|
Name |
Accession |
Description |
Interval |
E-value |
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
30-251 |
2.81e-22 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 100.37 E-value: 2.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 30 TKELVSWMRGHESSVCSISVHASGRYAITTSSD-TAQLWDLDTFQRKRKLNIRQSvGIQKVFFLPLSNTILSCFKDNSIF 108
Cdd:COG2319 193 TGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADgTVRLWDLATGKLLRTLTGHSG-SVRSVAFSPDGRLLASGSADGTVR 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 109 AWECDTLFCKYQLPGPPEGSNILykvfAVTRDGRILAAGGKSNHLHLWCLEATGLFRIIQmpAKVRAVRHLEFLPDsfda 188
Cdd:COG2319 272 LWDLATGELLRTLTGHSGGVNSV----AFSPDGKLLASGSDDGTVRLWDLATGKLLRTLT--GHTGAVRSVAFSPD---- 341
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568991892 189 gsNQVLGVLSQDGIMRFVNIQTCKLLFEIGTVEEGISSSVISPHGRYIASIMENGSLNVYSVQ 251
Cdd:COG2319 342 --GKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
8-251 |
5.49e-22 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 99.60 E-value: 5.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 8 AIPSLLGTIRetsmfltCMETVTKELVSWMRGHESSVCSISVHASGRYAITTSSD-TAQLWDLDTFQRKRKLNiRQSVGI 86
Cdd:COG2319 94 ASASADGTVR-------LWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADgTVRLWDLATGKLLRTLT-GHSGAV 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 87 QKVFFLPLSNTILSCFKDNSIFAWECDTLFCKYQLPGPPEGSNILykvfAVTRDGRILAAGGKSNHLHLWCLEATGLFRI 166
Cdd:COG2319 166 TSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSV----AFSPDGKLLASGSADGTVRLWDLATGKLLRT 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 167 IQMPAkvRAVRHLEFLPDSfdagsnQVLGVLSQDGIMRFVNIQTCKLLFEIGTVEEGISSSVISPHGRYIASIMENGSLN 246
Cdd:COG2319 242 LTGHS--GSVRSVAFSPDG------RLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVR 313
|
....*
gi 568991892 247 VYSVQ 251
Cdd:COG2319 314 LWDLA 318
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
30-255 |
2.85e-21 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 97.29 E-value: 2.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 30 TKELVSWMRGHESSVCSISVHASGRYAITTSSD-TAQLWDLDTFQRKRKLNIRQSvGIQKVFFLPLSNTILSCFKDNSIF 108
Cdd:COG2319 151 TGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDgTVRLWDLATGKLLRTLTGHTG-AVRSVAFSPDGKLLASGSADGTVR 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 109 AWECDTLFCKYQLPGPPEGSNILykvfAVTRDGRILAAGGKSNHLHLWCLEATGLFRIIQMPAkvRAVRHLEFLPDSfda 188
Cdd:COG2319 230 LWDLATGKLLRTLTGHSGSVRSV----AFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHS--GGVNSVAFSPDG--- 300
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568991892 189 gsnQVLGVLSQDGIMRFVNIQTCKLLFEIGTVEEGISSSVISPHGRYIASIMENGSLNVYSVQALTQ 255
Cdd:COG2319 301 ---KLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGEL 364
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
30-251 |
4.87e-20 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 93.82 E-value: 4.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 30 TKELVSWMRGHESSVCSISVHASGRYAITTSSD-TAQLWDLDTFQRKRKLNIRQSvGIQKVFFLPLSNTILSCFKDNSIF 108
Cdd:COG2319 67 AGALLATLLGHTAAVLSVAFSPDGRLLASASADgTVRLWDLATGLLLRTLTGHTG-AVRSVAFSPDGKTLASGSADGTVR 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 109 AWECDTLFCKYQLPGPPEGSNILykvfAVTRDGRILAAGGKSNHLHLWCLEATGLFRIIQmpAKVRAVRHLEFLPDSfda 188
Cdd:COG2319 146 LWDLATGKLLRTLTGHSGAVTSV----AFSPDGKLLASGSDDGTVRLWDLATGKLLRTLT--GHTGAVRSVAFSPDG--- 216
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568991892 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 |
1.05e-17 |
|
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: 1.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 30 TKELVSWMRGHESSVCSISVHASGRYAITTSSD-TAQLWDLDTFQRKRKLNIRQSvGIQKVFFLPLSNTILSCFKDNSIF 108
Cdd:cd00200 82 TGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDkTIKVWDVETGKCLTTLRGHTD-WVNSVAFSPDGTFVASSSQDGTIK 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 109 AWECDTLFCKYQLPGpPEGSnilykVFAVT--RDGRILAAGGKSNHLHLWclEATGLFRIIQMPAKVRAVRHLEFLPDsf 186
Cdd:cd00200 161 LWDLRTGKCVATLTG-HTGE-----VNSVAfsPDGEKLLSSSSDGTIKLW--DLSTGKCLGTLRGHENGVNSVAFSPD-- 230
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568991892 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 |
2.88e-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: 2.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 38 RGHESSVCSISVHASGRYAITTSSD-TAQLWDLDTFQRKRKLNIrQSVGIQKVFFLPLSNTILSCFKDNSIFAWECDTLF 116
Cdd:cd00200 6 KGHTGGVTCVAFSPDGKLLATGSGDgTIKVWDLETGELLRTLKG-HTGPVRDVAASADGTYLASGSSDKTIRLWDLETGE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 117 CKYQLPGPPEGsnilykVFAV--TRDGRILAAGGKSNHLHLWCLEATGLfrIIQMPAKVRAVRHLEFLPDsfdagsNQVL 194
Cdd:cd00200 85 CVRTLTGHTSY------VSSVafSPDGRILSSSSRDKTIKVWDVETGKC--LTTLRGHTDWVNSVAFSPD------GTFV 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568991892 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 |
7.28e-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: 7.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 27 ETVTKELVSWMRGHESSVCSISVHASGRYAITTSSD-TAQLWDLDTFQRKRKLNIRQSvGIQKVFFLPLSNTILSCFKDN 105
Cdd:cd00200 121 DVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDgTIKLWDLRTGKCVATLTGHTG-EVNSVAFSPDGEKLLSSSSDG 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 106 SIFAWECDTLFCKYQLPGPPEGSNILykvfAVTRDGRILAAGGKSNHLHLWCLEATGLFRIIQMPAK-VRAVRhleFLPD 184
Cdd:cd00200 200 TIKLWDLSTGKCLGTLRGHENGVNSV----AFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNsVTSLA---WSPD 272
|
170 180
....*....|....*....|.
gi 568991892 185 SfdagsnQVLGVLSQDGIMRF 205
Cdd:cd00200 273 G------KRLASGSADGTIRI 287
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
38-251 |
7.63e-14 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 74.56 E-value: 7.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 38 RGHESSVCSISVHASGRYAITTSSDTAQLWDLDTFQRKRKLNIRQSVGIQKVFFLPLSNTILSCFKDNSIFAWECDTLFC 117
Cdd:COG2319 33 LGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 118 KYQLPGPPEGSNILykvfAVTRDGRILAAGGKSNHLHLWCLEATGLFRIIQMPAkvRAVRHLEFLPDSfdagsnQVLGVL 197
Cdd:COG2319 113 LRTLTGHTGAVRSV----AFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHS--GAVTSVAFSPDG------KLLASG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 568991892 198 SQDGIMRFVNIQTCKLLFEIGTVEEGISSSVISPHGRYIASIMENGSLNVYSVQ 251
Cdd:COG2319 181 SDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLA 234
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
599-921 |
4.40e-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: 4.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 599 IVDYQTREWERIRNDELDFL---RERQTVENMQAEVDEQRAKDEAwyqkqELLRRAEETRREILLQEEEKMAQQRQRlaa 675
Cdd:pfam17380 277 IVQHQKAVSERQQQEKFEKMeqeRLRQEKEEKAREVERRRKLEEA-----EKARQAEMDRQAAIYAEQERMAMERER--- 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 676 vkrelEIKEIHLQDaARRRLLKLQQDQREMELRRLEdEIERkVQMRDQEiaataKDLEIRQlELEAQK--RLYEKDlttS 753
Cdd:pfam17380 349 -----ELERIRQEE-RKRELERIRQEEIAMEISRMR-ELER-LQMERQQ-----KNERVRQ-ELEAARkvKILEEE---R 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 754 QEAVAKEIREDTDAHRRKAALEEHMFQKLLENSQmggRRAQRVMEDNLAKAEqaclnadwQIQTLHKQKcADQQRSQGYY 833
Cdd:pfam17380 412 QRKIQQQKVEMEQIRAEQEEARQREVRRLEEERA---REMERVRLEEQERQQ--------QVERLRQQE-EERKRKKLEL 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 834 DvatllRENR-RKEVEVLNAM-----MEEEAQKWKEAEEKEFHLQS--AKKASALSDASRKWFLRQETSAALEHEEMPWL 905
Cdd:pfam17380 480 E-----KEKRdRKRAEEQRRKilekeLEERKQAMIEEERKRKLLEKemEERQKAIYEEERRREAEEERRKQQEMEERRRI 554
|
330
....*....|....*.
gi 568991892 906 QRQYMDSAylPQTSRL 921
Cdd:pfam17380 555 QEQMRKAT--EERSRL 568
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
608-868 |
7.23e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.05 E-value: 7.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 608 ERIRNDELDFLRERQTVENMQAEVDEQRAK--------DEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRE 679
Cdd:COG1196 246 AELEELEAELEELEAELAELEAELEELRLEleelelelEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 680 LEIKEIHLQDAARRRLLKLQQDQREMELRRLEDEIERKVQMRD------QEIAATAKDLEIRQLELEAQKRLYEKDLTTS 753
Cdd:COG1196 326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLeaeaelAEAEEELEELAEELLEALRAAAELAAQLEEL 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 754 QEAVAKEIREDTDAHRRKAALEEHmfQKLLENSQMGGRRAQRVMEDNLAKAEQACLNADWQIQTLHKQkcADQQRSQGYY 833
Cdd:COG1196 406 EEAEEALLERLERLEEELEELEEA--LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE--AALLEAALAE 481
|
250 260 270
....*....|....*....|....*....|....*.
gi 568991892 834 DVATLLRENRRKEV-EVLNAMMEEEAQKWKEAEEKE 868
Cdd:COG1196 482 LLEELAEAAARLLLlLEAEADYEGFLEGVKAALLLA 517
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
603-780 |
2.90e-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: 67.46 E-value: 2.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 603 QTREWERIRNDELDflrERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEE----KMAQQRQRLAAVKR 678
Cdd:pfam17380 444 RAREMERVRLEEQE---RQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEerkqAMIEEERKRKLLEK 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 679 ELEIKEIHLQDAARRRLLKLQQ-DQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEKDLTTSQEAV 757
Cdd:pfam17380 521 EMEERQKAIYEEERRREAEEERrKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAEYEATTPITTI 600
|
170 180
....*....|....*....|...
gi 568991892 758 AKEIREDTDAHrRKAALEEHMFQ 780
Cdd:pfam17380 601 KPIYRPRISEY-QPPDVESHMIR 622
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
608-876 |
7.52e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 66.70 E-value: 7.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 608 ERIRNDELdflreRQTVENMQAEVDEQRAKDEAwYQKQELLRRAEETRR--EILLQEEEKMAQQRQRLAAVKRELEIKei 685
Cdd:PTZ00121 1481 EAKKADEA-----KKKAEEAKKKADEAKKAAEA-KKKADEAKKAEEAKKadEAKKAEEAKKADEAKKAEEKKKADELK-- 1552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 686 hlqdaaRRRLLKLQQDQREMELRRLEDEiERKVQMRDQEIAATAKDLEIrqlelEAQKRLYEKDLTTSQEAVAKEIREDT 765
Cdd:PTZ00121 1553 ------KAEELKKAEEKKKAEEAKKAEE-DKNMALRKAEEAKKAEEARI-----EEVMKLYEEEKKMKAEEAKKAEEAKI 1620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 766 DAHR-RKAALEEHMFQKLLENSQMGGRRAQRVM---EDNLAKAEQACLNADWQIQTLHKQKCADQQRSQGyyDVATLLRE 841
Cdd:PTZ00121 1621 KAEElKKAEEEKKKVEQLKKKEAEEKKKAEELKkaeEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKA--AEALKKEA 1698
|
250 260 270
....*....|....*....|....*....|....*....
