|
Name |
Accession |
Description |
Interval |
E-value |
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
48-336 |
6.17e-28 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 117.32 E-value: 6.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 48 VAFDGSGDSFIAGDHQGNIYVFDLH-GNRFNLVQRTAQACTALAFNlrRKSEFLV-ALADYSIKCFDTVTKELVSWMRGH 125
Cdd:COG2319 126 VAFSPDGKTLASGSADGTVRLWDLAtGKLLRTLTGHSGAVTSVAFS--PDGKLLAsGSDDGTVRLWDLATGKLLRTLTGH 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 126 ESSVCSISVHASGRYAITTSSD-TAQLWDLDTFQRKRKLNIRQSvGIQKVFFLPLSNTILSCFKDNSIFAWECDTLFCKY 204
Cdd:COG2319 204 TGAVRSVAFSPDGKLLASGSADgTVRLWDLATGKLLRTLTGHSG-SVRSVAFSPDGRLLASGSADGTVRLWDLATGELLR 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 205 QLPGPPEGSNILykvfAVTRDGRILAAGGKSNHLHLWCLEATGLFRIIQmpAKVRAVRHLEFLPDsfdagsNQVLGVLSQ 284
Cdd:COG2319 283 TLTGHSGGVNSV----AFSPDGKLLASGSDDGTVRLWDLATGKLLRTLT--GHTGAVRSVAFSPD------GKTLASGSD 350
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 264681543 285 DGIMRFVNIQTCKLLFEIGTVEEGISSSVISPHGRYIASIMENGSLNVYSVQ 336
Cdd:COG2319 351 DGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
44-340 |
1.60e-26 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 113.47 E-value: 1.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 44 RFLNVAFDGSGDSFIAGDHQGNIYVFDL-HGNRFNLVQRTAQACTALAFNLRRKSeFLVALADYSIKCFDTVTKELVSWM 122
Cdd:COG2319 80 AVLSVAFSPDGRLLASASADGTVRLWDLaTGLLLRTLTGHTGAVRSVAFSPDGKT-LASGSADGTVRLWDLATGKLLRTL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 123 RGHESSVCSISVHASGRYAITTSSD-TAQLWDLDTFQRKRKLNIRQSvGIQKVFFLPLSNTILSCFKDNSIFAWECDTLF 201
Cdd:COG2319 159 TGHSGAVTSVAFSPDGKLLASGSDDgTVRLWDLATGKLLRTLTGHTG-AVRSVAFSPDGKLLASGSADGTVRLWDLATGK 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 202 CKYQLPGPPEGSNILykvfAVTRDGRILAAGGKSNHLHLWCLEATGLFRIIQMPAkvRAVRHLEFLPDSfdagsnQVLGV 281
Cdd:COG2319 238 LLRTLTGHSGSVRSV----AFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHS--GGVNSVAFSPDG------KLLAS 305
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 264681543 282 LSQDGIMRFVNIQTCKLLFEIGTVEEGISSSVISPHGRYIASIMENGSLNVYSVQALTQ 340
Cdd:COG2319 306 GSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGEL 364
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
39-334 |
9.31e-25 |
|
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: 105.49 E-value: 9.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 39 HPKVLRFlnVAFDGSGDSFIAGDHQGNIYVFDLHGNRFNLVQR----TAQACTALAFNLRrkseFLVALADYSIKCFDTV 114
Cdd:cd00200 8 HTGGVTC--VAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKghtgPVRDVAASADGTY----LASGSSDKTIRLWDLE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 115 TKELVSWMRGHESSVCSISVHASGRYAITTSSD-TAQLWDLDTFQRKRKLNIRQSvGIQKVFFLPLSNTILSCFKDNSIF 193
Cdd:cd00200 82 TGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDkTIKVWDVETGKCLTTLRGHTD-WVNSVAFSPDGTFVASSSQDGTIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 194 AWECDTLFCKYQLPGpPEGSnilykVFAVT--RDGRILAAGGKSNHLHLWclEATGLFRIIQMPAKVRAVRHLEFLPDsf 271
Cdd:cd00200 161 LWDLRTGKCVATLTG-HTGE-----VNSVAfsPDGEKLLSSSSDGTIKLW--DLSTGKCLGTLRGHENGVNSVAFSPD-- 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 264681543 272 dagsNQVLGVLSQDGIMRFVNIQTCKLLFEIGTVEEGISSSVISPHGRYIASIMENGSLNVYS 334
Cdd:cd00200 231 ----GYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
39-336 |
1.97e-24 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 106.92 E-value: 1.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 39 HPKVLRFLNVAFDGSGDSFIAGDHQGNIYVFDLHGNRFNLVQRTAQAcTALAFNLRRKSeFLVALADYSIKCFDTVTKEL 118
Cdd:COG2319 35 LAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAV-LSVAFSPDGRL-LASASADGTVRLWDLATGLL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 119 VSWMRGHESSVCSISVHASGRYAITTSSD-TAQLWDLDTFQRKRKLNiRQSVGIQKVFFLPLSNTILSCFKDNSIFAWEC 197
Cdd:COG2319 113 LRTLTGHTGAVRSVAFSPDGKTLASGSADgTVRLWDLATGKLLRTLT-GHSGAVTSVAFSPDGKLLASGSDDGTVRLWDL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 198 DTLFCKYQLPGPPEGSNILykvfAVTRDGRILAAGGKSNHLHLWCLEATGLFRIIQMPAkvRAVRHLEFLPDSfdagsnQ 277
Cdd:COG2319 192 ATGKLLRTLTGHTGAVRSV----AFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHS--GSVRSVAFSPDG------R 259
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 264681543 278 VLGVLSQDGIMRFVNIQTCKLLFEIGTVEEGISSSVISPHGRYIASIMENGSLNVYSVQ 336
Cdd:COG2319 260 LLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLA 318
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
49-336 |
9.03e-21 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 96.13 E-value: 9.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 49 AFDGSGDSFIAGDHQGNIYVFDLHGNRFNLVQRTAQACTALAFNLRRKSEFLVALADYSIKCFDTVTKELVSWMRGHESS 128
Cdd:COG2319 1 ALSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 129 VCSISVHASGRYAITTSSD-TAQLWDLDTFQRKRKLNIRQSvGIQKVFFLPLSNTILSCFKDNSIFAWECDTLFCKYQLP 207
Cdd:COG2319 81 VLSVAFSPDGRLLASASADgTVRLWDLATGLLLRTLTGHTG-AVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 208 GPPEGSNILykvfAVTRDGRILAAGGKSNHLHLWCLEATGLFRIIQmpAKVRAVRHLEFLPDSfdagsnQVLGVLSQDGI 287
Cdd:COG2319 160 GHSGAVTSV----AFSPDGKLLASGSDDGTVRLWDLATGKLLRTLT--GHTGAVRSVAFSPDG------KLLASGSADGT 227
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 264681543 288 MRFVNIQTCKLLFEIGTVEEGISSSVISPHGRYIASIMENGSLNVYSVQ 336
Cdd:COG2319 228 VRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLA 276
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
123-337 |
2.96e-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: 2.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 123 RGHESSVCSISVHASGRYAITTSSD-TAQLWDLDTFQRKRKLNIrQSVGIQKVFFLPLSNTILSCFKDNSIFAWECDTLF 201
Cdd:cd00200 6 KGHTGGVTCVAFSPDGKLLATGSGDgTIKVWDLETGELLRTLKG-HTGPVRDVAASADGTYLASGSSDKTIRLWDLETGE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 202 CKYQLPGPPEGsnilykVFAV--TRDGRILAAGGKSNHLHLWCLEATGLfrIIQMPAKVRAVRHLEFLPDsfdagsNQVL 279
Cdd:cd00200 85 CVRTLTGHTSY------VSSVafSPDGRILSSSSRDKTIKVWDVETGKC--LTTLRGHTDWVNSVAFSPD------GTFV 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 264681543 280 GVLSQDGIMRFVNIQTCKLLFEIGTVEEGISSSVISPHGRYIASIMENGSLNVYSVQA 337
Cdd:cd00200 151 ASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLST 208
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
684-941 |
6.10e-14 |
|
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: 76.32 E-value: 6.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 684 IVDYQTREWERIRNDELDFL---RERQTVENMQAEVDEQRAKDEAwyqkqELLRRAEETRREILLQEEEKMAQQRQR--- 757
Cdd:pfam17380 277 IVQHQKAVSERQQQEKFEKMeqeRLRQEKEEKAREVERRRKLEEA-----EKARQAEMDRQAAIYAEQERMAMERERele 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 758 ---LAAVKRELE-------------IKEIH-LQ--------------DAARR-------RLLKLQQDQREMELRRLEDEI 799
Cdd:pfam17380 352 rirQEERKRELErirqeeiameisrMRELErLQmerqqknervrqelEAARKvkileeeRQRKIQQQKVEMEQIRAEQEE 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 800 ERKVQMRDQEiAATAKDLE-IRQLELEAQKRLyekDLTTSQEAVAKEIREDTDAHRRKAALEEHMFQKLLENSQMGGRRA 878
Cdd:pfam17380 432 ARQREVRRLE-EERAREMErVRLEEQERQQQV---ERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQA 507
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 264681543 879 QRWKEAEEKEFHLQSAKKASALSDASRKWFLRQETSAALEHEEMPWLQRQYMDSAylPQTSRL 941
Cdd:pfam17380 508 MIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKAT--EERSRL 568
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
688-928 |
6.35e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 76.51 E-value: 6.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 688 QTREWE-RIRNDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQELL---RRAEETRREILLQEEEKMAQQRQRLAAVKR 763
Cdd:COG1196 261 ELAELEaELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLeerRRELEERLEELEEELAELEEELEELEEELE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 764 ELEIKEIHLQDAARRRLLKLQQ--DQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRL---------YE 832
Cdd:COG1196 341 ELEEELEEAEEELEEAEAELAEaeEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEeallerlerLE 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 833 KDLTTSQEAVAKEIREDTDAHRRKAALEEHMFQKLLENSQMGGRRAQRWKEAEEKEfHLQSAKKASALSDASRKWfLRQE 912
Cdd:COG1196 421 EELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE-AALAELLEELAEAAARLL-LLLE 498
|
250
....*....|....*.
gi 264681543 913 TSAALEHEEMPWLQRQ 928
Cdd:COG1196 499 AEADYEGFLEGVKAAL 514
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
699-921 |
7.64e-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: 7.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 699 ELDFLRERQtvENMQAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELEIKE---IHLQDA 775
Cdd:COG1196 233 KLRELEAEL--EELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEqdiARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 776 ARRRLLKLQQDQREME--LRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRL--YEKDLTTSQEAVAKEIREDTD 851
Cdd:COG1196 311 RRELEERLEELEEELAelEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALleAEAELAEAEEELEELAEELLE 390
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 852 AHRRKAALEEHMFQKLLENSQMGGRRAQRWKEAEEKEfhlQSAKKASALSDASRKWFLRQETSAALEHEE 921
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELE---EALAELEEEEEEEEEALEEAAEEEAELEEE 457
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
693-921 |
3.45e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.74 E-value: 3.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 693 ERIRNDELDFLRERQTVENMQAEVDEQRAK--------DEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRE 764
Cdd:COG1196 246 AELEELEAELEELEAELAELEAELEELRLEleelelelEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 765 LEIKEIHLQDAARRRLLKLQQDQREMELRRLEDEIERKVQMRD------QEIAATAKDLEIRQLELEAQKRLYEKDLTTS 838
Cdd:COG1196 326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLeaeaelAEAEEELEELAEELLEALRAAAELAAQLEEL 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 839 QEAVAKEIREDTDAHRRKAALEEHMFQKLLEnsqmggRRAQRWKEAEEKEFHLQSAKKASALSDASRKWFLRQETSAALE 918
Cdd:COG1196 406 EEAEEALLERLERLEEELEELEEALAELEEE------EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAAL 479
|
...
gi 264681543 919 HEE 921
Cdd:COG1196 480 AEL 482
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
688-865 |
5.20e-12 |
|
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: 69.77 E-value: 5.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 688 QTREWERIRNDELDflrERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEE----KMAQQRQRLAAVKR 763
Cdd:pfam17380 444 RAREMERVRLEEQE---RQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEerkqAMIEEERKRKLLEK 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 764 ELEIKEIHLQDAARRRLLKLQQ-DQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEKDLTTSQEAV 842
Cdd:pfam17380 521 EMEERQKAIYEEERRREAEEERrKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAEYEATTPITTI 600
|
170 180
....*....|....*....|...
gi 264681543 843 AKEIREDTDAHrRKAALEEHMFQ 865
Cdd:pfam17380 601 KPIYRPRISEY-QPPDVESHMIR 622
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
689-927 |
5.41e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.97 E-value: 5.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 689 TREWERIRNDELDFLRERQTVENMQAEVDEQRAKDEAwyqkqellRRAEETRREILLQEEEKMAQQRQRLAAVKRELEIK 768
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEERLEELEEELAELEE--------ELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 769 EIHLQDAARRRLLKLQQDQREMELRRLEDEIERKVQMrdQEIAATAKDLEIRQLELEAQKRLYEKDLTTSQEAVAKEIRE 848
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL--EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 264681543 849 DTDAHRRKAALEEHMfQKLLENSQMGGRRAQRWKEAEEKEFHLQSAKKASALSDASRKWFLRQETSAALEHEEMPWLQR 927
Cdd:COG1196 444 LEEAAEEEAELEEEE-EALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRG 521
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
687-921 |
6.17e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.50 E-value: 6.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 687 YQT-REWERIRNDELdFLRERQTVENMQAEVDEQRAkdeawyQKQELLRRAEETRREIllqeEEKMAQQRQRLAAVKREL 765
Cdd:COG1196 215 YRElKEELKELEAEL-LLLKLRELEAELEELEAELE------ELEAELEELEAELAEL----EAELEELRLELEELELEL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 766 EIKEIHLQdAARRRLLKLQQDQR--EMELRRLEDEIERKvQMRDQEIAATAKDLEIRQLELEAQKRLYEKDLTTSQEAVA 843
Cdd:COG1196 284 EEAQAEEY-ELLAELARLEQDIArlEERRRELEERLEEL-EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 264681543 844 KEIREDTDAHRRKAALEEHMFQKLLENSqmggRRAQRWKEAEEKEFHLQSAKKASALSDASRKWFLRQETSAALEHEE 921
Cdd:COG1196 362 EAEEALLEAEAELAEAEEELEELAEELL----EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE 435
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
691-872 |
7.79e-10 |
|
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: 62.66 E-value: 7.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 691 EWERIRNDELDFLRERQ----TVENMQAEVD--EQRAKDEAWYQKQellRRAEETRReillQEEEKMAQQRQRLAAVKRE 764
Cdd:pfam15709 349 EVERKRREQEEQRRLQQeqleRAEKMREELEleQQRRFEEIRLRKQ---RLEEERQR----QEEEERKQRLQLQAAQERA 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 765 leikeiHLQDAA-RRRLLKLQQDQREMELRRLEDEIERKVQMRDQeIAATAKDL-EIRQLE-LEAQKRLYEKDLTTSQEA 841
Cdd:pfam15709 422 ------RQQQEEfRRKLQELQRKKQQEEAERAEAEKQRQKELEMQ-LAEEQKRLmEMAEEErLEYQRQKQEAEEKARLEA 494
|
170 180 190
....*....|....*....|....*....|.
gi 264681543 842 VAKEIREDTDAhrrKAALEEHMFQKLLENSQ 872
Cdd:pfam15709 495 EERRQKEEEAA---RLALEEAMKQAQEQARQ 522
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
713-922 |
8.47e-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: 8.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 713 QAEV---------DEQRAKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELEIKEIHLQdAARRRLLKL 783
Cdd:COG1196 208 QAEKaeryrelkeELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELE-ELELELEEA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 784 QQDQRE--MELRRLEDEIERKVQMRdqeiaataKDLEIRQLELEAQKRLYEKDLTTSQEAVAKEIREDTDAHRRKAALEE 861
Cdd:COG1196 287 QAEEYEllAELARLEQDIARLEERR--------RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA 358
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 264681543 862 HMFQKLLENSQMGGRRAQRWKEAEEKEFHLQSAKKASALSDASRKWFLRQETSAALEHEEM 922
Cdd:COG1196 359 ELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL 419
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
48-156 |
2.09e-09 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 60.70 E-value: 2.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 48 VAFDGSGDSFIAGDHQGNIYVFDLH-GNRFNLVQRTAQACTALAFNlrRKSEFLV-ALADYSIKCFDTVTKELVSWMRGH 125
Cdd:COG2319 294 VAFSPDGKLLASGSDDGTVRLWDLAtGKLLRTLTGHTGAVRSVAFS--PDGKTLAsGSDDGTVRLWDLATGELLRTLTGH 371
|
90 100 110
....*....|....*....|....*....|..
