|
Name |
Accession |
Description |
Interval |
E-value |
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
2-215 |
1.04e-21 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 98.83 E-value: 1.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 2 RGHESSVCSISVHASGRYAITTSSD-TAQLWDLDTFQRKRKLNIRQSvGIQKVFFLPLSNTILSCFKDNSIFAWECDTLF 80
Cdd:COG2319 201 TGHTGAVRSVAFSPDGKLLASGSADgTVRLWDLATGKLLRTLTGHSG-SVRSVAFSPDGRLLASGSADGTVRLWDLATGE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 81 CKYQLPGPPEGSNILykvfAVTRDGRILAAGGKSNHLHLWCLEATGLFRIIQmpAKVRAVRHLEFLPDsfdagsNQVLGV 160
Cdd:COG2319 280 LLRTLTGHSGGVNSV----AFSPDGKLLASGSDDGTVRLWDLATGKLLRTLT--GHTGAVRSVAFSPD------GKTLAS 347
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1720383800 161 LSQDGIMRFVNIQTCKLLFEIGTVEEGISSSVISPHGRYIASIMENGSLNVYSVQ 215
Cdd:COG2319 348 GSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
2-215 |
5.56e-21 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 96.52 E-value: 5.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 2 RGHESSVCSISVHASGRYAITTSSD-TAQLWDLDTFQRKRKLNiRQSVGIQKVFFLPLSNTILSCFKDNSIFAWECDTLF 80
Cdd:COG2319 117 TGHTGAVRSVAFSPDGKTLASGSADgTVRLWDLATGKLLRTLT-GHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGK 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 81 CKYQLPGPPEGSNILykvfAVTRDGRILAAGGKSNHLHLWCLEATGLFRIIQMPAkvRAVRHLEFLPDSfdagsnQVLGV 160
Cdd:COG2319 196 LLRTLTGHTGAVRSV----AFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHS--GSVRSVAFSPDG------RLLAS 263
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1720383800 161 LSQDGIMRFVNIQTCKLLFEIGTVEEGISSSVISPHGRYIASIMENGSLNVYSVQ 215
Cdd:COG2319 264 GSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLA 318
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
2-219 |
1.87e-20 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 94.98 E-value: 1.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 2 RGHESSVCSISVHASGRYAITTSSD-TAQLWDLDTFQRKRKLNIRQSvGIQKVFFLPLSNTILSCFKDNSIFAWECDTLF 80
Cdd:COG2319 159 TGHSGAVTSVAFSPDGKLLASGSDDgTVRLWDLATGKLLRTLTGHTG-AVRSVAFSPDGKLLASGSADGTVRLWDLATGK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 81 CKYQLPGPPEGSNILykvfAVTRDGRILAAGGKSNHLHLWCLEATGLFRIIQMPAkvRAVRHLEFLPDSfdagsnQVLGV 160
Cdd:COG2319 238 LLRTLTGHSGSVRSV----AFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHS--GGVNSVAFSPDG------KLLAS 305
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720383800 161 LSQDGIMRFVNIQTCKLLFEIGTVEEGISSSVISPHGRYIASIMENGSLNVYSVQALTQ 219
Cdd:COG2319 306 GSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGEL 364
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
2-215 |
5.59e-20 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 93.44 E-value: 5.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 2 RGHESSVCSISVHASGRYAITTSSD-TAQLWDLDTFQRKRKLNIRQSvGIQKVFFLPLSNTILSCFKDNSIFAWECDTLF 80
Cdd:COG2319 75 LGHTAAVLSVAFSPDGRLLASASADgTVRLWDLATGLLLRTLTGHTG-AVRSVAFSPDGKTLASGSADGTVRLWDLATGK 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 81 CKYQLPGPPEGSNILykvfAVTRDGRILAAGGKSNHLHLWCLEATGLFRIIQmpAKVRAVRHLEFLPDSfdagsnQVLGV 160
Cdd:COG2319 154 LLRTLTGHSGAVTSV----AFSPDGKLLASGSDDGTVRLWDLATGKLLRTLT--GHTGAVRSVAFSPDG------KLLAS 221
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1720383800 161 LSQDGIMRFVNIQTCKLLFEIGTVEEGISSSVISPHGRYIASIMENGSLNVYSVQ 215
Cdd:COG2319 222 GSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLA 276
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
1-213 |
3.95e-17 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 82.77 E-value: 3.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 1 MRGHESSVCSISVHASGRYAITTSSD-TAQLWDLDTFQRKRKLNIRQSvGIQKVFFLPLSNTILSCFKDNSIFAWECDTL 79
Cdd:cd00200 89 LTGHTSYVSSVAFSPDGRILSSSSRDkTIKVWDVETGKCLTTLRGHTD-WVNSVAFSPDGTFVASSSQDGTIKLWDLRTG 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 80 FCKYQLPGpPEGSnilykVFAVT--RDGRILAAGGKSNHLHLWclEATGLFRIIQMPAKVRAVRHLEFLPDsfdagsNQV 157
Cdd:cd00200 168 KCVATLTG-HTGE-----VNSVAfsPDGEKLLSSSSDGTIKLW--DLSTGKCLGTLRGHENGVNSVAFSPD------GYL 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720383800 158 LGVLSQDGIMRFVNIQTCKLLFEIGTVEEGISSSVISPHGRYIASIMENGSLNVYS 213
Cdd:cd00200 234 LASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
2-216 |
2.75e-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: 2.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 2 RGHESSVCSISVHASGRYAITTSSD-TAQLWDLDTFQRKRKLNIrQSVGIQKVFFLPLSNTILSCFKDNSIFAWECDTLF 80
Cdd:cd00200 6 KGHTGGVTCVAFSPDGKLLATGSGDgTIKVWDLETGELLRTLKG-HTGPVRDVAASADGTYLASGSSDKTIRLWDLETGE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 81 CKYQLPGPPEGsnilykVFAV--TRDGRILAAGGKSNHLHLWCLEATGLfrIIQMPAKVRAVRHLEFLPDsfdagsNQVL 158
Cdd:cd00200 85 CVRTLTGHTSY------VSSVafSPDGRILSSSSRDKTIKVWDVETGKC--LTTLRGHTDWVNSVAFSPD------GTFV 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720383800 159 GVLSQDGIMRFVNIQTCKLLFEIGTVEEGISSSVISPHGRYIASIMENGSLNVYSVQA 216
Cdd:cd00200 151 ASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLST 208
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
1-174 |
3.00e-15 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 78.80 E-value: 3.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 1 MRGHESSVCSISVHASGRYAITTSSD-TAQLWDLDTFQRKRKLNiRQSVGIQKVFFLPLSNTILSCFKDNSIFAWECDTL 79
Cdd:COG2319 242 LTGHSGSVRSVAFSPDGRLLASGSADgTVRLWDLATGELLRTLT-GHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATG 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 80 FCKYQLPGPPEGSNILykvfAVTRDGRILAAGGKSNHLHLWCLEATGLFRIIQMPAkvRAVRHLEFLPDSfdagsnQVLG 159
Cdd:COG2319 321 KLLRTLTGHTGAVRSV----AFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHT--GAVTSVAFSPDG------RTLA 388
|
170
....*....|....*
gi 1720383800 160 VLSQDGIMRFVNIQT 174
Cdd:COG2319 389 SGSADGTVRLWDLAT 403
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
2-215 |
7.25e-14 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 74.56 E-value: 7.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 2 RGHESSVCSISVHASGRYAITTSSDTAQLWDLDTFQRKRKLNIRQSVGIQKVFFLPLSNTILSCFKDNSIFAWECDTLFC 81
Cdd:COG2319 33 LGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 82 KYQLPGPPEGSNILykvfAVTRDGRILAAGGKSNHLHLWCLEATGLFRIIQMPAkvRAVRHLEFLPDSfdagsnQVLGVL 161
Cdd:COG2319 113 LRTLTGHTGAVRSV----AFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHS--GAVTSVAFSPDG------KLLASG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1720383800 162 SQDGIMRFVNIQTCKLLFEIGTVEEGISSSVISPHGRYIASIMENGSLNVYSVQ 215
Cdd:COG2319 181 SDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLA 234
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
563-874 |
5.87e-13 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 72.85 E-value: 5.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 563 IVDYQTREWERIRNDELDFL---RERQTVENMQAEVDEQRAKDEAwyqkqELLRRAEETRREILLQEEEKMAQQRQRlaa 639
Cdd:pfam17380 277 IVQHQKAVSERQQQEKFEKMeqeRLRQEKEEKAREVERRRKLEEA-----EKARQAEMDRQAAIYAEQERMAMERER--- 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 640 vkrelEIKEIHLQDaARRRLLKLQQDQREMELRRLEdEIERkVQMRDQEiaataKDLEIRQlELEAQK--RLYEKDlttS 717
Cdd:pfam17380 349 -----ELERIRQEE-RKRELERIRQEEIAMEISRMR-ELER-LQMERQQ-----KNERVRQ-ELEAARkvKILEEE---R 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 718 QEAVAKEIREDTDAHRRKAALEEHMFQKLLENSQmggRRAQRVMEDNLAKAEqaclnadwQIQTLHKQKcADQQRSQGYY 797
Cdd:pfam17380 412 QRKIQQQKVEMEQIRAEQEEARQREVRRLEEERA---REMERVRLEEQERQQ--------QVERLRQQE-EERKRKKLEL 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 798 DvatllRENR-RKEVEVLNAM-----MEEEAQKWKEAEEKEFHLQS--AKKASALSDASRKWFLRQETSAALEHEEMPWL 869
Cdd:pfam17380 480 E-----KEKRdRKRAEEQRRKilekeLEERKQAMIEEERKRKLLEKemEERQKAIYEEERRREAEEERRKQQEMEERRRI 554
|
....*
gi 1720383800 870 QRQYM 874
Cdd:pfam17380 555 QEQMR 559
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
566-842 |
8.57e-13 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 72.46 E-value: 8.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 566 YQTREWERIRNDELDFLRE----RQTVEN---MQAEVDEQRA-----KDEAWYQKQELLR-RAEETRREI--LLQEE--- 627
Cdd:pfam17380 293 FEKMEQERLRQEKEEKAREverrRKLEEAekaRQAEMDRQAAiyaeqERMAMERERELERiRQEERKRELerIRQEEiam 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 628 --------EKMAQQRQRL-AAVKRELEI-KEIHLQDAARRRllKLQQDQREMELRRLEDEIERKVQMRDQEiAATAKDLE 697
Cdd:pfam17380 373 eisrmrelERLQMERQQKnERVRQELEAaRKVKILEEERQR--KIQQQKVEMEQIRAEQEEARQREVRRLE-EERAREME 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 698 -IRQLELEAQKRLyekDLTTSQEAVAKEIREDTDAHRRKAALEEHMFQKLLENsQMGGRRAQRVMEDNLAKaeqaclnad 776
Cdd:pfam17380 450 rVRLEEQERQQQV---ERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEK-ELEERKQAMIEEERKRK--------- 516
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720383800 777 wqiqTLHKQKcadQQRSQGYYDvatllrENRRKEVEvlnammeEEAQKWKEAEEKEFHLQSAKKAS 842
Cdd:pfam17380 517 ----LLEKEM---EERQKAIYE------EERRREAE-------EERRKQQEMEERRRIQEQMRKAT 562
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
572-832 |
9.22e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 72.66 E-value: 9.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 572 ERIRNDELDFLRERQTVENMQAEVDEQRAK--------DEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRE 643
Cdd:COG1196 246 AELEELEAELEELEAELAELEAELEELRLEleelelelEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 644 LEIKEIHLQDAARRRLLKLQQDQREMELRRLEDEIERKVQMRD------QEIAATAKDLEIRQLELEAQKRLYEKDLTTS 717
Cdd:COG1196 326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLeaeaelAEAEEELEELAEELLEALRAAAELAAQLEEL 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 718 QEAVAKEIREDTDAHRRKAALEEHmfQKLLENSQMGGRRAQRVMEDNLAKAEQACLNADWQIQTLHKQkcADQQRSQGYY 797
Cdd:COG1196 406 EEAEEALLERLERLEEELEELEEA--LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE--AALLEAALAE 481
|
250 260 270
....*....|....*....|....*....|....*.