gi 568991892 842 NRRKEVEVLNAMMEEEAQKW----KEAEEKEFHLQSAKK 876
Cdd:PTZ00121 1699 EEAKKAEELKKKEAEEKKKAeelkKAEEENKIKAEEAKK 1737
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
602-900 |
8.80e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.11 E-value: 8.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 602 YQT-REWERIRNDELdFLRERQTVENMQAEVDEQRAkdeawyQKQELLRRAEETRREIllqeEEKMAQQRQRLAAVKREL 680
Cdd:COG1196 215 YRElKEELKELEAEL-LLLKLRELEAELEELEAELE------ELEAELEELEAELAEL----EAELEELRLELEELELEL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 681 EIKEIHLQdAARRRLLKLQQDQR--EMELRRLEDEIERKvQMRDQEIAATAKDLEIRQLELEAQKRLYEKDLTTSQEAVA 758
Cdd:COG1196 284 EEAQAEEY-ELLAELARLEQDIArlEERRRELEERLEEL-EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 759 KEIREDTDAHRRKAALEEHMFQKLLENSQMggRRAQRVMEDNLAKAEQaclnadwQIQTLHKQKCADQQRSQGYYDVATL 838
Cdd:COG1196 362 EAEEALLEAEAELAEAEEELEELAEELLEA--LRAAAELAAQLEELEE-------AEEALLERLERLEEELEELEEALAE 432
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568991892 839 LRENRRKEVEVLNAMMEEEAQKWKEAEEKEFHLQSAKKASALSDASRKWFLRQETSAALEHE 900
Cdd:COG1196 433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
605-900 |
1.75e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 65.55 E-value: 1.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 605 REWERIRNDELdflreRQTVENMQAevDEQRAKDEAwyQKQELLRRAEETRR--EILLQEEEKMAQQRQRLAAVKRELEI 682
Cdd:PTZ00121 1505 AAEAKKKADEA-----KKAEEAKKA--DEAKKAEEA--KKADEAKKAEEKKKadELKKAEELKKAEEKKKAEEAKKAEED 1575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 683 KEIHLQDAARRRllKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEKDLTTSQEAVAKEIR 762
Cdd:PTZ00121 1576 KNMALRKAEEAK--KAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELK 1653
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 763 EDTDAHRRKAALEehmfQKLLENSQMGGRRAQRVMEDNLAKAEQACLNADwqiqtlhKQKCADQQRSQGYYDV--ATLLR 840
Cdd:PTZ00121 1654 KAEEENKIKAAEE----AKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAE-------EAKKAEELKKKEAEEKkkAEELK 1722
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568991892 841 ---ENRRKEVEVLNAMMEEEAQKWKEAEEKEfhlQSAKKASALSDASRKWF--LRQETSAALEHE 900
Cdd:PTZ00121 1723 kaeEENKIKAEEAKKEAEEDKKKAEEAKKDE---EEKKKIAHLKKEEEKKAeeIRKEKEAVIEEE 1784
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
608-868 |
6.45e-10 |
|
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: 61.86 E-value: 6.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 608 ERIRNDELDFLRERQTVENMQAEVDEQRAKDEAWYQ-KQELLRRAEETRREILLQEEEKMAQQRQRLAAVKR-ELEIKEI 685
Cdd:pfam13868 38 EKEEERRLDEMMEEERERALEEEEEKEEERKEERKRyRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERiQEEDQAE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 686 HLQDAARRRLLK--------LQQDQREMElRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEKDLTTSQEAv 757
Cdd:pfam13868 118 AEEKLEKQRQLReeidefneEQAEWKELE-KEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEK- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 758 AKEIREDTDAHRRKAALEEHMF-----------QKLLENSQMGGRRAQRVMEDNLAKAEQACLNADWQIQTLHKQKCAD- 825
Cdd:pfam13868 196 AQDEKAERDELRAKLYQEEQERkerqkereeaeKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEe 275
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 568991892 826 ----------QQRSQGYYDVATLLRENRRKEVEVLNAMMEEEAQKWKEAEEKE 868
Cdd:pfam13868 276 ieqeeaekrrMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERR 328
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
645-901 |
8.24e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.03 E-value: 8.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 645 QELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELEIKEIHLQ---DAARRRLLKLQQDQREME---------LRRLED 712
Cdd:COG1196 216 RELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEaelAELEAELEELRLELEELEleleeaqaeEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 713 EIERKVQMRDQEiAATAKDLEIRQLELEAQKRLYEKDLTTSQEAVAKEIREDTDAHRRKAALEEHMFQKLLENSQMGGRR 792
Cdd:COG1196 296 ELARLEQDIARL-EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 793 AQRVME-DNLAKAEQACLNADWQIQTLHKQKCADQQRSQGyyDVATLLRENRRKEVEVLNAMMEEEAQKWKEAEEKEFHL 871
Cdd:COG1196 375 AEAEEElEELAEELLEALRAAAELAAQLEELEEAEEALLE--RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
250 260 270
....*....|....*....|....*....|
gi 568991892 872 QSAKKASALSDASRKWFLRQETSAALEHEE 901
Cdd:COG1196 453 ELEEEEEALLELLAELLEEAALLEAALAEL 482
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
648-901 |
1.23e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.26 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 648 LRRAEE--TRREILLQEeekMAQQRQRLA----------AVKRELEIKEIHLQdAARRRLLKLQQDQREMELRRLEDEIE 715
Cdd:COG1196 181 LEATEEnlERLEDILGE---LERQLEPLErqaekaeryrELKEELKELEAELL-LLKLRELEAELEELEAELEELEAELE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 716 R-KVQMRDQEIAATAKDLEIRQLELE---AQKRLYEkdlttSQEAVAKEIREDTDAHRRKAALEEHMFQKLLENSQMGGR 791
Cdd:COG1196 257 ElEAELAELEAELEELRLELEELELEleeAQAEEYE-----LLAELARLEQDIARLEERRRELEERLEELEEELAELEEE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 792 RAQRVMEDNLAKAEQACLNADWQIQTLHKQKCADQQRSQgyydvATLLRENRRKEVEVLNAMMEEEAQKwKEAEEKEFHL 871
Cdd:COG1196 332 LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA-----EAELAEAEEELEELAEELLEALRAA-AELAAQLEEL 405
|
250 260 270
....*....|....*....|....*....|
gi 568991892 872 QSAKKASALSDASRKWFLRQETSAALEHEE 901
Cdd:COG1196 406 EEAEEALLERLERLEEELEELEEALAELEE 435
|
|
| RabGAP-TBC |
pfam00566 |
Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are ... |
376-520 |
2.58e-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: 57.65 E-value: 2.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 376 SLQKKYPIKSRKLLRVLQRTLSALAHWsaiFSDTPY---LPLLAFPFVkLFQNNQLICFEVVATLIINwcQHWFEYFPN- 451
Cdd:pfam00566 19 TFPHSFFFDNGPGQNSLRRILKAYSIY---NPDVGYcqgMNFIAAPLL-LVYLDEEDAFWCFVSLLEN--YLLRDFYTPd 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568991892 452 -PPINILSMI-ENVLAFHDKELLQHFIDRDITSQVYAWPLLETLFSEVLTREEWLRLFDNIFSNHPSFLLM 520
Cdd:pfam00566 93 fPGLKRDLYVfEELLKKKLPKLYKHLKELGLDPDLFASQWFLTLFAREFPLSTVLRIWDYFFLEGEKFVLF 163
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
613-886 |
8.29e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.77 E-value: 8.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 613 DELDFLRERQTVENMQAEvdEQRAKDEAwYQKQELLRRAEETRR--EILLQEEEKMAQQRQRLAAVKReleikeihLQDA 690
Cdd:PTZ00121 1095 EAFGKAEEAKKTETGKAE--EARKAEEA-KKKAEDARKAEEARKaeDARKAEEARKAEDAKRVEIARK--------AEDA 1163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 691 ARRRLLKLQQDQREMELRRLEDEIERKVQMRDQE----IAATAKDLEIRQLEleaQKRLYEKDLTTSQEAVAKEIREDTD 766
Cdd:PTZ00121 1164 RKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEdarkAEAARKAEEERKAE---EARKAEDAKKAEAVKKAEEAKKDAE 1240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 767 AHRRKAALEEHMFQKLLENSQMggrrAQRVMEDNLAKAEQAcLNADWQIQTLHKQKCADQQRSQGYYDVATLLRE-NRRK 845
Cdd:PTZ00121 1241 EAKKAEEERNNEEIRKFEEARM----AHFARRQAAIKAEEA-RKADELKKAEEKKKADEAKKAEEKKKADEAKKKaEEAK 1315
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 568991892 846 EVEVLNAMMEEEAQKWKEAEEKEfhlQSAKKASALSDASRK 886
Cdd:PTZ00121 1316 KADEAKKKAEEAKKKADAAKKKA---EEAKKAAEAAKAEAE 1353
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
606-787 |
9.76e-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: 59.19 E-value: 9.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 606 EWERIRNDELDFLRERQ----TVENMQAEVD--EQRAKDEAWYQKQellRRAEETRReillQEEEKMAQQRQRLAAVKRE 679
Cdd:pfam15709 349 EVERKRREQEEQRRLQQeqleRAEKMREELEleQQRRFEEIRLRKQ---RLEEERQR----QEEEERKQRLQLQAAQERA 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 680 leikeiHLQDAA-RRRLLKLQQDQREMELRRLEDEIERKVQMRDQeIAATAKDL-EIRQLE-LEAQKRLYEKDLTTSQEA 756
Cdd:pfam15709 422 ------RQQQEEfRRKLQELQRKKQQEEAERAEAEKQRQKELEMQ-LAEEQKRLmEMAEEErLEYQRQKQEAEEKARLEA 494
|
170 180 190
....*....|....*....|....*....|.
gi 568991892 757 VAKEIREDTDAhrrKAALEEHMFQKLLENSQ 787
Cdd:pfam15709 495 EERRQKEEEAA---RLALEEAMKQAQEQARQ 522
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
605-837 |
3.26e-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: 57.44 E-value: 3.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 605 REWERIRNdELDFLR-------ERQ-TVENMQAEVDEQRAKDEAwyQKQELLRRAEETR-REILLQEEEKMAQQRQrlaa 675
Cdd:pfam17380 389 QKNERVRQ-ELEAARkvkileeERQrKIQQQKVEMEQIRAEQEE--ARQREVRRLEEERaREMERVRLEEQERQQQ---- 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 676 vkreleiKEIHLQDAARRRLLKLQQDQREMELRRLEDE----IERKVQMRDQEIaatakdleirqLELEAQKRLYEKDLT 751
Cdd:pfam17380 462 -------VERLRQQEEERKRKKLELEKEKRDRKRAEEQrrkiLEKELEERKQAM-----------IEEERKRKLLEKEME 523
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 752 TSQEAVAKEiredtdaHRRKAALEEHMFQKLLENSqmggRRAQRVMEdnLAKAEQACLNADWQIQTLHKQkCADQQRSQG 831
Cdd:pfam17380 524 ERQKAIYEE-------ERRREAEEERRKQQEMEER----RRIQEQMR--KATEERSRLEAMEREREMMRQ-IVESEKARA 589
|
....*.
gi 568991892 832 YYDVAT 837
Cdd:pfam17380 590 EYEATT 595
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
603-886 |
4.69e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.46 E-value: 4.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 603 QTREWERIRNDEldflRERQTVENMQAEvDEQRA----KDEAWYQKQELLRRAEETR--REILLQEEEKMAQQRQRLAAV 676
Cdd:PTZ00121 1198 DARKAEAARKAE----EERKAEEARKAE-DAKKAeavkKAEEAKKDAEEAKKAEEERnnEEIRKFEEARMAHFARRQAAI 1272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 677 KRELEIKEIHLQDAARRRllKLQQDQREMELRRLeDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYE-KDLTTSQE 755
Cdd:PTZ00121 1273 KAEEARKADELKKAEEKK--KADEAKKAEEKKKA-DEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEaKKAAEAAK 1349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 756 AVAKEIREDTDAHRRKAALEEHMFQKLLENSQMGGRRAQRV--MEDNLAKAEQACLNADWQIQTLHKQKCADQQRSQGyy 833
Cdd:PTZ00121 1350 AEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKkkADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKA-- 1427
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 568991892 834 dvatllrENRRKEVEVLNAmmEEEAQKWKEAEEKEFHLQSAKKASALSDASRK 886
Cdd:PTZ00121 1428 -------EEKKKADEAKKK--AEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK 1471
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
603-886 |
6.31e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.07 E-value: 6.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 603 QTREWERIRNDELdfLRERQTVENMQA--EVDEQRAKDEAwyQKQELLRRAEETRReilLQEEEKMAQQRQRLAAVKREL 680
Cdd:PTZ00121 1180 AARKAEEVRKAEE--LRKAEDARKAEAarKAEEERKAEEA--RKAEDAKKAEAVKK---AEEAKKDAEEAKKAEEERNNE 1252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 681 EIKEIhlqDAARRRLLKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKdlEIRQLElEAQKRLYEKDLTTSQEAVAKE 760
Cdd:PTZ00121 1253 EIRKF---EEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAE--EKKKAD-EAKKKAEEAKKADEAKKKAEE 1326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 761 IREDTDAHRRKA----------ALEEHMFQKLLENSQMGGRRAQRVMEDNLAKAEQACLNADwqiqtlhKQKCADQQRSQ 830
Cdd:PTZ00121 1327 AKKKADAAKKKAeeakkaaeaaKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAE-------EKKKADEAKKK 1399
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 568991892 831 GyydvatllRENRRKEVEVLNAmmEEEAQKWKEAEEKEFHLQSAKKASALSDASRK 886
Cdd:PTZ00121 1400 A--------EEDKKKADELKKA--AAAKKKADEAKKKAEEKKKADEAKKKAEEAKK 1445
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
605-909 |
6.34e-08 |
|
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: 57.00 E-value: 6.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 605 REWERIRNdELDFLRERqtVENMQAEVDE--------QRAKDEAwYQKQELLRRAEETRREILLQEEEKMAQQRQR---- 672
Cdd:TIGR02169 170 RKKEKALE-ELEEVEEN--IERLDLIIDEkrqqlerlRREREKA-ERYQALLKEKREYEGYELLKEKEALERQKEAierq 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 673 LAAVKRELEIKEIHLQDAARRrllklqQDQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEKDLTT 752
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKR------LEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELED 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 753 SQEAVAKEIREDTDAHRRKAALEEHMFQKLLENSQMGGRRAQR--VMEDNLAKAEQ-ACLNADWQIQTLHKQKCADQQRS 829
Cdd:TIGR02169 320 AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELkeELEDLRAELEEvDKEFAETRDELKDYREKLEKLKR 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 830 QGY---YDVATLLRENRRKEVEV-------------LNAMMEEEAQKWKEAEEKEFHLQSAKKasALSDASRKWFLRQET 893
Cdd:TIGR02169 400 EINelkRELDRLQEELQRLSEELadlnaaiagieakINELEEEKEDKALEIKKQEWKLEQLAA--DLSKYEQELYDLKEE 477
|
330
....*....|....*.
gi 568991892 894 SAALEhEEMPWLQRQY 909
Cdd:TIGR02169 478 YDRVE-KELSKLQREL 492
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
601-776 |
9.48e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.46 E-value: 9.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 601 DYQTREWERIRNDELDFLRERQTVENMQaevdeqrakdeawyQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKREL 680
Cdd:COG4913 260 LAERYAAARERLAELEYLRAALRLWFAQ--------------RRLELLEAELEELRAELARLEAELERLEARLDALREEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 681 EIKEIHLQDAARRRLLKLQQdqremELRRLEDEIERKVQMRDQ----------EIAATAKDLEIRQLELEAQKRLYEKDL 750
Cdd:COG4913 326 DELEAQIRGNGGDRLEQLER-----EIERLERELEERERRRARleallaalglPLPASAEEFAALRAEAAALLEALEEEL 400
|
170 180
....*....|....*....|....*.
gi 568991892 751 TTSQEAVAKEIREDTDAHRRKAALEE 776
Cdd:COG4913 401 EALEEALAEAEAALRDLRRELRELEA 426
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
608-877 |
2.82e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.76 E-value: 2.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 608 ERIRNDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREillQEEEKMAQQRQRLAAVKRELEIKEIHL 687
Cdd:PTZ00121 1364 EKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKA---AAAKKKADEAKKKAEEKKKADEAKKKA 1440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 688 QDAARRRLLKLQ-QDQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEKDLTTSQEAVAKEIREDTD 766
Cdd:PTZ00121 1441 EEAKKADEAKKKaEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEE 1520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 767 AHRRKAALEEHMFQKLLEnsqmgGRRAQRVME-DNLAKAEQacLNADWQIQTLHKQKCADQQRSQGYYDvATLLRENRRK 845
Cdd:PTZ00121 1521 AKKADEAKKAEEAKKADE-----AKKAEEKKKaDELKKAEE--LKKAEEKKKAEEAKKAEEDKNMALRK-AEEAKKAEEA 1592
|
250 260 270
....*....|....*....|....*....|....*.
gi 568991892 846 EVEVLNAMMEEE----AQKWKEAEEKEFHLQSAKKA 877
Cdd:PTZ00121 1593 RIEEVMKLYEEEkkmkAEEAKKAEEAKIKAEELKKA 1628
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
622-819 |
3.06e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 54.58 E-value: 3.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 622 QTVENMQAEVDEQRAKDEAwyqkQELLRRAEETR--------REILLQEEEKMAQQRQRLAAVKRELEIK-EIHLQDAAr 692
Cdd:PRK04863 480 QLVRKIAGEVSRSEAWDVA----RELLRRLREQRhlaeqlqqLRMRLSELEQRLRQQQRAERLLAEFCKRlGKNLDDED- 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 693 rrLLKLQQDQREMELRRLEDE----IERKVQMRDQEIAATAkdlEIRQLELEAQKRLyekdltTSQEAVAK--EIREDTD 766
Cdd:PRK04863 555 --ELEQLQEELEARLESLSESvseaRERRMALRQQLEQLQA---RIQRLAARAPAWL------AAQDALARlrEQSGEEF 623
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568991892 767 AHRrkAALEEHMfQKLLENsqmggRRAQRVMEDNLAKAEQAClnaDWQIQTLH 819
Cdd:PRK04863 624 EDS--QDVTEYM-QQLLER-----ERELTVERDELAARKQAL---DEEIERLS 665
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
598-869 |
3.16e-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: 54.59 E-value: 3.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 598 FIVDYQTREWE-RIRNDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRR-EILLQEEEKMAQQRQRLAA 675
Cdd:pfam02463 168 KRKKKEALKKLiEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLyLDYLKLNEERIDLLQELLR 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 676 VKRELEIKEIHLQDAARRrllKLQQDQREMElrrledEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEKDLTTSQE 755
Cdd:pfam02463 248 DEQEEIESSKQEIEKEEE---KLAQVLKENK------EEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 756 AVAKEIREDTDAHRRKAALEEhmFQKLLENSQmGGRRAQRVMEDNLAKAEQACLNADWQIQTLHKQKCADQQRSQGYYDV 835
Cdd:pfam02463 319 SEKEKKKAEKELKKEKEEIEE--LEKELKELE-IKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEE 395
|
250 260 270
....*....|....*....|....*....|....*.