gi 264681543 126 ESSVCSISVHASGRYAITTSSD-TAQLWDLDT 156
Cdd:COG2319 372 TGAVTSVAFSPDGRTLASGSADgTVRLWDLAT 403
|
|
| RabGAP-TBC |
pfam00566 |
Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are ... |
461-605 |
2.33e-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: 2.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 461 SLQKKYPIKSRKLLRVLQRTLSALAHWsaiFSDTPY---LPLLAFPFVkLFQNNQLICFEVVATLIINwcQHWFEYFPN- 536
Cdd:pfam00566 19 TFPHSFFFDNGPGQNSLRRILKAYSIY---NPDVGYcqgMNFIAAPLL-LVYLDEEDAFWCFVSLLEN--YLLRDFYTPd 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 264681543 537 -PPINILSMI-ENVLAFHDKELLQHFIDRDITSQVYAWPLLETLFSEVLTREEWLRLFDNIFSNHPSFLLM 605
Cdd:pfam00566 93 fPGLKRDLYVfEELLKKKLPKLYKHLKELGLDPDLFASQWFLTLFAREFPLSTVLRIWDYFFLEGEKFVLF 163
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
691-888 |
2.40e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 61.70 E-value: 2.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 691 EWERIRNDELDFLRE--RQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREilLQEEEKMAQQrqrlaaVKRELEIK 768
Cdd:PTZ00121 1657 EENKIKAAEEAKKAEedKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKK--EAEEKKKAEE------LKKAEEEN 1728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 769 EIHLQDAARrrllKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQ-------LELEAQKRLYEKDLTT---- 837
Cdd:PTZ00121 1729 KIKAEEAKK----EAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKeavieeeLDEEDEKRRMEVDKKIkdif 1804
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 264681543 838 -------------------SQEAVAKEIREDTDAH---RRKA-ALEEHMFQKLLENSQMGGRRAQRWKEAEEKE 888
Cdd:PTZ00121 1805 dnfaniieggkegnlvindSKEMEDSAIKEVADSKnmqLEEAdAFEKHKFNKNNENGEDGNKEADFNKEKDLKE 1878
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
690-896 |
4.66e-09 |
|
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: 60.52 E-value: 4.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 690 REWERIRNdELDFLR-------ERQ-TVENMQAEVDEQRAKDEAwyQKQELLRRAEETR-REILLQEEEKMAQQRQrlaa 760
Cdd:pfam17380 389 QKNERVRQ-ELEAARkvkileeERQrKIQQQKVEMEQIRAEQEE--ARQREVRRLEEERaREMERVRLEEQERQQQ---- 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 761 vkreleiKEIHLQDAARRRLLKLQQDQREMELRRLEDE----IERKVQMRDQEIaatakdleirqLELEAQKRLYEKDLT 836
Cdd:pfam17380 462 -------VERLRQQEEERKRKKLELEKEKRDRKRAEEQrrkiLEKELEERKQAM-----------IEEERKRKLLEKEME 523
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 837 TSQEAVAKEiredtdaHRRKAALEEHMFQKLLENSQmggRRAQRWKEAEEKEFHLQSAKK 896
Cdd:pfam17380 524 ERQKAIYEE-------ERRREAEEERRKQQEMEERR---RIQEQMRKATEERSRLEAMER 573
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
733-921 |
7.73e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.95 E-value: 7.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 733 LRRAEE--TRREILLQEeekMAQQRQRLA----------AVKRELEIKEIHLQdAARRRLLKLQQDQREMELRRLEDEIE 800
Cdd:COG1196 181 LEATEEnlERLEDILGE---LERQLEPLErqaekaeryrELKEELKELEAELL-LLKLRELEAELEELEAELEELEAELE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 801 R-KVQMRDQEIAATAKDLEIRQLELE---AQKRLYE--KDLTTSQEAVAKEIREDTDAHRRKAALEEhmfQKLLENSQMG 874
Cdd:COG1196 257 ElEAELAELEAELEELRLELEELELEleeAQAEEYEllAELARLEQDIARLEERRRELEERLEELEE---ELAELEEELE 333
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 264681543 875 GRRAQRwKEAEEKEFHLQSAKKASALSDASRKWFLRQETSAALEHEE 921
Cdd:COG1196 334 ELEEEL-EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
693-906 |
1.23e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.38 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 693 ERIRNDELdflreRQTVENMQAEVDEQRAKDEAwYQKQELLRRAEETRR--EILLQEEEKMAQQRQRLAAVKRELEIKei 770
Cdd:PTZ00121 1481 EAKKADEA-----KKKAEEAKKKADEAKKAAEA-KKKADEAKKAEEAKKadEAKKAEEAKKADEAKKAEEKKKADELK-- 1552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 771 hlqdaaRRRLLKLQQDQREMELRRLEDEiERKVQMRDQEIAATAKDLEIrqlelEAQKRLYEKDLTTSQEAVAKEIREDT 850
Cdd:PTZ00121 1553 ------KAEELKKAEEKKKAEEAKKAEE-DKNMALRKAEEAKKAEEARI-----EEVMKLYEEEKKMKAEEAKKAEEAKI 1620
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 264681543 851 DAHR-RKAALEEHMFQKLLENSQMGGRRAQRWKEAEEkEFHLQSAKKASALSDASRK 906
Cdd:PTZ00121 1621 KAEElKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEE-ENKIKAAEEAKKAEEDKKK 1676
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
698-906 |
1.55e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.00 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 698 DELDFLRERQTVENMQAEvdEQRAKDEAwYQKQELLRRAEETRR--EILLQEEEKMAQQRQRLAAVKReleikeihLQDA 775
Cdd:PTZ00121 1095 EAFGKAEEAKKTETGKAE--EARKAEEA-KKKAEDARKAEEARKaeDARKAEEARKAEDAKRVEIARK--------AEDA 1163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 776 ARRRLLKLQQDQREMELRRLEDEIERKVQMRDQE----IAATAKDLEIRQLE----------LEAQKRLYEKDLTTSQEA 841
Cdd:PTZ00121 1164 RKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEdarkAEAARKAEEERKAEearkaedakkAEAVKKAEEAKKDAEEAK 1243
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 264681543 842 VAKEIREDTDAHRRKAALEEHMFQKLLENSQMGGRRAQRWKEAEEKefhlqsaKKASALSDASRK 906
Cdd:PTZ00121 1244 KAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEK-------KKADEAKKAEEK 1301
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
690-920 |
2.23e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.61 E-value: 2.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 690 REWERIRNDELDFLRERQtvENMQAEvdeQRAKDEAWYQKQELLRRAEETRREILlQEEEKMAQQRQRLAAVKRELEIKE 769
Cdd:PTZ00121 1587 KKAEEARIEEVMKLYEEE--KKMKAE---EAKKAEEAKIKAEELKKAEEEKKKVE-QLKKKEAEEKKKAEELKKAEEENK 1660
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 770 IHLQDAARrrllKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKDLE-IRQLELEAQKRlyekdlttsqeavAKEIRE 848
Cdd:PTZ00121 1661 IKAAEEAK----KAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEeLKKKEAEEKKK-------------AEELKK 1723
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 264681543 849 DTDAHRRKAaleehmfQKLLENSQMGGRRAQRWKEAEEKEFHLQSAKKasalSDASRKWFLRQETSAALEHE 920
Cdd:PTZ00121 1724 AEEENKIKA-------EEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKK----EEEKKAEEIRKEKEAVIEEE 1784
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
693-887 |
2.24e-08 |
|
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: 57.24 E-value: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 693 ERIRNDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRL---------AAVKR 763
Cdd:pfam13868 138 EQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERdelraklyqEEQER 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 764 ELEIKEIhlQDAARRR-----LLKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEKdlttS 838
Cdd:pfam13868 218 KERQKER--EEAEKKArqrqeLQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLE----H 291
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 264681543 839 QEAVAKEIREdtdAHRRKAALEEHMFQKLLENSQMGGRRAQRWKEAEEK 887
Cdd:pfam13868 292 RRELEKQIEE---REEQRAAEREEELEEGERLREEEAERRERIEEERQK 337
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
735-921 |
2.46e-08 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 57.65 E-value: 2.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 735 RAEETRREILLQEEEKMAQQRQRL---AAVKRELEIKEIHLQDAARRRLlklQQDQREMElRRLEDEIERKVQMRDQEIA 811
Cdd:pfam15709 315 RSEEDPSKALLEKREQEKASRDRLraeRAEMRRLEVERKRREQEEQRRL---QQEQLERA-EKMREELELEQQRRFEEIR 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 812 ATAKDLE---IRQLELEAQKRLyekdlttsQEAVAKE-IREDTDAHRRKaaLEEHMFQKLLENSQMGGRRAQRWKEAEEK 887
Cdd:pfam15709 391 LRKQRLEeerQRQEEEERKQRL--------QLQAAQErARQQQEEFRRK--LQELQRKKQQEEAERAEAEKQRQKELEMQ 460
|
170 180 190
....*....|....*....|....*....|....*...
gi 264681543 888 EFHLQsaKKASALSDASRKWFLRQ----ETSAALEHEE 921
Cdd:pfam15709 461 LAEEQ--KRLMEMAEEERLEYQRQkqeaEEKARLEAEE 496
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
690-900 |
2.83e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.23 E-value: 2.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 690 REWERIRNDELdflreRQTVENMQAevDEQRAKDEAwyQKQELLRRAEETRR--EILLQEEEKMAQQRQRLAAVKRELEI 767
Cdd:PTZ00121 1505 AAEAKKKADEA-----KKAEEAKKA--DEAKKAEEA--KKADEAKKAEEKKKadELKKAEELKKAEEKKKAEEAKKAEED 1575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 768 KEIHLQDAARRRllKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEKDLTTSQEAVAKEIR 847
Cdd:PTZ00121 1576 KNMALRKAEEAK--KAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELK 1653
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 264681543 848 EDTDAHRRKAAleehmfqKLLENSQMGGRRAQRWKEAEEKEfhlqsAKKASAL 900
Cdd:PTZ00121 1654 KAEEENKIKAA-------EEAKKAEEDKKKAEEAKKAEEDE-----KKAAEAL 1694
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
713-921 |
2.97e-08 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 57.36 E-value: 2.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 713 QAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELE--IKEIHLQDAARRRLLKLQQDQREM 790
Cdd:COG3064 1 AQEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEeeAREAKAEAEQRAAELAAEAAKKLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 791 ELRRLEDEIERKVQMRDQEIAATA-KDLEIRQLELEAQKRLYEKdlttSQEAVAKEIREDTDAHRRKAALEEHMFQKLLE 869
Cdd:COG3064 81 EAEKAAAEAEKKAAAEKAKAAKEAeAAAAAEKAAAAAEKEKAEE----AKRKAEEEAKRKAEEERKAAEAEAAAKAEAEA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 264681543 870 NSQMGGRRAQRWKEAEEKEFHLQSAKKASALSDASRKWFLRQETSAALEHEE 921
Cdd:COG3064 157 ARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAA 208
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
686-861 |
4.61e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.23 E-value: 4.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 686 DYQTREWERIRNDELDFLRERQTVENMQaevdeqrakdeawyQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKREL 765
Cdd:COG4913 260 LAERYAAARERLAELEYLRAALRLWFAQ--------------RRLELLEAELEELRAELARLEAELERLEARLDALREEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 766 EIKEIHLQDAARRRLLKLQQdqremELRRLEDEIERKVQMRDQ----------EIAATAKDLEIRQLELEAQKRLYEKDL 835
Cdd:COG4913 326 DELEAQIRGNGGDRLEQLER-----EIERLERELEERERRRARleallaalglPLPASAEEFAALRAEAAALLEALEEEL 400
|
170 180
....*....|....*....|....*.
gi 264681543 836 TTSQEAVAKEIREDTDAHRRKAALEE 861
Cdd:COG4913 401 EALEEALAEAEAALRDLRRELRELEA 426
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
696-921 |
6.31e-08 |
|
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: 55.81 E-value: 6.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 696 RNDELDFLRERQTVENMQAEvdEQRAKDEawyQKQELLRRaeETRREILLQEEEKMAQQRQRLAAVKRELE------IKE 769
Cdd:pfam15558 16 RHKEEQRMRELQQQAALAWE--ELRRRDQ---KRQETLER--ERRLLLQQSQEQWQAEKEQRKARLGREERrradrrEKQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 770 IHLQDAARRRLLKLQQDQRE--MELRRLEDEIERKVQ-------------MRDQEIAATAKDLEI----RQL-ELEAQKR 829
Cdd:pfam15558 89 VIEKESRWREQAEDQENQRQekLERARQEAEQRKQCQeqrlkekeeelqaLREQNSLQLQERLEEachkRQLkEREEQKK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 830 LYEKDLttsQEAVAKEIREDTDAHRRKAalEEHMFQKLLENS---------QMGGRRAQRWKE-AEEKEFHLQSAKKASA 899
Cdd:pfam15558 169 VQENNL---SELLNHQARKVLVDCQAKA--EELLRRLSLEQSlqrsqenyeQLVEERHRELREkAQKEEEQFQRAKWRAE 243
|
250 260
....*....|....*....|....*
gi 264681543 900 LSDASRKWFLR---QETSAALEHEE 921
Cdd:pfam15558 244 EKEEERQEHKEalaELADRKIQQAR 268
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
699-898 |
1.79e-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: 55.45 E-value: 1.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 699 ELDFLRER-QTVENMQAEVDEQRAKDEawyQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELEIKEIHLQD--- 774
Cdd:TIGR02168 303 QKQILRERlANLERQLEELEAQLEELE---SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEElee 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 775 -----AARRRLLKLQQDQREMELRRLEDEIERKVQMRDQEIAatakdlEIRQLEleaqKRLYEKDLTTSQEAVAKEIRED 849
Cdd:TIGR02168 380 qletlRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQ------EIEELL----KKLEEAELKELQAELEELEEEL 449
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 264681543 850 TDAHRRKAALEEhmfqkLLENSQMGGRRAQRWKEAEEKEFHLQSAKKAS 898
Cdd:TIGR02168 450 EELQEELERLEE-----ALEELREELEEAEQALDAAERELAQLQARLDS 493
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
692-888 |
1.80e-07 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 54.15 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 692 WERIRNDELDFLRERQT-VENMQAEVDEQRAKDEAWYQKQ-----ELLRRAEETRREILLQEEEKMAQQRQRLAAVKREL 765
Cdd:pfam13868 107 VERIQEEDQAEAEEKLEkQRQLREEIDEFNEEQAEWKELEkeeerEEDERILEYLKEKAEREEEREAEREEIEEEKEREI 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 766 ---------EIKEIHLQDAARRRLL------KLQQDQREMELRRLEDEIERKvQMRDQEIAATAkdlEIRQLELEAQKRL 830
Cdd:pfam13868 187 arlraqqekAQDEKAERDELRAKLYqeeqerKERQKEREEAEKKARQRQELQ-QAREEQIELKE---RRLAEEAEREEEE 262
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 264681543 831 YEKDLTTSQEAVAKEIREdtdAHRRKAALEEHmfQKLLENsQMGGRRAQRWKEAEEKE 888
Cdd:pfam13868 263 FERMLRKQAEDEEIEQEE---AEKRRMKRLEH--RRELEK-QIEEREEQRAAEREEEL 314
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
682-832 |
2.62e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 54.40 E-value: 2.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 682 KFIVDYQTREWERIRNDEL-----DFLRERQTVENmqaEVDEQRAKdeawYQKQEL-LRRAEET---RREILLQEEEKMA 752
Cdd:PRK12704 41 KRILEEAKKEAEAIKKEALleakeEIHKLRNEFEK---ELRERRNE----LQKLEKrLLQKEENldrKLELLEKREEELE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 753 QQRQRLAAVKRELEIKEIHLQDAARRRLLKLQQ-------DQREMELRRLEDEIErkvqmrdQEIAATAKDLEiRQLELE 825
Cdd:PRK12704 114 KKEKELEQKQQELEKKEEELEELIEEQLQELERisgltaeEAKEILLEKVEEEAR-------HEAAVLIKEIE-EEAKEE 185
|
....*..