gi 1720383800 798 DVATLLRENRRKEV-EVLNAMMEEEAQKWKEAEEKE 832
Cdd:COG1196 482 LLEELAEAAARLLLlLEAEADYEGFLEGVKAALLLA 517
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
567-744 |
3.38e-11 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 67.07 E-value: 3.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 567 QTREWERIRNDELDflrERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEE----KMAQQRQRLAAVKR 642
Cdd:pfam17380 444 RAREMERVRLEEQE---RQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEerkqAMIEEERKRKLLEK 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 643 ELEIKEIHLQDAARRRLLKLQQ-DQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEKDLTTSQEAV 721
Cdd:pfam17380 521 EMEERQKAIYEEERRREAEEERrKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAEYEATTPITTI 600
|
170 180
....*....|....*....|...
gi 1720383800 722 AKEIREDTDAHrRKAALEEHMFQ 744
Cdd:pfam17380 601 KPIYRPRISEY-QPPDVESHMIR 622
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
566-864 |
1.33e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.34 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 566 YQT-REWERIRNDELdFLRERQTVENMQAEVDEQRAkdeawyQKQELLRRAEETRREIllqeEEKMAQQRQRLAAVKREL 644
Cdd:COG1196 215 YRElKEELKELEAEL-LLLKLRELEAELEELEAELE------ELEAELEELEAELAEL----EAELEELRLELEELELEL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 645 EIKEIHLQdAARRRLLKLQQDQR--EMELRRLEDEIERKvQMRDQEIAATAKDLEIRQLELEAQKRLYEKDLTTSQEAVA 722
Cdd:COG1196 284 EEAQAEEY-ELLAELARLEQDIArlEERRRELEERLEEL-EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 723 KEIREDTDAHRRKAALEEHMFQKLLENSQMggRRAQRVMEDNLAKAEQaclnadwQIQTLHKQKCADQQRSQGYYDVATL 802
Cdd:COG1196 362 EAEEALLEAEAELAEAEEELEELAEELLEA--LRAAAELAAQLEELEE-------AEEALLERLERLEEELEELEEALAE 432
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720383800 803 LRENRRKEVEVLNAMMEEEAQKWKEAEEKEFHLQSAKKASALSDASRKWFLRQETSAALEHE 864
Cdd:COG1196 433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
572-840 |
1.39e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 65.55 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 572 ERIRNDELdflreRQTVENMQAEVDEQRAKDEAwYQKQELLRRAEETRR--EILLQEEEKMAQQRQRLAAVKRELEIKei 649
Cdd:PTZ00121 1481 EAKKADEA-----KKKAEEAKKKADEAKKAAEA-KKKADEAKKAEEAKKadEAKKAEEAKKADEAKKAEEKKKADELK-- 1552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 650 hlqdaaRRRLLKLQQDQREMELRRLEDEiERKVQMRDQEIAATAKDLEIrqlelEAQKRLYEKDLTTSQEAVAKEIREDT 729
Cdd:PTZ00121 1553 ------KAEELKKAEEKKKAEEAKKAEE-DKNMALRKAEEAKKAEEARI-----EEVMKLYEEEKKMKAEEAKKAEEAKI 1620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 730 DAHR-RKAALEEHMFQKLLENSQMGGRRAQRVM---EDNLAKAEQACLNADWQIQTLHKQKCADQQRSQGyyDVATLLRE 805
Cdd:PTZ00121 1621 KAEElKKAEEEKKKVEQLKKKEAEEKKKAEELKkaeEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKA--AEALKKEA 1698
|
250 260 270
....*....|....*....|....*....|....*....
gi 1720383800 806 NRRKEVEVLNAMMEEEAQKW----KEAEEKEFHLQSAKK 840
Cdd:PTZ00121 1699 EEAKKAEELKKKEAEEKKKAeelkKAEEENKIKAEEAKK 1737
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
569-864 |
2.98e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 64.78 E-value: 2.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 569 REWERIRNDELdflreRQTVENMQAevDEQRAKDEAwyQKQELLRRAEETRR--EILLQEEEKMAQQRQRLAAVKRELEI 646
Cdd:PTZ00121 1505 AAEAKKKADEA-----KKAEEAKKA--DEAKKAEEA--KKADEAKKAEEKKKadELKKAEELKKAEEKKKAEEAKKAEED 1575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 647 KEIHLQDAARRRllKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEKDLTTSQEAVAKEIR 726
Cdd:PTZ00121 1576 KNMALRKAEEAK--KAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELK 1653
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 727 EDTDAHRRKAALEehmfQKLLENSQMGGRRAQRVMEDNLAKAEQACLNADwqiqtlhKQKCADQQRSQGYYDV--ATLLR 804
Cdd:PTZ00121 1654 KAEEENKIKAAEE----AKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAE-------EAKKAEELKKKEAEEKkkAEELK 1722
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720383800 805 ---ENRRKEVEVLNAMMEEEAQKWKEAEEKEfhlQSAKKASALSDASRKWF--LRQETSAALEHE 864
Cdd:PTZ00121 1723 kaeEENKIKAEEAKKEAEEDKKKAEEAKKDE---EEKKKIAHLKKEEEKKAeeIRKEKEAVIEEE 1784
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
609-865 |
1.08e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.65 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 609 QELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELEIKEIHLQ---DAARRRLLKLQQDQREME---------LRRLED 676
Cdd:COG1196 216 RELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEaelAELEAELEELRLELEELEleleeaqaeEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 677 EIERKVQMRDQEiAATAKDLEIRQLELEAQKRLYEKDLTTSQEAVAKEIREDTDAHRRKAALEEHMFQKLLENSQMGGRR 756
Cdd:COG1196 296 ELARLEQDIARL-EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 757 AQRVME-DNLAKAEQACLNADWQIQTLHKQKCADQQRSQGyyDVATLLRENRRKEVEVLNAMMEEEAQKWKEAEEKEFHL 835
Cdd:COG1196 375 AEAEEElEELAEELLEALRAAAELAAQLEELEEAEEALLE--RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
250 260 270
....*....|....*....|....*....|
gi 1720383800 836 QSAKKASALSDASRKWFLRQETSAALEHEE 865
Cdd:COG1196 453 ELEEEEEALLELLAELLEEAALLEAALAEL 482
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
572-832 |
1.40e-09 |
|
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: 60.70 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 572 ERIRNDELDFLRERQTVENMQAEVDEQRAKDEAWYQ-KQELLRRAEETRREILLQEEEKMAQQRQRLAAVKR-ELEIKEI 649
Cdd:pfam13868 38 EKEEERRLDEMMEEERERALEEEEEKEEERKEERKRyRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERiQEEDQAE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 650 HLQDAARRRLLK--------LQQDQREMElRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEKDLTTSQEAv 721
Cdd:pfam13868 118 AEEKLEKQRQLReeidefneEQAEWKELE-KEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEK- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 722 AKEIREDTDAHRRKAALEEHMF-----------QKLLENSQMGGRRAQRVMEDNLAKAEQACLNADWQIQTLHKQKCAD- 789
Cdd:pfam13868 196 AQDEKAERDELRAKLYQEEQERkerqkereeaeKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEe 275
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1720383800 790 ----------QQRSQGYYDVATLLRENRRKEVEVLNAMMEEEAQKWKEAEEKE 832
Cdd:pfam13868 276 ieqeeaekrrMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERR 328
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
612-865 |
1.76e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.88 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 612 LRRAEE--TRREILLQEeekMAQQRQRLA----------AVKRELEIKEIHLQdAARRRLLKLQQDQREMELRRLEDEIE 679
Cdd:COG1196 181 LEATEEnlERLEDILGE---LERQLEPLErqaekaeryrELKEELKELEAELL-LLKLRELEAELEELEAELEELEAELE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 680 R-KVQMRDQEIAATAKDLEIRQLELE---AQKRLYEkdlttSQEAVAKEIREDTDAHRRKAALEEHMFQKLLENSQMGGR 755
Cdd:COG1196 257 ElEAELAELEAELEELRLELEELELEleeAQAEEYE-----LLAELARLEQDIARLEERRRELEERLEELEEELAELEEE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 756 RAQRVMEDNLAKAEQACLNADWQIQTLHKQKCADQQRSQgyydvATLLRENRRKEVEVLNAMMEEEAQKwKEAEEKEFHL 835
Cdd:COG1196 332 LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA-----EAELAEAEEELEELAEELLEALRAA-AELAAQLEEL 405
|
250 260 270
....*....|....*....|....*....|
gi 1720383800 836 QSAKKASALSDASRKWFLRQETSAALEHEE 865
Cdd:COG1196 406 EEAEEALLERLERLEEELEELEEALAELEE 435
|
|
| RabGAP-TBC |
pfam00566 |
Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are ... |
340-484 |
2.01e-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: 2.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 340 SLQKKYPIKSRKLLRVLQRTLSALAHWsaiFSDTPY---LPLLAFPFVkLFQNNQLICFEVVATLIINwcQHWFEYFPN- 415
Cdd:pfam00566 19 TFPHSFFFDNGPGQNSLRRILKAYSIY---NPDVGYcqgMNFIAAPLL-LVYLDEEDAFWCFVSLLEN--YLLRDFYTPd 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720383800 416 -PPINILSMI-ENVLAFHDKELLQHFIDRDITSQVYAWPLLETLFSEVLTREEWLRLFDNIFSNHPSFLLM 484
Cdd:pfam00566 93 fPGLKRDLYVfEELLKKKLPKLYKHLKELGLDPDLFASQWFLTLFAREFPLSTVLRIWDYFFLEGEKFVLF 163
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
577-850 |
1.30e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.38 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 577 DELDFLRERQTVENMQAEvdEQRAKDEAwYQKQELLRRAEETRR--EILLQEEEKMAQQRQRLAAVKReleikeihLQDA 654
Cdd:PTZ00121 1095 EAFGKAEEAKKTETGKAE--EARKAEEA-KKKAEDARKAEEARKaeDARKAEEARKAEDAKRVEIARK--------AEDA 1163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 655 ARRRLLKLQQDQREMELRRLEDEIERKVQMRDQE----IAATAKDLEIRQLEleaQKRLYEKDLTTSQEAVAKEIREDTD 730
Cdd:PTZ00121 1164 RKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEdarkAEAARKAEEERKAE---EARKAEDAKKAEAVKKAEEAKKDAE 1240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 731 AHRRKAALEEHMFQKLLENSQMggrrAQRVMEDNLAKAEQAcLNADWQIQTLHKQKCADQQRSQGYYDVATLLRE-NRRK 809
Cdd:PTZ00121 1241 EAKKAEEERNNEEIRKFEEARM----AHFARRQAAIKAEEA-RKADELKKAEEKKKADEAKKAEEKKKADEAKKKaEEAK 1315
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1720383800 810 EVEVLNAMMEEEAQKWKEAEEKEfhlQSAKKASALSDASRK 850
Cdd:PTZ00121 1316 KADEAKKKAEEAKKKADAAKKKA---EEAKKAAEAAKAEAE 1353
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
570-751 |
1.79e-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: 58.04 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 570 EWERIRNDELDFLRERQ----TVENMQAEVD--EQRAKDEAWYQKQellRRAEETRReillQEEEKMAQQRQRLAAVKRE 643
Cdd:pfam15709 349 EVERKRREQEEQRRLQQeqleRAEKMREELEleQQRRFEEIRLRKQ---RLEEERQR----QEEEERKQRLQLQAAQERA 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 644 leikeiHLQDAA-RRRLLKLQQDQREMELRRLEDEIERKVQMRDQeIAATAKDL-EIRQLE-LEAQKRLYEKDLTTSQEA 720
Cdd:pfam15709 422 ------RQQQEEfRRKLQELQRKKQQEEAERAEAEKQRQKELEMQ-LAEEQKRLmEMAEEErLEYQRQKQEAEEKARLEA 494
|
170 180 190
....*....|....*....|....*....|.