gi 568991892 836 ATLLRENRRKEVEVLN--AMMEEEAQKWKEAEEKEF 869
Cdd:pfam02463 396 ELELKSEEEKEAQLLLelARQLEDLLKEEKKEELEI 431
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
605-912 |
3.82e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.38 E-value: 3.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 605 REWERIRNDELDFLRERQtvENMQAEvdeQRAKDEAWYQKQELLRRAEETRREILlQEEEKMAQQRQRLAAVKRELEIKE 684
Cdd:PTZ00121 1587 KKAEEARIEEVMKLYEEE--KKMKAE---EAKKAEEAKIKAEELKKAEEEKKKVE-QLKKKEAEEKKKAEELKKAEEENK 1660
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 685 IHLQDAARrrllKLQQDQREMELRRLEDEIERKVQ---MRDQEIAATAKDL------------------EIRQLELEAQK 743
Cdd:PTZ00121 1661 IKAAEEAK----KAEEDKKKAEEAKKAEEDEKKAAealKKEAEEAKKAEELkkkeaeekkkaeelkkaeEENKIKAEEAK 1736
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 744 RLYEKDLTTSQEAVAKEIREDTDAHRRKAALEEhmfqkllenSQMGGRRAQRVMEDNLAKA-EQACLNADWQIQTLHKQK 822
Cdd:PTZ00121 1737 KEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKK---------AEEIRKEKEAVIEEELDEEdEKRRMEVDKKIKDIFDNF 1807
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 823 CADQQ---RSQGYYDVATLLRENRRKEVEVLNAMMEEEAqkwKEAEEKEFHLQSAKKASALSDA---SRKWFLRQETSAA 896
Cdd:PTZ00121 1808 ANIIEggkEGNLVINDSKEMEDSAIKEVADSKNMQLEEA---DAFEKHKFNKNNENGEDGNKEAdfnKEKDLKEDDEEEI 1884
|
330
....*....|....*.
gi 568991892 897 LEHEEMPWLQRQYMDS 912
Cdd:PTZ00121 1885 EEADEIEKIDKDDIER 1900
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
597-747 |
5.63e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 53.24 E-value: 5.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 597 KFIVDYQTREWERIRNDEL-----DFLRERQTVENmqaEVDEQRAKdeawYQKQEL-LRRAEET---RREILLQEEEKMA 667
Cdd:PRK12704 41 KRILEEAKKEAEAIKKEALleakeEIHKLRNEFEK---ELRERRNE----LQKLEKrLLQKEENldrKLELLEKREEELE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 668 QQRQRLAAVKRELEIKEIHLQDAARRRLLKLQQ-------DQREMELRRLEDEIErkvqmrdQEIAATAKDLEiRQLELE 740
Cdd:PRK12704 114 KKEKELEQKQQELEKKEEELEELIEEQLQELERisgltaeEAKEILLEKVEEEAR-------HEAAVLIKEIE-EEAKEE 185
|
....*..
gi 568991892 741 AQKRLYE 747
Cdd:PRK12704 186 ADKKAKE 192
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
608-883 |
6.06e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 53.58 E-value: 6.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 608 ERIRNDELDFLRE----RQTVENMQAEVDEQRAKDE---AWYQKQELLRRAE----ETRREILLQEEEKMAQQRQRLAA- 675
Cdd:pfam15921 306 EQARNQNSMYMRQlsdlESTVSQLRSELREAKRMYEdkiEELEKQLVLANSElteaRTERDQFSQESGNLDDQLQKLLAd 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 676 -VKREleiKEIHLQDAARRRL-------------LKLQQDQREMELRRLEDEI-----ERKVQMRDQEIAATAKDLEIRQ 736
Cdd:pfam15921 386 lHKRE---KELSLEKEQNKRLwdrdtgnsitidhLRRELDDRNMEVQRLEALLkamksECQGQMERQMAAIQGKNESLEK 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 737 L-ELEAQkrlyekdLTTSQEAVAKEIREDTdahRRKAALEEHmfQKLLENSQMGGRRAQRVMEDNLAKAEQACLNADWQI 815
Cdd:pfam15921 463 VsSLTAQ-------LESTKEMLRKVVEELT---AKKMTLESS--ERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKL 530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 816 QTLHKQKCADQ--QRSQGYYDVATLLRENRRKEVEVL------------------NAMMEEEAQKWKEAEEKEFHLQSAK 875
Cdd:pfam15921 531 QELQHLKNEGDhlRNVQTECEALKLQMAEKDKVIEILrqqienmtqlvgqhgrtaGAMQVEKAQLEKEINDRRLELQEFK 610
|
....*...
gi 568991892 876 KASALSDA 883
Cdd:pfam15921 611 ILKDKKDA 618
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
614-801 |
7.63e-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: 53.52 E-value: 7.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 614 ELDFLRER-QTVENMQAEVDEQRAKDEawyQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELEIKEIHLQD--- 689
Cdd:TIGR02168 303 QKQILRERlANLERQLEELEAQLEELE---SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEElee 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 690 -----AARRRLLKLQQDQREMELRRLEDEIER---KVQMRDQEIAATAKDLEIRQLElEAQKRLYEKD--LTTSQEAVAK 759
Cdd:TIGR02168 380 qletlRSKVAQLELQIASLNNEIERLEARLERledRRERLQQEIEELLKKLEEAELK-ELQAELEELEeeLEELQEELER 458
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 568991892 760 EIREDTDAHRRKAALEEHMFQKLLENSQMGGR-RAQRVMEDNL 801
Cdd:TIGR02168 459 LEEALEELREELEEAEQALDAAERELAQLQARlDSLERLQENL 501
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
620-877 |
7.90e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.61 E-value: 7.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 620 ERQTVENMQAEVDEQRAKDEAWYQKQE------LLRRAEETRREillQEEEKMAQQRQRLAAVKRELEIKEIHLQDAARR 693
Cdd:PTZ00121 1429 EKKKADEAKKKAEEAKKADEAKKKAEEakkaeeAKKKAEEAKKA---DEAKKKAEEAKKADEAKKKAEEAKKKADEAKKA 1505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 694 RLLKLQQDQ-REMELRRLEDEIERKVQMRDQEIAATAKdlEIRQLELEAQKRLYEKDLTTSQEAVAKEIREDTDAHRRKA 772
Cdd:PTZ00121 1506 AEAKKKADEaKKAEEAKKADEAKKAEEAKKADEAKKAE--EKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKA 1583
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 773 ALEEHMFQKLLENSQMGGRRAQRVMEDNLAKAEQACLNADWQIQTLHKQKCADQQRSQGYYDVATllRENRRKEVEVLNA 852
Cdd:PTZ00121 1584 EEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKK--AEELKKAEEENKI 1661
|
250 260
....*....|....*....|....*
gi 568991892 853 MMEEEAQKwkeAEEKEFHLQSAKKA 877
Cdd:PTZ00121 1662 KAAEEAKK---AEEDKKKAEEAKKA 1683
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
607-866 |
1.41e-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: 51.46 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 607 WERIRNDELDFLRERQT-VENMQAEVDEQRAKDEAWYQKQELLRRAEETRreilLQEEEKMAQQRQRL-AAVKRELEIKE 684
Cdd:pfam13868 107 VERIQEEDQAEAEEKLEkQRQLREEIDEFNEEQAEWKELEKEEEREEDER----ILEYLKEKAEREEErEAEREEIEEEK 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 685 IHLQDAARRRLLKLQQDQREME---LRRLEDEIERKvqMRDQEIAATAKDLEIRQLELEAQKrlyekdlttsQEAVAKEI 761
Cdd:pfam13868 183 EREIARLRAQQEKAQDEKAERDelrAKLYQEEQERK--ERQKEREEAEKKARQRQELQQARE----------EQIELKER 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 762 REdtdahRRKAALEEHMFQKLLENSQMGGRRAQRVMEDNLAKAEQACLNADWQIQTLHKQKcadqqrsqgyydvatllRE 841
Cdd:pfam13868 251 RL-----AEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQR-----------------AA 308
|
250 260
....*....|....*....|....*
gi 568991892 842 NRRKEVEVLNAMMEEEAQKWKEAEE 866
Cdd:pfam13868 309 EREEELEEGERLREEEAERRERIEE 333
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
636-761 |
1.45e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 52.09 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 636 AKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLaavKRELEIKEIHLQDAARRRLlklqqdQREMELRRLEDEIE 715
Cdd:PRK12704 36 AEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEF---EKELRERRNELQKLEKRLL------QKEENLDRKLELLE 106
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 568991892 716 RkvqmRDQEIAATAKDLEIRQLELEAQKRLYEKdLTTSQEAVAKEI 761
Cdd:PRK12704 107 K----REEELEKKEKELEQKQQELEKKEEELEE-LIEEQLQELERI 147
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
628-943 |
1.57e-06 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 51.96 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 628 QAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELE--IKEIHLQDAARRRLLKLQQDQREM 705
Cdd:COG3064 1 AQEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEeeAREAKAEAEQRAAELAAEAAKKLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 706 ELRRLEDEIERKVQMRDQEIAATA-KDLEIRQLELEAQKRLYEKdlttSQEAVAKEIREDTDAHRRKAALEEHMFQKLLE 784
Cdd:COG3064 81 EAEKAAAEAEKKAAAEKAKAAKEAeAAAAAEKAAAAAEKEKAEE----AKRKAEEEAKRKAEEERKAAEAEAAAKAEAEA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 785 NSQMG-GRRAQRVMEDNLAKAEQACLNADWQIQTLHKQKCADQQRSQGYYDVATLLRENRRKEVEVLNAMMEEEAQKWKE 863
Cdd:COG3064 157 ARAAAaAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 864 AEEKEFHLQSAKKASALSDASRKWFLRQETSAALEHEEMPWLQRQYMDSAYLPQTSRLHDVSDMDPSTHIFSRNYPTEWN 943
Cdd:COG3064 237 VEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEA 316
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
603-743 |
1.63e-06 |
|
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: 51.88 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 603 QTREWE--RIRNDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKREL 680
Cdd:pfam15709 382 QQRRFEeiRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQL 461
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568991892 681 EIKEIHLQD-AARRRLLKLQQDQREMELRRLEDEIERKvqmRDQEIAATAKDLEIRQLELEAQK 743
Cdd:pfam15709 462 AEEQKRLMEmAEEERLEYQRQKQEAEEKARLEAEERRQ---KEEEAARLALEEAMKQAQEQARQ 522
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
618-799 |
2.16e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.86 E-value: 2.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 618 LRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELEIKEIHLQDAARRRLLK 697
Cdd:COG1196 680 ELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEP 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 698 LQQDQREMELRRLEDEIER--KVQMR-DQEIAATAKDLEirqlELEAQKrlyeKDLTTSQEAVAKEIRE-DTDAHRR-KA 772
Cdd:COG1196 760 PDLEELERELERLEREIEAlgPVNLLaIEEYEELEERYD----FLSEQR----EDLEEARETLEEAIEEiDRETRERfLE 831
|
170 180 190
....*....|....*....|....*....|...
gi 568991892 773 ALEE------HMFQKLLensqmGGRRAQRVMED 799
Cdd:COG1196 832 TFDAvnenfqELFPRLF-----GGGEAELLLTD 859
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
633-821 |
3.21e-06 |
|
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: 50.72 E-value: 3.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 633 EQRAKDEAWYQKQELLR-RAEETRREillQEEEKMAQQRQ--RLAAVKRELEIKEIHLQDAARRRllklQQDQREMELRR 709
Cdd:pfam15709 331 EKASRDRLRAERAEMRRlEVERKRRE---QEEQRRLQQEQleRAEKMREELELEQQRRFEEIRLR----KQRLEEERQRQ 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 710 LEDEIERKVQMRDQEIAATAKDLEIRQ--LELEAQKRLYEKDLTTSQEAVAKEIRED-TDAHRRKAALEEHMFQKLLENS 786
Cdd:pfam15709 404 EEEERKQRLQLQAAQERARQQQEEFRRklQELQRKKQQEEAERAEAEKQRQKELEMQlAEEQKRLMEMAEEERLEYQRQK 483
|
170 180 190
....*....|....*....|....*....|....*....
gi 568991892 787 QMGGRRAQRVMEDNLAKAEQACL----NADWQIQTLHKQ 821
Cdd:pfam15709 484 QEAEEKARLEAEERRQKEEEAARlaleEAMKQAQEQARQ 522
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
625-903 |
3.32e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 51.38 E-value: 3.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 625 ENMQAEVDEQRAKDEAWYQKQELLRRAEETRREILL--QEEEKMAQQRQRLAAVKREleIKEIHLQDAARRRLLKLQQDQ 702
Cdd:pfam12128 210 GVVPPKSRLNRQQVEHWIRDIQAIAGIMKIRPEFTKlqQEFNTLESAELRLSHLHFG--YKSDETLIASRQEERQETSAE 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 703 REMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEA---QKRLYEKD--------------LTTSQEAVAKEIREDT 765
Cdd:pfam12128 288 LNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEAledQHGAFLDAdietaaadqeqlpsWQSELENLEERLKALT 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 766 DAH--------RRKAALEEHMFQKL------LENSQMGGRRAQRVMEDNLAKAEQAcLNADWQIQTLHKQKCADQQRS-- 829
Cdd:pfam12128 368 GKHqdvtakynRRRSKIKEQNNRDIagikdkLAKIREARDRQLAVAEDDLQALESE-LREQLEAGKLEFNEEEYRLKSrl 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 830 ---QGYYDVATL---LRENRRKEVEVLNAMMEEEAQKWKEAEEKEFHLQSAKKAS-----ALSDASRKWFLRQETSAALE 898
Cdd:pfam12128 447 gelKLRLNQATAtpeLLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRdqaseALRQASRRLEERQSALDELE 526
|
....*
gi 568991892 899 HEEMP 903
Cdd:pfam12128 527 LQLFP 531
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
627-868 |
4.01e-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: 49.92 E-value: 4.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 627 MQAEVDEQRA-----KDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELeikEIHLQDAARRRLLKLQQD 701
Cdd:pfam13868 20 CNKERDAQIAekkriKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQEL---EEQIEEREQKRQEEYEEK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 702 QREMEL-----RRLEDEIERKVQMRDQEIAATAKDL--------EIRQLELEAQKRL------YEKDLTTSQEAVAKEIR 762
Cdd:pfam13868 97 LQEREQmdeivERIQEEDQAEAEEKLEKQRQLREEIdefneeqaEWKELEKEEEREEderileYLKEKAEREEEREAERE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 763 EDTDAH-RRKAALEEHMFQKLLENSQMGGRRAQRVMEDNLAKAEQAclnadwQIQTLHKQKCADQQRSQGYYDVATLLRE 841
Cdd:pfam13868 177 EIEEEKeREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQK------EREEAEKKARQRQELQQAREEQIELKER 250
|
250 260
....*....|....*....|....*..