gi 264681543 826 AQKRLYE 832
Cdd:PRK12704 186 ADKKAKE 192
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
683-907 |
3.62e-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: 3.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 683 FIVDYQTREWE-RIRNDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRR-EILLQEEEKMAQQRQRLAA 760
Cdd:pfam02463 168 KRKKKEALKKLiEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLyLDYLKLNEERIDLLQELLR 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 761 VKRELEIKEIHLQDAARRRLLKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRlyEKDLTTSQE 840
Cdd:pfam02463 248 DEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKL--KESEKEKKK 325
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 264681543 841 AVAKEIREDTDAHRRKAALEEHMFQKLLENSQMGGRRAQRWKEAEEKEFHLQSAKKASA--LSDASRKW 907
Cdd:pfam02463 326 AEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESErlSSAAKLKE 394
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
688-828 |
3.90e-07 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 53.80 E-value: 3.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 688 QTREWE--RIRNDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKREL 765
Cdd:pfam15709 382 QQRRFEeiRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQL 461
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 264681543 766 EIKEIHLQD-AARRRLLKLQQDQREMELRRLEDEIERKvqmRDQEIAATAKDLEIRQLELEAQK 828
Cdd:pfam15709 462 AEEQKRLMEmAEEERLEYQRQKQEAEEKARLEAEERRQ---KEEEAARLALEEAMKQAQEQARQ 522
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
690-922 |
4.03e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 54.30 E-value: 4.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 690 REWERIRNdELDFLRERqtVENMQAEVDE--------QRAKDEAwYQKQELLRRAEETRREILLQEEEKMAQQRQR---- 757
Cdd:TIGR02169 170 RKKEKALE-ELEEVEEN--IERLDLIIDEkrqqlerlRREREKA-ERYQALLKEKREYEGYELLKEKEALERQKEAierq 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 758 LAAVKRELEIKEIHLQDAARRrllklqQDQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEKDLTT 837
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKR------LEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELED 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 838 SQEAVAKEIREDTDAHRRKAALEEHMFQKLLENSQMGGRRAQRWKEAEEKEFHLQSAKKASALsdasrkwfLRQETSAAL 917
Cdd:TIGR02169 320 AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAE--------TRDELKDYR 391
|
....*
gi 264681543 918 EHEEM 922
Cdd:TIGR02169 392 EKLEK 396
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
688-897 |
4.93e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.99 E-value: 4.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 688 QTREWERIRNDEldflRERQTVENMQAEvDEQRA----KDEAWYQKQELLRRAEETR--REILLQEEEKMAQQRQRLAAV 761
Cdd:PTZ00121 1198 DARKAEAARKAE----EERKAEEARKAE-DAKKAeavkKAEEAKKDAEEAKKAEEERnnEEIRKFEEARMAHFARRQAAI 1272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 762 KRELEIKEIHLQDAARRRllKLQQDQREMELRRLeDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEKdlttSQEA 841
Cdd:PTZ00121 1273 KAEEARKADELKKAEEKK--KADEAKKAEEKKKA-DEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEA----KKAA 1345
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 264681543 842 VAKEIREDTDAHRRKAALEEHMFQKLlENSQMGGRRAQRWKEAEEKEFHLQSAKKA 897
Cdd:PTZ00121 1346 EAAKAEAEAAADEAEAAEEKAEAAEK-KKEEAKKKADAAKKKAEEKKKADEAKKKA 1400
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
703-867 |
6.14e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.79 E-value: 6.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 703 LRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELEIKEIHLQDAARRRLLK 782
Cdd:COG1196 680 ELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEP 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 783 LQQDQREMELRRLEDEIER--KVQMR-DQEIAATAKDLEirqlELEAQKrlyeKDLTTSQEAVAKEIRE-DTDAHRR-KA 857
Cdd:COG1196 760 PDLEELERELERLEREIEAlgPVNLLaIEEYEELEERYD----FLSEQR----EDLEEARETLEEAIEEiDRETRERfLE 831
|
170
....*....|....*.
gi 264681543 858 ALEE------HMFQKL 867
Cdd:COG1196 832 TFDAvnenfqELFPRL 847
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
721-897 |
7.94e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 52.86 E-value: 7.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 721 AKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLaavKRELEIKEIHLQDAARRRLlklqqdQREMELRRLEDEIE 800
Cdd:PRK12704 36 AEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEF---EKELRERRNELQKLEKRLL------QKEENLDRKLELLE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 801 RkvqmRDQEIAATAKDLEIRQLELEAQKRLYEKdLTTSQEAVAKEIredtdahrrkAAL-EEHMFQKLLEN--SQMGGRR 877
Cdd:PRK12704 107 K----REEELEKKEKELEQKQQELEKKEEELEE-LIEEQLQELERI----------SGLtAEEAKEILLEKveEEARHEA 171
|
170 180
....*....|....*....|
gi 264681543 878 AQRWKEAEEkEFHLQSAKKA 897
Cdd:PRK12704 172 AVLIKEIEE-EAKEEADKKA 190
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
712-920 |
1.05e-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: 51.84 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 712 MQAEVDEQRA-----KDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELeikEIHLQDAARRRLLKLQQD 786
Cdd:pfam13868 20 CNKERDAQIAekkriKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQEL---EEQIEEREQKRQEEYEEK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 787 QREMEL-----RRLEDEIERKVQMRDQEIAATAKDL--------EIRQLELEAQKRL------YEKDLTTSQEAVAKEIR 847
Cdd:pfam13868 97 LQEREQmdeivERIQEEDQAEAEEKLEKQRQLREEIdefneeqaEWKELEKEEEREEderileYLKEKAEREEEREAERE 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 264681543 848 EDTDAH-RRKAALEEHMFQKLLENSQMGGRRAQRWKEAEEKEFHLQsakkasALSDASRKWFLRQETSAALEHE 920
Cdd:pfam13868 177 EIEEEKeREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQK------EREEAEKKARQRQELQQAREEQ 244
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
691-928 |
1.16e-06 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 51.77 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 691 EWERIRNDELDFLR-ERQT---VENMQAEVDEQRAKDEAwyQKQELLRRAEEtrreillQEEEKMAQQRQRLAAVKR--E 764
Cdd:TIGR02794 51 QANRIQQQKKPAAKkEQERqkkLEQQAEEAEKQRAAEQA--RQKELEQRAAA-------EKAAKQAEQAAKQAEEKQkqA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 765 LEIKEIHLQDAArrrllklqqdqremelRRLEDEIERKVQmrdQEIAATAKDLEIRQLELEAQKRLYEKDLTTSQEAVAK 844
Cdd:TIGR02794 122 EEAKAKQAAEAK----------------AKAEAEAERKAK---EEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 845 EiredtDAhRRKAALEEHMFQKLlensqmgGRRAQRWKEAEEKefhLQSAKKASALSDASRK-WFLRQETSAALEHEEMP 923
Cdd:TIGR02794 183 A-----EA-EAKAKAEEAKAKAE-------AAKAKAAAEAAAK---AEAEAAAAAAAEAERKaDEAELGDIFGLASGSNA 246
|
....*
gi 264681543 924 WLQRQ 928
Cdd:TIGR02794 247 EKQGG 251
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
688-873 |
1.32e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.46 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 688 QTREWERIRNDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREiLLQEEEKMAQQRQRLAAVKRelei 767
Cdd:COG4717 86 KEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAE-LAELPERLEELEERLEELRE---- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 768 keihlqdaarrrlLKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEKDLTTSQEAVaKEIR 847
Cdd:COG4717 161 -------------LEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEEL-EELE 226
|
170 180
....*....|....*....|....*.
gi 264681543 848 EDTDAHRRKAALEEhMFQKLLENSQM 873
Cdd:COG4717 227 EELEQLENELEAAA-LEERLKEARLL 251
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
691-855 |
1.74e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.45 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 691 EWERIRNDELDFLRE-RQTVENMQAEVDEQ--------RAKDEAWYQKQELLRRAEETRR--EILLQEEE---KMAQQRQ 756
Cdd:PTZ00121 1616 EEAKIKAEELKKAEEeKKKVEQLKKKEAEEkkkaeelkKAEEENKIKAAEEAKKAEEDKKkaEEAKKAEEdekKAAEALK 1695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 757 RLAAVKRELEikEIHLQDAARRRllKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKDLE-----IRQLELEAQKRLY 831
Cdd:PTZ00121 1696 KEAEEAKKAE--ELKKKEAEEKK--KAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEeekkkIAHLKKEEEKKAE 1771
|
170 180
....*....|....*....|....
gi 264681543 832 EkdLTTSQEAVAKEIREDTDAHRR 855
Cdd:PTZ00121 1772 E--IRKEKEAVIEEELDEEDEKRR 1793
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
684-888 |
2.18e-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: 51.07 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 684 IVDYQTREWERIR------NDELDFLRERQTVENMQAEVDEQRAKDEAWYQ-KQEL-----------LRRAEETRREILL 745
Cdd:pfam13868 23 ERDAQIAEKKRIKaeekeeERRLDEMMEEERERALEEEEEKEEERKEERKRyRQELeeqieereqkrQEEYEEKLQEREQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 746 --------QEEEKMAQQRQRlaavKRELEIKEIHLQDAARRRLLKLQQDQREMELRRLEDEIERKVQMRDQEIAAtakdl 817
Cdd:pfam13868 103 mdeiveriQEEDQAEAEEKL----EKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREA----- 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 264681543 818 eiRQLELEAQKRLYEKDLTTSQEAvAKEIREDTDAHRRKAALEEHmfqkllensqmggRRAQRWKEAEEKE 888
Cdd:pfam13868 174 --EREEIEEEKEREIARLRAQQEK-AQDEKAERDELRAKLYQEEQ-------------ERKERQKEREEAE 228
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
704-832 |
3.67e-06 |
|
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: 47.73 E-value: 3.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 704 RERQTVENMQAEVDEQRAKDEAWYQ-KQELLRRAEETRREillQEEE--KMAQQRQRLAAVKRELEIKEIHLQDAARRRL 780
Cdd:pfam05672 19 KRRQAREQREREEQERLEKEEEERLrKEELRRRAEEERAR---REEEarRLEEERRREEEERQRKAEEEAEEREQREQEE 95
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 264681543 781 LKLQQDQREMELRRLEDEIERKVQMRDQEIaatakdLEIRQLELEAQKRLYE 832
Cdd:pfam05672 96 QERLQKQKEEAEAKAREEAERQRQEREKIM------QQEEQERLERKKRIEE 141
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
688-900 |
3.87e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.30 E-value: 3.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 688 QTREWERIRNDELdfLRERQTVENMQA--EVDEQRAKDEAwyQKQELLRRAEETRReilLQEEEKMAQQRQRLAAVKREL 765
Cdd:PTZ00121 1180 AARKAEEVRKAEE--LRKAEDARKAEAarKAEEERKAEEA--RKAEDAKKAEAVKK---AEEAKKDAEEAKKAEEERNNE 1252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 766 EIKEIhlqDAARRRLLKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKdlEIRQLElEAQKRLYEKDLTTSQEAVAKE 845
Cdd:PTZ00121 1253 EIRKF---EEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAE--EKKKAD-EAKKKAEEAKKADEAKKKAEE 1326
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 846 IREDTDAHRRKAalEE-----HMFQKLLENSQMGGRRAQRWKEAEEKEFHlQSAKKASAL 900
Cdd:PTZ00121 1327 AKKKADAAKKKA--EEakkaaEAAKAEAEAAADEAEAAEEKAEAAEKKKE-EAKKKADAA 1383
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
707-897 |
4.05e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.11 E-value: 4.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 707 QTVENMQAEVDEQRAKDEAwyqkQELLRRAEETR--------REILLQEEEKMAQQRQRLAAVKRELEIK-EIHLQDAAr 777
Cdd:PRK04863 480 QLVRKIAGEVSRSEAWDVA----RELLRRLREQRhlaeqlqqLRMRLSELEQRLRQQQRAERLLAEFCKRlGKNLDDED- 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 778 rrLLKLQQDQREMELRRLEDE----IERKVQMRDQEIAATAkdlEIRQLELEAQKRLyekdltTSQEAVAK--EIREDTD 851
Cdd:PRK04863 555 --ELEQLQEELEARLESLSESvseaRERRMALRQQLEQLQA---RIQRLAARAPAWL------AAQDALARlrEQSGEEF 623
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 264681543 852 AHRrkAALEEHMfQKLLEnsqmggrraqRWKEAEEKEFHLQSAKKA 897
Cdd:PRK04863 624 EDS--QDVTEYM-QQLLE----------RERELTVERDELAARKQA 656
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
696-944 |
4.12e-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: 4.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 696 RNDELDFLRERqtVENMQAEVDEQRAKDEAWYQKQE--------LLRRAEETRREI---------LLQEEEKMAQQRQRL 758
Cdd:TIGR02168 675 RRREIEELEEK--IEELEEKIAELEKALAELRKELEeleeeleqLRKELEELSRQIsalrkdlarLEAEVEQLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 759 aavkrELEIKEIhlqdAARRRLLKLQQDQREMELRRLEDEIErKVQMRDQEIAATAKDLEIRQLELEAQKRLYEKDLTTS 838
Cdd:TIGR02168 753 -----SKELTEL----EAEIEELEERLEEAEEELAEAEAEIE-ELEAQIEQLKEELKALREALDELRAELTLLNEEAANL 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 839 QEAVAKEIREDTDAHRRKAALEEHMFQKLLENSQMGGRRAQRWKEAEEKEFHLQSAKKASALSDASRKWFLRQETSAALE 918
Cdd:TIGR02168 823 RERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEE 902
|
250 260
....*....|....*....|....*.
gi 264681543 919 HEEMPwLQRQYMDSAYLPQTSRLHDV 944
Cdd:TIGR02168 903 LRELE-SKRSELRRELEELREKLAQL 927
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
693-896 |
4.62e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 4.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 693 ERIRNDELDFLRERQTVENMQaEVDEQRAKDEawyQKQELLRRAEETRreillQEEEKMAQQRQRLAAVKRELEIKEIHL 772
Cdd:PTZ00121 1544 EKKKADELKKAEELKKAEEKK-KAEEAKKAEE---DKNMALRKAEEAK-----KAEEARIEEVMKLYEEEKKMKAEEAKK 1614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 773 QDAARrrlLKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEKDLTTSQEA--VAKEIREDT 850
Cdd:PTZ00121 1615 AEEAK---IKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAkkAEEDEKKAA 1691
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 264681543 851 DAHRRKAAlEEHMFQKLLENSQMGGRRAQRWKEAEE-KEFHLQSAKK 896
Cdd:PTZ00121 1692 EALKKEAE-EAKKAEELKKKEAEEKKKAEELKKAEEeNKIKAEEAKK 1737
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
706-861 |
4.66e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.21 E-value: 4.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 706 RQTVENMQAEVDE-QRAKDEAWYQKQELLRRAEETRREILlQEEEKMAQQRQRLAAVKRELEIKEI------------HL 772
Cdd:COG3883 36 QAELDALQAELEElNEEYNELQAELEALQAEIDKLQAEIA-EAEAEIEERREELGERARALYRSGGsvsyldvllgseSF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 773 QDAARRRLL--KLQQDQREM--ELRRLEDEIERKvqmrDQEIAATAKDLEIRQLELEAQKRLYEKDLTTSQEAVAKEIRE 848
Cdd:COG3883 115 SDFLDRLSAlsKIADADADLleELKADKAELEAK----KAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAE 190
|
170
....*....|...
gi 264681543 849 DTDAHRRKAALEE 861
Cdd:COG3883 191 EAAAEAQLAELEA 203
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
691-808 |
5.03e-06 |
|
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: 47.34 E-value: 5.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 691 EWERIRNDELdflRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEEKMA-QQRQRLAAVKRELEike 769
Cdd:pfam05672 39 EEERLRKEEL---RRRAEEERARREEEARRLEEERRREEEERQRKAEEEAEEREQREQEEQErLQKQKEEAEAKARE--- 112
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 264681543 770 ihlqDAARRRLLKLQQDQREMELR-----RLEdEIERKVQMRDQ 808
Cdd:pfam05672 113 ----EAERQRQEREKIMQQEEQERlerkkRIE-EIMKRTRKSDQ 151
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
714-861 |
5.20e-06 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 50.26 E-value: 5.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 714 AEVDEQRAKDEAwyqkqELLRRAEETRREILLQEEEKMAQQrqrlaavKRELEIKEIHLQDAARRRllKLQQDQREMELR 793
Cdd:COG2268 195 AEIIRDARIAEA-----EAERETEIAIAQANREAEEAELEQ-------EREIETARIAEAEAELAK--KKAEERREAETA 260
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 264681543 794 RLEDEIERKVQmrdQEIAATAKDLEIRQLELEAQKRLYEKDLTTSQEAVAKEIREDTDAHRRKAALEE 861
Cdd:COG2268 261 RAEAEAAYEIA---EANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEA 325
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
686-937 |
1.01e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 686 DYQTREWERIRnDELDFLRErqtvenmqAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKREL 765
Cdd:COG4717 315 ELEEEELEELL-AALGLPPD--------LSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEE 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 766 EIKEIHLQDAARRRLLKlQQDQREMELRRLEDEIERKVQMRDQEiaatakDLEIRQLELEAQKRLYEKDLttsqeavake 845
Cdd:COG4717 386 ELRAALEQAEEYQELKE-ELEELEEQLEELLGELEELLEALDEE------ELEEELEELEEELEELEEEL---------- 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 846 iredTDAHRRKAALEEHMfqKLLENSQmggrraqrwkEAEEKEFHLQSAKkaSALSDASRKWFLRQETSAALEHeempwL 925
Cdd:COG4717 449 ----EELREELAELEAEL--EQLEEDG----------ELAELLQELEELK--AELRELAEEWAALKLALELLEE-----A 505
|
250
....*....|..
gi 264681543 926 QRQYMDSaYLPQ 937
Cdd:COG4717 506 REEYREE-RLPP 516
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
699-849 |
1.05e-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: 48.00 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 699 ELDFLRERQtvENMQAEVDEQRAKDEAWYQKQELLRRA-EETRREI------LLQEEEKMAQQRQRLAAVK--RELEI-- 767
Cdd:COG1579 18 ELDRLEHRL--KELPAELAELEDELAALEARLEAAKTElEDLEKEIkrleleIEEVEARIKKYEEQLGNVRnnKEYEAlq 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 768 KEIHLqdaarrrlLKLQQDQREMELRRLEDEIERKVQMRDQ---EIAATAKDLEIRQLELEAQKRLYEKD---LTTSQEA 841
Cdd:COG1579 96 KEIES--------LKRRISDLEDEILELMERIEELEEELAEleaELAELEAELEEKKAELDEELAELEAEleeLEAEREE 167
|
....*...
gi 264681543 842 VAKEIRED 849
Cdd:COG1579 168 LAAKIPPE 175
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
719-886 |
1.24e-05 |
|
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 198 and 469 amino acids in length. There are two completely conserved L residues that may be functionally important.
