKEFHLQ---SAKKASALSDASRkwflRQETSAALEHEEMPWLQ 841
Cdd:pfam01576 840 AELLQ--LQEDLAASERARRQAQQERDELADEiasGASGKSALQDEKR----RLEARIAQLEEELEEEQ 902
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
615-757 |
2.32e-03 |
|
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: 41.86 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 615 LDFLRERQT---VENMQAEVDEQRAKDEAWYQKqelLRRAEETR---REILLQEEEKMAQQRQRLAAVKRELEIKEIHLQ 688
Cdd:COG3096 960 LSEVVQRRPhfsYEDAVGLLGENSDLNEKLRAR---LEQAEEARreaREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQ 1036
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1248026918 689 DAARR-RLLKLQQDQrEMELR-RLE-DEIERKVQMRDQEIAATAKDLEIRQLELE-AQKRL--YEKDLTTSQEAV 757
Cdd:COG3096 1037 ELEQElEELGVQADA-EAEERaRIRrDELHEELSQNRSRRSQLEKQLTRCEAEMDsLQKRLrkAERDYKQEREQV 1110
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
664-819 |
2.60e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 41.53 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 664 EKMAQQRQRLAAVKREL-EIKEIHLQDAARR-RLLKLQQDQREMELRRLEDEIERKvqmrdQEIAATAKDlEIRQLELEA 741
Cdd:pfam05262 184 EALREDNEKGVNFRRDMtDLKERESQEDAKRaQQLKEELDKKQIDADKAQQKADFA-----QDNADKQRD-EVRQKQQEA 257
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1248026918 742 QKRlyEKDLTTSQEAVAKEIREDTDAHRRKAALE-EHMFQKLLENSQMGGRRAQRWKEAEEKEFHLQSAKKASALSDAS 819
Cdd:pfam05262 258 KNL--PKPADTSSPKEDKQVAENQKREIEKAQIEiKKNDEEALKAKDHKAFDLKQESKASEKEAEDKELEAQKKREPVA 334
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
643-823 |
2.80e-03 |
|
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: 41.48 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 643 QKQELLRRAEETRREiLLQEEEKMAQQRQRLAAVKRELEIK---EIHLQ---DAARRRLLKLQQDQREMElrrledeier 716
Cdd:COG3096 279 ERRELSERALELRRE-LFGARRQLAEEQYRLVEMARELEELsarESDLEqdyQAASDHLNLVQTALRQQE---------- 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 717 KVQMRDQEIAATAKDLEIRQLELEA---QKRLYEKDLTTSQEAVaKEIR-------EDTDAHRRKA--------ALEEHm 778
Cdd:COG3096 348 KIERYQEDLEELTERLEEQEEVVEEaaeQLAEAEARLEAAEEEV-DSLKsqladyqQALDVQQTRAiqyqqavqALEKA- 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1248026918 779 fQKLLENSQMGGRRAQRWKE---AEEKEFH--LQSAKKASALSDASRKWF 823
Cdd:COG3096 426 -RALCGLPDLTPENAEDYLAafrAKEQQATeeVLELEQKLSVADAARRQF 474
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
639-787 |
2.84e-03 |
|
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.
Pssm-ID: 464032 [Multi-domain] Cd Length: 221 Bit Score: 40.07 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 639 EAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRE--LEIKEihlQDAARRRLLKLQQDQREMELRRLeDEIER 716
Cdd:pfam13904 58 ENWLAAKQRQRQKELQAQKEEREKEEQEAELRKRLAKEKYQewLQRKA---RQQTKKREESHKQKAAESASKSL-AKPER 133
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1248026918 717 KVQMRdqEIAATAKDLEIRQLELEAQKRLYEKDlttsqeavAKEIREDTDAHRRKAAleEHMFQKLLENSQ 787
Cdd:pfam13904 134 KVSQE--EAKEVLQEWERKKLEQQQRKREEEQR--------EQLKKEEEEQERKQLA--EKAWQKWMKNVK 192
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
610-802 |
2.97e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 41.10 E-value: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 610 IRNDELDFLRERQTVENMQAEVD------EQRA--KDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELE 681
Cdd:COG5185 231 IEEALKGFQDPESELEDLAQTSDkleklvEQNTdlRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKA 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 682 IKEIHLQDAARRRLLKLQQDQRE--MELRRLEDEIERKVqmRDQEIAATAKDLEIRQLELEAQKRLYEKDL---TTSQEA 756
Cdd:COG5185 311 TESLEEQLAAAEAEQELEESKREteTGIQNLTAEIEQGQ--ESLTENLEAIKEEIENIVGEVELSKSSEELdsfKDTIES 388
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1248026918 757 VAKEIREDTDAHRRKA-----ALEEHMFQKLLENSQMGGRRAQRWKEAEEK 802
Cdd:COG5185 389 TKESLDEIPQNQRGYAqeilaTLEDTLKAADRQIEELQRQIEQATSSNEEV 439
|
|
| DUF5384 |
pfam17358 |
Family of unknown function (DUF5384); This is a family of unknown function found in ... |
620-764 |
3.07e-03 |
|
Family of unknown function (DUF5384); This is a family of unknown function found in Proteobacteria.