gi 568991892 842 NRRKEVEVLNAMMEEEAQKWKEAEEKE 868
Cdd:pfam13868 251 RLAEEAEREEEEFERMLRKQAEDEEIE 277
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
611-874 |
4.60e-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: 50.83 E-value: 4.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 611 RNDELDFLRERqtVENMQAEVDEQRAKDEAWYQKQE--------LLRRAEETRREI---------LLQEEEKMAQQRQRL 673
Cdd:TIGR02168 675 RRREIEELEEK--IEELEEKIAELEKALAELRKELEeleeeleqLRKELEELSRQIsalrkdlarLEAEVEQLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 674 aavkrELEIKEIhlqdAARRRLLKLQQDQREMELRRLEDEIErKVQMRDQEIAATAKDLEIRQLELEAQKRLYEKDLTTS 753
Cdd:TIGR02168 753 -----SKELTEL----EAEIEELEERLEEAEEELAEAEAEIE-ELEAQIEQLKEELKALREALDELRAELTLLNEEAANL 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 754 QEAVAKE-------IREDTDAHRRKAALEEHMfqKLLENSQMGGRRAQRVMEDNLAKAEQAclnADWQIQTLHKQKCADQ 826
Cdd:TIGR02168 823 RERLESLerriaatERRLEDLEEQIEELSEDI--ESLAAEIEELEELIEELESELEALLNE---RASLEEALALLRSELE 897
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 568991892 827 QRSQGYYDVATLLRENRRkEVEVLNAMMEEEAQKWKEAEEKEFHLQSA 874
Cdd:TIGR02168 898 ELSEELRELESKRSELRR-ELEELREKLAQLELRLEGLEVRIDNLQER 944
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
642-924 |
6.25e-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: 50.44 E-value: 6.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 642 YQKQELlrraEETRREILLQEEeKMAQQRQRLAAVKRELEIKEIHLQDAARRRLLKLQQ-DQREMELRRLEDEIERKVQM 720
Cdd:TIGR02168 674 ERRREI----EELEEKIEELEE-KIAELEKALAELRKELEELEEELEQLRKELEELSRQiSALRKDLARLEAEVEQLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 721 RDQeiaatakdLEIRQLELEAQKRLYEKDLTTSQ------EAVAKEIREDTDAHRRKAALEEHMFQKL---LENSQMGGR 791
Cdd:TIGR02168 749 IAQ--------LSKELTELEAEIEELEERLEEAEeelaeaEAEIEELEAQIEQLKEELKALREALDELraeLTLLNEEAA 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 792 RAQRVMEDNLAKAEQaclnADWQIQTLHKQKcadqqrsqgyydvatllrENRRKEVEVLNAMMEEEAQKWKEAEEKEFHL 871
Cdd:TIGR02168 821 NLRERLESLERRIAA----TERRLEDLEEQI------------------EELSEDIESLAAEIEELEELIEELESELEAL 878
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 568991892 872 QSAKKASALSDASRKWFLRQETSAALEHEEmpwlQRQYMDSAYLPQTSRLHDV 924
Cdd:TIGR02168 879 LNERASLEEALALLRSELEELSEELRELES----KRSELRRELEELREKLAQL 927
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
650-867 |
6.83e-06 |
|
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: 49.95 E-value: 6.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 650 RAEETRREILLQEEEKMAQQRQRL---AAVKRELEIKEIHLQDAARRRLlklQQDQREMElRRLEDEIERKVQMRDQEIA 726
Cdd:pfam15709 315 RSEEDPSKALLEKREQEKASRDRLraeRAEMRRLEVERKRREQEEQRRL---QQEQLERA-EKMREELELEQQRRFEEIR 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 727 atakdLEIRQLELEAQKRLYEKDLTTSQEAVAKE-IREDTDAHRRKaaLEEHMFQKLLENSQMGGRRAQRVMEDNLAKAE 805
Cdd:pfam15709 391 -----LRKQRLEEERQRQEEEERKQRLQLQAAQErARQQQEEFRRK--LQELQRKKQQEEAERAEAEKQRQKELEMQLAE 463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568991892 806 QACLNADWQiqtlHKQKCADQQRSQGYYDVATLLRENRRKEVEVLNAMMEEEAQkwKEAEEK 867
Cdd:pfam15709 464 EQKRLMEMA----EEERLEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEAM--KQAQEQ 519
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
603-788 |
7.26e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 7.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 603 QTREWERIRNDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREiLLQEEEKMAQQRQRLAAVKRelei 682
Cdd:COG4717 86 KEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAE-LAELPERLEELEERLEELRE---- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 683 keihlqdaarrrlLKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEKDLTTSQEAVaKEIR 762
Cdd:COG4717 161 -------------LEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEEL-EELE 226
|
170 180
....*....|....*....|....*.
gi 568991892 763 EDTDAHRRKAALEEhMFQKLLENSQM 788
Cdd:COG4717 227 EELEQLENELEAAA-LEERLKEARLL 251
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
606-828 |
8.36e-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: 49.07 E-value: 8.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 606 EWERIRNDELDFLR-ERQT---VENMQAEVDEQRAKDEAwyQKQELLRRAEEtrreillQEEEKMAQQRQRLAAVKR--E 679
Cdd:TIGR02794 51 QANRIQQQKKPAAKkEQERqkkLEQQAEEAEKQRAAEQA--RQKELEQRAAA-------EKAAKQAEQAAKQAEEKQkqA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 680 LEIKEIHLQDAARRRLLKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKdleiRQLELEAQKrlyEKDltTSQEAVAK 759
Cdd:TIGR02794 122 EEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAK----KKAEAEAKA---KAE--AEAKAKAE 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568991892 760 EIREDTDAHRRKAALEEHMfqkllensqmgGRRAQRVMEDNLAKAEQACLNADWQIQTLHKQKCADQQR 828
Cdd:TIGR02794 193 EAKAKAEAAKAKAAAEAAA-----------KAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQG 250
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
621-776 |
1.43e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 621 RQTVENMQAEVDE-QRAKDEAWYQKQELLRRAEETRREILlQEEEKMAQQRQRLAAVKRELEIKEI------------HL 687
Cdd:COG3883 36 QAELDALQAELEElNEEYNELQAELEALQAEIDKLQAEIA-EAEAEIEERREELGERARALYRSGGsvsyldvllgseSF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 688 QDAARRRLL--KLQQDQREM--ELRRLEDEIERKvqmrDQEIAATAKDLEIRQLELEAQKRLYEKDLTTSQEAVAKEIRE 763
Cdd:COG3883 115 SDFLDRLSAlsKIADADADLleELKADKAELEAK----KAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAE 190
|
170
....*....|...
gi 568991892 764 DTDAHRRKAALEE 776
Cdd:COG3883 191 EAAAEAQLAELEA 203
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
619-911 |
1.43e-05 |
|
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: 49.28 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 619 RERQTVENMQAEVDEQRAKdEAWYQKQELLRRAEETRReiLLQEEEKMAQQRQRLAAVKRELEIK--EIHLQDA-ARRRL 695
Cdd:TIGR02168 207 RQAEKAERYKELKAELREL-ELALLVLRLEELREELEE--LQEELKEAEEELEELTAELQELEEKleELRLEVSeLEEEI 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 696 LKLQQDQREM--ELRRLEDEIERKVQmRDQEIAATAKDLEIRQLELEAQKRLYEKDLTTSQE--AVAKEIREDTdahrrK 771
Cdd:TIGR02168 284 EELQKELYALanEISRLEQQKQILRE-RLANLERQLEELEAQLEELESKLDELAEELAELEEklEELKEELESL-----E 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 772 AALEEhmFQKLLENSQMGGRRAQRVMED-----NLAKAEQACLNAdwQIQTLHKQKCADQQR----SQGYYDVATLLREN 842
Cdd:TIGR02168 358 AELEE--LEAELEELESRLEELEEQLETlrskvAQLELQIASLNN--EIERLEARLERLEDRrerlQQEIEELLKKLEEA 433
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 843 RRKEV-EVLNAMMEEEAQKWKEAEEKEFHLQSAKKASALSDASRKWFLRQETSAALEHEEMPWLQRQYMD 911
Cdd:TIGR02168 434 ELKELqAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
629-776 |
1.47e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 48.72 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 629 AEVDEQRAKDEAwyqkqELLRRAEETRREILLQEEEKMAQQrqrlaavKRELEIKEIHLQDAARRRllKLQQDQREMELR 708
Cdd:COG2268 195 AEIIRDARIAEA-----EAERETEIAIAQANREAEEAELEQ-------EREIETARIAEAEAELAK--KKAEERREAETA 260
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568991892 709 RLEDEIERKVQmrdQEIAATAKDLEIRQLELEAQKRLYEKDLTTSQEAVAKEIREDTDAHRRKAALEE 776
Cdd:COG2268 261 RAEAEAAYEIA---EANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEA 325
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
622-807 |
1.79e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 48.80 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 622 QTVENMQAEVDeqraKDEAWYQKQELLRRAEETRreillqeeeKMAQQRQRLAAVKRELEiKEIHLQDAARRRL------ 695
Cdd:COG3096 479 ELVCKIAGEVE----RSQAWQTARELLRRYRSQQ---------ALAQRLQQLRAQLAELE-QRLRQQQNAERLLeefcqr 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 696 ----------LKLQQDQREMELRRLEDE----IERKVQMRDQEIAATAKDLEIRQLE---LEAQKRlyekdLTTSQEAVA 758
Cdd:COG3096 545 igqqldaaeeLEELLAELEAQLEELEEQaaeaVEQRSELRQQLEQLRARIKELAARApawLAAQDA-----LERLREQSG 619
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 568991892 759 KEIredTDAHrrkaALEEHMfQKLLENsqmggRRAQRVMEDNLAKAEQA 807
Cdd:COG3096 620 EAL---ADSQ----EVTAAM-QQLLER-----EREATVERDELAARKQA 655
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
611-874 |
1.82e-05 |
|
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: 48.11 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 611 RNDELDFLRERQTVENMQAEvdEQRAKDEawyQKQELLRRaeETRREILLQEEEKMAQQRQRLAAVKRELE------IKE 684
Cdd:pfam15558 16 RHKEEQRMRELQQQAALAWE--ELRRRDQ---KRQETLER--ERRLLLQQSQEQWQAEKEQRKARLGREERrradrrEKQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 685 IHLQDAARRRLLKLQQDQRE--MELRRLEDEIERKVQMRD-QEIAATAKDLEIRQlELEAQKRLyekdlttsQEAVAKEI 761
Cdd:pfam15558 89 VIEKESRWREQAEDQENQRQekLERARQEAEQRKQCQEQRlKEKEEELQALREQN-SLQLQERL--------EEACHKRQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 762 REDTDAHRRKAALEehmfQKLLENSQmggrrAQRVMEDNLAKAEQACLNADWQIQTLHKQ---KCADQQRSQGyydvatl 838
Cdd:pfam15558 160 LKEREEQKKVQENN----LSELLNHQ-----ARKVLVDCQAKAEELLRRLSLEQSLQRSQenyEQLVEERHRE------- 223
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 568991892 839 LRENRRKEVEVLN------AMMEEEAQKWKEA--EEKEFHLQSA 874
Cdd:pfam15558 224 LREKAQKEEEQFQrakwraEEKEEERQEHKEAlaELADRKIQQA 267
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
694-879 |
2.20e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 48.20 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 694 RLLKLQQD--QREMELRRLEDEIERKVqmrdqeiAATAKDLEI---RQLELEAQKRLYEKDLTTSQEAvakeIREDTDAH 768
Cdd:pfam05557 10 RLSQLQNEkkQMELEHKRARIELEKKA-------SALKRQLDResdRNQELQKRIRLLEKREAEAEEA----LREQAELN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 769 RRKAALEEHMFQKLLENSQMGG--RRAQRVMEDNLAKAEQACLNADWQIQTLhkqkcadqqrsqgyydvatllrenrRKE 846
Cdd:pfam05557 79 RLKKKYLEALNKKLNEKESQLAdaREVISCLKNELSELRRQIQRAELELQST-------------------------NSE 133
|
170 180 190
....*....|....*....|....*....|...
gi 568991892 847 VEVLNAMMEEEAQKWKEAEEKEFHLQSAKKASA 879
Cdd:pfam05557 134 LEELQERLDLLKAKASEAEQLRQNLEKQQSSLA 166
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
604-873 |
2.88e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 48.25 E-value: 2.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 604 TREWERIRNdeLDFLRERQtvENMQAEVDEQRAKDEAWYQKQELLRRAEETRREILlqeEEKMAQQRQRLAAVKRELEIK 683
Cdd:pfam01576 169 AEEEEKAKS--LSKLKNKH--EAMISDLEERLKKEEKGRQELEKAKRKLEGESTDL---QEQIAELQAQIAELRAQLAKK 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 684 EIHLQDAARR------RLLKLQQDQREME--LRRLEDEIERKVQMRDQeIAATAKDLEirqLELEAQKRLYEKDLTTS-- 753
Cdd:pfam01576 242 EEELQAALARleeetaQKNNALKKIRELEaqISELQEDLESERAARNK-AEKQRRDLG---EELEALKTELEDTLDTTaa 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 754 -QEAVAKEIREDTDAhrrKAALEEHMFQKLLENSQMGGRRAQRVME--DNLAKAEQACLNADWQIQTLHKQ----KCADQ 826
Cdd:pfam01576 318 qQELRSKREQEVTEL---KKALEEETRSHEAQLQEMRQKHTQALEEltEQLEQAKRNKANLEKAKQALESEnaelQAELR 394
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 568991892 827 QRSQGYYDVatllrENRRKEVEV----LNAMMEEEAQKWKEAEEKEFHLQS 873
Cdd:pfam01576 395 TLQQAKQDS-----EHKRKKLEGqlqeLQARLSESERQRAELAEKLSKLQS 440
|
|
| COG5210 |
COG5210 |
GTPase-activating protein [General function prediction only]; |
457-573 |
3.26e-05 |
|
GTPase-activating protein [General function prediction only];
Pssm-ID: 227535 [Multi-domain] Cd Length: 496 Bit Score: 47.49 E-value: 3.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 457 LSMIENVLAFHDKELLQHFIDRDITSQVYAWPLLETLFSEVLTREEWLRLFDNIFSNHPSFLLMTVVAYSTCSRAPLLNC 536
Cdd:COG5210 350 LKVLDDLVEELDPELYEHLLREGVVLLMFAFRWFLTLFVREFPLEYALRIWDCLFLEGSSMLFQLALAILKLLRDKLLKL 429
|
90 100 110
....*....|....*....|....*....|....*..