Pssm-ID: 405647 [Multi-domain] Cd Length: 206 Bit Score: 47.46 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 719 QRAKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLaaVKRELEIKEIHLQDAARRRLLKLQQDQrEMELRRLEDE 798
Cdd:pfam14988 17 QKKIEKLWNQYVQECEEIERRRQELASRYTQQTAELQTQL--LQKEKEQASLKKELQALRPFAKLKESQ-EREIQDLEEE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 799 IeRKVQmrdQEIAATAKDLEIRQLELEA--QKRLYEKDLTTSQEAVAKEIREDTDAHRRKA--ALEEHM----------- 863
Cdd:pfam14988 94 K-EKVR---AETAEKDREAHLQFLKEKAllEKQLQELRILELGERATRELKRKAQALKLAAkqALSEFCrsikrenrqlq 169
|
170 180 190
....*....|....*....|....*....|..
gi 264681543 864 ---------FQKLLENSQMGGRRAQRWKEAEE 886
Cdd:pfam14988 170 kellqliqeTQALEAIKSKLENRKQRLKEEQW 201
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
713-850 |
1.38e-05 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 47.19 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 713 QAEVDEQRAKDEAwyqKQEllrrAEETRREILLQEEEKMAQQRQRLaavkrELEIKEihlqdaaRRRLLKLQQD---QRE 789
Cdd:pfam12072 31 SAEELAKRIIEEA---KKE----AETKKKEALLEAKEEIHKLRAEA-----ERELKE-------RRNELQRQERrllQKE 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 264681543 790 MEL-RRLE--DEIERKVQMRDQEIAATAKDLEIRQLELEA-----QKRLYEKDLTTSQEA-------VAKEIREDT 850
Cdd:pfam12072 92 ETLdRKDEslEKKEESLEKKEKELEAQQQQLEEKEEELEElieeqRQELERISGLTSEEAkeilldeVEEELRHEA 167
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
704-858 |
1.47e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 704 RERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREiLLQEEEKMAQQRQRLAAVKRELE--------IKEIHLQ-D 774
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQERREALQRLAE-YSWDEIDVASAEREIAELEAELErldassddLAALEEQlE 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 775 AARRRLLKLQQDQREM--ELRRLEDEIERKVQMRD--QEIAATAKDLEIRQLELEAQKRLYEkdltTSQEAVAKEIREDT 850
Cdd:COG4913 696 ELEAELEELEEELDELkgEIGRLEKELEQAEEELDelQDRLEAAEDLARLELRALLEERFAA----ALGDAVERELRENL 771
|
....*...
gi 264681543 851 DAHRRKAA 858
Cdd:COG4913 772 EERIDALR 779
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
693-922 |
1.63e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 693 ERIRNDELdflreRQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREILLQ---EEEKMAQQRQRLAAVKRELEIKE 769
Cdd:PTZ00121 1389 EKKKADEA-----KKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKkkaEEAKKADEAKKKAEEAKKAEEAK 1463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 770 IHLQDAARRRLLKLQQDQREM--ELRRLEDEIERKVQMRDQEIAATAKDLEIRQLElEAQK----RLYEKDLTTSQEAVA 843
Cdd:PTZ00121 1464 KKAEEAKKADEAKKKAEEAKKadEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAE-EAKKadeaKKAEEAKKADEAKKA 1542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 844 KEIREDTDAHR----RKAALEEHMFQ--KLLENSQMGGRRAQRWKEAEEKEfhLQSAKKASALSDASRKWFLRQETSAAL 917
Cdd:PTZ00121 1543 EEKKKADELKKaeelKKAEEKKKAEEakKAEEDKNMALRKAEEAKKAEEAR--IEEVMKLYEEEKKMKAEEAKKAEEAKI 1620
|
....*
gi 264681543 918 EHEEM 922
Cdd:PTZ00121 1621 KAEEL 1625
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
689-922 |
1.74e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 48.26 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 689 TREWERIRNDELDFLR---ERQTVENMQAEvdEQRAKDEAWYQK-----------QELLRRAEETRREILLQEEEKMAQQ 754
Cdd:PRK09510 61 VEQYNRQQQQQKSAKRaeeQRKKKEQQQAE--ELQQKQAAEQERlkqlekerlaaQEQKKQAEEAAKQAALKQKQAEEAA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 755 RQRLAAVKRELEIKEIHLQDAArrrllklqqdqremelRRLEDEIERKvqmrdqEIAATAKdleirQLELEAQKRLYEKd 834
Cdd:PRK09510 139 AKAAAAAKAKAEAEAKRAAAAA----------------KKAAAEAKKK------AEAEAAK-----KAAAEAKKKAEAE- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 835 lttSQEAVAKEIREDTDAHRRKAALEEhmfqkllensqmggrrAQRWKEAEEKEFHLQSAKKASALSDASRKWFLRQETS 914
Cdd:PRK09510 191 ---AAAKAAAEAKKKAEAEAKKKAAAE----------------AKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAA 251
|
....*...
gi 264681543 915 AALEHEEM 922
Cdd:PRK09510 252 AAKAAAEV 259
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
697-869 |
2.65e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 697 NDELDFLRERQTVENMQAEVDEQ----RAKDEAWYQKQELLRRAEETRREIllqeeekmAQQRQRLAAVKRELeikeihl 772
Cdd:COG4913 637 EAELDALQERREALQRLAEYSWDeidvASAEREIAELEAELERLDASSDDL--------AALEEQLEELEAEL------- 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 773 qDAARRRLLKLQQDQR--EMELRRLEDEIERKvqmrdQEIAATAKDLEIRQLELEAQKRLYEKDLTTSQEAVAKEIREDT 850
Cdd:COG4913 702 -EELEEELDELKGEIGrlEKELEQAEEELDEL-----QDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERI 775
|
170
....*....|....*....
gi 264681543 851 DAHRRKAALEEHMFQKLLE 869
Cdd:COG4913 776 DALRARLNRAEEELERAMR 794
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
693-925 |
2.73e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.59 E-value: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 693 ERIRNDELDFLRERQTVENMQAEVDEQRAKDEAwyQKQELLRRAEETRREiLLQEEEKMAQQRQRLAAVKRELEIKEIHL 772
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALF--ELDKLQEELEQLREE-LEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 773 QDAaRRRLLKLQQDQREM--ELRRLEDEIERKVQMRdQEIAATAKDLEIRQLELEAQKRLYEKDLTtSQEAVAKEIREDT 850
Cdd:COG4372 83 EEL-NEQLQAAQAELAQAqeELESLQEEAEELQEEL-EELQKERQDLEQQRKQLEAQIAELQSEIA-EREEELKELEEQL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 264681543 851 dahrrkAALEEHMFQKLLENSQMGGRRAQRWKEAEEKEFHLQSAKKASALSDASRKWFLRQETSAALEHEEMPWL 925
Cdd:COG4372 160 ------ESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLE 228
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
735-886 |
2.83e-05 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 45.42 E-value: 2.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 735 RAEETRReiLLQEEEKMA-QQRQRLAAVKRELEIKEIHLQDAARRRLLKLQQDQREmELRRLEDeiERKVQMRDQEIAAT 813
Cdd:pfam05672 8 DAEEAAR--ILAEKRRQArEQREREEQERLEKEEEERLRKEELRRRAEEERARREE-EARRLEE--ERRREEEERQRKAE 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 264681543 814 AKDLEIRQLELEAQKRLYEKdlttSQEAVAKEiREdtDAHRRKAALEEHMFQKLLEnsqmggrRAQRWKEAEE 886
Cdd:pfam05672 83 EEAEEREQREQEEQERLQKQ----KEEAEAKA-RE--EAERQRQEREKIMQQEEQE-------RLERKKRIEE 141
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
707-886 |
3.34e-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: 48.02 E-value: 3.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 707 QTVENMQAEVDeqraKDEAWYQKQELLRRAEETRreillqeeeKMAQQRQRLAAVKRELEiKEIHLQDAARRRL------ 780
Cdd:COG3096 479 ELVCKIAGEVE----RSQAWQTARELLRRYRSQQ---------ALAQRLQQLRAQLAELE-QRLRQQQNAERLLeefcqr 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 781 ----------LKLQQDQREMELRRLEDE----IERKVQMRDQEIAATAKDLEIRQLE---LEAQKRLyEKDLTTSQEAVA 843
Cdd:COG3096 545 igqqldaaeeLEELLAELEAQLEELEEQaaeaVEQRSELRQQLEQLRARIKELAARApawLAAQDAL-ERLREQSGEALA 623
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 264681543 844 KeiREDTDAHRRKAALEEHMFQklLENSQMGGRRAQRWKEAEE 886
Cdd:COG3096 624 D--SQEVTAAMQQLLEREREAT--VERDELAARKQALESQIER 662
|
|
| COG5210 |
COG5210 |
GTPase-activating protein [General function prediction only]; |
542-658 |
3.54e-05 |
|
GTPase-activating protein [General function prediction only];
Pssm-ID: 227535 [Multi-domain] Cd Length: 496 Bit Score: 47.49 E-value: 3.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 542 LSMIENVLAFHDKELLQHFIDRDITSQVYAWPLLETLFSEVLTREEWLRLFDNIFSNHPSFLLMTVVAYSTCSRAPLLNC 621
Cdd:COG5210 350 LKVLDDLVEELDPELYEHLLREGVVLLMFAFRWFLTLFVREFPLEYALRIWDCLFLEGSSMLFQLALAILKLLRDKLLKL 429
|
90 100 110
....*....|....*....|....*....|....*..
gi 264681543 622 TLKNDFEYFFHHRNNLDINVVIREVYHLMETTPADIH 658
Cdd:COG5210 430 DSDELLDLLLKQLFLHSGKEAWSSILKFRHGTDRDIL 466
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
684-897 |
3.64e-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: 47.76 E-value: 3.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 684 IVDYQTREWERIRN--DELDFL-RERQTVENMQAEVD---EQRAKDEAWYQKQ--ELLRRAEETRREILLQEEEKMAQQR 755
Cdd:TIGR02169 728 LEQEEEKLKERLEEleEDLSSLeQEIENVKSELKELEariEELEEDLHKLEEAlnDLEARLSHSRIPEIQAELSKLEEEV 807
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 756 QRLAAVKRELEIKEihlqdaaRRRLLKLQQDQREM-ELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEaQKRLYEKD 834
Cdd:TIGR02169 808 SRIEARLREIEQKL-------NRLTLEKEYLEKEIqELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELE-ELEAALRD 879
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 264681543 835 LTTSQEAVAKEiREDTDAHRRKA--ALEEHMFQKLLENSQMGGRRAQRwKEAEEKEFHLQSAKKA 897
Cdd:TIGR02169 880 LESRLGDLKKE-RDELEAQLRELerKIEELEAQIEKKRKRLSELKAKL-EALEEELSEIEDPKGE 942
|
|
| Fibrinogen_BP |
pfam08017 |
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family ... |
704-887 |
4.26e-05 |
|
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family includes the fibrinogen receptor, FbsA, which mediates platelet aggregation.
Pssm-ID: 311808 [Multi-domain] Cd Length: 393 Bit Score: 47.17 E-value: 4.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 704 RERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEetrREILLQEEEKMAQQRQRLAAVKRELEIKEIHLQDAARRRLLK- 782
Cdd:pfam08017 130 RQRDAENRSQGNVLERRQRDAENRSQGNVLERRQ---RDAENRSQGNVLERRQRDAENKSQGNVLERRQRDAENRSQGNv 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 783 LQQDQREMELRRLEDEIERKvqMRDQEIAATAKDLEIRQLELEAQkrlyekdlttSQEAVAKEIREDTDAHRRKAALEEH 862
Cdd:pfam08017 207 LERRQRDAENRSQGNVLERR--QRDAENRSQGNVLERRQRDAENK----------SQGNVLERRQRDAENRSQGNVLERR 274
|
170 180
....*....|....*....|....*
gi 264681543 863 mfQKLLENSQMGGRRAQRWKEAEEK 887
Cdd:pfam08017 275 --QRDAENRSQGNVLERRQRDAENK 297
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
696-896 |
4.64e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.82 E-value: 4.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 696 RNDELDFLRERqtVENMQAEVDEQRAKDEAwyQKQELLRRAEETRReiLLQEEEKMAQQRQRLAAVKRELE--IKEIHLQ 773
Cdd:COG4372 71 ARSELEQLEEE--LEELNEQLQAAQAELAQ--AQEELESLQEEAEE--LQEELEELQKERQDLEQQRKQLEaqIAELQSE 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 774 DAARRRLLKlqqdQREMELRRLEDEIERkVQMRDQEIAATAKDLEIRQLELEAQKRLYEKDLTTSQEAVAKEIREDTDAH 853
Cdd:COG4372 145 IAEREEELK----ELEEQLESLQEELAA-LEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEE 219
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 264681543 854 RRKAALEEHMFQKLLENSQMGGRRAQRWKEAEEKEFHLQSAKK 896
Cdd:COG4372 220 LLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEE 262
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
690-858 |
6.03e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.24 E-value: 6.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 690 REWERIRNDELDFLRERQTVENMQAEVDEQRAKDEawyQKQELLRRAEETRREILLQEEEKMAQQRQRL-AAVKRELEIK 768
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEAEEALL---ERLERLEEELEELEEALAELEEEEEEEEEALeEAAEEEAELE 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 769 EIHLQDAARRRLLKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKDLE----IRQLELEAQKRL-------------- 830
Cdd:COG1196 456 EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGflegVKAALLLAGLRGlagavavligveaa 535
|
170 180 190
....*....|....*....|....*....|....*....
gi 264681543 831 YEKDLTTS-----------QEAVAKEIREDTDAHRRKAA 858
Cdd:COG1196 536 YEAALEAAlaaalqnivveDDEVAAAAIEYLKAAKAGRA 574
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
713-847 |
6.04e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 46.63 E-value: 6.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 713 QAEVDEQRAKDEAWYQKQELLRRAEET-------RREILLQEEEKMAQQRQRLAAVKRELEIKEIHLqdAARRRLLKLQQ 785
Cdd:PRK12705 41 EAQKEAEEKLEAALLEAKELLLRERNQqrqearrEREELQREEERLVQKEEQLDARAEKLDNLENQL--EEREKALSARE 118
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 264681543 786 DQREMELRRLEDEIERKVQMRDQEiaatAKDLEIRQL--ELEAQK-RLYEKDLTTSQEAVAKEIR 847
Cdd:PRK12705 119 LELEELEKQLDNELYRVAGLTPEQ----ARKLLLKLLdaELEEEKaQRVKKIEEEADLEAERKAQ 179
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
115-153 |
6.67e-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: 6.67e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 264681543 115 TKELVSWMRGHESSVCSISVHASGRYAITTSSD-TAQLWD 153
Cdd:smart00320 1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDgTIKLWD 40
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
693-905 |
6.71e-05 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 46.57 E-value: 6.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 693 ERIRNDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQE---LLRRAEETRREILLQEE--EKMAQQRQRLAAVKRELEI 767
Cdd:COG3064 16 ERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEeeaREAKAEAEQRAAELAAEaaKKLAEAEKAAAEAEKKAAA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 768 KEIHLQDAARRRlLKLQQDQREMELRRLEdEIERKVQmRDQEIAATAKDLEIRQLELEAQKRLYEKDLTTSQEAVAKEIR 847
Cdd:COG3064 96 EKAKAAKEAEAA-AAAEKAAAAAEKEKAE-EAKRKAE-EEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAA 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 264681543 848 EDTDAHRRKAALEEHMFQKLLENSQMGGRRAQRWKEAEEKEFHLQSAKKASALSDASR 905
Cdd:COG3064 173 RAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASR 230
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
703-870 |
7.80e-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: 46.89 E-value: 7.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 703 LRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEE---TRREIL------------LQEEEKMAQQRQRLAAVKRELEI 767
Cdd:TIGR00618 327 LMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEvatSIREIScqqhtltqhihtLQQQKTTLTQKLQSLCKELDILQ 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 768 KEIHLQDAARRRLLKLQQDqremeLRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEK-DLTTSQEAVAKEI 846
Cdd:TIGR00618 407 REQATIDTRTSAFRDLQGQ-----LAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSlKEREQQLQTKEQI 481
|
170 180
....*....|....*....|....
gi 264681543 847 redTDAHRRKAALEEHMFQKLLEN 870
Cdd:TIGR00618 482 ---HLQETRKKAVVLARLLELQEE 502
|
|
| EVC2_like |
pfam12297 |
Ellis van Creveld protein 2 like protein; This family of proteins is found in eukaryotes. ... |
689-873 |
9.76e-05 |
|
Ellis van Creveld protein 2 like protein; This family of proteins is found in eukaryotes. Proteins in this family are typically between 571 and 1310 amino acids in length. There are two conserved sequence motifs: LPA and ELH. EVC2 is implicated in Ellis van Creveld chondrodysplastic dwarfism in humans. Mutations in this protein can give rise to this congenital condition. LIMBIN is a protein which shares around 80% sequence homology with EVC2 and it is implicated in a similar condition in bovine chondrodysplastic dwarfism.