gi 1720383800 721 VAKEIREDTDAhrrKAALEEHMFQKLLENSQ 751
Cdd:pfam15709 495 EERRQKEEEAA---RLALEEAMKQAQEQARQ 522
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
569-801 |
3.81e-08 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 57.44 E-value: 3.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 569 REWERIRNdELDFLR-------ERQ-TVENMQAEVDEQRAKDEAwyQKQELLRRAEETR-REILLQEEEKMAQQRQrlaa 639
Cdd:pfam17380 389 QKNERVRQ-ELEAARkvkileeERQrKIQQQKVEMEQIRAEQEE--ARQREVRRLEEERaREMERVRLEEQERQQQ---- 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 640 vkreleiKEIHLQDAARRRLLKLQQDQREMELRRLEDE----IERKVQMRDQEIaatakdleirqLELEAQKRLYEKDLT 715
Cdd:pfam17380 462 -------VERLRQQEEERKRKKLELEKEKRDRKRAEEQrrkiLEKELEERKQAM-----------IEEERKRKLLEKEME 523
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 716 TSQEAVAKEiredtdaHRRKAALEEHMFQKLLENSqmggRRAQRVMEdnLAKAEQACLNADWQIQTLHKQkCADQQRSQG 795
Cdd:pfam17380 524 ERQKAIYEE-------ERRREAEEERRKQQEMEER----RRIQEQMR--KATEERSRLEAMEREREMMRQ-IVESEKARA 589
|
....*.
gi 1720383800 796 YYDVAT 801
Cdd:pfam17380 590 EYEATT 595
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
567-850 |
7.94e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.69 E-value: 7.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 567 QTREWERIRNDEldflRERQTVENMQAEvDEQRA----KDEAWYQKQELLRRAEETR--REILLQEEEKMAQQRQRLAAV 640
Cdd:PTZ00121 1198 DARKAEAARKAE----EERKAEEARKAE-DAKKAeavkKAEEAKKDAEEAKKAEEERnnEEIRKFEEARMAHFARRQAAI 1272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 641 KRELEIKEIHLQDAARRRllKLQQDQREMELRRLeDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYE-KDLTTSQE 719
Cdd:PTZ00121 1273 KAEEARKADELKKAEEKK--KADEAKKAEEKKKA-DEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEaKKAAEAAK 1349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 720 AVAKEIREDTDAHRRKAALEEHMFQKLLENSQMGGRRAQRV--MEDNLAKAEQACLNADWQIQTLHKQKCADQQRSQGyy 797
Cdd:PTZ00121 1350 AEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKkkADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKA-- 1427
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1720383800 798 dvatllrENRRKEVEVLNAmmEEEAQKWKEAEEKEFHLQSAKKASALSDASRK 850
Cdd:PTZ00121 1428 -------EEKKKADEAKKK--AEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK 1471
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
569-873 |
9.87e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 56.23 E-value: 9.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 569 REWERIRNdELDFLRERqtVENMQAEVDE--------QRAKDEAwYQKQELLRRAEETRREILLQEEEKMAQQRQR---- 636
Cdd:TIGR02169 170 RKKEKALE-ELEEVEEN--IERLDLIIDEkrqqlerlRREREKA-ERYQALLKEKREYEGYELLKEKEALERQKEAierq 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 637 LAAVKRELEIKEIHLQDAARRrllklqQDQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEKDLTT 716
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKR------LEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELED 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 717 SQEAVAKEIREDTDAHRRKAALEEHMFQKLLENSQMGGRRAQR--VMEDNLAKAEQ-ACLNADWQIQTLHKQKCADQQRS 793
Cdd:TIGR02169 320 AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELkeELEDLRAELEEvDKEFAETRDELKDYREKLEKLKR 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 794 QGY---YDVATLLRENRRKEVEV-------------LNAMMEEEAQKWKEAEEKEFHLQSAKKasALSDASRKWFLRQET 857
Cdd:TIGR02169 400 EINelkRELDRLQEELQRLSEELadlnaaiagieakINELEEEKEDKALEIKKQEWKLEQLAA--DLSKYEQELYDLKEE 477
|
330
....*....|....*.
gi 1720383800 858 SAALEhEEMPWLQRQY 873
Cdd:TIGR02169 478 YDRVE-KELSKLQREL 492
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
567-850 |
1.11e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.30 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 567 QTREWERIRNDELdfLRERQTVENMQA--EVDEQRAKDEAwyQKQELLRRAEETRReilLQEEEKMAQQRQRLAAVKREL 644
Cdd:PTZ00121 1180 AARKAEEVRKAEE--LRKAEDARKAEAarKAEEERKAEEA--RKAEDAKKAEAVKK---AEEAKKDAEEAKKAEEERNNE 1252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 645 EIKEIhlqDAARRRLLKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKdlEIRQLElEAQKRLYEKDLTTSQEAVAKE 724
Cdd:PTZ00121 1253 EIRKF---EEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAE--EKKKAD-EAKKKAEEAKKADEAKKKAEE 1326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 725 IREDTDAHRRKA----------ALEEHMFQKLLENSQMGGRRAQRVMEDNLAKAEQACLNADwqiqtlhKQKCADQQRSQ 794
Cdd:PTZ00121 1327 AKKKADAAKKKAeeakkaaeaaKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAE-------EKKKADEAKKK 1399
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720383800 795 GyydvatllRENRRKEVEVLNAmmEEEAQKWKEAEEKEFHLQSAKKASALSDASRK 850
Cdd:PTZ00121 1400 A--------EEDKKKADELKKA--AAAKKKADEAKKKAEEKKKADEAKKKAEEAKK 1445
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
565-740 |
1.14e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.08 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 565 DYQTREWERIRNDELDFLRERQTVENMQaevdeqrakdeawyQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKREL 644
Cdd:COG4913 260 LAERYAAARERLAELEYLRAALRLWFAQ--------------RRLELLEAELEELRAELARLEAELERLEARLDALREEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 645 EIKEIHLQDAARRRLLKLQQdqremELRRLEDEIERKVQMRDQ----------EIAATAKDLEIRQLELEAQKRLYEKDL 714
Cdd:COG4913 326 DELEAQIRGNGGDRLEQLER-----EIERLERELEERERRRARleallaalglPLPASAEEFAALRAEAAALLEALEEEL 400
|
170 180
....*....|....*....|....*.
gi 1720383800 715 TTSQEAVAKEIREDTDAHRRKAALEE 740
Cdd:COG4913 401 EALEEALAEAEAALRDLRRELRELEA 426
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
586-783 |
4.20e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 54.19 E-value: 4.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 586 QTVENMQAEVDEQRAKDEAwyqkQELLRRAEETR--------REILLQEEEKMAQQRQRLAAVKRELEIK-EIHLQDAAr 656
Cdd:PRK04863 480 QLVRKIAGEVSRSEAWDVA----RELLRRLREQRhlaeqlqqLRMRLSELEQRLRQQQRAERLLAEFCKRlGKNLDDED- 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 657 rrLLKLQQDQREMELRRLEDE----IERKVQMRDQEIAATAkdlEIRQLELEAQKRLyekdltTSQEAVAK--EIREDTD 730
Cdd:PRK04863 555 --ELEQLQEELEARLESLSESvseaRERRMALRQQLEQLQA---RIQRLAARAPAWL------AAQDALARlrEQSGEEF 623
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1720383800 731 AHRrkAALEEHMfQKLLENsqmggRRAQRVMEDNLAKAEQAClnaDWQIQTLH 783
Cdd:PRK04863 624 EDS--QDVTEYM-QQLLER-----ERELTVERDELAARKQAL---DEEIERLS 665
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
572-841 |
4.61e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.99 E-value: 4.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 572 ERIRNDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREillQEEEKMAQQRQRLAAVKRELEIKEIHL 651
Cdd:PTZ00121 1364 EKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKA---AAAKKKADEAKKKAEEKKKADEAKKKA 1440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 652 QDAARRRLLKLQ-QDQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEKDLTTSQEAVAKEIREDTD 730
Cdd:PTZ00121 1441 EEAKKADEAKKKaEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEE 1520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 731 AHRRKAALEEHMFQKLLEnsqmgGRRAQRVME-DNLAKAEQacLNADWQIQTLHKQKCADQQRSQGYYDvATLLRENRRK 809
Cdd:PTZ00121 1521 AKKADEAKKAEEAKKADE-----AKKAEEKKKaDELKKAEE--LKKAEEKKKAEEAKKAEEDKNMALRK-AEEAKKAEEA 1592
|
250 260 270
....*....|....*....|....*....|....*.
gi 1720383800 810 EVEVLNAMMEEE----AQKWKEAEEKEFHLQSAKKA 841
Cdd:PTZ00121 1593 RIEEVMKLYEEEkkmkAEEAKKAEEAKIKAEELKKA 1628
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
562-833 |
5.78e-07 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 53.82 E-value: 5.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 562 FIVDYQTREWE-RIRNDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRR-EILLQEEEKMAQQRQRLAA 639
Cdd:pfam02463 168 KRKKKEALKKLiEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLyLDYLKLNEERIDLLQELLR 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 640 VKRELEIKEIHLQDAARRrllKLQQDQREMElrrledEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEKDLTTSQE 719
Cdd:pfam02463 248 DEQEEIESSKQEIEKEEE---KLAQVLKENK------EEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 720 AVAKEIREDTDAHRRKAALEEhmFQKLLENSQmGGRRAQRVMEDNLAKAEQACLNADWQIQTLHKQKCADQQRSQGYYDV 799
Cdd:pfam02463 319 SEKEKKKAEKELKKEKEEIEE--LEKELKELE-IKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEE 395
|
250 260 270
....*....|....*....|....*....|....*.