Pssm-ID: 407453 [Multi-domain] Cd Length: 145 Bit Score: 39.20 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 620 ERQTVENMQAEVDEQR---AKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELEIKEihlqdaarrrll 696
Cdd:pfam17358 12 ERQAAYEREWEEEQARaeaAAAAARRARAAAAAAAAAAAKERAKAEALADKKRDQSYEDELRALEIEE------------ 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 697 klqqdqREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYE--KDLTTSqEAVAKEIRED 764
Cdd:pfam17358 80 ------RKLALAAQKARAKRENDFIDQELKSQAAQTDVIQSEADANRNVSEgtKSLMES-EGKAREKKSS 142
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
645-776 |
3.78e-03 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 39.00 E-value: 3.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 645 QELLRRAEETRREIllqeEEKMAQQRQRLAAVKRELEikEIhlQDAARRRLLKLQQDQREmelrRLEDEIERKVQMRDQE 724
Cdd:COG0711 37 ADGLAEAERAKEEA----EAALAEYEEKLAEARAEAA--EI--IAEARKEAEAIAEEAKA----EAEAEAERIIAQAEAE 104
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1248026918 725 IAAtAKDLEIRQLELEAQkrlyekdlTTSQEAVAKEIREDTDAHRRKAALEE 776
Cdd:COG0711 105 IEQ-ERAKALAELRAEVA--------DLAVAIAEKILGKELDAAAQAALVDR 147
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
608-711 |
4.52e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 40.62 E-value: 4.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 608 ERIRndeldflRERQTVENMQAEVDEQRaKDEAWYQKQELLRRAEEtRREILLQEEEKMAQQRQrLAAVKRELEikeihl 687
Cdd:pfam02029 251 EELR-------RRRQEKESEEFEKLRQK-QQEAELELEELKKKREE-RRKLLEEEEQRRKQEEA-ERKLREEEE------ 314
|
90 100
....*....|....*....|....
gi 1248026918 688 qdaaRRRLlklqqdQREMELRRLE 711
Cdd:pfam02029 315 ----KRRM------KEEIERRRAE 328
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
618-737 |
5.02e-03 |
|
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: 40.71 E-value: 5.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 618 LRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREILLQE-----EEKMA--QQRQRLAAVKRELEIKE---IHL 687
Cdd:COG3096 528 LRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQaaeavEQRSElrQQLEQLRARIKELAARApawLAA 607
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1248026918 688 QDAARR-------RLLKLQQ--DQREMELRRledeiERKVQMRDQEIAATAKDLE--IRQL 737
Cdd:COG3096 608 QDALERlreqsgeALADSQEvtAAMQQLLER-----EREATVERDELAARKQALEsqIERL 663
|
|
| PRK03963 |
PRK03963 |
V-type ATP synthase subunit E; Provisional |
645-764 |
5.15e-03 |
|
V-type ATP synthase subunit E; Provisional
Pssm-ID: 167649 [Multi-domain] Cd Length: 198 Bit Score: 39.35 E-value: 5.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 645 QELLRRAEETRREIlLQEEEKMAQQrqrlaavkreleIKEihlqdAARRRllklQQDQREMELRRLEDEIErkvqMRDQE 724
Cdd:PRK03963 9 QEINREAEQKIEYI-LEEAQKEAEK------------IKE-----EARKR----AESKAEWILRKAKTQAE----LEKQR 62
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1248026918 725 IAATAKdLEIRQLELEAQKRLYEKDLTTSQEAVAkEIRED 764
Cdd:PRK03963 63 IIANAK-LEVRRKRLAVQEELISEVLEAVRERLA-ELPED 100
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
632-776 |
5.29e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 5.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 632 DEQRAKDEAWY-------QKQELLRRAEETRREIllqeeEKMAQQRQRLAAVKRELEIKEIHLQDAARRRLLKLQQDQRE 704
Cdd:COG4913 593 DDRRRIRSRYVlgfdnraKLAALEAELAELEEEL-----AEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAE 667
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1248026918 705 MELRRLEDEIERkvqmrdqeIAATAKDLEirqlELEAQKRLYEKDLTTSQEAVAKEIREDTDAHRRKAALEE 776
Cdd:COG4913 668 REIAELEAELER--------LDASSDDLA----ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEE 727
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
605-776 |
5.30e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.27 E-value: 5.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 605 REWERIRNDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELEIKE 684
Cdd:COG4372 101 EELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 685 I-----HLQDAARRRLLKLQQDqrEMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEKDLTTSQEAVAK 759
Cdd:COG4372 181 AeqaldELLKEANRNAEKEEEL--AEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILK 258
|
170
....*....|....*..