Pssm-ID: 463525 [Multi-domain] Cd Length: 428 Bit Score: 45.84 E-value: 9.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 689 TREWERIRNDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQELLRR-----AEETRREILLQEEEKMAQQRQRLaAVKR 763
Cdd:pfam12297 223 AAECNLETREKMEAQHQREMAEKEEAEELLKHADEQEALECSSLLDKlhkleQEHLQRSLLLRQEEDFAKAQRQL-AVFQ 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 764 ELEIKEI---HLQDAARRRLLKLQQDQREM-ELRRLEDEIERkvqMRDQEIAATAKDLEIR--QLE-----LEAQKRLYE 832
Cdd:pfam12297 302 RVELHKIfftQLKEATRKGELKPEAAKRLLqDYSKIQEQIEE---LMDFFQANQRYHLSERfaQREylvqsLQSLETRVS 378
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 264681543 833 KDLTTSQEAVAKEIREdtdaHRRKAALEEHMFQKLLENSQM 873
Cdd:pfam12297 379 GLLNTAATQLTSLIQK----MERAGYLDEEQMEMLLERAQK 415
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
691-931 |
9.81e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 46.04 E-value: 9.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 691 EWERIRND----------ELDFLRERQTvENMQAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEE------------ 748
Cdd:pfam07888 70 QWERQRRElesrvaelkeELRQSREKHE-ELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEdiktltqrvler 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 749 -----------EKMAQQRQRLAAVKRELEIKEIHLQDAARRRLLKLQ-----QDQREMELRRLEDEIERKVQMRDQeiaA 812
Cdd:pfam07888 149 etelermkeraKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQelrnsLAQRDTQVLQLQDTITTLTQKLTT---A 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 813 TAKDLEIRQleLEAQKRLYEKDLTTSQEAVA--KEIREDTDAHRRKAALEEHmfQKLLENSQMGGRRAQ---RWKE---- 883
Cdd:pfam07888 226 HRKEAENEA--LLEELRSLQERLNASERKVEglGEELSSMAAQRDRTQAELH--QARLQAAQLTLQLADaslALREgrar 301
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 264681543 884 -AEEKEFHLQSAKKasalsDASRKwflrQETSAALEHEEmPWLQRQYMD 931
Cdd:pfam07888 302 wAQERETLQQSAEA-----DKDRI----EKLSAELQRLE-ERLQEERME 340
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
727-906 |
9.82e-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: 46.59 E-value: 9.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 727 YQKQELlrraEETRREILLQEEeKMAQQRQRLAAVKRELEIKEIHLQDAARRRLLKLQQ-DQREMELRRLEDEIERKVQM 805
Cdd:TIGR02168 674 ERRREI----EELEEKIEELEE-KIAELEKALAELRKELEELEEELEQLRKELEELSRQiSALRKDLARLEAEVEQLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 806 RDQeiaatakdLEIRQLELEAQKRLYEKDLTTSQEAVAKEIREdtdahrrKAALEEHMFQKLLENSQmgGRRAQRWKEAE 885
Cdd:TIGR02168 749 IAQ--------LSKELTELEAEIEELEERLEEAEEELAEAEAE-------IEELEAQIEQLKEELKA--LREALDELRAE 811
|
170 180
....*....|....*....|.
gi 264681543 886 EKEFHLQSAKKASALSDASRK 906
Cdd:TIGR02168 812 LTLLNEEAANLRERLESLERR 832
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
693-907 |
1.08e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.53 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 693 ERIRNDELDFLRERQTVENMQAEVDEQRAKDEAwyQKQELLRRAEETRREILlQEEEKMAQQRQRLAAVKRELEIKEIH- 771
Cdd:COG4942 44 AALKKEEKALLKQLAALERRIAALARRIRALEQ--ELAALEAELAELEKEIA-ELRAELEAQKEELAELLRALYRLGRQp 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 772 ----------LQDAARR-RLLKLQQDQREMELRRLEDEIERKVQMRdQEIAATAKDLEIRQLELEAQKRLYEKdLTTSQE 840
Cdd:COG4942 121 plalllspedFLDAVRRlQYLKYLAPARREQAEELRADLAELAALR-AELEAERAELEALLAELEEERAALEA-LKAERQ 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 264681543 841 AVAKEIREDTDAHRRKAAleehmfqKLLENSQmggRRAQRWKEAEEKEFHLQSAKKASALSDASRKW 907
Cdd:COG4942 199 KLLARLEKELAELAAELA-------ELQQEAE---ELEALIARLEAEAAAAAERTPAAGFAALKGKL 255
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
693-832 |
1.09e-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: 45.68 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 693 ERIRN--DELDFLRERQTVENMQAEvDEQRAKDEAwYQKQELLRRAEETRREILLQEEEKMAQQRQR-----LAAVKREL 765
Cdd:pfam13868 194 EKAQDekAERDELRAKLYQEEQERK-ERQKEREEA-EKKARQRQELQQAREEQIELKERRLAEEAEReeeefERMLRKQA 271
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 766 EIKEIHLQDAARRRL--LKLQQD-QREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYE 832
Cdd:pfam13868 272 EDEEIEQEEAEKRRMkrLEHRRElEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKKLKE 341
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
688-860 |
1.25e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.21 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 688 QTREWERIRND---ELDFLR-ERQTVENMQAEVDEQRAK-----DEAWYQKQELLRRAEETRREI--LLQEEEKMAQQRQ 756
Cdd:TIGR02169 813 RLREIEQKLNRltlEKEYLEkEIQELQEQRIDLKEQIKSiekeiENLNGKKEELEEELEELEAALrdLESRLGDLKKERD 892
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 757 RLAAVKRELEIK--EIHLQDAARRRLLKLQQDQREM---ELRRLEDEI------------ERKVQMRDQEIAATAKDLE- 818
Cdd:TIGR02169 893 ELEAQLRELERKieELEAQIEKKRKRLSELKAKLEAleeELSEIEDPKgedeeipeeelsLEDVQAELQRVEEEIRALEp 972
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 264681543 819 -----IRQLElEAQKRLyeKDLTTSQEAVAKEIR------EDTDAHRRKAALE 860
Cdd:TIGR02169 973 vnmlaIQEYE-EVLKRL--DELKEKRAKLEEERKaileriEEYEKKKREVFME 1022
|
|
| Pinin_SDK_memA |
pfam04696 |
pinin/SDK/memA/ protein conserved region; Members of this family have very varied ... |
719-809 |
1.34e-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: 42.66 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 719 QRAKDEAWYQKQELLRRAEETRREillqeEEKMAQQRQRLAAVKREleikeihlqdaaRRRLLKLQQDQREMELRRLEDE 798
Cdd:pfam04696 19 QKFKKEESKQKEKEERRAEIEKRL-----EEKAKQEKEELEERKRE------------EREELFEERRAEQIELRALEEK 81
|
90
....*....|.
gi 264681543 799 IERKVQMRDQE 809
Cdd:pfam04696 82 LELKELMETWH 92
|
|
| TBC |
smart00164 |
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and ... |
501-609 |
1.37e-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: 44.22 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 501 AFP-FVKLFQNNQLIcFEVVATLIINWCQHWFEYFpnppinilsmienvLAFHDKELLQHFIDRDITSQVYAWPLLETLF 579
Cdd:smart00164 112 AFWcLVKLMERYGPN-FYLPDMSGLQLDLLQLDRL--------------VKEYDPDLYKHLKDLGITPSLYALRWFLTLF 176
|
90 100 110
....*....|....*....|....*....|
gi 264681543 580 SEVLTREEWLRLFDNIFSNHPSFLLMTVVA 609
Cdd:smart00164 177 ARELPLEIVLRIWDVLFAEGSDFLFRVALA 206
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
697-916 |
1.48e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 45.63 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 697 NDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAavKRELEIKEIHLQDAA 776
Cdd:pfam02029 211 NGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEQKLEELRRRRQEKESEEFEKLRQKQQ--EAELELEELKKKREE 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 777 RRRLLKLQQDQREMElrrlEDEierkvqmrdqeiaatakdleiRQLELEAQKRlyekdlttsqeavakEIREDTDahRRK 856
Cdd:pfam02029 289 RRKLLEEEEQRRKQE----EAE---------------------RKLREEEEKR---------------RMKEEIE--RRR 326
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 264681543 857 AALEEHMfQKLLENSQMGGR--------RAQRWKEAEEKEFHLQSAKKASALSDASRKWF-------LRQETSAA 916
Cdd:pfam02029 327 AEAAEKR-QKLPEDSSSEGKkpfkcfspKGSSLKITERAEFLNKSLQKSSSVKKTHPPAVvskidsrLEQYTSAI 400
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
693-835 |
1.49e-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: 44.53 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 693 ERIRNDELDFLRERQTVENMQAEVDEQRAKDEawyQKQELLRRAEEtrREILLQEEEKMAQQRQRLAavKRELEIKEIHl 772
Cdd:COG1579 48 EAAKTELEDLEKEIKRLELEIEEVEARIKKYE---EQLGNVRNNKE--YEALQKEIESLKRRISDLE--DEILELMERI- 119
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 264681543 773 qDAARRRLLKLQQdqremELRRLEDEIERKVQMRDQEIAATAKDLEirqlELEAQKRLYEKDL 835
Cdd:COG1579 120 -EELEEELAELEA-----ELAELEAELEEKKAELDEELAELEAELE----ELEAEREELAAKI 172
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
697-841 |
1.50e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.78 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 697 NDELDFLRER-QTVENMQAEVDEQRAKDEAWYQK-QELLRRAEETRREI------------LLQEEEKMAQQRQRL---- 758
Cdd:COG3206 211 SEEAKLLLQQlSELESQLAEARAELAEAEARLAAlRAQLGSGPDALPELlqspviqqlraqLAELEAELAELSARYtpnh 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 759 ---AAVKRELEIKEIHLQDAARRRLLKLQQD-----QREMELRRLEDEIERKVQmrdqEIAATAKDLEIRQLELEAQKRL 830
Cdd:COG3206 291 pdvIALRAQIAALRAQLQQEAQRILASLEAElealqAREASLQAQLAQLEARLA----ELPELEAELRRLEREVEVAREL 366
|
170
....*....|.
gi 264681543 831 YEKDLTTSQEA 841
Cdd:COG3206 367 YESLLQRLEEA 377
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
717-941 |
1.51e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 45.98 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 717 DEQRAKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELEIKEIHLQDAarRRLLKlqqdQREMELRRLE 796
Cdd:pfam12128 586 DLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFA--RTALK----NARLDLRRLF 659
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 797 DEiERKVQMRDQEIAATAKDLEIRQL-ELEAQKRLYEKDLTTSQEAVAKEIREDTDA--HRRKAALEEHMFQKLLENSQM 873
Cdd:pfam12128 660 DE-KQSEKDKKNKALAERKDSANERLnSLEAQLKQLDKKHQAWLEEQKEQKREARTEkqAYWQVVEGALDAQLALLKAAI 738
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 264681543 874 GGRRAQRWKE--AEEKEFHLQSAKKA------SALSDASRKWFLRQETSAALEHEEMPWlqRQYMDSAYLPQTSRL 941
Cdd:pfam12128 739 AARRSGAKAElkALETWYKRDLASLGvdpdviAKLKREIRTLERKIERIAVRRQEVLRY--FDWYQETWLQRRPRL 812
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
702-810 |
1.59e-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: 44.97 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 702 FLRERQTVENM-----QAEVDEQRAKdEAWYQKQELLRRAEETRREILLQEEEKMAQQRQR----LAAVKRELEIKEIHL 772
Cdd:pfam02841 181 FLQSKEAVEEAilqtdQALTAKEKAI-EAERAKAEAAEAEQELLREKQKEEEQMMEAQERSyqehVKQLIEKMEAEREQL 259
|
90 100 110
....*....|....*....|....*....|....*...
gi 264681543 773 QDAARRRLLKLQQDQREMelrrLEDEIERKVQMRDQEI 810
Cdd:pfam02841 260 LAEQERMLEHKLQEQEEL----LKEGFKTEAESLQKEI 293
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
693-900 |
1.85e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 693 ERIRNDELDFLRER-QTVENMQAEVDEQRAKDEAWYQKQELLRRAEEtRREILLQEEEKMAQQRQRLAAVKRELEIKEIH 771
Cdd:COG4717 49 ERLEKEADELFKPQgRKPELNLKELKELEEELKEAEEKEEEYAELQE-ELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 772 LQDAARRRLLKLQQDQREMELRRLEDEIERKVQMRDQeiaatakdleIRQLELEAQK------RLYEKDLTTSQEAVAKE 845
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEERLEELRELEEE----------LEELEAELAElqeeleELLEQLSLATEEELQDL 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 264681543 846 IREDTDAHRRKAALEEHmfqkLLENSQMGGRRAQRWKEAEEKEFHLQSAKKASAL 900
Cdd:COG4717 198 AEELEELQQRLAELEEE----LEEAQEELEELEEELEQLENELEAAALEERLKEA 248
|
|
| Fibrinogen_BP |
pfam08017 |
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family ... |
713-887 |
1.91e-04 |
|
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family includes the fibrinogen receptor, FbsA, which mediates platelet aggregation.
Pssm-ID: 311808 [Multi-domain] Cd Length: 393 Bit Score: 44.86 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 713 QAEVDEQRAKDEAWYQKQELLRRAEetrREILLQEEEKMAQQRQRLAAVKRELEIKEIHLQDAARRRLLK-LQQDQREME 791
Cdd:pfam08017 27 QGNVLERRQRDAENRSQGNVLERRQ---RDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNvLERRQRDAE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 792 LRRLEDEIERKvqMRDQEIAATAKDLEIRQLELEAQkrlyekdlttSQEAVAKEIREDTDAHRRKAALEEHmfQKLLENS 871
Cdd:pfam08017 104 NRSQGNVLERR--QRDAENKSQGNVLERRQRDAENR----------SQGNVLERRQRDAENRSQGNVLERR--QRDAENR 169
|
170
....*....|....*.
gi 264681543 872 QMGGRRAQRWKEAEEK 887
Cdd:pfam08017 170 SQGNVLERRQRDAENK 185
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
700-872 |
1.96e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 700 LDFLRERqtVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREI---------LLQEEEKMAQQRQRLAAVKRELEIKEI 770
Cdd:COG3206 177 LEFLEEQ--LPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLqqlselesqLAEARAELAEAEARLAALRAQLGSGPD 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 771 HLQDAA--------RRRLLKLQQDQREM---------ELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEK 833
Cdd:COG3206 255 ALPELLqspviqqlRAQLAELEAELAELsarytpnhpDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQA 334
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 264681543 834 DLTTSQEAVAK--EIREDTDAHRRKAALEEHMFQKLLENSQ 872
Cdd:COG3206 335 QLAQLEARLAElpELEAELRRLEREVEVARELYESLLQRLE 375
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
778-897 |
2.09e-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: 44.15 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 778 RRLLKLQQ-DQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLE---LEAQKRLYEKDLTTSQEAVA---------- 843
Cdd:COG1579 7 RALLDLQElDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTEledLEKEIKRLELEIEEVEARIKkyeeqlgnvr 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 844 --KEI----REDTDAHRRKAALEEHMFQKLLENSQMGGRRAQRWKEAEEKEFHLQSAKKA 897
Cdd:COG1579 87 nnKEYealqKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAE 146
|
|
| DUF4200 |
pfam13863 |
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ... |
740-833 |
2.30e-04 |
|
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.