gi 568991892 537 TLKNDFEYFFHHRNNLDINVVIREVYHLMETTPADIH 573
Cdd:COG5210 430 DSDELLDLLLKQLFLHSGKEAWSSILKFRHGTDRDIL 466
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
618-868 |
4.16e-05 |
|
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: 47.66 E-value: 4.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 618 LRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEE---TRREIL------------LQEEEKMAQQRQRLAAVKRELEI 682
Cdd:TIGR00618 327 LMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEvatSIREIScqqhtltqhihtLQQQKTTLTQKLQSLCKELDILQ 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 683 KEIHLQDAARRRLLKLQQDqremeLRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEK-DLTTSQEAVAKEI 761
Cdd:TIGR00618 407 REQATIDTRTSAFRDLQGQ-----LAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSlKEREQQLQTKEQI 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 762 redTDAHRRKAALEEHMFQKLLEN--------------------SQMGGRRAQRVmEDNLAKAEQACLNADWQIQTLHKQ 821
Cdd:TIGR00618 482 ---HLQETRKKAVVLARLLELQEEpcplcgscihpnparqdidnPGPLTRRMQRG-EQTYAQLETSEEDVYHQLTSERKQ 557
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 568991892 822 KCADQQRSQGYYDVATLLRENRRKEVEVLNAM--MEEEAQKWKEAEEKE 868
Cdd:TIGR00618 558 RASLKEQMQEIQQSFSILTQCDNRSKEDIPNLqnITVRLQDLTEKLSEA 606
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
604-902 |
4.22e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 47.11 E-value: 4.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 604 TREWERIRNDELDflrerqtvenmQAEVDEQRAKDEAwyqkqellRRAEETRREILLQEEEKMAQQRQRLAAvkreLEIK 683
Cdd:PRK09510 61 VEQYNRQQQQQKS-----------AKRAEEQRKKKEQ--------QQAEELQQKQAAEQERLKQLEKERLAA----QEQK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 684 EihlQDAARRRLLKLQQDQREmelrrledeierkvqmrdqeiAATAKDLEIRQLELEAQ-KRLyekdlttsqEAVAKEIR 762
Cdd:PRK09510 118 K---QAEEAAKQAALKQKQAE---------------------EAAAKAAAAAKAKAEAEaKRA---------AAAAKKAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 763 EDTDAhrrKAALEEhmfqkllensqmggrrAQRVMEDNLAKAEQAClnadwqiqtlhKQKCADqqrsqgyydvatllrEN 842
Cdd:PRK09510 165 AEAKK---KAEAEA----------------AKKAAAEAKKKAEAEA-----------AAKAAA---------------EA 199
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 843 RRKEVEVLNAMMEEEAQKWKEAEEKEFHLQSAKKASALSDASRKWFLRQETSAALEHEEM 902
Cdd:PRK09510 200 KKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
612-784 |
4.93e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 4.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 612 NDELDFLRERQTVENMQAEVDEQ----RAKDEAWYQKQELLRRAEETRREIllqeeekmAQQRQRLAAVKRELeikeihl 687
Cdd:COG4913 637 EAELDALQERREALQRLAEYSWDeidvASAEREIAELEAELERLDASSDDL--------AALEEQLEELEAEL------- 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 688 qDAARRRLLKLQQDQR--EMELRRLEDEIERKvqmrdQEIAATAKDLEIRQLELEAQKRLYEKDLTTSQEAVAKEIREDT 765
Cdd:COG4913 702 -EELEEELDELKGEIGrlEKELEQAEEELDEL-----QDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERI 775
|
170
....*....|....*....
gi 568991892 766 DAHRRKAALEEHMFQKLLE 784
Cdd:COG4913 776 DALRARLNRAEEELERAMR 794
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
619-747 |
5.54e-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: 44.26 E-value: 5.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 619 RERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELEIKEIHLQDAARRRLLKL 698
Cdd:pfam05672 19 KRRQAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQRKAEEEAEEREQREQEEQER 98
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 568991892 699 QQDQREMELRRLEDEIERKVQMRDQEIaatakdLEIRQLELEAQKRLYE 747
Cdd:pfam05672 99 LQKQKEEAEAKAREEAERQRQEREKIM------QQEEQERLERKKRIEE 141
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
30-68 |
6.54e-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: 6.54e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 568991892 30 TKELVSWMRGHESSVCSISVHASGRYAITTSSD-TAQLWD 68
Cdd:smart00320 1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDgTIKLWD 40
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
603-880 |
7.08e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.06 E-value: 7.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 603 QTREWERIRNDEldflrERQTVENMQAEVDEQRAKDE----AWYQKQELLRRAEETRREILLQEEEK-MAQQRQRLAAVK 677
Cdd:PTZ00121 1216 EARKAEDAKKAE-----AVKKAEEAKKDAEEAKKAEEernnEEIRKFEEARMAHFARRQAAIKAEEArKADELKKAEEKK 1290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 678 RELEIKEIHLQDAARRRLLKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEKDLTTSQEAV 757
Cdd:PTZ00121 1291 KADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAE 1370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 758 AK--EIREDTDAHRRKAAlEEHMFQKLLENSQMGGRRAqrvmeDNLAKAEQACLNADWQIQTLHKQKCADQQRSQGyydv 835
Cdd:PTZ00121 1371 KKkeEAKKKADAAKKKAE-EKKKADEAKKKAEEDKKKA-----DELKKAAAAKKKADEAKKKAEEKKKADEAKKKA---- 1440
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 568991892 836 atllrENRRKEVEvlnamMEEEAQKWKEAEEKEFHLQSAKKASAL 880
Cdd:PTZ00121 1441 -----EEAKKADE-----AKKKAEEAKKAEEAKKKAEEAKKADEA 1475
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
601-776 |
7.55e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 7.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 601 DYQTREWERIRnDELDFLRErqtvenmqAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKREL 680
Cdd:COG4717 315 ELEEEELEELL-AALGLPPD--------LSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEE 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 681 EIKEIHLQDAARRRLLKlQQDQREMELRRLEDEIERKVQMRDQEiaatakDLEIRQLELEAQKRLYEKDLTTSQEAVA-- 758
Cdd:COG4717 386 ELRAALEQAEEYQELKE-ELEELEEQLEELLGELEELLEALDEE------ELEEELEELEEELEELEEELEELREELAel 458
|
170 180
....*....|....*....|..
gi 568991892 759 ----KEIREDTDAHRRKAALEE 776
Cdd:COG4717 459 eaelEQLEEDGELAELLQELEE 480
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
628-762 |
8.31e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 46.24 E-value: 8.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 628 QAEVDEQRAKDEAWYQKQELLRRAEET-------RREILLQEEEKMAQQRQRLAAVKRELEIKEIHLqdAARRRLLKLQQ 700
Cdd:PRK12705 41 EAQKEAEEKLEAALLEAKELLLRERNQqrqearrEREELQREEERLVQKEEQLDARAEKLDNLENQL--EEREKALSARE 118
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568991892 701 DQREMELRRLEDEIERKVQMRDQEiaatAKDLEIRQL--ELEAQK-RLYEKDLTTSQEAVAKEIR 762
Cdd:PRK12705 119 LELEELEKQLDNELYRVAGLTPEQ----ARKLLLKLLdaELEEEKaQRVKKIEEEADLEAERKAQ 179
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
604-901 |
8.52e-05 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 46.74 E-value: 8.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 604 TREWERIRNDELdflrERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREI------LLQEEEKMAQQRQ------ 671
Cdd:NF041483 501 TAESERVRTEAI----ERATTLRRQAEETLERTRAEAERLRAEAEEQAEEVRAAAeraareLREETERAIAARQaeaaee 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 672 ----------RLAAVKREL----------------EIKEIHLQDAARRRLLklqQDQREMELRRLEDEIERKVQMRDQEI 725
Cdd:NF041483 577 ltrlhteaeeRLTAAEEALadaraeaerirreaaeETERLRTEAAERIRTL---QAQAEQEAERLRTEAAADASAARAEG 653
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 726 AATAKDL------EIRQLELEAQK---RLyEKDLTTSQEAVAKEIRE-----DTDAHRRKAALEEHMFQKLLENSQMGGr 791
Cdd:NF041483 654 ENVAVRLrseaaaEAERLKSEAQEsadRV-RAEAAAAAERVGTEAAEalaaaQEEAARRRREAEETLGSARAEADQERE- 731
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 792 RAQRVMEDNLAKAEQACLNADWQIQTLHKQK--------CADQQRSQGYYDVATLLRENRRKEVEVLNAMMEEEAQKWK- 862
Cdd:NF041483 732 RAREQSEELLASARKRVEEAQAEAQRLVEEAdrratelvSAAEQTAQQVRDSVAGLQEQAEEEIAGLRSAAEHAAERTRt 811
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 568991892 863 EAEEKEFHLQS---AKKASALSDASR-KWFLRQETSAALEHEE 901
Cdd:NF041483 812 EAQEEADRVRSdayAERERASEDANRlRREAQEETEAAKALAE 854
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
659-874 |
9.38e-05 |
|
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: 45.91 E-value: 9.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 659 LLQEEEKMAQQRQRLAAVKRELEIKEIHLQDAARRRLLKLQQ----DQREMELRRLEDEIERKVQMRDQEIAATAKDLEI 734
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQlaalERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 735 RQLELEAQKRLYEKDLTTSQ-------EAVAKEIREDTDAHRRKAALEehmfqkllensQMGGRRAQRVMEDNLAKAEQA 807
Cdd:COG4942 95 LRAELEAQKEELAELLRALYrlgrqppLALLLSPEDFLDAVRRLQYLK-----------YLAPARREQAEELRADLAELA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568991892 808 CLNADWQIQTLHKQKCADQQRSQgyYDVATLLRENRRKEVEVLNAMMEEEAQKWKEAEEKEFHLQSA 874
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEE--RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
614-764 |
9.58e-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: 44.92 E-value: 9.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 614 ELDFLRERQtvENMQAEVDEQRAKDEAWYQKQELLRRA-EETRREILLQEEE------KMAQQRQRLAAVK--RELEI-- 682
Cdd:COG1579 18 ELDRLEHRL--KELPAELAELEDELAALEARLEAAKTElEDLEKEIKRLELEieeveaRIKKYEEQLGNVRnnKEYEAlq 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 683 KEIHLqdaarrrlLKLQQDQREMELRRLEDEIERKVQMRDQ---EIAATAKDLEIRQLELEAQKRLYEKD---LTTSQEA 756
Cdd:COG1579 96 KEIES--------LKRRISDLEDEILELMERIEELEEELAEleaELAELEAELEEKKAELDEELAELEAEleeLEAEREE 167
|
....*...
gi 568991892 757 VAKEIRED 764
Cdd:COG1579 168 LAAKIPPE 175
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
599-805 |
9.81e-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: 46.60 E-value: 9.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 599 IVDYQTREWERIRN--DELDFL-RERQTVENMQAEVD---EQRAKDEAWYQKQ--ELLRRAEETRREILLQEEEKMAQQR 670
Cdd:TIGR02169 728 LEQEEEKLKERLEEleEDLSSLeQEIENVKSELKELEariEELEEDLHKLEEAlnDLEARLSHSRIPEIQAELSKLEEEV 807
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 671 QRLAAVKRELEIKEihlqdaaRRRLLKLQQDQREM-ELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEaQKRLYEKD 749
Cdd:TIGR02169 808 SRIEARLREIEQKL-------NRLTLEKEYLEKEIqELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELE-ELEAALRD 879
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568991892 750 LTTSQEAVAKEiREDTDAHRRKA--ALEEHMFQKLLENSQMGGRRAQR-VMEDNLAKAE 805
Cdd:TIGR02169 880 LESRLGDLKKE-RDELEAQLRELerKIEELEAQIEKKRKRLSELKAKLeALEEELSEIE 937
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
628-765 |
1.09e-04 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 44.49 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 628 QAEVDEQRAKDEAwyqKQEllrrAEETRREILLQEEEKMAQQRQRLaavkrELEIKEihlqdaaRRRLLKLQQD---QRE 704
Cdd:pfam12072 31 SAEELAKRIIEEA---KKE----AETKKKEALLEAKEEIHKLRAEA-----ERELKE-------RRNELQRQERrllQKE 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568991892 705 MEL-RRLE--DEIERKVQMRDQEIAATAKDLEIRQLELEA-----QKRLYEKDLTTSQEA-------VAKEIREDT 765
Cdd:pfam12072 92 ETLdRKDEslEKKEESLEKKEKELEAQQQQLEEKEEELEElieeqRQELERISGLTSEEAkeilldeVEEELRHEA 167
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
605-784 |
1.19e-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: 45.29 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 605 REWERIRNDELD-----FLRERQ-TVENMQAEVDEQRAKDEAWYQK----QELLRRAEETRREIL--LQEEEKMAQQRQR 672
Cdd:pfam13868 143 KELEKEEEREEDerileYLKEKAeREEEREAEREEIEEEKEREIARlraqQEKAQDEKAERDELRakLYQEEQERKERQK 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 673 LaavkRELEIKEIHLQDA---ARRRLLKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEKD 749
Cdd:pfam13868 223 E----REEAEKKARQRQElqqAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQ 298
|
170 180 190
....*....|....*....|....*....|....*
gi 568991892 750 LTTSQEAVAKEIREDTDAHRRKAALEEHMFQKLLE 784
Cdd:pfam13868 299 IEEREEQRAAEREEELEEGERLREEEAERRERIEE 333
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
606-723 |
1.21e-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: 43.49 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 606 EWERIRNDELdflRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEEKMA-QQRQRLAAVKRELEike 684
Cdd:pfam05672 39 EEERLRKEEL---RRRAEEERARREEEARRLEEERRREEEERQRKAEEEAEEREQREQEEQErLQKQKEEAEAKARE--- 112
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 568991892 685 ihlqDAARRRLLKLQQDQREMELR-----RLEdEIERKVQMRDQ 723
Cdd:pfam05672 113 ----EAERQRQEREKIMQQEEQERlerkkRIE-EIMKRTRKSDQ 151
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
605-773 |
1.59e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.70 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 605 REWERIRNDELDFLRERQTVEN-----MQAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRE 679
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAqleelEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 680 LEIKEIHLQDAARRRLLKLQQDQREMELRRLEDEIERKVQMRDQ----------------------EIAATAKDLEIRQL 737
Cdd:COG1196 459 EALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADyegflegvkaalllaglrglagAVAVLIGVEAAYEA 538
|
170 180 190
....*....|....*....|....*....|....*.
gi 568991892 738 ELEAQKRLYEKDLTTSQEAVAKEIREDTDAHRRKAA 773
Cdd:COG1196 539 ALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRA 574
|
|
| TBC |
smart00164 |
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and ... |
416-524 |
1.64e-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: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 416 AFP-FVKLFQNNQLIcFEVVATLIINWCQHWFEYFpnppinilsmienvLAFHDKELLQHFIDRDITSQVYAWPLLETLF 494
Cdd:smart00164 112 AFWcLVKLMERYGPN-FYLPDMSGLQLDLLQLDRL--------------VKEYDPDLYKHLKDLGITPSLYALRWFLTLF 176
|
90 100 110
....*....|....*....|....*....|
gi 568991892 495 SEVLTREEWLRLFDNIFSNHPSFLLMTVVA 524
Cdd:smart00164 177 ARELPLEIVLRIWDVLFAEGSDFLFRVALA 206
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
645-879 |
2.12e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 45.18 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 645 QELLRRAEETRReiLLQEEEKMAQQRQRL-AAVKRELEIKEiHLQDAARrrllklQQDQREMELRRLEDEIERKVQMRDQ 723
Cdd:PRK10246 558 KQLQRDESEAQS--LRQEEQALTQQWQAVcASLNITLQPQD-DIQPWLD------AQEEHERQLRLLSQRHELQGQIAAH 628
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 724 E--IAATAKDLEIRQLELEAQKRLY------EKDLTTSQEAVAKEIREDTDAHRRKAALEEHMFQ-----KLLENSQMGG 790
Cdd:PRK10246 629 NqqIIQYQQQIEQRQQQLLTALAGYaltlpqEDEEASWLATRQQEAQSWQQRQNELTALQNRIQQltpllETLPQSDDLP 708
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 791 RRAQRVMEDNLAKAEQACLNADWQIQTLHKQKCADQQR-SQGYYDVATLLRENRRKEVEV-LNAMMEEEAQKWKEAEEK- 867
Cdd:PRK10246 709 HSEETVALDNWRQVHEQCLSLHSQLQTLQQQDVLEAQRlQKAQAQFDTALQASVFDDQQAfLAALLDEETLTQLEQLKQn 788
|
250
....*....|...