gi 1720383800 800 ATLLRENRRKEVEVLN--AMMEEEAQKWKEAEEKEF 833
Cdd:pfam02463 396 ELELKSEEEKEAQLLLelARQLEDLLKEEKKEELEI 431
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
569-850 |
6.58e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.61 E-value: 6.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 569 REWERIRNDELDFLRERQtvENMQAEvdeQRAKDEAWYQKQELLRRAEETRREILlQEEEKMAQQRQRLAAVKRELEIKE 648
Cdd:PTZ00121 1587 KKAEEARIEEVMKLYEEE--KKMKAE---EAKKAEEAKIKAEELKKAEEEKKKVE-QLKKKEAEEKKKAEELKKAEEENK 1660
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 649 IHLQDAARrrllKLQQDQREMELRRLEDEIERKVQ---MRDQEIAATAKDL------------------EIRQLELEAQK 707
Cdd:PTZ00121 1661 IKAAEEAK----KAEEDKKKAEEAKKAEEDEKKAAealKKEAEEAKKAEELkkkeaeekkkaeelkkaeEENKIKAEEAK 1736
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 708 RLYEKDLTTSQEAVAKEIREDTDAHRRKAALEEhmfqkllenSQMGGRRAQRVMEDNLAKAEQaclnadwqiqtlhKQKC 787
Cdd:PTZ00121 1737 KEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKK---------AEEIRKEKEAVIEEELDEEDE-------------KRRM 1794
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720383800 788 ADQQRSQGYYDVATLLRENRRKEVEVLNAMMEEEAQKWKEA---------EEKEFHLQSAKKASALSDASRK 850
Cdd:PTZ00121 1795 EVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVadsknmqleEADAFEKHKFNKNNENGEDGNK 1866
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
561-711 |
6.95e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 52.86 E-value: 6.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 561 KFIVDYQTREWERIRNDEL-----DFLRERQTVENmqaEVDEQRAKdeawYQKQEL-LRRAEET---RREILLQEEEKMA 631
Cdd:PRK12704 41 KRILEEAKKEAEAIKKEALleakeEIHKLRNEFEK---ELRERRNE----LQKLEKrLLQKEENldrKLELLEKREEELE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 632 QQRQRLAAVKRELEIKEIHLQDAARRRLLKLQQ-------DQREMELRRLEDEIErkvqmrdQEIAATAKDLEiRQLELE 704
Cdd:PRK12704 114 KKEKELEQKQQELEKKEEELEELIEEQLQELERisgltaeEAKEILLEKVEEEAR-------HEAAVLIKEIE-EEAKEE 185
|
....*..
gi 1720383800 705 AQKRLYE 711
Cdd:PRK12704 186 ADKKAKE 192
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
572-847 |
8.25e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 53.20 E-value: 8.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 572 ERIRNDELDFLRE----RQTVENMQAEVDEQRAKDE---AWYQKQELLRRAE----ETRREILLQEEEKMAQQRQRLAA- 639
Cdd:pfam15921 306 EQARNQNSMYMRQlsdlESTVSQLRSELREAKRMYEdkiEELEKQLVLANSElteaRTERDQFSQESGNLDDQLQKLLAd 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 640 -VKREleiKEIHLQDAARRRL-------------LKLQQDQREMELRRLEDEI-----ERKVQMRDQEIAATAKDLEIRQ 700
Cdd:pfam15921 386 lHKRE---KELSLEKEQNKRLwdrdtgnsitidhLRRELDDRNMEVQRLEALLkamksECQGQMERQMAAIQGKNESLEK 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 701 L-ELEAQkrlyekdLTTSQEAVAKEIREDTdahRRKAALEEHmfQKLLENSQMGGRRAQRVMEDNLAKAEQACLNADWQI 779
Cdd:pfam15921 463 VsSLTAQ-------LESTKEMLRKVVEELT---AKKMTLESS--ERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKL 530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 780 QTLHKQKCADQ--QRSQGYYDVATLLRENRRKEVEVL------------------NAMMEEEAQKWKEAEEKEFHLQSAK 839
Cdd:pfam15921 531 QELQHLKNEGDhlRNVQTECEALKLQMAEKDKVIEILrqqienmtqlvgqhgrtaGAMQVEKAQLEKEINDRRLELQEFK 610
|
....*...
gi 1720383800 840 KASALSDA 847
Cdd:pfam15921 611 ILKDKKDA 618
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
578-765 |
1.12e-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: 52.75 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 578 ELDFLRER-QTVENMQAEVDEQRAKDEawyQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELEIKEIHLQD--- 653
Cdd:TIGR02168 303 QKQILRERlANLERQLEELEAQLEELE---SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEElee 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 654 -----AARRRLLKLQQDQREMELRRLEDEIER---KVQMRDQEIAATAKDLEIRQLElEAQKRLYEKD--LTTSQEAVAK 723
Cdd:TIGR02168 380 qletlRSKVAQLELQIASLNNEIERLEARLERledRRERLQQEIEELLKKLEEAELK-ELQAELEELEeeLEELQEELER 458
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1720383800 724 EIREDTDAHRRKAALEEHMFQKLLENSQMGGR-RAQRVMEDNL 765
Cdd:TIGR02168 459 LEEALEELREELEEAEQALDAAERELAQLQARlDSLERLQENL 501
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
584-841 |
1.14e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.84 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 584 ERQTVENMQAEVDEQRAKDEAWYQKQE------LLRRAEETRREillQEEEKMAQQRQRLAAVKRELEIKEIHLQDAARR 657
Cdd:PTZ00121 1429 EKKKADEAKKKAEEAKKADEAKKKAEEakkaeeAKKKAEEAKKA---DEAKKKAEEAKKADEAKKKAEEAKKKADEAKKA 1505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 658 RLLKLQQDQ-REMELRRLEDEIERKVQMRDQEIAATAKdlEIRQLELEAQKRLYEKDLTTSQEAVAKEIREDTDAHRRKA 736
Cdd:PTZ00121 1506 AEAKKKADEaKKAEEAKKADEAKKAEEAKKADEAKKAE--EKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKA 1583
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 737 ALEEHMFQKLLENSQMGGRRAQRVMEDNLAKAEQACLNADWQIQTLHKQKCADQQRSQGYYDVATllRENRRKEVEVLNA 816
Cdd:PTZ00121 1584 EEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKK--AEELKKAEEENKI 1661
|
250 260
....*....|....*....|....*
gi 1720383800 817 MMEEEAQKwkeAEEKEFHLQSAKKA 841
Cdd:PTZ00121 1662 KAAEEAKK---AEEDKKKAEEAKKA 1683
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
600-725 |
1.56e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 51.70 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 600 AKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLaavKRELEIKEIHLQDAARRRLlklqqdQREMELRRLEDEIE 679
Cdd:PRK12704 36 AEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEF---EKELRERRNELQKLEKRLL------QKEENLDRKLELLE 106
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1720383800 680 RkvqmRDQEIAATAKDLEIRQLELEAQKRLYEKdLTTSQEAVAKEI 725
Cdd:PRK12704 107 K----REEELEKKEKELEQKQQELEKKEEELEE-LIEEQLQELERI 147
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
567-707 |
2.23e-06 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 51.49 E-value: 2.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 567 QTREWE--RIRNDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKREL 644
Cdd:pfam15709 382 QQRRFEeiRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQL 461
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720383800 645 EIKEIHLQD-AARRRLLKLQQDQREMELRRLEDEIERKvqmRDQEIAATAKDLEIRQLELEAQK 707
Cdd:pfam15709 462 AEEQKRLMEmAEEERLEYQRQKQEAEEKARLEAEERRQ---KEEEAARLALEEAMKQAQEQARQ 522
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
582-763 |
2.50e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.48 E-value: 2.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 582 LRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELEIKEIHLQDAARRRLLK 661
Cdd:COG1196 680 ELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEP 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 662 LQQDQREMELRRLEDEIER--KVQMR-DQEIAATAKDLEirqlELEAQKrlyeKDLTTSQEAVAKEIRE-DTDAHRR-KA 736
Cdd:COG1196 760 PDLEELERELERLEREIEAlgPVNLLaIEEYEELEERYD----FLSEQR----EDLEEARETLEEAIEEiDRETRERfLE 831
|
170 180 190
....*....|....*....|....*....|...
gi 1720383800 737 ALEE------HMFQKLLensqmGGRRAQRVMED 763
Cdd:COG1196 832 TFDAvnenfqELFPRLF-----GGGEAELLLTD 859
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
571-830 |
2.87e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 50.30 E-value: 2.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 571 WERIRNDELDFLRERQT-VENMQAEVDEQRAKDEAWYQKQELLRRAEETRreilLQEEEKMAQQRQRL-AAVKRELEIKE 648
Cdd:pfam13868 107 VERIQEEDQAEAEEKLEkQRQLREEIDEFNEEQAEWKELEKEEEREEDER----ILEYLKEKAEREEErEAEREEIEEEK 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 649 IHLQDAARRRLLKLQQDQREME---LRRLEDEIERKvqMRDQEIAATAKDLEIRQLELEAQKrlyekdlttsQEAVAKEI 725
Cdd:pfam13868 183 EREIARLRAQQEKAQDEKAERDelrAKLYQEEQERK--ERQKEREEAEKKARQRQELQQARE----------EQIELKER 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 726 REdtdahRRKAALEEHMFQKLLENSQMGGRRAQRVMEDNLAKAEQACLNADWQIQTLHKQKcadqqrsqgyydvatllRE 805
Cdd:pfam13868 251 RL-----AEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQR-----------------AA 308
|
250 260
....*....|....*....|....*
gi 1720383800 806 NRRKEVEVLNAMMEEEAQKWKEAEE 830
Cdd:pfam13868 309 EREEELEEGERLREEEAERRERIEE 333
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
592-907 |
3.84e-06 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 50.42 E-value: 3.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 592 QAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELE--IKEIHLQDAARRRLLKLQQDQREM 669
Cdd:COG3064 1 AQEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEeeAREAKAEAEQRAAELAAEAAKKLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 670 ELRRLEDEIERKVQMRDQEIAATA-KDLEIRQLELEAQKRLYEKdlttSQEAVAKEIREDTDAHRRKAALEEHMFQKLLE 748
Cdd:COG3064 81 EAEKAAAEAEKKAAAEKAKAAKEAeAAAAAEKAAAAAEKEKAEE----AKRKAEEEAKRKAEEERKAAEAEAAAKAEAEA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 749 NSQMG-GRRAQRVMEDNLAKAEQACLNADWQIQTLHKQKCADQQRSQGYYDVATLLRENRRKEVEVLNAMMEEEAQKWKE 827
Cdd:COG3064 157 ARAAAaAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 828 AEEKEFHLQSAKKASALSDASRKWFLRQETSAALEHEEMPWLQRQYMDSAYLPQTSRLHDVSDMDPSTHIFSRNYPTEWN 907
Cdd:COG3064 237 VEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEA 316
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
589-867 |
5.41e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 50.61 E-value: 5.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 589 ENMQAEVDEQRAKDEAWYQKQELLRRAEETRREILL--QEEEKMAQQRQRLAAVKREleIKEIHLQDAARRRLLKLQQDQ 666
Cdd:pfam12128 210 GVVPPKSRLNRQQVEHWIRDIQAIAGIMKIRPEFTKlqQEFNTLESAELRLSHLHFG--YKSDETLIASRQEERQETSAE 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 667 REMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEA---QKRLYEKD--------------LTTSQEAVAKEIREDT 729
Cdd:pfam12128 288 LNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEAledQHGAFLDAdietaaadqeqlpsWQSELENLEERLKALT 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 730 DAH--------RRKAALEEHMFQKL------LENSQMGGRRAQRVMEDNLAKAEQAcLNADWQIQTLHKQKCADQQRS-- 793
Cdd:pfam12128 368 GKHqdvtakynRRRSKIKEQNNRDIagikdkLAKIREARDRQLAVAEDDLQALESE-LREQLEAGKLEFNEEEYRLKSrl 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 794 ---QGYYDVATL---LRENRRKEVEVLNAMMEEEAQKWKEAEEKEFHLQSAKKAS-----ALSDASRKWFLRQETSAALE 862
Cdd:pfam12128 447 gelKLRLNQATAtpeLLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRdqaseALRQASRRLEERQSALDELE 526
|
....*
gi 1720383800 863 HEEMP 867
Cdd:pfam12128 527 LQLFP 531
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
597-785 |
5.54e-06 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 49.95 E-value: 5.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 597 EQRAKDEAWYQKQELLR-RAEETRREillQEEEKMAQQRQ--RLAAVKRELEIKEIHLQDAARRRllklQQDQREMELRR 673
Cdd:pfam15709 331 EKASRDRLRAERAEMRRlEVERKRRE---QEEQRRLQQEQleRAEKMREELELEQQRRFEEIRLR----KQRLEEERQRQ 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 674 LEDEIERKVQMRDQEIAATAKDLEIRQ--LELEAQKRLYEKDLTTSQEAVAKEIRED-TDAHRRKAALEEHMFQKLLENS 750
Cdd:pfam15709 404 EEEERKQRLQLQAAQERARQQQEEFRRklQELQRKKQQEEAERAEAEKQRQKELEMQlAEEQKRLMEMAEEERLEYQRQK 483
|
170 180 190
....*....|....*....|....*....|....*....