Pssm-ID: 464003 [Multi-domain] Cd Length: 119 Bit Score: 41.78 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 740 RREI-LLQEE-----EKMAQQRQRLAAVKRELEIKEIHLQDAARR--RLLKLQQDQREMELRRLEDEIERKVQmRDQEIA 811
Cdd:pfam13863 5 KREMfLVQLAldakrEEIERLEELLKQREEELEKKEQELKEDLIKfdKFLKENDAKRRRALKKAEEETKLKKE-KEKEIK 83
|
90 100
....*....|....*....|..
gi 264681543 812 ATAKDLEIRQLELEAQKRLYEK 833
Cdd:pfam13863 84 KLTAQIEELKSEISKLEEKLEE 105
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
693-897 |
2.53e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.13 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 693 ERIRNDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREillQEEEKMAQQrqrlaAVKRELEIKEIHL 772
Cdd:PTZ00121 1288 EKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKK---AEEAKKAAE-----AAKAEAEAAADEA 1359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 773 QDAARRrllKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEKDLTTSQEAVAKEIREDTDA 852
Cdd:PTZ00121 1360 EAAEEK---AEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEA 1436
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 264681543 853 hRRKAalEEhmfqkllensqmgGRRAQRWKE-AEEKEFHLQSAKKA 897
Cdd:PTZ00121 1437 -KKKA--EE-------------AKKADEAKKkAEEAKKAEEAKKKA 1466
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
744-839 |
2.66e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 2.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 744 LLQEEEKMAQQRQRLAAVKRELEIKEIHLQDAARRRLLKLQQ----DQREMELRRLEDEIERKVQMRDQEIAATAKDLEI 819
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQlaalERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100
....*....|....*....|
gi 264681543 820 RQLELEAQKRLYEKDLTTSQ 839
Cdd:COG4942 95 LRAELEAQKEELAELLRALY 114
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
696-928 |
2.73e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 44.65 E-value: 2.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 696 RNDELDFLRE-RQTVENMQAEVDEQRAKDEAwyQKQELLRRAEETRREI---LLQEEEKMAQQRQRLAAVKRELEI-KEI 770
Cdd:COG3064 43 RLAELEAKRQaEEEAREAKAEAEQRAAELAA--EAAKKLAEAEKAAAEAekkAAAEKAKAAKEAEAAAAAEKAAAAaEKE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 771 HLQDAARR--RLLKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEKDLTTSQEAVAKEIRE 848
Cdd:COG3064 121 KAEEAKRKaeEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAA 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 849 DTDAHRRKAALEEHMFQKLLENSQMGGRRAQRWKEAEEKEFHLQSAKKASALSDASRKWFLRQETSAALEHEEMPWLQRQ 928
Cdd:COG3064 201 AALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVV 280
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
702-932 |
2.79e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.17 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 702 FLRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEE---TRREILLQEEEKmaqQRQRLAAVKREL--EIKEIHLQDA- 775
Cdd:pfam01576 150 LSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEamiSDLEERLKKEEK---GRQELEKAKRKLegESTDLQEQIAe 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 776 --ARRRLLKLQQDQREMELR----RLEDEIERKVQ----MRDQE--IAATAKDLEI-RQLELEAQKRlyEKDLTTSQEAV 842
Cdd:pfam01576 227 lqAQIAELRAQLAKKEEELQaalaRLEEETAQKNNalkkIRELEaqISELQEDLESeRAARNKAEKQ--RRDLGEELEAL 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 843 AKEIRE--DTDAH----RRKAALEEHMFQKLLEN------SQMGGRRAQRWKEAEEKEFHLQSAKKASALSDASRkwflr 910
Cdd:pfam01576 305 KTELEDtlDTTAAqqelRSKREQEVTELKKALEEetrsheAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAK----- 379
|
250 260
....*....|....*....|....*...
gi 264681543 911 qetsAALEHE------EMPWLQRQYMDS 932
Cdd:pfam01576 380 ----QALESEnaelqaELRTLQQAKQDS 403
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
717-894 |
2.82e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.93 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 717 DEQRAKDEAWYQKQELLRRAE---------------------ETRREILLQEEEKMAQQRQRLAAVKRELEIKEIHLQDA 775
Cdd:COG1196 555 DDEVAAAAIEYLKAAKAGRATflpldkiraraalaaalargaIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEA 634
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 776 ARRRLLKLQQDQREMELRRlEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEKDLTTSQEAVAKEIREDTDAHRR 855
Cdd:COG1196 635 ALRRAVTLAGRLREVTLEG-EGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAE 713
|
170 180 190
....*....|....*....|....*....|....*....
gi 264681543 856 KAALEEHMFQKLLENSQMGGRRAQRWKEAEEKEFHLQSA 894
Cdd:COG1196 714 EERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEA 752
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
693-895 |
3.17e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 3.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 693 ERIRNDELDF---LRERQTVENMQAEVDEQRAKDEAWYQKQELLR-RAEETRREILLQE------EEKMAQQRQRLAAVK 762
Cdd:PRK03918 193 ELIKEKEKELeevLREINEISSELPELREELEKLEKEVKELEELKeEIEELEKELESLEgskrklEEKIRELEERIEELK 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 763 REL--------EIKEIHLQDAARRRLLKLQQDQREmELRRLEDEIER------KVQMRDQEIAATAKDL-EIRQLELEAQ 827
Cdd:PRK03918 273 KEIeeleekvkELKELKEKAEEYIKLSEFYEEYLD-ELREIEKRLSRleeeinGIEERIKELEEKEERLeELKKKLKELE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 828 KRL--YEKDLTTSQEAVAKE------------------IREDTDAHRRKAALEEHMFQKLLENSQMGGRRAQRWKEAEEk 887
Cdd:PRK03918 352 KRLeeLEERHELYEEAKAKKeelerlkkrltgltpeklEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEE- 430
|
....*...
gi 264681543 888 efhLQSAK 895
Cdd:PRK03918 431 ---LKKAK 435
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
689-905 |
3.27e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 44.82 E-value: 3.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 689 TREWERIRNDELdflrERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREI------LLQEEEKMAQQRQ------ 756
Cdd:NF041483 501 TAESERVRTEAI----ERATTLRRQAEETLERTRAEAERLRAEAEEQAEEVRAAAeraareLREETERAIAARQaeaaee 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 757 ----------RLAAVKREL----------------EIKEIHLQDAARRRLLklqQDQREMELRRLEDEIERKVQMRDQEI 810
Cdd:NF041483 577 ltrlhteaeeRLTAAEEALadaraeaerirreaaeETERLRTEAAERIRTL---QAQAEQEAERLRTEAAADASAARAEG 653
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 811 AATAKDL------EIRQLELEAQKrlyEKDLTTSQEAVAKEiREDTDAHRRKAALEEHMFQKLLENSQ-MGGRRA----Q 879
Cdd:NF041483 654 ENVAVRLrseaaaEAERLKSEAQE---SADRVRAEAAAAAE-RVGTEAAEALAAAQEEAARRRREAEEtLGSARAeadqE 729
|
250 260
....*....|....*....|....*...
gi 264681543 880 RWKEAEEKEFHLQSAKK--ASALSDASR 905
Cdd:NF041483 730 RERAREQSEELLASARKrvEEAQAEAQR 757
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
697-921 |
3.76e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 3.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 697 NDELDFLRER-QTVENMQAEVDEQRAKDEAWYQKQellRRAEETRREILLQEEEKMAQQRQRLAAVKRELEIKEIHLQDA 775
Cdd:PRK02224 341 NEEAESLREDaDDLEERAEELREEAAELESELEEA---REAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEEL 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 776 ARRR-LLKLQQDQREMELRRLEDEIERKVQMR-------------DQEIAATAKD-------LEIRQLELEAQKRLYEKD 834
Cdd:PRK02224 418 REERdELREREAELEATLRTARERVEEAEALLeagkcpecgqpveGSPHVETIEEdrerveeLEAELEDLEEEVEEVEER 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 835 LTTSQEAVAKEIREDTDAHRRKAALEehmfqkllensqmggRRAQRWKEAEEKEFHLQSAKK-ASALSDASRKWflrqET 913
Cdd:PRK02224 498 LERAEDLVEAEDRIERLEERREDLEE---------------LIAERRETIEEKRERAEELRErAAELEAEAEEK----RE 558
|
....*...
gi 264681543 914 SAALEHEE 921
Cdd:PRK02224 559 AAAEAEEE 566
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
698-920 |
4.30e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 4.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 698 DELDFLR-ERQTVENMQAEVDEQR-----AKDEAwyqkQELLRRAEETRREILLQEEEkMAQQRQRLAAVKREleikeih 771
Cdd:PRK02224 206 ERLNGLEsELAELDEEIERYEEQReqareTRDEA----DEVLEEHEERREELETLEAE-IEDLRETIAETERE------- 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 772 lQDAARRRLlklqQDQREmELRRLEDEIERKVQMRDQEiAATAKDLEIRQLELEAQKRLYEKDLTTSQEAvAKEIREDTD 851
Cdd:PRK02224 274 -REELAEEV----RDLRE-RLEELEEERDDLLAEAGLD-DADAEAVEARREELEDRDEELRDRLEECRVA-AQAHNEEAE 345
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 264681543 852 AHRRKAA-LEEhmfqkllensqmggrRAQRWKE-AEEKEFHLQSAKkaSALSDasrkwflRQETSAALEHE 920
Cdd:PRK02224 346 SLREDADdLEE---------------RAEELREeAAELESELEEAR--EAVED-------RREEIEELEEE 392
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
752-916 |
4.37e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 43.68 E-value: 4.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 752 AQQRQRLAAVKRELEIKEIHLQDAARRRLLKLQQDQR--EMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKR 829
Cdd:TIGR02794 49 AQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAaeQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQ 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 830 lyEKDLTTSQEAVAkEIREDTDAhRRKAALEehmfqKLLEnsqmggRRAQRWKEAEEKEFHLQSAKKASAlsDASRKwfL 909
Cdd:TIGR02794 129 --AAEAKAKAEAEA-ERKAKEEA-AKQAEEE-----AKAK------AAAEAKKKAEEAKKKAEAEAKAKA--EAEAK--A 189
|
....*..
gi 264681543 910 RQETSAA 916
Cdd:TIGR02794 190 KAEEAKA 196
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
696-829 |
4.39e-04 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 44.25 E-value: 4.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 696 RNDELDFLRER-----QTVENMQAEVDE-----QRAKDEAWYQKQELLRRAEETRR-----EILLQEEEKMAQ-QR---- 755
Cdd:pfam05667 333 REEELEELQEQledleSSIQELEKEIKKlessiKQVEEELEELKEQNEELEKQYKVkkktlDLLPDAEENIAKlQAlvda 412
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 264681543 756 --QRLAAVKRELEIKEIHLQDAARRrlLKLQQDQREMELRRLEDEIER-KVQMRDQEIAATAKDLEIRQLELEAQKR 829
Cdd:pfam05667 413 saQRLVELAGQWEKHRVPLIEEYRA--LKEAKSNKEDESQRKLEEIKElREKIKEVAEEAKQKEELYKQLVAEYERL 487
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
684-829 |
4.66e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.16 E-value: 4.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 684 IVDYQTREWERIRNDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEEKmAQQRQRLAAVKR 763
Cdd:COG1196 623 LGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLA-EEELELEEALLA 701
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 264681543 764 ELEIKEIHLQDAARRRLLKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKR 829
Cdd:COG1196 702 EEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELER 767
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
704-922 |
4.75e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.28 E-value: 4.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 704 RERQTVENMQAEVDEQRAKdEAWYQKQELLRRAEETRReiLLQEEEKMAQQRQRLAAVKRELEIK--EIHLQDA-ARRRL 780
Cdd:TIGR02168 207 RQAEKAERYKELKAELREL-ELALLVLRLEELREELEE--LQEELKEAEEELEELTAELQELEEKleELRLEVSeLEEEI 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 781 LKLQQDQREM--ELRRLEDEIERKVQmRDQEIAATAKDLEIRQLELEAQKRLYEKDLTTSQE--AVAKEIREDTdahrrK 856
Cdd:TIGR02168 284 EELQKELYALanEISRLEQQKQILRE-RLANLERQLEELEAQLEELESKLDELAEELAELEEklEELKEELESL-----E 357
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 264681543 857 AALEEhmFQKLLENSqmggrrAQRWKEAEEkefHLQSAKKASALsdasrkwFLRQETSAALEHEEM 922
Cdd:TIGR02168 358 AELEE--LEAELEEL------ESRLEELEE---QLETLRSKVAQ-------LELQIASLNNEIERL 405
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
688-896 |
4.90e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 4.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 688 QTREWERIRNDEldflrERQTVENMQAEVDEQRAKDE----AWYQKQELLRRAEETRREILLQEEEK-MAQQRQRLAAVK 762
Cdd:PTZ00121 1216 EARKAEDAKKAE-----AVKKAEEAKKDAEEAKKAEEernnEEIRKFEEARMAHFARRQAAIKAEEArKADELKKAEEKK 1290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 763 RELEIKEIHLQDAARRRLLKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEKDLTTSQEAV 842
Cdd:PTZ00121 1291 KADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAE 1370
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 264681543 843 AK--EIREDTDAHRRKAAlEEHMFQKLLENSQMGGRRAQRWKEAEEKEFHLQSAKK 896
Cdd:PTZ00121 1371 KKkeEAKKKADAAKKKAE-EKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKK 1425
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
711-926 |
5.89e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.01 E-value: 5.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 711 NMQA-----EVDEQrAKDEAwyqkqellrrAEETRREILLQ----EEEKMAQQRQRLAAVkreleikeihlqdAARRRLl 781
Cdd:pfam01576 721 NMQAlkaqfERDLQ-ARDEQ----------GEEKRRQLVKQvrelEAELEDERKQRAQAV-------------AAKKKL- 775
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 782 klqqdqrEMELRRLEDEIerkvqmrdqEIAATAKDLEIRQL-ELEAQKRLYEKDLTTSQEAVAKEIREDTDAHRRKAALE 860
Cdd:pfam01576 776 -------ELDLKELEAQI---------DAANKGREEAVKQLkKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLE 839
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 264681543 861 EHMFQklLENSQMGGRRAQRWKEAEEKEFHLQ---SAKKASALSDASRkwflRQETSAALEHEEMPWLQ 926
Cdd:pfam01576 840 AELLQ--LQEDLAASERARRQAQQERDELADEiasGASGKSALQDEKR----RLEARIAQLEEELEEEQ 902
|
|
| DegS |
pfam05384 |
Sensor protein DegS; This is small family of Bacillus DegS proteins. The DegS-DegU ... |
708-803 |
6.65e-04 |
|
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: 41.31 E-value: 6.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 708 TVENMQAEVDE--QRAKDEAWYQKQELlrraEETRREIL--------LQEEEKMAqqRQRLAAVKR------ELEIKEIH 771
Cdd:pfam05384 10 TIENSKEEIFEiaENARQEYERLKQEL----EELKEEVSetikevdkLEKKERRA--RQRLMEVSRdfnrysEEDIKEAY 83
|
90 100 110
....*....|....*....|....*....|...
gi 264681543 772 LQ-DAARRRLLKLQQdqREMELRRLEDEIERKV 803
Cdd:pfam05384 84 EEaKDLQVELALLRE--REKQLRERRDELERRL 114
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
697-834 |
7.22e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 43.67 E-value: 7.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 697 NDELDFlrerQTVENMQAEVDEQ-----------RAKDEAWYQKQELLRRAEETRREILL--QEEEKMAQQRQRLAAVKR 763
Cdd:pfam12128 190 SKEGKF----RDVKSMIVAILEDdgvvppksrlnRQQVEHWIRDIQAIAGIMKIRPEFTKlqQEFNTLESAELRLSHLHF 265
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 264681543 764 EleIKEIHLQDAARRRLLKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEA---QKRLYEKD 834
Cdd:pfam12128 266 G--YKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEAledQHGAFLDA 337
|
|
| Nop53 |
pfam07767 |
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ... |
714-833 |
7.53e-04 |
|
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ribosomal biogenesis. They are specifically involved in the processing beyond the 27S stage of 25S rRNA maturation. This family contains sequences that bear similarity to the glioma tumour suppressor candidate region gene 2 protein (p60). This protein has been found to interact with herpes simplex type 1 regulatory proteins.