gi 568991892 868 -EFHLQSAKKASA 879
Cdd:PRK10246 789 lENQRQQAQTLVT 801
|
|
| EVC2_like |
pfam12297 |
Ellis van Creveld protein 2 like protein; This family of proteins is found in eukaryotes. ... |
604-788 |
2.73e-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: 44.69 E-value: 2.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 604 TREWERIRNDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQELLRR-----AEETRREILLQEEEKMAQQRQRLaAVKR 678
Cdd:pfam12297 223 AAECNLETREKMEAQHQREMAEKEEAEELLKHADEQEALECSSLLDKlhkleQEHLQRSLLLRQEEDFAKAQRQL-AVFQ 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 679 ELEIKEI---HLQDAARRRLLKLQQDQREM-ELRRLEDEIERkvqMRDQEIAATAKDLEIR--QLE-----LEAQKRLYE 747
Cdd:pfam12297 302 RVELHKIfftQLKEATRKGELKPEAAKRLLqDYSKIQEQIEE---LMDFFQANQRYHLSERfaQREylvqsLQSLETRVS 378
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 568991892 748 KDLTTSQEAVAKEIREdtdaHRRKAALEEHMFQKLLENSQM 788
Cdd:pfam12297 379 GLLNTAATQLTSLIQK----MERAGYLDEEQMEMLLERAQK 415
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
617-808 |
2.86e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 44.70 E-value: 2.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 617 FLRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREillqeeekMAQQRQRLAAVKRELEIKEihlqdaarRRLL 696
Cdd:PRK12705 24 LLKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRE--------RNQQRQEARREREELQREE--------ERLV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 697 KL--QQDQREMELRRLEDEIERkvqmRDQEIAATAKDLEIRQLELEAqkRLYEKDLTTSQEAVAKEIRE-DTDAHRRKAA 773
Cdd:PRK12705 88 QKeeQLDARAEKLDNLENQLEE----REKALSARELELEELEKQLDN--ELYRVAGLTPEQARKLLLKLlDAELEEEKAQ 161
|
170 180 190
....*....|....*....|....*....|....*
gi 568991892 774 LEEHMFQKLLENSQmggRRAQrvmeDNLAKAEQAC 808
Cdd:PRK12705 162 RVKKIEEEADLEAE---RKAQ----NILAQAMQRI 189
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
634-788 |
3.44e-04 |
|
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: 42.83 E-value: 3.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 634 QRAKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLaaVKRELEIKEIHLQDAARRRLLKLQQDQrEMELRRLEDE 713
Cdd:pfam14988 17 QKKIEKLWNQYVQECEEIERRRQELASRYTQQTAELQTQL--LQKEKEQASLKKELQALRPFAKLKESQ-EREIQDLEEE 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568991892 714 IErKVQmrdQEIAATAKDLEIRQLELEA--QKRLYEKDLTTSQEAVAKEIREDTDAHRRKA--ALEEHMFQKLLENSQM 788
Cdd:pfam14988 94 KE-KVR---AETAEKDREAHLQFLKEKAllEKQLQELRILELGERATRELKRKAQALKLAAkqALSEFCRSIKRENRQL 168
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
612-898 |
3.67e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 3.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 612 NDELDFLRER-QTVENMQAEVDEQRAKDEAWYQKQellRRAEETRREILLQEEEKMAQQRQRLAAVKRELEIKEIHLQDA 690
Cdd:PRK02224 341 NEEAESLREDaDDLEERAEELREEAAELESELEEA---REAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEEL 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 691 ARRR-LLKLQQDQREMELRRLEDEIERKVQMR-------------DQEIAATAKD-------LEIRQLELEAQKRLYEKD 749
Cdd:PRK02224 418 REERdELREREAELEATLRTARERVEEAEALLeagkcpecgqpveGSPHVETIEEdrerveeLEAELEDLEEEVEEVEER 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 750 LTTSQEAVAKEIREDTDAHRRKAA---LEEHMFQKLLENSQMGGRRAQ--------RVMEDNLAKAEQACLNADWQIQTL 818
Cdd:PRK02224 498 LERAEDLVEAEDRIERLEERREDLeelIAERRETIEEKRERAEELRERaaeleaeaEEKREAAAEAEEEAEEAREEVAEL 577
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 819 HKQKCADQQRSQGYYDVATLL---------RENRRKEVEVLNAMMEEEAQKWKEAEEKEFHLQSAKKASALSDASRKwfl 889
Cdd:PRK02224 578 NSKLAELKERIESLERIRTLLaaiadaedeIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARIEEARED--- 654
|
....*....
gi 568991892 890 RQETSAALE 898
Cdd:PRK02224 655 KERAEEYLE 663
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
612-756 |
4.25e-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: 4.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 612 NDELDFLRER-QTVENMQAEVDEQRAKDEAWYQK-QELLRRAEETRREI------------LLQEEEKMAQQRQRL---- 673
Cdd:COG3206 211 SEEAKLLLQQlSELESQLAEARAELAEAEARLAAlRAQLGSGPDALPELlqspviqqlraqLAELEAELAELSARYtpnh 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 674 ---AAVKRELEIKEIHLQDAARRRLLKLQQD-----QREMELRRLEDEIERKVQmrdqEIAATAKDLEIRQLELEAQKRL 745
Cdd:COG3206 291 pdvIALRAQIAALRAQLQQEAQRILASLEAElealqAREASLQAQLAQLEARLA----ELPELEAELRRLEREVEVAREL 366
|
170
....*....|.
gi 568991892 746 YEKDLTTSQEA 756
Cdd:COG3206 367 YESLLQRLEEA 377
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
608-882 |
4.34e-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: 4.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 608 ERIRNDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQEllRRAEETRREILLQEEEKMAQQRQRLAAVKRELEIKEIHL 687
Cdd:COG3064 16 ERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAE--EEAREAKAEAEQRAAELAAEAAKKLAEAEKAAAEAEKKA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 688 QDAARRRLLKLQQDQREmelrrledeiERKVQMRDQEIAATAKDLEIRQLELEAQKrlyEKDLTTSQEAVAKEIREDTDA 767
Cdd:COG3064 94 AAEKAKAAKEAEAAAAA----------EKAAAAAEKEKAEEAKRKAEEEAKRKAEE---ERKAAEAEAAAKAEAEAARAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 768 HRRKAALEEHMFQKLLENSQMGGRRAQRVMEDNLAKAEQACLNADWQIQTLHKQKCADQQRSQGYYDVATLLRENRRKEV 847
Cdd:COG3064 161 AAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEAT 240
|
250 260 270
....*....|....*....|....*....|....*
gi 568991892 848 EVLNAMMEEEAQKWKEAEEKEFHLQSAKKASALSD 882
Cdd:COG3064 241 EEAALGGAEEAADLAAVGVLGAALAAAAAGAAALS 275
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
612-717 |
4.83e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 43.70 E-value: 4.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 612 NDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAavKRELEIKEIHLQDAA 691
Cdd:pfam02029 211 NGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEQKLEELRRRRQEKESEEFEKLRQKQQ--EAELELEELKKKREE 288
|
90 100 110
....*....|....*....|....*....|....*..
gi 568991892 692 RRRLLKLQQDQR-----------EMELRRLEDEIERK 717
Cdd:pfam02029 289 RRKLLEEEEQRRkqeeaerklreEEEKRRMKEEIERR 325
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
615-787 |
5.27e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.85 E-value: 5.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 615 LDFLRERqtVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREI---------LLQEEEKMAQQRQRLAAVKRELEIKEI 685
Cdd:COG3206 177 LEFLEEQ--LPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLqqlselesqLAEARAELAEAEARLAALRAQLGSGPD 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 686 HLQDAA--------RRRLLKLQQDQREM---------ELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEK 748
Cdd:COG3206 255 ALPELLqspviqqlRAQLAELEAELAELsarytpnhpDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQA 334
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 568991892 749 DLTTSQEAVAK--EIREDTDAHRRKAALEEHMFQKLLENSQ 787
Cdd:COG3206 335 QLAQLEARLAElpELEAELRRLEREVEVARELYESLLQRLE 375
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
30-71 |
5.52e-04 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 43.36 E-value: 5.52e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 568991892 30 TKELVSWMRGHESSVCSISVHASGRYAITTSSD-TAQLWDLDT 71
Cdd:COG2319 361 TGELLRTLTGHTGAVTSVAFSPDGRTLASGSADgTVRLWDLAT 403
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
617-725 |
5.64e-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: 43.04 E-value: 5.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 617 FLRERQTVENM-----QAEVDEQRAKdEAWYQKQELLRRAEETRREILLQEEEKMAQQRQR----LAAVKRELEIKEIHL 687
Cdd:pfam02841 181 FLQSKEAVEEAilqtdQALTAKEKAI-EAERAKAEAAEAEQELLREKQKEEEQMMEAQERSyqehVKQLIEKMEAEREQL 259
|
90 100 110
....*....|....*....|....*....|....*...
gi 568991892 688 QDAARRRLLKLQQDQREMelrrLEDEIERKVQMRDQEI 725
Cdd:pfam02841 260 LAEQERMLEHKLQEQEEL----LKEGFKTEAESLQKEI 293
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
632-855 |
5.77e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 5.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 632 DEQRAKDEAWY-------QKQELLRRAEETRREIllqeeEKMAQQRQRLAAVKRELEIKEIHLQDAARRRLLKLQQDQRE 704
Cdd:COG4913 593 DDRRRIRSRYVlgfdnraKLAALEAELAELEEEL-----AEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAE 667
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 705 MELRRLEDEIERkvqmrdqeIAATAKDLEirqlELEAQKRLYEKDLTTSQEAVAKEIREDTDAHRRKAALEEhmfqkLLE 784
Cdd:COG4913 668 REIAELEAELER--------LDASSDDLA----ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEE-----ELD 730
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568991892 785 NSQmggrRAQRVMEDNLAKAEQACLNADWqiQTLHKQKCADQQRSQGYYDVATLLRENRRKEVEVLNAMME 855
Cdd:COG4913 731 ELQ----DRLEAAEDLARLELRALLEERF--AAALGDAVERELRENLEERIDALRARLNRAEEELERAMRA 795
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
621-868 |
5.80e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 5.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 621 RQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELEIKEIHLQDAARRRLlklQQ 700
Cdd:COG4372 51 REELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQ---DL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 701 DQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEKDLTTSQEAVAKEIREDtdaHRRKAALEEHMFQ 780
Cdd:COG4372 128 EQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKE---ANRNAEKEEELAE 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 781 KLLENSQMGGRRAQRVMEDNLAKAEQACLNADwQIQTLHKQKCADQQRSQGYYDVATLLRENRRKEVEVLNAMMEEEAQK 860
Cdd:COG4372 205 AEKLIESLPRELAEELLEAKDSLEAKLGLALS-ALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAAL 283
|
....*...
gi 568991892 861 WKEAEEKE 868
Cdd:COG4372 284 ELEALEEA 291
|
|
| Pinin_SDK_memA |
pfam04696 |
pinin/SDK/memA/ protein conserved region; Members of this family have very varied ... |
634-724 |
5.82e-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: 40.74 E-value: 5.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 634 QRAKDEAWYQKQELLRRAEETRREillqeEEKMAQQRQRLAAVKREleikeihlqdaaRRRLLKLQQDQREMELRRLEDE 713
Cdd:pfam04696 19 QKFKKEESKQKEKEERRAEIEKRL-----EEKAKQEKEELEERKRE------------EREELFEERRAEQIELRALEEK 81
|
90
....*....|.
gi 568991892 714 IERKVQMRDQE 724
Cdd:pfam04696 82 LELKELMETWH 92
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
603-775 |
5.96e-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: 43.90 E-value: 5.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 603 QTREWERIRND---ELDFLR-ERQTVENMQAEVDEQRAK-----DEAWYQKQELLRRAEETRREI--LLQEEEKMAQQRQ 671
Cdd:TIGR02169 813 RLREIEQKLNRltlEKEYLEkEIQELQEQRIDLKEQIKSiekeiENLNGKKEELEEELEELEAALrdLESRLGDLKKERD 892
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 672 RLAAVKRELEIK--EIHLQDAARRRLLKLQQDQREM---ELRRLEDEI------------ERKVQMRDQEIAATAKDLE- 733
Cdd:TIGR02169 893 ELEAQLRELERKieELEAQIEKKRKRLSELKAKLEAleeELSEIEDPKgedeeipeeelsLEDVQAELQRVEEEIRALEp 972
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568991892 734 -----IRQLElEAQKRLyeKDLTTSQEAVAKEIR------EDTDAHRRKAALE 775
Cdd:TIGR02169 973 vnmlaIQEYE-EVLKRL--DELKEKRAKLEEERKaileriEEYEKKKREVFME 1022
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
618-922 |
7.99e-04 |
|
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: 43.40 E-value: 7.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 618 LRERQTVENMQAEVDEQRAKdeawyqkqelLRRAEETRREilLQEEEKMAQQRQRLAavkrELEIKEIHLQDAARRRLLK 697
Cdd:COG3096 343 LRQQEKIERYQEDLEELTER----------LEEQEEVVEE--AAEQLAEAEARLEAA----EEEVDSLKSQLADYQQALD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 698 LQQD---QREMELRRLE--------DEI------ERKVQMRDQEIAATAKDLEIRQ-LEL-EAQKRLYEKDL-------- 750
Cdd:COG3096 407 VQQTraiQYQQAVQALEkaralcglPDLtpenaeDYLAAFRAKEQQATEEVLELEQkLSVaDAARRQFEKAYelvckiag 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 751 -TTSQEA--VAKEIREDTDAHRRKAALEEHMFQKL-----LENSQmggRRAQRVMEDnLAKAEQACLNADWQIQTLHKQK 822
Cdd:COG3096 487 eVERSQAwqTARELLRRYRSQQALAQRLQQLRAQLaeleqRLRQQ---QNAERLLEE-FCQRIGQQLDAAEELEELLAEL 562
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 823 CADQQRSQGYYDVATLLRENRRKEVEVLNAMMEEEAQK---WKEAEEKEFHL-----QSAKKASALSDAsRKWFLRQETS 894
Cdd:COG3096 563 EAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARapaWLAAQDALERLreqsgEALADSQEVTAA-MQQLLERERE 641
|
330 340
....*....|....*....|....*...
gi 568991892 895 AALEHEEMPwLQRQYMDSaylpQTSRLH 922
Cdd:COG3096 642 ATVERDELA-ARKQALES----QIERLS 664
|
|
| Fibrinogen_BP |
pfam08017 |
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family ... |
628-867 |
8.72e-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: 42.93 E-value: 8.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 628 QAEVDEQRAKDEAWYQKQELLRRAEetrREILLQEEEKMAQQRQRLAAVKRELEIKEIHLQDAARRRLLK-LQQDQREME 706
Cdd:pfam08017 27 QGNVLERRQRDAENRSQGNVLERRQ---RDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNvLERRQRDAE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 707 LRRLEDEIERKvqMRDQEIAATAKDLEIRQLELEAQkrlyekdlttSQEAVAKEIREDTDAHRRKAALEEHmfQKLLENS 786
Cdd:pfam08017 104 NRSQGNVLERR--QRDAENKSQGNVLERRQRDAENR----------SQGNVLERRQRDAENRSQGNVLERR--QRDAENR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 787 QMGG--RRAQRVMED----NLAKAEQACLNADWQIQTLHKQKCADQQRSQGyydvATLLRENRRKEVEVLNAMMEeeaQK 860
Cdd:pfam08017 170 SQGNvlERRQRDAENksqgNVLERRQRDAENRSQGNVLERRQRDAENRSQG----NVLERRQRDAENRSQGNVLE---RR 242
|
....*..