gi 1720383800 751 QMGGRRAQRVMEDNLAKAEQACL----NADWQIQTLHKQ 785
Cdd:pfam15709 484 QEAEEKARLEAEERRQKEEEAARlaleEAMKQAQEQARQ 522
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
575-838 |
5.91e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.44 E-value: 5.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 575 RNDELDFLRERqtVENMQAEVDEQRAKDEAWYQKQE--------LLRRAEETRREI---------LLQEEEKMAQQRQRL 637
Cdd:TIGR02168 675 RRREIEELEEK--IEELEEKIAELEKALAELRKELEeleeeleqLRKELEELSRQIsalrkdlarLEAEVEQLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 638 aavkrELEIKEIhlqdAARRRLLKLQQDQREMELRRLEDEIErKVQMRDQEIAATAKDLEIRQLELEAQKRLYEKDLTTS 717
Cdd:TIGR02168 753 -----SKELTEL----EAEIEELEERLEEAEEELAEAEAEIE-ELEAQIEQLKEELKALREALDELRAELTLLNEEAANL 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 718 QEAVAKE-------IREDTDAHRRKAALEEHMfqKLLENSQMGGRRAQRVMEDNLAKAEQAclnADWQIQTLHKQKCADQ 790
Cdd:TIGR02168 823 RERLESLerriaatERRLEDLEEQIEELSEDI--ESLAAEIEELEELIEELESELEALLNE---RASLEEALALLRSELE 897
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1720383800 791 QRSQGYYDVATLLRENRRkEVEVLNAMMEEEAQKWKEAEEKEFHLQSA 838
Cdd:TIGR02168 898 ELSEELRELESKRSELRR-ELEELREKLAQLELRLEGLEVRIDNLQER 944
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
591-832 |
7.68e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 49.15 E-value: 7.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 591 MQAEVDEQRA-----KDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELeikEIHLQDAARRRLLKLQQD 665
Cdd:pfam13868 20 CNKERDAQIAekkriKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQEL---EEQIEEREQKRQEEYEEK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 666 QREMEL-----RRLEDEIERKVQMRDQEIAATAKDL--------EIRQLELEAQKRL------YEKDLTTSQEAVAKEIR 726
Cdd:pfam13868 97 LQEREQmdeivERIQEEDQAEAEEKLEKQRQLREEIdefneeqaEWKELEKEEEREEderileYLKEKAEREEEREAERE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 727 EDTDAH-RRKAALEEHMFQKLLENSQMGGRRAQRVMEDNLAKAEQAclnadwQIQTLHKQKCADQQRSQGYYDVATLLRE 805
Cdd:pfam13868 177 EIEEEKeREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQK------EREEAEKKARQRQELQQAREEQIELKER 250
|
250 260
....*....|....*....|....*..
gi 1720383800 806 NRRKEVEVLNAMMEEEAQKWKEAEEKE 832
Cdd:pfam13868 251 RLAEEAEREEEEFERMLRKQAEDEEIE 277
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
567-752 |
8.73e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 8.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 567 QTREWERIRNDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREiLLQEEEKMAQQRQRLAAVKRelei 646
Cdd:COG4717 86 KEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAE-LAELPERLEELEERLEELRE---- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 647 keihlqdaarrrlLKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEKDLTTSQEAVaKEIR 726
Cdd:COG4717 161 -------------LEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEEL-EELE 226
|
170 180
....*....|....*....|....*.
gi 1720383800 727 EDTDAHRRKAALEEhMFQKLLENSQM 752
Cdd:COG4717 227 EELEQLENELEAAA-LEERLKEARLL 251
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
606-888 |
8.73e-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: 49.67 E-value: 8.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 606 YQKQELlrraEETRREILLQEEeKMAQQRQRLAAVKRELEIKEIHLQDAARRRLLKLQQ-DQREMELRRLEDEIERKVQM 684
Cdd:TIGR02168 674 ERRREI----EELEEKIEELEE-KIAELEKALAELRKELEELEEELEQLRKELEELSRQiSALRKDLARLEAEVEQLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 685 RDQeiaatakdLEIRQLELEAQKRLYEKDLTTSQ------EAVAKEIREDTDAHRRKAALEEHMFQKL---LENSQMGGR 755
Cdd:TIGR02168 749 IAQ--------LSKELTELEAEIEELEERLEEAEeelaeaEAEIEELEAQIEQLKEELKALREALDELraeLTLLNEEAA 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 756 RAQRVMEDNLAKAEQaclnADWQIQTLHKQKcadqqrsqgyydvatllrENRRKEVEVLNAMMEEEAQKWKEAEEKEFHL 835
Cdd:TIGR02168 821 NLRERLESLERRIAA----TERRLEDLEEQI------------------EELSEDIESLAAEIEELEELIEELESELEAL 878
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1720383800 836 QSAKKASALSDASRKWFLRQETSAALEHEEmpwlQRQYMDSAYLPQTSRLHDV 888
Cdd:TIGR02168 879 LNERASLEEALALLRSELEELSEELRELES----KRSELRRELEELREKLAQL 927
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
614-831 |
1.18e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 49.18 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 614 RAEETRREILLQEEEKMAQQRQRL---AAVKRELEIKEIHLQDAARRRLlklQQDQREMElRRLEDEIERKVQMRDQEIA 690
Cdd:pfam15709 315 RSEEDPSKALLEKREQEKASRDRLraeRAEMRRLEVERKRREQEEQRRL---QQEQLERA-EKMREELELEQQRRFEEIR 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 691 atakdLEIRQLELEAQKRLYEKDLTTSQEAVAKE-IREDTDAHRRKaaLEEHMFQKLLENSQMGGRRAQRVMEDNLAKAE 769
Cdd:pfam15709 391 -----LRKQRLEEERQRQEEEERKQRLQLQAAQErARQQQEEFRRK--LQELQRKKQQEEAERAEAEKQRQKELEMQLAE 463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720383800 770 QACLNADWQiqtlHKQKCADQQRSQGYYDVATLLRENRRKEVEVLNAMMEEEAQkwKEAEEK 831
Cdd:pfam15709 464 EQKRLMEMA----EEERLEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEAM--KQAQEQ 519
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
570-792 |
1.46e-05 |
|
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: 48.30 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 570 EWERIRNDELDFLR-ERQT---VENMQAEVDEQRAKDEAwyQKQELLRRAEEtrreillQEEEKMAQQRQRLAAVKR--E 643
Cdd:TIGR02794 51 QANRIQQQKKPAAKkEQERqkkLEQQAEEAEKQRAAEQA--RQKELEQRAAA-------EKAAKQAEQAAKQAEEKQkqA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 644 LEIKEIHLQDAARRRLLKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKdleiRQLELEAQKrlyEKDltTSQEAVAK 723
Cdd:TIGR02794 122 EEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAK----KKAEAEAKA---KAE--AEAKAKAE 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720383800 724 EIREDTDAHRRKAALEEHMfqkllensqmgGRRAQRVMEDNLAKAEQACLNADWQIQTLHKQKCADQQR 792
Cdd:TIGR02794 193 EAKAKAEAAKAKAAAEAAA-----------KAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQG 250
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
593-740 |
1.63e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 48.33 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 593 AEVDEQRAKDEAwyqkqELLRRAEETRREILLQEEEKMAQQrqrlaavKRELEIKEIHLQDAARRRllKLQQDQREMELR 672
Cdd:COG2268 195 AEIIRDARIAEA-----EAERETEIAIAQANREAEEAELEQ-------EREIETARIAEAEAELAK--KKAEERREAETA 260
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720383800 673 RLEDEIERKVQmrdQEIAATAKDLEIRQLELEAQKRLYEKDLTTSQEAVAKEIREDTDAHRRKAALEE 740
Cdd:COG2268 261 RAEAEAAYEIA---EANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEA 325
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
583-875 |
1.95e-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: 48.51 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 583 RERQTVENMQAEVDEQRAKdEAWYQKQELLRRAEETRReiLLQEEEKMAQQRQRLAAVKRELEIK--EIHLQDA-ARRRL 659
Cdd:TIGR02168 207 RQAEKAERYKELKAELREL-ELALLVLRLEELREELEE--LQEELKEAEEELEELTAELQELEEKleELRLEVSeLEEEI 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 660 LKLQQDQREM--ELRRLEDEIERKVQmRDQEIAATAKDLEIRQLELEAQKRLYEKDLTTSQE--AVAKEIREDTdahrrK 735
Cdd:TIGR02168 284 EELQKELYALanEISRLEQQKQILRE-RLANLERQLEELEAQLEELESKLDELAEELAELEEklEELKEELESL-----E 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 736 AALEEhmFQKLLENSQMGGRRAQRVMED-----NLAKAEQACLNAdwQIQTLHKQKCADQQR----SQGYYDVATLLREN 806
Cdd:TIGR02168 358 AELEE--LEAELEELESRLEELEEQLETlrskvAQLELQIASLNN--EIERLEARLERLEDRrerlQQEIEELLKKLEEA 433
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 807 RRKEV-EVLNAMMEEEAQKWKEAEEKEFHLQSAKKASALSDASRKWFLRQETSAALEHEEMPWLQRQYMD 875
Cdd:TIGR02168 434 ELKELqAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
585-740 |
2.03e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 585 RQTVENMQAEVDE-QRAKDEAWYQKQELLRRAEETRREILlQEEEKMAQQRQRLAAVKRELEIKEI------------HL 651
Cdd:COG3883 36 QAELDALQAELEElNEEYNELQAELEALQAEIDKLQAEIA-EAEAEIEERREELGERARALYRSGGsvsyldvllgseSF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 652 QDAARRRLL--KLQQDQREM--ELRRLEDEIERKvqmrDQEIAATAKDLEIRQLELEAQKRLYEKDLTTSQEAVAKEIRE 727
Cdd:COG3883 115 SDFLDRLSAlsKIADADADLleELKADKAELEAK----KAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAE 190
|
170
....*....|...
gi 1720383800 728 DTDAHRRKAALEE 740
Cdd:COG3883 191 EAAAEAQLAELEA 203
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
586-771 |
2.27e-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: 48.41 E-value: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 586 QTVENMQAEVDeqraKDEAWYQKQELLRRAEETRreillqeeeKMAQQRQRLAAVKRELEiKEIHLQDAARRRL------ 659
Cdd:COG3096 479 ELVCKIAGEVE----RSQAWQTARELLRRYRSQQ---------ALAQRLQQLRAQLAELE-QRLRQQQNAERLLeefcqr 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 660 ----------LKLQQDQREMELRRLEDE----IERKVQMRDQEIAATAKDLEIRQLE---LEAQKRlyekdLTTSQEAVA 722
Cdd:COG3096 545 igqqldaaeeLEELLAELEAQLEELEEQaaeaVEQRSELRQQLEQLRARIKELAARApawLAAQDA-----LERLREQSG 619
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1720383800 723 KEIredTDAHrrkaALEEHMfQKLLENsqmggRRAQRVMEDNLAKAEQA 771
Cdd:COG3096 620 EAL---ADSQ----EVTAAM-QQLLER-----EREATVERDELAARKQA 655
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
658-843 |
2.78e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 47.81 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 658 RLLKLQQD--QREMELRRLEDEIERKVqmrdqeiAATAKDLEI---RQLELEAQKRLYEKDLTTSQEAvakeIREDTDAH 732
Cdd:pfam05557 10 RLSQLQNEkkQMELEHKRARIELEKKA-------SALKRQLDResdRNQELQKRIRLLEKREAEAEEA----LREQAELN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 733 RRKAALEEHMFQKLLENSQMGG--RRAQRVMEDNLAKAEQACLNADWQIQTLhkqkcadqqrsqgyydvatllrenrRKE 810
Cdd:pfam05557 79 RLKKKYLEALNKKLNEKESQLAdaREVISCLKNELSELRRQIQRAELELQST-------------------------NSE 133
|
170 180 190
....*....|....*....|....*....|...