Pssm-ID: 462259 [Multi-domain] Cd Length: 353 Bit Score: 43.05 E-value: 7.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 714 AEVDEQRAKDEAwyQKQELLRRAEETRREILLQEEEKMAQQrQRLAAVKRELEIKEihlqdAARRRLLKLQQDQremeLR 793
Cdd:pfam07767 205 VEAEKKRLKEEE--KLERVLEKIAESAATAEAREEKRKTKA-QRNKEKRRKEEERE-----AKEEKALKKKLAQ----LE 272
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 264681543 794 RLEdEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEK 833
Cdd:pfam07767 273 RLK-EIAKEIAEKEKEREEKAEARKREKRKKKKEEKKLRP 311
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
702-879 |
9.43e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 42.77 E-value: 9.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 702 FLRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREillqeeekMAQQRQRLAAVKRELEIKEihlqdaarRRLL 781
Cdd:PRK12705 24 LLKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRE--------RNQQRQEARREREELQREE--------ERLV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 782 KL--QQDQREMELRRLEDEIERkvqmRDQEIAATAKDLEIRQLELEAqkRLYEKDLTTSQEAVAKEIRE-DTDAHRRKAA 858
Cdd:PRK12705 88 QKeeQLDARAEKLDNLENQLEE----REKALSARELELEELEKQLDN--ELYRVAGLTPEQARKLLLKLlDAELEEEKAQ 161
|
170 180
....*....|....*....|.
gi 264681543 859 LEEHMFQKLLENSQmggRRAQ 879
Cdd:PRK12705 162 RVKKIEEEADLEAE---RKAQ 179
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
714-933 |
9.51e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 43.28 E-value: 9.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 714 AEVDEQRAKDEAWYQKQELLRRAEETrreillQEEEKMAQQRQRLAAVKRELEIKeihlqdaarrrllklqqDQREMELR 793
Cdd:NF041483 500 ATAESERVRTEAIERATTLRRQAEET------LERTRAEAERLRAEAEEQAEEVR-----------------AAAERAAR 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 794 RLEDEIERKVQMRDQEIAAtakdlEIRQLELEAQKRlyekdLTTSQEAVAkEIREDTDAHRRKAALEEhmfQKLLENSQM 873
Cdd:NF041483 557 ELREETERAIAARQAEAAE-----ELTRLHTEAEER-----LTAAEEALA-DARAEAERIRREAAEET---ERLRTEAAE 622
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 874 GGRRAQRWKEAEEKEFHLQSAKKASALSDASRKWFLRQETSAALEHEEmpwLQRQYMDSA 933
Cdd:NF041483 623 RIRTLQAQAEQEAERLRTEAAADASAARAEGENVAVRLRSEAAAEAER---LKSEAQESA 679
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
703-899 |
9.77e-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: 9.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 703 LRERQTVENMQAEVDEQRAKdeawyqkqelLRRAEETRREilLQEEEKMAQQRQRLAavkrELEIKEIHLQDAARRRLLK 782
Cdd:COG3096 343 LRQQEKIERYQEDLEELTER----------LEEQEEVVEE--AAEQLAEAEARLEAA----EEEVDSLKSQLADYQQALD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 783 LQQD---QREMELRRLE--------DEI------ERKVQMRDQEIAATAKDLEIRQ-LEL-EAQKRLYEKDL-------- 835
Cdd:COG3096 407 VQQTraiQYQQAVQALEkaralcglPDLtpenaeDYLAAFRAKEQQATEEVLELEQkLSVaDAARRQFEKAYelvckiag 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 264681543 836 -TTSQEA--VAKEIREDTDAHRRKAALEEHMFQKLLENSQmggrRAQRWKEAEE--KEFHLQSAKKASA 899
Cdd:COG3096 487 eVERSQAwqTARELLRRYRSQQALAQRLQQLRAQLAELEQ----RLRQQQNAERllEEFCQRIGQQLDA 551
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
116-153 |
1.01e-03 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 37.71 E-value: 1.01e-03
10 20 30
....*....|....*....|....*....|....*....
gi 264681543 116 KELVSWMRGHESSVCSISVHASGRYAITTSSD-TAQLWD 153
Cdd:pfam00400 1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDgTVKVWD 39
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
719-872 |
1.07e-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: 41.61 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 719 QRAKDEAWY--------QKQELLRRAEETRREillqeEEKMAQQRQRLAAVKRE--LEIKEihlQDAARRRLLKLQQDQR 788
Cdd:pfam13904 50 ERQPLEAYEnwlaakqrQRQKELQAQKEEREK-----EEQEAELRKRLAKEKYQewLQRKA---RQQTKKREESHKQKAA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 789 EMELRRLeDEIERKVQMRdqEIAATAKDLEIRQLELEAQKRLYEKDlttsqeavAKEIREDTDAHRRKAAleEHMFQKLL 868
Cdd:pfam13904 122 ESASKSL-AKPERKVSQE--EAKEVLQEWERKKLEQQQRKREEEQR--------EQLKKEEEEQERKQLA--EKAWQKWM 188
|
....
gi 264681543 869 ENSQ 872
Cdd:pfam13904 189 KNVK 192
|
|
| G_path_suppress |
pfam15991 |
G-protein pathway suppressor; This family of proteins inhibits G-protein- and ... |
704-790 |
1.24e-03 |
|
G-protein pathway suppressor; This family of proteins inhibits G-protein- and mitogen-activated protein kinase-mediated signal transduction.
Pssm-ID: 464961 [Multi-domain] Cd Length: 272 Bit Score: 41.83 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 704 RERQTVEnMQAEVDEQRAKDEAWYQKQELLRRAEETRREIlLQEEEKMAQQRQRlaavKREL--EIKEIHLQDAARRRLL 781
Cdd:pfam15991 22 RERKKQE-QEAKMEEERLRREREEREKEDRMTLEETKEQI-LKLEKKLADLKEE----KHQLflQLKKVLHEDETRKRQL 95
|
....*....
gi 264681543 782 KLQQDQREM 790
Cdd:pfam15991 96 KEQSELFAL 104
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
706-828 |
1.25e-03 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 39.52 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 706 RQTVENMQAEVdEQRAKdeawyQKQELLRRAEE-----TRREILLQEEEKMAQ-QRQRLAAVKRELE-----IKEIHLQD 774
Cdd:pfam20492 1 REEAEREKQEL-EERLK-----QYEEETKKAQEeleesEETAEELEEERRQAEeEAERLEQKRQEAEeekerLEESAEME 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 264681543 775 AARRRLLKLQQDQREMELRRLEDEIERkvqmrdqeiaataKDLEIRQLELEAQK 828
Cdd:pfam20492 75 AEEKEQLEAELAEAQEEIARLEEEVER-------------KEEEARRLQEELEE 115
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
707-848 |
1.30e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.54 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 707 QTVENMQAEVDEQRAKDEAwyQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELEiKEIHLQDAARRRL---LKL 783
Cdd:COG2433 376 LSIEEALEELIEKELPEEE--PEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELE-AELEEKDERIERLereLSE 452
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 264681543 784 QQDQREMELRRledeiERKVQMRDQEIAATAKDLE-----IRQLE--LEAQKRLYEKDLttSQEAVA-KEIRE 848
Cdd:COG2433 453 ARSEERREIRK-----DREISRLDREIERLERELEeererIEELKrkLERLKELWKLEH--SGELVPvKVVEK 518
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
700-845 |
1.62e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 42.63 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 700 LDFLRERQT---VENMQAEVDEQRAKDEAWYQKqelLRRAEETR---REILLQEEEKMAQQRQRLAAVKRELEIKEIHLQ 773
Cdd:COG3096 960 LSEVVQRRPhfsYEDAVGLLGENSDLNEKLRAR---LEQAEEARreaREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQ 1036
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 774 DAARR-RLLKLQQDQrEMELR-RLE-DEIERKVQMRDQEIAATAKDLEIRQLELE-AQKRL--YEKDLTTSQEAV--AKE 845
Cdd:COG3096 1037 ELEQElEELGVQADA-EAEERaRIRrDELHEELSQNRSRRSQLEKQLTRCEAEMDsLQKRLrkAERDYKQEREQVvqAKA 1115
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
728-908 |
1.86e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 42.25 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 728 QKQELLRRAEETRREiLLQEEEKMAQQRQRLAAVKRELEIK---EIHLQ---DAARRRLLKLQQDQREMElrrledeier 801
Cdd:COG3096 279 ERRELSERALELRRE-LFGARRQLAEEQYRLVEMARELEELsarESDLEqdyQAASDHLNLVQTALRQQE---------- 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 802 KVQMRDQEIAATAKDLEIRQLELEA---QKRLYEKDLTTSQEAVaKEIR-------EDTDAHRRKA--------ALEEHm 863
Cdd:COG3096 348 KIERYQEDLEELTERLEEQEEVVEEaaeQLAEAEARLEAAEEEV-DSLKsqladyqQALDVQQTRAiqyqqavqALEKA- 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 264681543 864 fQKLLENSQMGGRRAQRWKE---AEEKEFH--LQSAKKASALSDASRKWF 908
Cdd:COG3096 426 -RALCGLPDLTPENAEDYLAafrAKEQQATeeVLELEQKLSVADAARRQF 474
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
695-887 |
1.88e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 42.25 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 695 IRNDELDFLRERQTVENMQAEVD------EQRA--KDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELE 766
Cdd:COG5185 231 IEEALKGFQDPESELEDLAQTSDkleklvEQNTdlRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKA 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 767 IKEIHLQDAARRRLLKLQQDQRE--MELRRLEDEIERKVqmRDQEIAATAKDLEIRQLELEAQKRLYEKDL---TTSQEA 841
Cdd:COG5185 311 TESLEEQLAAAEAEQELEESKREteTGIQNLTAEIEQGQ--ESLTENLEAIKEEIENIVGEVELSKSSEELdsfKDTIES 388
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 264681543 842 VAKEIREDTDAHRRKA-----ALEEHMFQKLLENSQMGGRRAQRWKEAEEK 887
Cdd:COG5185 389 TKESLDEIPQNQRGYAqeilaTLEDTLKAADRQIEELQRQIEQATSSNEEV 439
|
|
| PRK03963 |
PRK03963 |
V-type ATP synthase subunit E; Provisional |
730-849 |
2.03e-03 |
|
V-type ATP synthase subunit E; Provisional
Pssm-ID: 167649 [Multi-domain] Cd Length: 198 Bit Score: 40.51 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 730 QELLRRAEETRREIlLQEEEKMAQQrqrlaavkreleIKEihlqdAARRRllklQQDQREMELRRLEDEIErkvqMRDQE 809
Cdd:PRK03963 9 QEINREAEQKIEYI-LEEAQKEAEK------------IKE-----EARKR----AESKAEWILRKAKTQAE----LEKQR 62
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 264681543 810 IAATAKdLEIRQLELEAQKRLYEKDLTTSQEAVAkEIRED 849
Cdd:PRK03963 63 IIANAK-LEVRRKRLAVQEELISEVLEAVRERLA-ELPED 100
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
690-861 |
2.06e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 690 REWERIRNDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELEIKE 769
Cdd:COG4372 101 EELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 770 I-----HLQDAARRRLLKLQQDqrEMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEKDLTTSQEAVAK 844
Cdd:COG4372 181 AeqaldELLKEANRNAEKEEEL--AEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILK 258
|
170
....*....|....*..
gi 264681543 845 EIREDTDAHRRKAALEE 861
Cdd:COG4372 259 EIEELELAILVEKDTEE 275
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
730-861 |
2.09e-03 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 39.77 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 730 QELLRRAEETRREIllqeEEKMAQQRQRLAAVKRELEikEIhlQDAARRRLLKLQQDQREmelrRLEDEIERKVQMRDQE 809
Cdd:COG0711 37 ADGLAEAERAKEEA----EAALAEYEEKLAEARAEAA--EI--IAEARKEAEAIAEEAKA----EAEAEAERIIAQAEAE 104
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 264681543 810 IAAtAKDLEIRQLELEAQkrlyekdlTTSQEAVAKEIREDTDAHRRKAALEE 861
Cdd:COG0711 105 IEQ-ERAKALAELRAEVA--------DLAVAIAEKILGKELDAAAQAALVDR 147
|
|
| DUF5384 |
pfam17358 |
Family of unknown function (DUF5384); This is a family of unknown function found in ... |
705-849 |
2.17e-03 |
|
Family of unknown function (DUF5384); This is a family of unknown function found in Proteobacteria.
Pssm-ID: 407453 [Multi-domain] Cd Length: 145 Bit Score: 39.59 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 705 ERQTVENMQAEVDEQR---AKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELEIKEihlqdaarrrll 781
Cdd:pfam17358 12 ERQAAYEREWEEEQARaeaAAAAARRARAAAAAAAAAAAKERAKAEALADKKRDQSYEDELRALEIEE------------ 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 782 klqqdqREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYE--KDLTTSqEAVAKEIRED 849
Cdd:pfam17358 80 ------RKLALAAQKARAKRENDFIDQELKSQAAQTDVIQSEADANRNVSEgtKSLMES-EGKAREKKSS 142
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
690-918 |
2.48e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 690 REWERIRNDELDFLRERQTVENMQaEVDEQRAK------DEAWYQKQELLRRAEETRREI--LLQEEEKMAQQRQRLAAV 761
Cdd:PRK03918 483 RELEKVLKKESELIKLKELAEQLK-ELEEKLKKynleelEKKAEEYEKLKEKLIKLKGEIksLKKELEKLEELKKKLAEL 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 762 KREL-----EIKEIHLQ---------DAARRRLLKLQQDQREM--------ELRRLEDEI---ERKVQMRDQEIAATAKD 816
Cdd:PRK03918 562 EKKLdeleeELAELLKEleelgfesvEELEERLKELEPFYNEYlelkdaekELEREEKELkklEEELDKAFEELAETEKR 641
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 817 LEIRQLELEAQKRLYEKDlttSQEAVAKEIREDTDAHRRKAA----LEEHM--FQKLLENSQmggrraQRWKEAEEKEFH 890
Cdd:PRK03918 642 LEELRKELEELEKKYSEE---EYEELREEYLELSRELAGLRAeleeLEKRReeIKKTLEKLK------EELEEREKAKKE 712
|
250 260
....*....|....*....|....*...
gi 264681543 891 LQSAKKASALSDASRKWFLRQETSAALE 918
Cdd:PRK03918 713 LEKLEKALERVEELREKVKKYKALLKER 740
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
693-796 |
2.48e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 41.39 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 693 ERIRndeldflRERQTVENMQAEVDEQRaKDEAWYQKQELLRRAEEtRREILLQEEEKMAQQRQrLAAVKRELEikeihl 772
Cdd:pfam02029 251 EELR-------RRRQEKESEEFEKLRQK-QQEAELELEELKKKREE-RRKLLEEEEQRRKQEEA-ERKLREEEE------ 314
|
90 100
....*....|....*....|....
gi 264681543 773 qdaaRRRLlklqqdQREMELRRLE 796
Cdd:pfam02029 315 ----KRRM------KEEIERRRAE 328
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
749-904 |
2.74e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 41.53 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 749 EKMAQQRQRLAAVKREL-EIKEIHLQDAARR-RLLKLQQDQREMELRRLEDEIERKvqmrdQEIAATAKDlEIRQLELEA 826
Cdd:pfam05262 184 EALREDNEKGVNFRRDMtDLKERESQEDAKRaQQLKEELDKKQIDADKAQQKADFA-----QDNADKQRD-EVRQKQQEA 257
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 264681543 827 QKRlyEKDLTTSQEAVAKEIREDTDAHRRKAALE-EHMFQKLLENSQMGGRRAQRWKEAEEKEFHLQSAKKASALSDAS 904
Cdd:pfam05262 258 KNL--PKPADTSSPKEDKQVAENQKREIEKAQIEiKKNDEEALKAKDHKAFDLKQESKASEKEAEDKELEAQKKREPVA 334
|
|
| YscO-like |
pfam16789 |
YscO-like protein; This family of proteins is similar to the type III secretion protein YscO. ... |
727-847 |
2.81e-03 |
|
YscO-like protein; This family of proteins is similar to the type III secretion protein YscO. The family includes Chlamydia trachomatis CT670 which is found in a type III secretion gene cluster. CT670 interacts with CT671, a putative YscP homolog and CT670 and CT671 may form a chaperone-effector pair.