gi 568991892 861 WKEAEEK 867
Cdd:pfam08017 243 QRDAENK 249
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
608-750 |
9.01e-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: 41.83 E-value: 9.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 608 ERIRNDELDFLRERQTVENMQAEVDEQRAKDEawyQKQELLRRAEEtrREILLQEEEKMAQQRQRLAavKRELEIKEIHl 687
Cdd:COG1579 48 EAAKTELEDLEKEIKRLELEIEEVEARIKKYE---EQLGNVRNNKE--YEALQKEIESLKRRISDLE--DEILELMERI- 119
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568991892 688 qDAARRRLLKLQQdqremELRRLEDEIERKVQMRDQEIAATAKDLEirqlELEAQKRLYEKDL 750
Cdd:COG1579 120 -EELEEELAELEA-----ELAELEAELEEKKAELDEELAELEAELE----ELEAEREELAAKI 172
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
599-744 |
9.04e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.39 E-value: 9.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 599 IVDYQTREWERIRNDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEEKmAQQRQRLAAVKR 678
Cdd:COG1196 623 LGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLA-EEELELEEALLA 701
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568991892 679 ELEIKEIHLQDAARRRLLKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKR 744
Cdd:COG1196 702 EEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELER 767
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
610-902 |
9.09e-04 |
|
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: 43.02 E-value: 9.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 610 IRNDELDFLRERQTVENMQAEVD------EQRA--KDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELE 681
Cdd:COG5185 231 IEEALKGFQDPESELEDLAQTSDkleklvEQNTdlRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKA 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 682 IKEIHLQDAARRRLLKLQQDQRE--MELRRLEDEIERKVqmRDQEIAATAKDLEIRQLELEAQKRLYEKDL---TTSQEA 756
Cdd:COG5185 311 TESLEEQLAAAEAEQELEESKREteTGIQNLTAEIEQGQ--ESLTENLEAIKEEIENIVGEVELSKSSEELdsfKDTIES 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 757 VAKEIREDTDAHRRKA-----ALEEHMFQKLLENSQMGG--RRAQRVMED--NLAKAEQACLNadwQIQTLHKQKcADQQ 827
Cdd:COG5185 389 TKESLDEIPQNQRGYAqeilaTLEDTLKAADRQIEELQRqiEQATSSNEEvsKLLNELISELN---KVMREADEE-SQSR 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 828 RSQGYYDVATLLRENRRKEVEVLNaMMEEEAQKWKEAEEK-----EFHLQSAKKASALSDASRKWFLRQETSAALEHEEM 902
Cdd:COG5185 465 LEEAYDEINRSVRSKKEDLNEELT-QIESRVSTLKATLEKlraklERQLEGVRSKLDQVAESLKDFMRARGYAHILALEN 543
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
31-68 |
9.53e-04 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 37.71 E-value: 9.53e-04
10 20 30
....*....|....*....|....*....|....*....
gi 568991892 31 KELVSWMRGHESSVCSISVHASGRYAITTSSD-TAQLWD 68
Cdd:pfam00400 1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDgTVKVWD 39
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
611-744 |
1.13e-03 |
|
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: 42.71 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 611 RNDELDFLRER-----QTVENMQAEVDE-----QRAKDEAWYQKQELLRRAEETRR-----EILLQEEEKMAQ-QR---- 670
Cdd:pfam05667 333 REEELEELQEQledleSSIQELEKEIKKlessiKQVEEELEELKEQNEELEKQYKVkkktlDLLPDAEENIAKlQAlvda 412
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568991892 671 --QRLAAVKRELEIKEIHLQDAARRrlLKLQQDQREMELRRLEDEIER-KVQMRDQEIAATAKDLEIRQLELEAQKR 744
Cdd:pfam05667 413 saQRLVELAGQWEKHRVPLIEEYRA--LKEAKSNKEDESQRKLEEIKElREKIKEVAEEAKQKEELYKQLVAEYERL 487
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
608-777 |
1.26e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 608 ERIRNDELDFLRER-QTVENMQAEVDEQRAKDEAWYQKQELLRRAEEtRREILLQEEEKMAQQRQRLAAVKRELEIKEIH 686
Cdd:COG4717 49 ERLEKEADELFKPQgRKPELNLKELKELEEELKEAEEKEEEYAELQE-ELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 687 LQDAARRRLLKLQQDQREMELRRLEDEIERKVQMRDQeiaatakdleIRQLELEAQK------RLYEKDLTTSQEAVAKE 760
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEERLEELRELEEE----------LEELEAELAElqeeleELLEQLSLATEEELQDL 197
|
170
....*....|....*..
gi 568991892 761 IREDTDAHRRKAALEEH 777
Cdd:COG4717 198 AEELEELQQRLAELEEE 214
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
630-901 |
1.58e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 630 EVDEQR-----AKDEAwyqkQELLRRAEETRREILLQEEEkMAQQRQRLAAVKRELEIKEIHLQDaARRRLLKLQQDQRE 704
Cdd:PRK02224 224 RYEEQReqareTRDEA----DEVLEEHEERREELETLEAE-IEDLRETIAETEREREELAEEVRD-LRERLEELEEERDD 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 705 M----ELRRLEDEI---------ERKVQMRD----QEIAAT------------AKDLEIRQLELEAQKRLYEKDLTTSQE 755
Cdd:PRK02224 298 LlaeaGLDDADAEAvearreeleDRDEELRDrleeCRVAAQahneeaeslredADDLEERAEELREEAAELESELEEARE 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 756 AVAK------EIREDTDAHRRKAA--------LEEHMFQKLLENSQMGGRRAQ-----RVMEDNLAKAEqaclnadwqiQ 816
Cdd:PRK02224 378 AVEDrreeieELEEEIEELRERFGdapvdlgnAEDFLEELREERDELREREAEleatlRTARERVEEAE----------A 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 817 TLHKQKCAD-QQRSQGYYDVATLlrENRRKEVEVLNAMMEEEAQKWKEAEEKEFHLQSAKKASALSDASRKwflRQETSA 895
Cdd:PRK02224 448 LLEAGKCPEcGQPVEGSPHVETI--EEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEE---RREDLE 522
|
....*...
gi 568991892 896 AL--EHEE 901
Cdd:PRK02224 523 ELiaERRE 530
|
|
| Nop53 |
pfam07767 |
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ... |
629-748 |
1.60e-03 |
|
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: 41.90 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 629 AEVDEQRAKDEAwyQKQELLRRAEETRREILLQEEEKMAQQrQRLAAVKRELEIKEihlqdAARRRLLKLQQDQremeLR 708
Cdd:pfam07767 205 VEAEKKRLKEEE--KLERVLEKIAESAATAEAREEKRKTKA-QRNKEKRRKEEERE-----AKEEKALKKKLAQ----LE 272
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 568991892 709 RLEdEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEK 748
Cdd:pfam07767 273 RLK-EIAKEIAEKEKEREEKAEARKREKRKKKKEEKKLRP 311
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
630-784 |
1.71e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 630 EVDEQRAKDEAWYQKQELLRRAE---ETRREILLQEEEKMAQQRQRLAAVKRELEIKEIHLQDA-----------ARRRL 695
Cdd:PRK03918 589 ELEERLKELEPFYNEYLELKDAEkelEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELekkyseeeyeeLREEY 668
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 696 LKLqqdqrEMELRRLEDEIERKVQMRDqEIAATAKDLEiRQLELEAQKRLYEKDLTTSQEAVaKEIREDTdaHRRKAALE 775
Cdd:PRK03918 669 LEL-----SRELAGLRAELEELEKRRE-EIKKTLEKLK-EELEEREKAKKELEKLEKALERV-EELREKV--KKYKALLK 738
|
....*....
gi 568991892 776 EHMFQKLLE 784
Cdd:PRK03918 739 ERALSKVGE 747
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
622-763 |
1.84e-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: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 622 QTVENMQAEVDEQRAKDEAwyQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELEiKEIHLQDAARRRL---LKL 698
Cdd:COG2433 376 LSIEEALEELIEKELPEEE--PEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELE-AELEEKDERIERLereLSE 452
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568991892 699 QQDQREMELRRledeiERKVQMRDQEIAATAKDLE-----IRQLE--LEAQKRLYEKDLttSQEAVA-KEIRE 763
Cdd:COG2433 453 ARSEERREIRK-----DREISRLDREIERLERELEeererIEELKrkLERLKELWKLEH--SGELVPvKVVEK 518
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
605-888 |
1.85e-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: 42.26 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 605 REWERIRNDELDFLRERQTVENMQAEVDEQRAKDEAwYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELEIKE 684
Cdd:TIGR00618 615 HALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHA-LQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLT 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 685 IHLQDAARRRLLKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEKDLTTSQEAVAKE--IR 762
Cdd:TIGR00618 694 YWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEvtAA 773
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 763 EDTDAHRRKAALEEHMFQKLLEnsqmggrraQRVMEDNLAKAE-QACLNADWQIQTLhkqkcADQQRSQGYYDVATLLRE 841
Cdd:TIGR00618 774 LQTGAELSHLAAEIQFFNRLRE---------EDTHLLKTLEAEiGQEIPSDEDILNL-----QCETLVQEEEQFLSRLEE 839
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 568991892 842 NRRKEVEVlnammeeeAQKWKEAEEKEFHLQSAKKASA-LSDASRKWF 888
Cdd:TIGR00618 840 KSATLGEI--------THQLLKYEECSKQLAQLTQEQAkIIQLSDKLN 879
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
693-806 |
1.89e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 693 RRLLKLQQ-DQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLE---LEAQKRLYEKDLTTSQEAVA---------- 758
Cdd:COG1579 7 RALLDLQElDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTEledLEKEIKRLELEIEEVEARIKkyeeqlgnvr 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 568991892 759 --KEI----REDTDAHRRKAALEEHMFQKLLENSQMggRRAQRVMEDNLAKAEQ 806
Cdd:COG1579 87 nnKEYealqKEIESLKRRISDLEDEILELMERIEEL--EEELAELEAELAELEA 138
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
650-780 |
1.90e-03 |
|
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: 40.02 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 650 RAEETRReiLLQEEEKMA-QQRQRLAAVKRELEIKEIHLQDAARRRLLKLQQDQREmELRRLEDeiERKVQMRDQEIAAT 728
Cdd:pfam05672 8 DAEEAAR--ILAEKRRQArEQREREEQERLEKEEEERLRKEELRRRAEEERARREE-EARRLEE--ERRREEEERQRKAE 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 568991892 729 AKDLEIRQLELEAQKRLYEKdlttSQEAVAKEiREdtDAHRRKAALEEHMFQ 780
Cdd:pfam05672 83 EEAEEREQREQEEQERLQKQ----KEEAEAKA-RE--EAERQRQEREKIMQQ 127
|
|
| DUF4200 |
pfam13863 |
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ... |
655-748 |
1.94e-03 |
|
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: 39.09 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 655 RREI-LLQEE-----EKMAQQRQRLAAVKRELEIKEIHLQDAARR--RLLKLQQDQREMELRRLEDEIERKVQmRDQEIA 726
Cdd:pfam13863 5 KREMfLVQLAldakrEEIERLEELLKQREEELEKKEQELKEDLIKfdKFLKENDAKRRRALKKAEEETKLKKE-KEKEIK 83
|
90 100
....*....|....*....|..
gi 568991892 727 ATAKDLEIRQLELEAQKRLYEK 748
Cdd:pfam13863 84 KLTAQIEELKSEISKLEEKLEE 105
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
667-908 |
2.30e-03 |
|
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: 41.37 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 667 AQQRQRLAAVKreleikeihlQDAARR---RLLKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKDLE-IRQLELEAQ 742
Cdd:TIGR02794 49 AQQANRIQQQK----------KPAAKKeqeRQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEqAAKQAEEKQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 743 KrlyekdlttsQEAVAKEIREDtdahRRKAALEEHMFQKLLENSQmggRRAQrvmEDNLAKAEQAClnadwqiqtlhKQK 822
Cdd:TIGR02794 119 K----------QAEEAKAKQAA----EAKAKAEAEAERKAKEEAA---KQAE---EEAKAKAAAEA-----------KKK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 823 CADQQRSQGYYDVATLLRENRRKEVEvlnAMMEEEAQKWKEAEEKEFHLQSAKKASALSDASRK-WFLRQETSAALEHEE 901
Cdd:TIGR02794 168 AEEAKKKAEAEAKAKAEAEAKAKAEE---AKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKaDEAELGDIFGLASGS 244
|
....*..
gi 568991892 902 MPWLQRQ 908
Cdd:TIGR02794 245 NAEKQGG 251
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
653-886 |
2.57e-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: 41.88 E-value: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 653 ETRREILLQEEEKMAQQRQRLAAVKRELEIKEIHLQdaaRRRLLKlQQDQREMELRRLEDEIERKVQMRDQE-----IAA 727
Cdd:TIGR00618 222 QVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLK---KQQLLK-QLRARIEELRAQEAVLEETQERINRArkaapLAA 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 728 TAKDL-EIRQ------LELEAQKRLYEKDLTTSQEAVAKE--IREDTDAHRRKAALEEHMFQkllENSQMGGRRAQRVME 798
Cdd:TIGR00618 298 HIKAVtQIEQqaqrihTELQSKMRSRAKLLMKRAAHVKQQssIEEQRRLLQTLHSQEIHIRD---AHEVATSIREISCQQ 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 799 DNLA---KAEQACLNADWQIQTLHKQKCADQQRSQGyyDVATLLRENRRKEVEVLNAMMEEEAQKwKEAEEKEFH----L 871
Cdd:TIGR00618 375 HTLTqhiHTLQQQKTTLTQKLQSLCKELDILQREQA--TIDTRTSAFRDLQGQLAHAKKQQELQQ-RYAELCAAAitctA 451
|
250
....*....|....*
gi 568991892 872 QSAKKASALSDASRK 886
Cdd:TIGR00618 452 QCEKLEKIHLQESAQ 466
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
614-872 |
2.60e-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: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 614 ELDFLRErQTVENMQAEVDEQRAKDEAwyQKQELLRRAEETRREilLQEE-EKMAQQRQRLAAVKRELEIKEIHLQDAAR 692
Cdd:pfam01576 320 ELRSKRE-QEVTELKKALEEETRSHEA--QLQEMRQKHTQALEE--LTEQlEQAKRNKANLEKAKQALESENAELQAELR 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 693 rrllKLQQDQREMELRRledeieRKVQMRDQEIAATAKDLEIRQLELE--AQKRLYEKDLTTS--QEAVAKEIREDTDA- 767
Cdd:pfam01576 395 ----TLQQAKQDSEHKR------KKLEGQLQELQARLSESERQRAELAekLSKLQSELESVSSllNEAEGKNIKLSKDVs 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 768 ------HRRKAALEEHMFQKLLENSQMGGRRAQRV-MEDNLAKAEQACLNADWQIQTLHKQKCADQQRSQGYYDVATLLR 840
Cdd:pfam01576 465 slesqlQDTQELLQEETRQKLNLSTRLRQLEDERNsLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALE 544
|
250 260 270
....*....|....*....|....*....|....*
gi 568991892 841 ENRRK---EVEVLNAMMEEEAQKWKEAEEKEFHLQ 872
Cdd:pfam01576 545 EGKKRlqrELEALTQQLEEKAAAYDKLEKTKNRLQ 579
|
|
| DegS |
pfam05384 |
Sensor protein DegS; This is small family of Bacillus DegS proteins. The DegS-DegU ... |
623-718 |
2.71e-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: 39.39 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 623 TVENMQAEVDE--QRAKDEAWYQKQELlrraEETRREIL--------LQEEEKMAqqRQRLAAVKR------ELEIKEIH 686
Cdd:pfam05384 10 TIENSKEEIFEiaENARQEYERLKQEL----EELKEEVSetikevdkLEKKERRA--RQRLMEVSRdfnrysEEDIKEAY 83
|
90 100 110
....*....|....*....|....*....|...