gi 1720383800 811 VEVLNAMMEEEAQKWKEAEEKEFHLQSAKKASA 843
Cdd:pfam05557 134 LEELQERLDLLKAKASEAEQLRQNLEKQQSSLA 166
|
|
| COG5210 |
COG5210 |
GTPase-activating protein [General function prediction only]; |
421-537 |
3.30e-05 |
|
GTPase-activating protein [General function prediction only];
Pssm-ID: 227535 [Multi-domain] Cd Length: 496 Bit Score: 47.49 E-value: 3.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 421 LSMIENVLAFHDKELLQHFIDRDITSQVYAWPLLETLFSEVLTREEWLRLFDNIFSNHPSFLLMTVVAYSTCSRAPLLNC 500
Cdd:COG5210 350 LKVLDDLVEELDPELYEHLLREGVVLLMFAFRWFLTLFVREFPLEYALRIWDCLFLEGSSMLFQLALAILKLLRDKLLKL 429
|
90 100 110
....*....|....*....|....*....|....*..
gi 1720383800 501 TLKNDFEYFFHHRNNLDINVVIREVYHLMETTPADIH 537
Cdd:COG5210 430 DSDELLDLLLKQLFLHSGKEAWSSILKFRHGTDRDIL 466
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
575-838 |
3.60e-05 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 46.95 E-value: 3.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 575 RNDELDFLRERQTVENMQAEvdEQRAKDEawyQKQELLRRaeETRREILLQEEEKMAQQRQRLAAVKRELE------IKE 648
Cdd:pfam15558 16 RHKEEQRMRELQQQAALAWE--ELRRRDQ---KRQETLER--ERRLLLQQSQEQWQAEKEQRKARLGREERrradrrEKQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 649 IHLQDAARRRLLKLQQDQRE--MELRRLEDEIERKVQMRD-QEIAATAKDLEIRQlELEAQKRLyekdlttsQEAVAKEI 725
Cdd:pfam15558 89 VIEKESRWREQAEDQENQRQekLERARQEAEQRKQCQEQRlKEKEEELQALREQN-SLQLQERL--------EEACHKRQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 726 REDTDAHRRKAALEehmfQKLLENSQmggrrAQRVMEDNLAKAEQACLNADWQIQTLHKQ---KCADQQRSQGyydvatl 802
Cdd:pfam15558 160 LKEREEQKKVQENN----LSELLNHQ-----ARKVLVDCQAKAEELLRRLSLEQSLQRSQenyEQLVEERHRE------- 223
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1720383800 803 LRENRRKEVEVLN------AMMEEEAQKWKEA--EEKEFHLQSA 838
Cdd:pfam15558 224 LREKAQKEEEQFQrakwraEEKEEERQEHKEAlaELADRKIQQA 267
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
568-837 |
4.27e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 47.48 E-value: 4.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 568 TREWERIRNdeLDFLRERQtvENMQAEVDEQRAKDEAWYQKQELLRRAEETRREILlqeEEKMAQQRQRLAAVKRELEIK 647
Cdd:pfam01576 169 AEEEEKAKS--LSKLKNKH--EAMISDLEERLKKEEKGRQELEKAKRKLEGESTDL---QEQIAELQAQIAELRAQLAKK 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 648 EIHLQDAARR------RLLKLQQDQREME--LRRLEDEIERKVQMRDQeIAATAKDLEirqLELEAQKRLYEKDLTTS-- 717
Cdd:pfam01576 242 EEELQAALARleeetaQKNNALKKIRELEaqISELQEDLESERAARNK-AEKQRRDLG---EELEALKTELEDTLDTTaa 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 718 -QEAVAKEIREDTDAhrrKAALEEHMFQKLLENSQMGGRRAQRVME--DNLAKAEQACLNADWQIQTLHKQ----KCADQ 790
Cdd:pfam01576 318 qQELRSKREQEVTEL---KKALEEETRSHEAQLQEMRQKHTQALEEltEQLEQAKRNKANLEKAKQALESEnaelQAELR 394
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1720383800 791 QRSQGYYDVatllrENRRKEVEV----LNAMMEEEAQKWKEAEEKEFHLQS 837
Cdd:pfam01576 395 TLQQAKQDS-----EHKRKKLEGqlqeLQARLSESERQRAELAEKLSKLQS 440
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
582-832 |
5.87e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 47.27 E-value: 5.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 582 LRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEE---TRREIL------------LQEEEKMAQQRQRLAAVKRELEI 646
Cdd:TIGR00618 327 LMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEvatSIREIScqqhtltqhihtLQQQKTTLTQKLQSLCKELDILQ 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 647 KEIHLQDAARRRLLKLQQDqremeLRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEK-DLTTSQEAVAKEI 725
Cdd:TIGR00618 407 REQATIDTRTSAFRDLQGQ-----LAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSlKEREQQLQTKEQI 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 726 redTDAHRRKAALEEHMFQKLLEN--------------------SQMGGRRAQRVmEDNLAKAEQACLNADWQIQTLHKQ 785
Cdd:TIGR00618 482 ---HLQETRKKAVVLARLLELQEEpcplcgscihpnparqdidnPGPLTRRMQRG-EQTYAQLETSEEDVYHQLTSERKQ 557
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1720383800 786 KCADQQRSQGYYDVATLLRENRRKEVEVLNAM--MEEEAQKWKEAEEKE 832
Cdd:TIGR00618 558 RASLKEQMQEIQQSFSILTQCDNRSKEDIPNLqnITVRLQDLTEKLSEA 606
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
576-748 |
6.28e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 6.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 576 NDELDFLRERQTVENMQAEVDEQ----RAKDEAWYQKQELLRRAEETRREIllqeeekmAQQRQRLAAVKRELeikeihl 651
Cdd:COG4913 637 EAELDALQERREALQRLAEYSWDeidvASAEREIAELEAELERLDASSDDL--------AALEEQLEELEAEL------- 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 652 qDAARRRLLKLQQDQR--EMELRRLEDEIERKvqmrdQEIAATAKDLEIRQLELEAQKRLYEKDLTTSQEAVAKEIREDT 729
Cdd:COG4913 702 -EELEEELDELKGEIGrlEKELEQAEEELDEL-----QDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERI 775
|
170
....*....|....*....
gi 1720383800 730 DAHRRKAALEEHMFQKLLE 748
Cdd:COG4913 776 DALRARLNRAEEELERAMR 794
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
568-866 |
7.68e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 45.95 E-value: 7.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 568 TREWERIRNDELDflrerqtvenmQAEVDEQRAKDEAwyqkqellRRAEETRREILLQEEEKMAQQRQRLAAvkreLEIK 647
Cdd:PRK09510 61 VEQYNRQQQQQKS-----------AKRAEEQRKKKEQ--------QQAEELQQKQAAEQERLKQLEKERLAA----QEQK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 648 EihlQDAARRRLLKLQQDQREmelrrledeierkvqmrdqeiAATAKDLEIRQLELEAQ-KRLyekdlttsqEAVAKEIR 726
Cdd:PRK09510 118 K---QAEEAAKQAALKQKQAE---------------------EAAAKAAAAAKAKAEAEaKRA---------AAAAKKAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 727 EDTDAhrrKAALEEhmfqkllensqmggrrAQRVMEDNLAKAEQAClnadwqiqtlhKQKCADqqrsqgyydvatllrEN 806
Cdd:PRK09510 165 AEAKK---KAEAEA----------------AKKAAAEAKKKAEAEA-----------AAKAAA---------------EA 199
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 807 RRKEVEVLNAMMEEEAQKWKEAEEKEFHLQSAKKASALSDASRKWFLRQETSAALEHEEM 866
Cdd:PRK09510 200 KKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
583-711 |
7.71e-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: 43.88 E-value: 7.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 583 RERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELEIKEIHLQDAARRRLLKL 662
Cdd:pfam05672 19 KRRQAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQRKAEEEAEEREQREQEEQER 98
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1720383800 663 QQDQREMELRRLEDEIERKVQMRDQEIaatakdLEIRQLELEAQKRLYE 711
Cdd:pfam05672 99 LQKQKEEAEAKAREEAERQRQEREKIM------QQEEQERLERKKRIEE 141
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
565-740 |
9.64e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 9.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 565 DYQTREWERIRnDELDFLRErqtvenmqAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKREL 644
Cdd:COG4717 315 ELEEEELEELL-AALGLPPD--------LSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEE 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 645 EIKEIHLQDAARRRLLKlQQDQREMELRRLEDEIERKVQMRDQEiaatakDLEIRQLELEAQKRLYEKDLTTSQEAVA-- 722
Cdd:COG4717 386 ELRAALEQAEEYQELKE-ELEELEEQLEELLGELEELLEALDEE------ELEEELEELEEELEELEEELEELREELAel 458
|
170 180
....*....|....*....|..