Pssm-ID: 435583 [Multi-domain] Cd Length: 160 Bit Score: 39.43 E-value: 2.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 727 YQKQELLR---RAEETRREILLQEEEKMAQQRQRLAAVKRELEIKEIHLQDaarrrllKLQQDQREME------------ 791
Cdd:pfam16789 3 YPLEQVLDikkKRVEEAEKVVKDKKRALEKEKEKLAELEAERDKVRKHKKA-------KMQQLRDEMDrgttsdkilqmk 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 264681543 792 --LRRLEDEI---ERKVQMRDQEIAATAKDLEIRQLELeAQKRLYEKDLTTSQEAVAKEIR 847
Cdd:pfam16789 76 ryIKVVKERLkqeEKKVQDQKEQVRTAARNLEIAREEL-KKKRQEVEKLEKHKKEWVKEMK 135
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
718-791 |
2.85e-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: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 718 EQRAKDEAwyQKQELLRRAEETRREILLQ--EEEKMAQQRQ--------RLAAVKRELEIKEIHLQ--DAARRRLlklqq 785
Cdd:pfam01576 984 EQESRERQ--AANKLVRRTEKKLKEVLLQveDERRHADQYKdqaekgnsRMKQLKRQLEEAEEEASraNAARRKL----- 1056
|
....*.
gi 264681543 786 dQREME 791
Cdd:pfam01576 1057 -QRELD 1061
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
738-928 |
2.97e-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: 41.49 E-value: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 738 ETRREILLQEEEKMAQQRQRLAAVKRELEIKEIHLQdaaRRRLLKlQQDQREMELRRLEDEIERKVQMRDQE-----IAA 812
Cdd:TIGR00618 222 QVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLK---KQQLLK-QLRARIEELRAQEAVLEETQERINRArkaapLAA 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 813 TAKDL-EIRQ------LELEAQKRLYEKDLTTSQEAVAKE--IREDTDAHRRKAALEEHMFQkllENSQMGGRRAQRWKE 883
Cdd:TIGR00618 298 HIKAVtQIEQqaqrihTELQSKMRSRAKLLMKRAAHVKQQssIEEQRRLLQTLHSQEIHIRD---AHEVATSIREISCQQ 374
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 264681543 884 AEEKEFHLQSAKKASALSDASRKWFLRQETSAALEHEEMPWLQRQ 928
Cdd:TIGR00618 375 HTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAF 419
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
703-822 |
3.51e-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: 3.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 703 LRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREILLQE-----EEKMA--QQRQRLAAVKRELEIKE---IHL 772
Cdd:COG3096 528 LRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQaaeavEQRSElrQQLEQLRARIKELAARApawLAA 607
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 264681543 773 QDAARR-------RLLKLQQ--DQREMELRRledeiERKVQMRDQEIAATAKDLE--IRQL 822
Cdd:COG3096 608 QDALERlreqsgeALADSQEvtAAMQQLLER-----EREATVERDELAARKQALEsqIERL 663
|
|
| DUF3375 |
pfam11855 |
Protein of unknown function (DUF3375); This family of proteins are functionally ... |
643-873 |
3.70e-03 |
|
Protein of unknown function (DUF3375); This family of proteins are functionally uncharacterized. This protein is found in bacteria. Proteins in this family are typically between 479 to 499 amino acids in length.
Pssm-ID: 463373 Cd Length: 469 Bit Score: 41.09 E-value: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 643 IREVYHLMETTPADIHpnSMLDAFVALTKGqypifnqypkfIVDyQTREWERIRNDELDF-LRERQTVenmqAEVDEQRA 721
Cdd:pfam11855 174 AREILQLARELPADFR--RVEDEFRQLDRE-----------LRE-RIIDWDGSRGEVLEElFDGYDAL----ADSDQGRS 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 722 KDEAWyqkqELLRRAEETR------REILLQEEEKM--AQQRQRLAAVKREL--EIKEIH--LQDAAR--RRLLKLQQDQ 787
Cdd:pfam11855 236 FEAFW----DLLMDPERQAeldellDTVLSRPFARGldADQRRFLRRLHRDLleAGEEVQrtRRRLSRslRRFVRSQAFL 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 788 REMELRRLEDEIERK-VQMRDQEIAATAKDLEI----RQLELEAQKRLY---EKDLTTSQEAVAKEIREDTDAHRR---- 855
Cdd:pfam11855 312 EDRRVDRLLREAEALaLALRDAPPADRRTGLELpltaPDIASPSERRLHdppALPVVDAPADDAGAGELDLEDLRAlggq 391
|
250 260
....*....|....*....|..
gi 264681543 856 ----KAALEEHMFQKLLENSQM 873
Cdd:pfam11855 392 sevdRAELTEAVRAALAERGQV 413
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
696-892 |
3.97e-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: 41.31 E-value: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 696 RNDELDFLRERQT-VENMQAEVDEQRA-KDEAWYQKQELLRRAEETRREIL-LQEEEKMAQQRQRLAAVKRELEIKEIH- 771
Cdd:pfam01576 793 REEAVKQLKKLQAqMKDLQRELEEARAsRDEILAQSKESEKKLKNLEAELLqLQEDLAASERARRQAQQERDELADEIAs 872
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 772 -------LQDAARRRLLKLQQDQREME-----LRRLEDEIERKVQMRDQ---EIAA---TAKDLEIRQLELEAQKRLYEK 833
Cdd:pfam01576 873 gasgksaLQDEKRRLEARIAQLEEELEeeqsnTELLNDRLRKSTLQVEQlttELAAersTSQKSESARQQLERQNKELKA 952
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 834 DLTTSQEAVAKEIREDTDAHRRK-AALEEHMFQKLLENSQMGgrRAQRWKEAEEKEFHLQ 892
Cdd:pfam01576 953 KLQEMEGTVKSKFKSSIAALEAKiAQLEEQLEQESRERQAAN--KLVRRTEKKLKEVLLQ 1010
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
697-901 |
4.21e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.28 E-value: 4.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 697 NDELDFLRE-RQTVENMQAEVDEQRakDEAWYQKQELLRRAEETR--REILLQEEEKMAQQRQRLAAVKREL--EIKEIH 771
Cdd:COG1340 21 REEIEELKEkRDELNEELKELAEKR--DELNAQVKELREEAQELRekRDELNEKVKELKEERDELNEKLNELreELDELR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 772 lQDAARRRLLKLQQDQREMELRRLEDEIERKVQMRDQEiaataKDL--EIRQLE--LEAQKRLYE--KDLTTSQEAVAKE 845
Cdd:COG1340 99 -KELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEE-----KELveKIKELEkeLEKAKKALEknEKLKELRAELKEL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 264681543 846 IREDTDAHRRKAALEEHMFQKLLENSQMGGRRAQRWKEAEE--KEFhLQSAKKASALS 901
Cdd:COG1340 173 RKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADElhKEI-VEAQEKADELH 229
|
|
| ARGLU |
pfam15346 |
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ... |
763-888 |
4.34e-03 |
|
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is required for the oestrogen-dependent expression of ESR1 target genes. It functions in cooperation with MED1. The family of proteins is found in eukaryotes.
Pssm-ID: 405931 [Multi-domain] Cd Length: 151 Bit Score: 38.88 E-value: 4.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 763 RELEIKEIhlQDAARRRLLKLQQDQREMELRRLEDEIERKVQMR-DQEIAATAKDLEI-----RQLELEAQKRLYE---K 833
Cdd:pfam15346 1 KEAESKLL--EEETARRVEEAVAKRVEEELEKRKDEIEAEVERRvEEARKIMEKQVLEelereREAELEEERRKEEeerK 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 264681543 834 DLTTSQEAVAKEIREDTDAHRRKAalEEHmfQKLLENSQMGGRRAQRWKEAEEKE 888
Cdd:pfam15346 79 KREELERILEENNRKIEEAQRKEA--EER--LAMLEEQRRMKEERQRREKEEEER 129
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
717-861 |
4.56e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 4.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 717 DEQRAKDEAWY-------QKQELLRRAEETRREIllqeeEKMAQQRQRLAAVKRELEIKEIHLQDAARRRLLKLQQDQRE 789
Cdd:COG4913 593 DDRRRIRSRYVlgfdnraKLAALEAELAELEEEL-----AEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAE 667
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 264681543 790 MELRRLEDEIERkvqmrdqeIAATAKDLEirqlELEAQKRLYEKDLTTSQEAVAKEIREDTDAHRRKAALEE 861
Cdd:COG4913 668 REIAELEAELER--------LDASSDDLA----ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEE 727
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
642-769 |
4.83e-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: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 642 VIREVYHLMETTPADI--HPNSMLDAFVALTKGQYpiFNQYPKFIVDYQTREWERIRNDELDFLRERQTVENMQAEVDEQ 719
Cdd:COG4942 109 LLRALYRLGRQPPLALllSPEDFLDAVRRLQYLKY--LAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEE 186
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 264681543 720 RAKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELEIKE 769
Cdd:COG4942 187 RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| PRK02292 |
PRK02292 |
V-type ATP synthase subunit E; Provisional |
748-886 |
4.96e-03 |
|
V-type ATP synthase subunit E; Provisional
Pssm-ID: 235026 [Multi-domain] Cd Length: 188 Bit Score: 39.21 E-value: 4.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 748 EEKMAQQRQRLAAVKRELEIKEIHLQDAARRRllklQQDQREMELRRLEDEIErkvQMRDQEIAaTAKdLEIRQLELEAQ 827
Cdd:PRK02292 8 EDIRDEARARASEIRAEADEEAEEIIAEAEAD----AEEILEDREAEAEREIE---QLREQELS-SAK-LEAKRERLNAR 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 264681543 828 KRLYEKdlttSQEAVAKEIReDTDAHRRKAALEehmfqKLLENSQMGGRRAQRWKEAEE 886
Cdd:PRK02292 79 KEVLED----VRNQVEDEIA-SLDGDKREELTK-----SLLDAADADGVRVYSRKDDED 127
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
714-891 |
5.30e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.93 E-value: 5.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 714 AEVDEQRAKDEAwyQKQEL--------LRRAEETRREILLQ-----------------EEEKMAQQRQRLAAVKRELEIK 768
Cdd:pfam01576 57 AEAEEMRARLAA--RKQELeeilheleSRLEEEEERSQQLQnekkkmqqhiqdleeqlDEEEAARQKLQLEKVTTEAKIK 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 769 EIH-----LQDAARrrllKLQQDQREMELRRLE-----DEIERKVQMRDQ---EIAATAKDLEIR-------QLELEAQK 828
Cdd:pfam01576 135 KLEedillLEDQNS----KLSKERKLLEERISEftsnlAEEEEKAKSLSKlknKHEAMISDLEERlkkeekgRQELEKAK 210
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 264681543 829 RLYEKDLTTSQEAVAKEIREDTDAHRRKAALEEHMFQKLLENSQMGGRRAQRWKEAEEKEFHL 891
Cdd:pfam01576 211 RKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQI 273
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
698-906 |
5.34e-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: 5.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 698 DELDFLRER--QTVENMQAEVDEQRAKDEAWYQKQEllrraeetRREILLQEEE----KMAQQRQRLAAVKRELEIKEIH 771
Cdd:pfam01576 569 DKLEKTKNRlqQELDDLLVDLDHQRQLVSNLEKKQK--------KFDQMLAEEKaisaRYAEERDRAEAEAREKETRALS 640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 772 LQdaarrRLLKLQQDQREmELRR----LEDEIERKVQMRDqeiaATAKDLEirqlELEAQKRLYEK---DLTTSQEAVAK 844
Cdd:pfam01576 641 LA-----RALEEALEAKE-ELERtnkqLRAEMEDLVSSKD----DVGKNVH----ELERSKRALEQqveEMKTQLEELED 706
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 845 EIREDTDAHRRkaaLEEHM------FQKLLENSQMGG--RRAQRWKEAEEKEFHLQSAKKASALSDASRK 906
Cdd:pfam01576 707 ELQATEDAKLR---LEVNMqalkaqFERDLQARDEQGeeKRRQLVKQVRELEAELEDERKQRAQAVAAKK 773
|
|
| ARGLU |
pfam15346 |
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ... |
704-767 |
6.27e-03 |
|
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is required for the oestrogen-dependent expression of ESR1 target genes. It functions in cooperation with MED1. The family of proteins is found in eukaryotes.
Pssm-ID: 405931 [Multi-domain] Cd Length: 151 Bit Score: 38.49 E-value: 6.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 704 RERQTVENMQAEVDEQRAKDEAWYQKQELL--------RRAEETRR-----------EILLQEEEKMAQQRQRLAAVKRE 764
Cdd:pfam15346 54 VLEELEREREAELEEERRKEEEERKKREELerileennRKIEEAQRkeaeerlamleEQRRMKEERQRREKEEEEREKRE 133
|
...
gi 264681543 765 LEI 767
Cdd:pfam15346 134 QQK 136
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
686-842 |
6.43e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.71 E-value: 6.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 686 DYQTRE--WERIRN--DELDFLRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREI---LLQEEEKMAQQRQRL 758
Cdd:PRK04863 943 DYQQAQqtQRDAKQqaFALTEVVQRRAHFSYEDAAEMLAKNSDLNEKLRQRLEQAEQERTRAreqLRQAQAQLAQYNQVL 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 759 AAVKRELEIKEIHLQDAARR-RLLKLQQDQ-REMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELE-AQKRL--YEK 833
Cdd:PRK04863 1023 ASLKSSYDAKRQMLQELKQElQDLGVPADSgAEERARARRDELHARLSANRSRRNQLEKQLTFCEAEMDnLTKKLrkLER 1102
|
....*....
gi 264681543 834 DLTTSQEAV 842
Cdd:PRK04863 1103 DYHEMREQV 1111
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
690-872 |
6.98e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 40.34 E-value: 6.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 690 REWERIRNDELDFLRERQTVENMQAEVDEQRAKDEAW-----YQKQE----LLRRAEETRREILLQEEEKMAQQRQRLAA 760
Cdd:TIGR00618 615 HALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALqltltQERVRehalSIRVLPKELLASRQLALQKMQSEKEQLTY 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 761 VKRELEIKEIHLQdaarrrllklQQDQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEKDLTTSQE 840
Cdd:TIGR00618 695 WKEMLAQCQTLLR----------ELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHF 764
|
170 180 190
....*....|....*....|....*....|....
gi 264681543 841 AVAKE--IREDTDAHRRKAALEEHMFQKLLENSQ 872
Cdd:TIGR00618 765 NNNEEvtAALQTGAELSHLAAEIQFFNRLREEDT 798
|
|
| PDCD7 |
pfam16021 |
Programmed cell death protein 7; |
756-857 |
8.91e-03 |
|
Programmed cell death protein 7;
Pssm-ID: 464979 [Multi-domain] Cd Length: 305 Bit Score: 39.32 E-value: 8.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 756 QRLAAVKRELEIKEIHLQDAARRRLLK--LQQDQREmELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEK 833
Cdd:pfam16021 42 SRAAELKHELQEKLLLLEDPELLESLKrkLERRQKK-RLRRKRRKEERKEEKKEEQERRAEREAKIDKWRRKQIQEVEEK 120
|
90 100
....*....|....*....|....
gi 264681543 834 DLTTSQEAVAKEIRedTDAHRRKA 857
Cdd:pfam16021 121 KRERELKLAADAVL--SEVRKKQA 142
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
779-872 |
9.96e-03 |
|
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: 39.72 E-value: 9.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 779 RLLKLQQD--QREMELRRLEDEIERKVqmrdqeiAATAKDLEI---RQLELEAQKRLYEKDLTTSQEAvakeIREDTDAH 853
Cdd:pfam05557 10 RLSQLQNEkkQMELEHKRARIELEKKA-------SALKRQLDResdRNQELQKRIRLLEKREAEAEEA----LREQAELN 78
|
90
....*....|....*....
gi 264681543 854 RRKAALEEHMFQKLLENSQ 872
Cdd:pfam05557 79 RLKKKYLEALNKKLNEKES 97
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
702-848 |
9.97e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 39.10 E-value: 9.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681543 702 FLRERQT-VENMQAEVDEQRAKDEAWyqkQELLRRAEETRREILlQEEEKMAQQRQRLAAVKRELEIKEihlqdaARRRL 780
Cdd:cd16269 147 YLEDREKlVEKYRQVPRKGVKAEEVL---QEFLQSKEAEAEAIL-QADQALTEKEKEIEAERAKAEAAE------QERKL 216
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 264681543 781 LklQQDQREMElRRLEDE-------IERKVQMRDQEIAATAKDLE-IRQLELEAQKRLYEKDLTTSQEAVAKEIRE 848
Cdd:cd16269 217 L--EEQQRELE-QKLEDQersyeehLRQLKEKMEEERENLLKEQErALESKLKEQEALLEEGFKEQAELLQEEIRS 289
|
|
|