gi 1248026918 760 EIREDTDAHRRKAALEE 776
Cdd:COG4372 259 EIEELELAILVEKDTEE 275
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
557-684 |
5.94e-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: 40.13 E-value: 5.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 557 VIREVYHLMETTPADI--HPNSMLDAFVALTKGQYpiFNQYPKFIVDYQTREWERIRNDELDFLRERQTVENMQAEVDEQ 634
Cdd:COG4942 109 LLRALYRLGRQPPLALllSPEDFLDAVRRLQYLKY--LAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEE 186
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1248026918 635 RAKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELEIKE 684
Cdd:COG4942 187 RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| DUF3375 |
pfam11855 |
Protein of unknown function (DUF3375); This family of proteins are functionally ... |
558-788 |
6.40e-03 |
|
Protein of unknown function (DUF3375); This family of proteins are functionally uncharacterized. This protein is found in bacteria. Proteins in this family are typically between 479 to 499 amino acids in length.
Pssm-ID: 463373 Cd Length: 469 Bit Score: 39.93 E-value: 6.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 558 IREVYHLMETTPADIHpnSMLDAFVALTKGqypifnqypkfIVDyQTREWERIRNDELDF-LRERQTVenmqAEVDEQRA 636
Cdd:pfam11855 174 AREILQLARELPADFR--RVEDEFRQLDRE-----------LRE-RIIDWDGSRGEVLEElFDGYDAL----ADSDQGRS 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 637 KDEAWyqkqELLRRAEETR------REILLQEEEKM--AQQRQRLAAVKREL--EIKEIH--LQDAAR--RRLLKLQQDQ 702
Cdd:pfam11855 236 FEAFW----DLLMDPERQAeldellDTVLSRPFARGldADQRRFLRRLHRDLleAGEEVQrtRRRLSRslRRFVRSQAFL 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 703 REMELRRLEDEIERK-VQMRDQEIAATAKDLEI----RQLELEAQKRLY---EKDLTTSQEAVAKEIREDTDAHRR---- 770
Cdd:pfam11855 312 EDRRVDRLLREAEALaLALRDAPPADRRTGLELpltaPDIASPSERRLHdppALPVVDAPADDAGAGELDLEDLRAlggq 391
|
250 260
....*....|....*....|..
gi 1248026918 771 ----KAALEEHMFQKLLENSQM 788
Cdd:pfam11855 392 sevdRAELTEAVRAALAERGQV 413
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
633-706 |
6.46e-03 |
|
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: 40.54 E-value: 6.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 633 EQRAKDEAwyQKQELLRRAEETRREILLQ--EEEKMAQQRQ--------RLAAVKRELEIKEIHLQ--DAARRRLlklqq 700
Cdd:pfam01576 984 EQESRERQ--AANKLVRRTEKKLKEVLLQveDERRHADQYKdqaekgnsRMKQLKRQLEEAEEEASraNAARRKL----- 1056
|
....*.
gi 1248026918 701 dQREME 706
Cdd:pfam01576 1057 -QRELD 1061
|
|
| PRK02292 |
PRK02292 |
V-type ATP synthase subunit E; Provisional |
663-801 |
6.75e-03 |
|
V-type ATP synthase subunit E; Provisional
Pssm-ID: 235026 [Multi-domain] Cd Length: 188 Bit Score: 38.83 E-value: 6.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 663 EEKMAQQRQRLAAVKRELEIKEIHLQDAARRRllklQQDQREMELRRLEDEIErkvQMRDQEIAaTAKdLEIRQLELEAQ 742
Cdd:PRK02292 8 EDIRDEARARASEIRAEADEEAEEIIAEAEAD----AEEILEDREAEAEREIE---QLREQELS-SAK-LEAKRERLNAR 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1248026918 743 KRLYEKdlttSQEAVAKEIReDTDAHRRKAALEehmfqKLLENSQMGGRRAQRWKEAEE 801
Cdd:PRK02292 79 KEVLED----VRNQVEDEIA-SLDGDKREELTK-----SLLDAADADGVRVYSRKDDED 127
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
653-843 |
7.02e-03 |
|
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: 40.34 E-value: 7.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 653 ETRREILLQEEEKMAQQRQRLAAVKRELEIKEIHLQdaaRRRLLKlQQDQREMELRRLEDEIERKVQMRDQE-----IAA 727
Cdd:TIGR00618 222 QVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLK---KQQLLK-QLRARIEELRAQEAVLEETQERINRArkaapLAA 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 728 TAKDL-EIRQ------LELEAQKRLYEKDLTTSQEAVAKE--IREDTDAHRRKAALEEHMFQkllENSQMGGRRAQRWKE 798