gi 1720383800 723 ----KEIREDTDAHRRKAALEE 740
Cdd:COG4717 459 eaelEQLEEDGELAELLQELEE 480
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
592-726 |
1.05e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 45.86 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 592 QAEVDEQRAKDEAWYQKQELLRRAEET-------RREILLQEEEKMAQQRQRLAAVKRELEIKEIHLqdAARRRLLKLQQ 664
Cdd:PRK12705 41 EAQKEAEEKLEAALLEAKELLLRERNQqrqearrEREELQREEERLVQKEEQLDARAEKLDNLENQL--EEREKALSARE 118
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720383800 665 DQREMELRRLEDEIERKVQMRDQEiaatAKDLEIRQL--ELEAQK-RLYEKDLTTSQEAVAKEIR 726
Cdd:PRK12705 119 LELEELEKQLDNELYRVAGLTPEQ----ARKLLLKLLdaELEEEKaQRVKKIEEEADLEAERKAQ 179
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
567-850 |
1.19e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 567 QTREWERIRNDEldflrERQTVENMQAEVDEQRAKDE----AWYQKQELLRRAEETRREILLQEEEKM-AQQRQRLAAVK 641
Cdd:PTZ00121 1216 EARKAEDAKKAE-----AVKKAEEAKKDAEEAKKAEEernnEEIRKFEEARMAHFARRQAAIKAEEARkADELKKAEEKK 1290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 642 RELEIKEIHLQDAARRRLLKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEKDLTTSQEAV 721
Cdd:PTZ00121 1291 KADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAE 1370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 722 AK--EIREDTDAHRRKAAlEEHMFQKLLENSQMGGRRAqrvmeDNLAKAEQACLNADWQIQTLHKQKCADQQRSQGyydv 799
Cdd:PTZ00121 1371 KKkeEAKKKADAAKKKAE-EKKKADEAKKKAEEDKKKA-----DELKKAAAAKKKADEAKKKAEEKKKADEAKKKA---- 1440
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1720383800 800 atllrENRRKEVEVLNAmmEEEAQKWKEAEEKEFHLQSAKKASALSDASRK 850
Cdd:PTZ00121 1441 -----EEAKKADEAKKK--AEEAKKAEEAKKKAEEAKKADEAKKKAEEAKK 1484
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
623-838 |
1.22e-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: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 623 LLQEEEKMAQQRQRLAAVKRELEIKEIHLQDAARRRLLKLQQ----DQREMELRRLEDEIERKVQMRDQEIAATAKDLEI 698
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQlaalERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 699 RQLELEAQKRLYEKDLTTSQ-------EAVAKEIREDTDAHRRKAALEehmfqkllensQMGGRRAQRVMEDNLAKAEQA 771
Cdd:COG4942 95 LRAELEAQKEELAELLRALYrlgrqppLALLLSPEDFLDAVRRLQYLK-----------YLAPARREQAEELRADLAELA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720383800 772 CLNADWQIQTLHKQKCADQQRSQgyYDVATLLRENRRKEVEVLNAMMEEEAQKWKEAEEKEFHLQSA 838
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEE--RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
568-865 |
1.29e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 45.97 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 568 TREWERIRNDELdflrERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREI------LLQEEEKMAQQRQ------ 635
Cdd:NF041483 501 TAESERVRTEAI----ERATTLRRQAEETLERTRAEAERLRAEAEEQAEEVRAAAeraareLREETERAIAARQaeaaee 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 636 ----------RLAAVKREL----------------EIKEIHLQDAARRRLLklqQDQREMELRRLEDEIERKVQMRDQEI 689
Cdd:NF041483 577 ltrlhteaeeRLTAAEEALadaraeaerirreaaeETERLRTEAAERIRTL---QAQAEQEAERLRTEAAADASAARAEG 653
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 690 AATAKDL------EIRQLELEAQK---RLyEKDLTTSQEAVAKEIRE-----DTDAHRRKAALEEHMFQKLLENSQMGGr 755
Cdd:NF041483 654 ENVAVRLrseaaaEAERLKSEAQEsadRV-RAEAAAAAERVGTEAAEalaaaQEEAARRRREAEETLGSARAEADQERE- 731
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 756 RAQRVMEDNLAKAEQACLNADWQIQTLHKQK--------CADQQRSQGYYDVATLLRENRRKEVEVLNAMMEEEAQKWK- 826
Cdd:NF041483 732 RAREQSEELLASARKRVEEAQAEAQRLVEEAdrratelvSAAEQTAQQVRDSVAGLQEQAEEEIAGLRSAAEHAAERTRt 811
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1720383800 827 EAEEKEFHLQS---AKKASALSDASR-KWFLRQETSAALEHEE 865
Cdd:NF041483 812 EAQEEADRVRSdayAERERASEDANRlRREAQEETEAAKALAE 854
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
578-728 |
1.34e-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: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 578 ELDFLRERQtvENMQAEVDEQRAKDEAWYQKQELLRRA-EETRREILLQEEE------KMAQQRQRLAAVK--RELEI-- 646
Cdd:COG1579 18 ELDRLEHRL--KELPAELAELEDELAALEARLEAAKTElEDLEKEIKRLELEieeveaRIKKYEEQLGNVRnnKEYEAlq 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 647 KEIHLqdaarrrlLKLQQDQREMELRRLEDEIERKVQMRDQ---EIAATAKDLEIRQLELEAQKRLYEKD---LTTSQEA 720
Cdd:COG1579 96 KEIES--------LKRRISDLEDEILELMERIEELEEELAEleaELAELEAELEEKKAELDEELAELEAEleeLEAEREE 167
|
....*...
gi 1720383800 721 VAKEIRED 728
Cdd:COG1579 168 LAAKIPPE 175
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
563-769 |
1.37e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.83 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 563 IVDYQTREWERIRN--DELDFL-RERQTVENMQAEVD---EQRAKDEAWYQKQ--ELLRRAEETRREILLQEEEKMAQQR 634
Cdd:TIGR02169 728 LEQEEEKLKERLEEleEDLSSLeQEIENVKSELKELEariEELEEDLHKLEEAlnDLEARLSHSRIPEIQAELSKLEEEV 807
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 635 QRLAAVKRELEIKEihlqdaaRRRLLKLQQDQREM-ELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEaQKRLYEKD 713
Cdd:TIGR02169 808 SRIEARLREIEQKL-------NRLTLEKEYLEKEIqELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELE-ELEAALRD 879
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720383800 714 LTTSQEAVAKEiREDTDAHRRKA--ALEEHMFQKLLENSQMGGRRAQR-VMEDNLAKAE 769
Cdd:TIGR02169 880 LESRLGDLKKE-RDELEAQLRELerKIEELEAQIEKKRKRLSELKAKLeALEEELSEIE 937
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
592-729 |
1.55e-04 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 43.72 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 592 QAEVDEQRAKDEAwyqKQEllrrAEETRREILLQEEEKMAQQRQRLaavkrELEIKEihlqdaaRRRLLKLQQD---QRE 668
Cdd:pfam12072 31 SAEELAKRIIEEA---KKE----AETKKKEALLEAKEEIHKLRAEA-----ERELKE-------RRNELQRQERrllQKE 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720383800 669 MEL-RRLE--DEIERKVQMRDQEIAATAKDLEIRQLELEA-----QKRLYEKDLTTSQEA-------VAKEIREDT 729
Cdd:pfam12072 92 ETLdRKDEslEKKEESLEKKEKELEAQQQQLEEKEEELEElieeqRQELERISGLTSEEAkeilldeVEEELRHEA 167
|
|
| TBC |
smart00164 |
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and ... |
380-488 |
1.59e-04 |
|
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and Gyp7, thereby giving rise to the notion that it performs a GTP-activator activity on Rab-like GTPases.
Pssm-ID: 214540 [Multi-domain] Cd Length: 216 Bit Score: 43.83 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 380 AFP-FVKLFQNNQLIcFEVVATLIINWCQHWFEYFpnppinilsmienvLAFHDKELLQHFIDRDITSQVYAWPLLETLF 458
Cdd:smart00164 112 AFWcLVKLMERYGPN-FYLPDMSGLQLDLLQLDRL--------------VKEYDPDLYKHLKDLGITPSLYALRWFLTLF 176
|
90 100 110
....*....|....*....|....*....|
gi 1720383800 459 SEVLTREEWLRLFDNIFSNHPSFLLMTVVA 488
Cdd:smart00164 177 ARELPLEIVLRIWDVLFAEGSDFLFRVALA 206
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
569-737 |
1.83e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.31 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 569 REWERIRNDELDFLRERQTVEN-----MQAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRE 643
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAqleelEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 644 LEIKEIHLQDAARRRLLKLQQDQREMELRRLEDEIERKVQMRDQ----------------------EIAATAKDLEIRQL 701
Cdd:COG1196 459 EALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADyegflegvkaalllaglrglagAVAVLIGVEAAYEA 538
|
170 180 190
....*....|....*....|....*....|....*.
gi 1720383800 702 ELEAQKRLYEKDLTTSQEAVAKEIREDTDAHRRKAA 737
Cdd:COG1196 539 ALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRA 574
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
570-687 |
1.96e-04 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 42.72 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 570 EWERIRNDELdflRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEEKMA-QQRQRLAAVKRELEike 648
Cdd:pfam05672 39 EEERLRKEEL---RRRAEEERARREEEARRLEEERRREEEERQRKAEEEAEEREQREQEEQErLQKQKEEAEAKARE--- 112
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1720383800 649 ihlqDAARRRLLKLQQDQREMELR-----RLEdEIERKVQMRDQ 687
Cdd:pfam05672 113 ----EAERQRQEREKIMQQEEQERlerkkRIE-EIMKRTRKSDQ 151
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
569-748 |
2.14e-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: 44.52 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 569 REWERIRNDELD-----FLRERQ-TVENMQAEVDEQRAKDEAWYQK----QELLRRAEETRREIL--LQEEEKMAQQRQR 636
Cdd:pfam13868 143 KELEKEEEREEDerileYLKEKAeREEEREAEREEIEEEKEREIARlraqQEKAQDEKAERDELRakLYQEEQERKERQK 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 637 LaavkRELEIKEIHLQDA---ARRRLLKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEKD 713
Cdd:pfam13868 223 E----REEAEKKARQRQElqqAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQ 298
|
170 180 190
....*....|....*....|....*....|....*
gi 1720383800 714 LTTSQEAVAKEIREDTDAHRRKAALEEHMFQKLLE 748
Cdd:pfam13868 299 IEEREEQRAAEREEELEEGERLREEEAERRERIEE 333
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
609-843 |
2.42e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 45.18 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 609 QELLRRAEETRReiLLQEEEKMAQQRQRL-AAVKRELEIKEiHLQDAARrrllklQQDQREMELRRLEDEIERKVQMRDQ 687
Cdd:PRK10246 558 KQLQRDESEAQS--LRQEEQALTQQWQAVcASLNITLQPQD-DIQPWLD------AQEEHERQLRLLSQRHELQGQIAAH 628
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 688 E--IAATAKDLEIRQLELEAQKRLY------EKDLTTSQEAVAKEIREDTDAHRRKAALEEHMFQ-----KLLENSQMGG 754
Cdd:PRK10246 629 NqqIIQYQQQIEQRQQQLLTALAGYaltlpqEDEEASWLATRQQEAQSWQQRQNELTALQNRIQQltpllETLPQSDDLP 708
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 755 RRAQRVMEDNLAKAEQACLNADWQIQTLHKQKCADQQR-SQGYYDVATLLRENRRKEVEV-LNAMMEEEAQKWKEAEEK- 831
Cdd:PRK10246 709 HSEETVALDNWRQVHEQCLSLHSQLQTLQQQDVLEAQRlQKAQAQFDTALQASVFDDQQAfLAALLDEETLTQLEQLKQn 788
|
250
....*....|...
gi 1720383800 832 -EFHLQSAKKASA 843
Cdd:PRK10246 789 lENQRQQAQTLVT 801
|
|
| EVC2_like |
pfam12297 |
Ellis van Creveld protein 2 like protein; This family of proteins is found in eukaryotes. ... |
568-752 |
3.00e-04 |
|
Ellis van Creveld protein 2 like protein; This family of proteins is found in eukaryotes. Proteins in this family are typically between 571 and 1310 amino acids in length. There are two conserved sequence motifs: LPA and ELH. EVC2 is implicated in Ellis van Creveld chondrodysplastic dwarfism in humans. Mutations in this protein can give rise to this congenital condition. LIMBIN is a protein which shares around 80% sequence homology with EVC2 and it is implicated in a similar condition in bovine chondrodysplastic dwarfism.