gi 568991892 687 LQ-DAARRRLLKLQQdqREMELRRLEDEIERKV 718
Cdd:pfam05384 84 EEaKDLQVELALLRE--REKQLRERRDELERRL 114
|
|
| G_path_suppress |
pfam15991 |
G-protein pathway suppressor; This family of proteins inhibits G-protein- and ... |
619-705 |
3.00e-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: 40.67 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 619 RERQTVEnMQAEVDEQRAKDEAWYQKQELLRRAEETRREIlLQEEEKMAQQRQRlaavKREL--EIKEIHLQDAARRRLL 696
Cdd:pfam15991 22 RERKKQE-QEAKMEEERLRREREEREKEDRMTLEETKEQI-LKLEKKLADLKEE----KHQLflQLKKVLHEDETRKRQL 95
|
....*....
gi 568991892 697 KLQQDQREM 705
Cdd:pfam15991 96 KEQSELFAL 104
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
632-767 |
3.44e-03 |
|
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: 41.36 E-value: 3.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 632 DEQRAKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELEIKEIHLQDAarRRLLKlqqdQREMELRRLE 711
Cdd:pfam12128 586 DLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFA--RTALK----NARLDLRRLF 659
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 568991892 712 DEiERKVQMRDQEIAATAKDLEIRQL-ELEAQKRLYEKDLTTSQEAVAKEIREDTDA 767
Cdd:pfam12128 660 DE-KQSEKDKKNKALAERKDSANERLnSLEAQLKQLDKKHQAWLEEQKEQKREARTE 715
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
615-812 |
3.72e-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: 3.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 615 LDFLRERQT---VENMQAEVDEQRAKDEAWYQKqelLRRAEETR---REILLQEEEKMAQQRQRLAAVKRELeikeihlq 688
Cdd:COG3096 960 LSEVVQRRPhfsYEDAVGLLGENSDLNEKLRAR---LEQAEEARreaREQLRQAQAQYSQYNQVLASLKSSR-------- 1028
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 689 DAARRRLLKLQQDQREMELrRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKrlyekdltTSQEAvakEIREdtdAH 768
Cdd:COG3096 1029 DAKQQTLQELEQELEELGV-QADAEAEERARIRRDELHEELSQNRSRRSQLEKQL--------TRCEA---EMDS---LQ 1093
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 568991892 769 RRKAALEEHMFQ--KLLENSQMGGRRAQRVMEDN-----LAKAEQACLNAD 812
Cdd:COG3096 1094 KRLRKAERDYKQerEQVVQAKAGWCAVLRLARDNdverrLHRRELAYLSAD 1144
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
629-858 |
4.33e-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: 40.93 E-value: 4.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 629 AEVDEQRAKDEAwyQKQELLR---------RAEETRREILLQEEEKMAQQ--------------RQRLAAVKRELEIKEI 685
Cdd:pfam01576 57 AEAEEMRARLAA--RKQELEEilhelesrlEEEEERSQQLQNEKKKMQQHiqdleeqldeeeaaRQKLQLEKVTTEAKIK 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 686 HLQDaaRRRLLKLQQDQREMELRRLEDEI-ERKVQMRDQE------------IAATAKDLEIR-------QLELEAQKRL 745
Cdd:pfam01576 135 KLEE--DILLLEDQNSKLSKERKLLEERIsEFTSNLAEEEekakslsklknkHEAMISDLEERlkkeekgRQELEKAKRK 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 746 YEKDLTTSQEAVAKEIREDTDAHRRKAALEEHMFQKLLENSQMGGRRAQRVMEDNLAKAEQACLNADWQIQTLHKQKCAD 825
Cdd:pfam01576 213 LEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEK 292
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 568991892 826 QQRSQGYYDVA-------TL--------LRENRRKEVEVLNAMMEEEA 858
Cdd:pfam01576 293 QRRDLGEELEAlkteledTLdttaaqqeLRSKREQEVTELKKALEEET 340
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
646-744 |
4.67e-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: 40.52 E-value: 4.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 646 ELLRRAEETRREILlqeeEKMAQQRQRLAAVKRELEIKEIHLQD-----AARRRLLKLQQDQREMELRRLEDEIERKvQM 720
Cdd:COG4942 139 QYLKYLAPARREQA----EELRADLAELAALRAELEAERAELEAllaelEEERAALEALKAERQKLLARLEKELAEL-AA 213
|
90 100
....*....|....*....|....*.
gi 568991892 721 RDQEIAATAKDLE--IRQLELEAQKR 744
Cdd:COG4942 214 ELAELQQEAEELEalIARLEAEAAAA 239
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
663-856 |
4.68e-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: 41.09 E-value: 4.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 663 EEKMAQQRQRLAAVKRELEIKEIHLQ------DAARRRLLKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQ 736
Cdd:COG3096 835 EAELAALRQRRSELERELAQHRAQEQqlrqqlDQLKEQLQLLNKLLPQANLLADETLADRLEELREELDAAQEAQAFIQQ 914
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 737 -----LELEAQKRLYEKDlTTSQEAVAKEIREDTDAHRR-KA---ALEE-----HMF------QKLLENSQMGGRRAQRv 796
Cdd:COG3096 915 hgkalAQLEPLVAVLQSD-PEQFEQLQADYLQAKEQQRRlKQqifALSEvvqrrPHFsyedavGLLGENSDLNEKLRAR- 992
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 797 mednLAKAEQACLNADWQIQTlhkqkcADQQRSQgYYDVATLLRENRRKEVEVLNAMMEE 856
Cdd:COG3096 993 ----LEQAEEARREAREQLRQ------AQAQYSQ-YNQVLASLKSSRDAKQQTLQELEQE 1041
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
613-745 |
4.80e-03 |
|
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: 40.29 E-value: 4.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 613 DELDFLRERQTVENMQAEvDEQRAKDEAwYQKQELLRRAEETRREILLQEEEKMAQQRQR-------LAAVKRELEIKEI 685
Cdd:pfam13868 201 AERDELRAKLYQEEQERK-ERQKEREEA-EKKARQRQELQQAREEQIELKERRLAEEAEReeeeferMLRKQAEDEEIEQ 278
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568991892 686 HLQDAARRRLLKLQQD-QREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRL 745
Cdd:pfam13868 279 EEAEKRRMKRLEHRRElEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKKL 339
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
632-807 |
5.80e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.69 E-value: 5.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 632 DEQRAKDEAWYQKQELLRRAE---------------------ETRREILLQEEEKMAQQRQRLAAVKRELEIKEIHLQDA 690
Cdd:COG1196 555 DDEVAAAAIEYLKAAKAGRATflpldkiraraalaaalargaIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEA 634
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 691 ARRRLLKLQQDQREMELRRlEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEKDLTTSQEAVAKEIREDTDAHRR 770
Cdd:COG1196 635 ALRRAVTLAGRLREVTLEG-EGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAE 713
|
170 180 190
....*....|....*....|....*....|....*..
gi 568991892 771 KAALEEHMFQKLLENSQMGGRRAQRVMEDNLAKAEQA 807
Cdd:COG1196 714 EERLEEELEEEALEEQLEAEREELLEELLEEEELLEE 750
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
643-757 |
5.88e-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: 5.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 643 QKQELLRRAEETRREiLLQEEEKMAQQRQRLAAVKRELEIK---EIHLQ---DAARRRLLKLQQDQREMElrrledeier 716
Cdd:COG3096 279 ERRELSERALELRRE-LFGARRQLAEEQYRLVEMARELEELsarESDLEqdyQAASDHLNLVQTALRQQE---------- 347
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 568991892 717 KVQMRDQEIAATAKDLEIRQLELEA---QKRLYEKDLTTSQEAV 757
Cdd:COG3096 348 KIERYQEDLEELTERLEEQEEVVEEaaeQLAEAEARLEAAEEEV 391
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
619-807 |
6.49e-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: 6.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 619 RERQTVENMQAEVDEQRAKDEAwyQKQELLRRAEETRREILLQE------EEKMAQQRQRLAAV---KRELEIKEIHLQD 689
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKK--EEKALLKQLAALERRIAALArriralEQELAALEAELAELekeIAELRAELEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 690 AARRRLLKLQQDQREMEL-------------RRLE--DEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEKDLTTsQ 754
Cdd:COG4942 105 ELAELLRALYRLGRQPPLalllspedfldavRRLQylKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAE-L 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568991892 755 EAVAKEIREDTDAHRRKAALEEHMFQKLLENSQMGGRRAQRvMEDNLAKAEQA 807
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE-LEALIARLEAE 235
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
614-869 |
6.62e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.42 E-value: 6.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 614 ELDFLRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEEKM-------------AQQRQRLAAVKREL 680
Cdd:TIGR00606 814 KLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTnelkseklqigtnLQRRQQFEEQLVEL 893
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 681 ---------EIKEIHLQDAARRRLLKLQQDQREMELRRLEDEiERKVQMRDQEIAATAKDLEIRQLELEAQ----KRLYE 747
Cdd:TIGR00606 894 stevqslirEIKDAKEQDSPLETFLEKDQQEKEELISSKETS-NKKAQDKVNDIKEKVKNIHGYMKDIENKiqdgKDDYL 972
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 748 KDLTTSQEAVAKEIREDtdaHRRKAALEEHMfqKLLENSQMGGRRAQRVMEDNLA--KAEQACLNADWQIQTLHKQKCAD 825
Cdd:TIGR00606 973 KQKETELNTVNAQLEEC---EKHQEKINEDM--RLMRQDIDTQKIQERWLQDNLTlrKRENELKEVEEELKQHLKEMGQM 1047
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 568991892 826 Q--QRSQGYYDVATLLRENRRKEVEVLNAMMEEEAQKW---KEAEEKEF 869
Cdd:TIGR00606 1048 QvlQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKhfkKELREPQF 1096
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
639-787 |
6.82e-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: 39.30 E-value: 6.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 639 EAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRE--LEIKEihlQDAARRRLLKLQQDQREMELRRLeDEIER 716
Cdd:pfam13904 58 ENWLAAKQRQRQKELQAQKEEREKEEQEAELRKRLAKEKYQewLQRKA---RQQTKKREESHKQKAAESASKSL-AKPER 133
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568991892 717 KVQMRdqEIAATAKDLEIRQLELEAQKRLYEKDlttsqeavAKEIREDTDAHRRKAAleEHMFQKLLENSQ 787
Cdd:pfam13904 134 KVSQE--EAKEVLQEWERKKLEQQQRKREEEQR--------EQLKKEEEEQERKQLA--EKAWQKWMKNVK 192
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
608-808 |
6.88e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 6.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 608 ERIRNDELDF---LRERQTVENMQAEVDEQRAKDEAWYQKQELLR-RAEETRREILLQE------EEKMAQQRQRLAAVK 677
Cdd:PRK03918 193 ELIKEKEKELeevLREINEISSELPELREELEKLEKEVKELEELKeEIEELEKELESLEgskrklEEKIRELEERIEELK 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 678 REL--------EIKEIHLQDAARRRLLKLQQDQREmELRRLEDEIER------KVQMRDQEIAATAKDL-EIRQLELEAQ 742
Cdd:PRK03918 273 KEIeeleekvkELKELKEKAEEYIKLSEFYEEYLD-ELREIEKRLSRleeeinGIEERIKELEEKEERLeELKKKLKELE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 743 KRL--YEKDLTTSQEAVAKE------------------IREDTDAHRRKAALEEHMFQKLLENSQMGGRRAQR---VMEd 799
Cdd:PRK03918 352 KRLeeLEERHELYEEAKAKKeelerlkkrltgltpeklEKELEELEKAKEEIEEEISKITARIGELKKEIKELkkaIEE- 430
|
....*....
gi 568991892 800 nLAKAEQAC 808
Cdd:PRK03918 431 -LKKAKGKC 438
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
621-729 |
7.40e-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: 39.75 E-value: 7.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 621 RQTVENMQAEVDEQRAKdeawYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELEIKEIHLQ---DAARRRLLK 697
Cdd:COG4942 142 KYLAPARREQAEELRAD----LAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEkelAELAAELAE 217
|
90 100 110
....*....|....*....|....*....|..
gi 568991892 698 LQQDQRemELRRLEDEIERKVQMRDQEIAATA 729
Cdd:COG4942 218 LQQEAE--ELEALIARLEAEAAAAAERTPAAG 247
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
608-711 |
8.94e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 39.85 E-value: 8.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 608 ERIRndeldflRERQTVENMQAEVDEQRaKDEAWYQKQELLRRAEEtRREILLQEEEKMAQQRQrLAAVKRELEikeihl 687
Cdd:pfam02029 251 EELR-------RRRQEKESEEFEKLRQK-QQEAELELEELKKKREE-RRKLLEEEEQRRKQEEA-ERKLREEEE------ 314
|
90 100
....*....|....*....|....
gi 568991892 688 qdaaRRRLlklqqdQREMELRRLE 711
Cdd:pfam02029 315 ----KRRM------KEEIERRRAE 328
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
557-684 |
9.51e-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: 39.36 E-value: 9.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 557 VIREVYHLMETTPADI--HPNSMLDAFVALTKGQYpiFNQYPKFIVDYQTREWERIRNDELDFLRERQTVENMQAEVDEQ 634
Cdd:COG4942 109 LLRALYRLGRQPPLALllSPEDFLDAVRRLQYLKY--LAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEE 186
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 568991892 635 RAKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELEIKE 684
Cdd:COG4942 187 RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| PRK03963 |
PRK03963 |
V-type ATP synthase subunit E; Provisional |
645-764 |
9.65e-03 |
|
V-type ATP synthase subunit E; Provisional
Pssm-ID: 167649 [Multi-domain] Cd Length: 198 Bit Score: 38.58 E-value: 9.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991892 645 QELLRRAEETRREIlLQEEEKMAQQrqrlaavkreleIKEihlqdAARRRllklQQDQREMELRRLEDEIErkvqMRDQE 724
Cdd:PRK03963 9 QEINREAEQKIEYI-LEEAQKEAEK------------IKE-----EARKR----AESKAEWILRKAKTQAE----LEKQR 62
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 568991892 725 IAATAKdLEIRQLELEAQKRLYEKDLTTSQEAVAkEIRED 764
Cdd:PRK03963 63 IIANAK-LEVRRKRLAVQEELISEVLEAVRERLA-ELPED 100
|
|
| |