Cdd:TIGR00618 298 HIKAVtQIEQqaqrihTELQSKMRSRAKLLMKRAAHVKQQssIEEQRRLLQTLHSQEIHIRD---AHEVATSIREISCQQ 374
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1248026918 799 AEEKEFHLQSAKKASALSDASRKWFLRQETSAALEHEEMPWLQRQ 843
Cdd:TIGR00618 375 HTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAF 419
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
605-833 |
7.26e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 7.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 605 REWERIRNDELDFLRERQTVENMQaEVDEQRAK------DEAWYQKQELLRRAEETRREI--LLQEEEKMAQQRQRLAAV 676
Cdd:PRK03918 483 RELEKVLKKESELIKLKELAEQLK-ELEEKLKKynleelEKKAEEYEKLKEKLIKLKGEIksLKKELEKLEELKKKLAEL 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 677 KREL-----EIKEIHLQ---------DAARRRLLKLQQDQREM--------ELRRLEDEI---ERKVQMRDQEIAATAKD 731
Cdd:PRK03918 562 EKKLdeleeELAELLKEleelgfesvEELEERLKELEPFYNEYlelkdaekELEREEKELkklEEELDKAFEELAETEKR 641
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 732 LEIRQLELEAQKRLYEKDlttSQEAVAKEIREDTDAHRRKAA----LEEHM--FQKLLENSQmggrraQRWKEAEEKEFH 805
Cdd:PRK03918 642 LEELRKELEELEKKYSEE---EYEELREEYLELSRELAGLRAeleeLEKRReeIKKTLEKLK------EELEEREKAKKE 712
|
250 260
....*....|....*....|....*...
gi 1248026918 806 LQSAKKASALSDASRKWFLRQETSAALE 833
Cdd:PRK03918 713 LEKLEKALERVEELREKVKKYKALLKER 740
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
601-757 |
8.46e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.94 E-value: 8.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 601 DYQTRE--WERIRN--DELDFLRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREI---LLQEEEKMAQQRQRL 673
Cdd:PRK04863 943 DYQQAQqtQRDAKQqaFALTEVVQRRAHFSYEDAAEMLAKNSDLNEKLRQRLEQAEQERTRAreqLRQAQAQLAQYNQVL 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 674 AAVKRELEIKEIHLQDAARR-RLLKLQQDQ-REMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELE-AQKRL--YEK 748
Cdd:PRK04863 1023 ASLKSSYDAKRQMLQELKQElQDLGVPADSgAEERARARRDELHARLSANRSRRNQLEKQLTFCEAEMDnLTKKLrkLER 1102
|
....*....
gi 1248026918 749 DLTTSQEAV 757
Cdd:PRK04863 1103 DYHEMREQV 1111
|
|
| YscO-like |
pfam16789 |
YscO-like protein; This family of proteins is similar to the type III secretion protein YscO. ... |
642-762 |
8.67e-03 |
|
YscO-like protein; This family of proteins is similar to the type III secretion protein YscO. The family includes Chlamydia trachomatis CT670 which is found in a type III secretion gene cluster. CT670 interacts with CT671, a putative YscP homolog and CT670 and CT671 may form a chaperone-effector pair.
Pssm-ID: 435583 [Multi-domain] Cd Length: 160 Bit Score: 37.89 E-value: 8.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 642 YQKQELLR---RAEETRREILLQEEEKMAQQRQRLAAVKRELEIKEIHLQDaarrrllKLQQDQREME------------ 706
Cdd:pfam16789 3 YPLEQVLDikkKRVEEAEKVVKDKKRALEKEKEKLAELEAERDKVRKHKKA-------KMQQLRDEMDrgttsdkilqmk 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1248026918 707 --LRRLEDEI---ERKVQMRDQEIAATAKDLEIRQLELeAQKRLYEKDLTTSQEAVAKEIR 762
Cdd:pfam16789 76 ryIKVVKERLkqeEKKVQDQKEQVRTAARNLEIAREEL-KKKRQEVEKLEKHKKEWVKEMK 135
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
619-717 |
9.09e-03 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 37.21 E-value: 9.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026918 619 RERQTVENMQAEVDEQRAKdeawyqKQELLRRAEETRREilLQEEEKMAQ-QRQRLAAVKRELE-----IKEIHLQDAAR 692
Cdd:pfam20492 6 REKQELEERLKQYEEETKK------AQEELEESEETAEE--LEEERRQAEeEAERLEQKRQEAEeekerLEESAEMEAEE 77
|
90 100
....*....|....*....|....*
gi 1248026918 693 RRLLKLQQDQREMELRRLEDEIERK 717
Cdd:pfam20492 78 KEQLEAELAEAQEEIARLEEEVERK 102
|
|
| |