Pssm-ID: 463525 [Multi-domain] Cd Length: 428 Bit Score: 44.30 E-value: 3.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 568 TREWERIRNDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQELLRR-----AEETRREILLQEEEKMAQQRQRLaAVKR 642
Cdd:pfam12297 223 AAECNLETREKMEAQHQREMAEKEEAEELLKHADEQEALECSSLLDKlhkleQEHLQRSLLLRQEEDFAKAQRQL-AVFQ 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 643 ELEIKEI---HLQDAARRRLLKLQQDQREM-ELRRLEDEIERkvqMRDQEIAATAKDLEIR--QLE-----LEAQKRLYE 711
Cdd:pfam12297 302 RVELHKIfftQLKEATRKGELKPEAAKRLLqDYSKIQEQIEE---LMDFFQANQRYHLSERfaQREylvqsLQSLETRVS 378
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1720383800 712 KDLTTSQEAVAKEIREdtdaHRRKAALEEHMFQKLLENSQM 752
Cdd:pfam12297 379 GLLNTAATQLTSLIQK----MERAGYLDEEQMEMLLERAQK 415
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
581-772 |
3.93e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.93 E-value: 3.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 581 FLRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREillqeeekMAQQRQRLAAVKRELEIKEihlqdaarRRLL 660
Cdd:PRK12705 24 LLKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRE--------RNQQRQEARREREELQREE--------ERLV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 661 KL--QQDQREMELRRLEDEIERkvqmRDQEIAATAKDLEIRQLELEAqkRLYEKDLTTSQEAVAKEIRE-DTDAHRRKAA 737
Cdd:PRK12705 88 QKeeQLDARAEKLDNLENQLEE----REKALSARELELEELEKQLDN--ELYRVAGLTPEQARKLLLKLlDAELEEEKAQ 161
|
170 180 190
....*....|....*....|....*....|....*
gi 1720383800 738 LEEHMFQKLLENSQmggRRAQrvmeDNLAKAEQAC 772
Cdd:PRK12705 162 RVKKIEEEADLEAE---RKAQ----NILAQAMQRI 189
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
576-720 |
4.78e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.85 E-value: 4.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 576 NDELDFLRER-QTVENMQAEVDEQRAKDEAWYQK-QELLRRAEETRREI------------LLQEEEKMAQQRQRL---- 637
Cdd:COG3206 211 SEEAKLLLQQlSELESQLAEARAELAEAEARLAAlRAQLGSGPDALPELlqspviqqlraqLAELEAELAELSARYtpnh 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 638 ---AAVKRELEIKEIHLQDAARRRLLKLQQD-----QREMELRRLEDEIERKVQmrdqEIAATAKDLEIRQLELEAQKRL 709
Cdd:COG3206 291 pdvIALRAQIAALRAQLQQEAQRILASLEAElealqAREASLQAQLAQLEARLA----ELPELEAELRRLEREVEVAREL 366
|
170
....*....|.
gi 1720383800 710 YEKDLTTSQEA 720
Cdd:COG3206 367 YESLLQRLEEA 377
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
598-752 |
4.86e-04 |
|
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 198 and 469 amino acids in length. There are two completely conserved L residues that may be functionally important.
Pssm-ID: 405647 [Multi-domain] Cd Length: 206 Bit Score: 42.45 E-value: 4.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 598 QRAKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLaaVKRELEIKEIHLQDAARRRLLKLQQDQrEMELRRLEDE 677
Cdd:pfam14988 17 QKKIEKLWNQYVQECEEIERRRQELASRYTQQTAELQTQL--LQKEKEQASLKKELQALRPFAKLKESQ-EREIQDLEEE 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720383800 678 IeRKVQmrdQEIAATAKDLEIRQLELEA--QKRLYEKDLTTSQEAVAKEIREDTDAHRRKA--ALEEHMFQKLLENSQM 752
Cdd:pfam14988 94 K-EKVR---AETAEKDREAHLQFLKEKAllEKQLQELRILELGERATRELKRKAQALKLAAkqALSEFCRSIKRENRQL 168
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
576-862 |
4.96e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 4.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 576 NDELDFLRER-QTVENMQAEVDEQRAKDEAWYQKQellRRAEETRREILLQEEEKMAQQRQRLAAVKRELEIKEIHLQDA 654
Cdd:PRK02224 341 NEEAESLREDaDDLEERAEELREEAAELESELEEA---REAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEEL 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 655 ARRR-LLKLQQDQREMELRRLEDEIERKVQMR-------------DQEIAATAKD-------LEIRQLELEAQKRLYEKD 713
Cdd:PRK02224 418 REERdELREREAELEATLRTARERVEEAEALLeagkcpecgqpveGSPHVETIEEdrerveeLEAELEDLEEEVEEVEER 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 714 LTTSQEAVAKEIREDTDAHRRKAA---LEEHMFQKLLENSQMGGRRAQ--------RVMEDNLAKAEQACLNADWQIQTL 782
Cdd:PRK02224 498 LERAEDLVEAEDRIERLEERREDLeelIAERRETIEEKRERAEELRERaaeleaeaEEKREAAAEAEEEAEEAREEVAEL 577
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 783 HKQKCADQQRSQGYYDVATLL---------RENRRKEVEVLNAMMEEEAQKWKEAEEKEFHLQSAKKASALSDASRKwfl 853
Cdd:PRK02224 578 NSKLAELKERIESLERIRTLLaaiadaedeIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARIEEARED--- 654
|
....*....
gi 1720383800 854 RQETSAALE 862
Cdd:PRK02224 655 KERAEEYLE 663
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
579-751 |
5.87e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.85 E-value: 5.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 579 LDFLRERqtVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREI---------LLQEEEKMAQQRQRLAAVKRELEIKEI 649
Cdd:COG3206 177 LEFLEEQ--LPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLqqlselesqLAEARAELAEAEARLAALRAQLGSGPD 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 650 HLQDAA--------RRRLLKLQQDQREM---------ELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEK 712
Cdd:COG3206 255 ALPELLqspviqqlRAQLAELEAELAELsarytpnhpDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQA 334
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1720383800 713 DLTTSQEAVAK--EIREDTDAHRRKAALEEHMFQKLLENSQ 751
Cdd:COG3206 335 QLAQLEARLAElpELEAELRRLEREVEVARELYESLLQRLE 375
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
576-681 |
6.07e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 43.32 E-value: 6.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 576 NDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAavKRELEIKEIHLQDAA 655
Cdd:pfam02029 211 NGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEQKLEELRRRRQEKESEEFEKLRQKQQ--EAELELEELKKKREE 288
|
90 100 110
....*....|....*....|....*....|....*..
gi 1720383800 656 RRRLLKLQQDQR-----------EMELRRLEDEIERK 681
Cdd:pfam02029 289 RRKLLEEEEQRRkqeeaerklreEEEKRRMKEEIERR 325
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
581-689 |
6.61e-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: 42.66 E-value: 6.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 581 FLRERQTVENM-----QAEVDEQRAKdEAWYQKQELLRRAEETRREILLQEEEKMAQQRQR----LAAVKRELEIKEIHL 651
Cdd:pfam02841 181 FLQSKEAVEEAilqtdQALTAKEKAI-EAERAKAEAAEAEQELLREKQKEEEQMMEAQERSyqehVKQLIEKMEAEREQL 259
|
90 100 110
....*....|....*....|....*....|....*...
gi 1720383800 652 QDAARRRLLKLQQDQREMelrrLEDEIERKVQMRDQEI 689
Cdd:pfam02841 260 LAEQERMLEHKLQEQEEL----LKEGFKTEAESLQKEI 293
|
|
| Pinin_SDK_memA |
pfam04696 |
pinin/SDK/memA/ protein conserved region; Members of this family have very varied ... |
598-688 |
6.98e-04 |
|
pinin/SDK/memA/ protein conserved region; Members of this family have very varied localizations within the eukaryotic cell. pinin is known to localize at the desmosomes and is implicated in anchoring intermediate filaments to the desmosomal plaque. SDK2/3 is a dynamically localized nuclear protein thought to be involved in modulation of alternative pre-mRNA splicing. memA is a tumour marker preferentially expressed in human melanoma cell lines. A common feature of the members of this family is that they may all participate in regulating protein-protein interactions.
Pssm-ID: 461396 [Multi-domain] Cd Length: 130 Bit Score: 40.74 E-value: 6.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 598 QRAKDEAWYQKQELLRRAEETRREillqeEEKMAQQRQRLAAVKREleikeihlqdaaRRRLLKLQQDQREMELRRLEDE 677
Cdd:pfam04696 19 QKFKKEESKQKEKEERRAEIEKRL-----EEKAKQEKEELEERKRE------------EREELFEERRAEQIELRALEEK 81
|
90
....*....|.
gi 1720383800 678 IERKVQMRDQE 688
Cdd:pfam04696 82 LELKELMETWH 92
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
567-730 |
8.14e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.52 E-value: 8.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 567 QTREWERIRND---ELDFLR-ERQTVENMQAEVDEQRAK-----DEAWYQKQELLRRAEETRREI--LLQEEEKMAQQRQ 635
Cdd:TIGR02169 813 RLREIEQKLNRltlEKEYLEkEIQELQEQRIDLKEQIKSiekeiENLNGKKEELEEELEELEAALrdLESRLGDLKKERD 892
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 636 RLAAVKRELEIK--EIHLQDAARRRLLKLQQDQREM---ELRRLEDEI------------ERKVQMRDQEIAATAKDLE- 697
Cdd:TIGR02169 893 ELEAQLRELERKieELEAQIEKKRKRLSELKAKLEAleeELSEIEDPKgedeeipeeelsLEDVQAELQRVEEEIRALEp 972
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1720383800 698 -----IRQLElEAQKRL--YEKDLTTSQEAvAKEIREDTD 730
Cdd:TIGR02169 973 vnmlaIQEYE-EVLKRLdeLKEKRAKLEEE-RKAILERIE 1010
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
596-819 |
8.36e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 8.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 596 DEQRAKDEAWY-------QKQELLRRAEETRREIllqeeEKMAQQRQRLAAVKRELEIKEIHLQDAARRRLLKLQQDQRE 668
Cdd:COG4913 593 DDRRRIRSRYVlgfdnraKLAALEAELAELEEEL-----AEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAE 667
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 669 MELRRLEDEIERkvqmrdqeIAATAKDLEirqlELEAQKRLYEKDLTTSQEAVAKEIREDTDAHRRKAALEEhmfqkLLE 748
Cdd:COG4913 668 REIAELEAELER--------LDASSDDLA----ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEE-----ELD 730
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720383800 749 NSQmggrRAQRVMEDNLAKAEQACLNADWqiQTLHKQKCADQQRSQGYYDVATLLRENRRKEVEVLNAMME 819
Cdd:COG4913 731 ELQ----DRLEAAEDLARLELRALLEERF--AAALGDAVERELRENLEERIDALRARLNRAEEELERAMRA 795
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
567-846 |
9.00e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 43.10 E-value: 9.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 567 QTREWERIRNDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQEllRRAEETRREILLQEEEKMAQQRQRLAAVKRELEI 646
Cdd:COG3064 11 EAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAE--EEAREAKAEAEQRAAELAAEAAKKLAEAEKAAAE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 647 KEIHLQDAARRRLLKLQQDQREmelrrledeiERKVQMRDQEIAATAKDLEIRQLELEAQKrlyEKDLTTSQEAVAKEIR 726
Cdd:COG3064 89 AEKKAAAEKAKAAKEAEAAAAA----------EKAAAAAEKEKAEEAKRKAEEEAKRKAEE---ERKAAEAEAAAKAEAE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 727 EDTDAHRRKAALEEHMFQKLLENSQMGGRRAQRVMEDNLAKAEQACLNADWQIQTLHKQKCADQQRSQGYYDVATLLREN 806
Cdd:COG3064 156 AARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALA 235
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1720383800 807 RRKEVEVLNAMMEEEAQKWKEAEEKEFHLQSAKKASALSD 846
Cdd:COG3064 236 AVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALS 275
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
1-32 |
9.27e-04 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 37.71 E-value: 9.27e-04
10 20 30
....*....|....*....|....*....|...
gi 1720383800 1 MRGHESSVCSISVHASGRYAITTSSD-TAQLWD 32
Cdd:pfam00400 7 LEGHTGSVTSLAFSPDGKLLASGSDDgTVKVWD 39
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
585-832 |
9.59e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 9.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 585 RQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELEIKEIHLQDAARRRLlklQQ 664
Cdd:COG4372 51 REELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQ---DL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 665 DQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEKDLTTSQEAVAKEIREDtdaHRRKAALEEHMFQ 744
Cdd:COG4372 128 EQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKE---ANRNAEKEEELAE 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 745 KLLENSQMGGRRAQRVMEDNLAKAEQACLNADwQIQTLHKQKCADQQRSQGYYDVATLLRENRRKEVEVLNAMMEEEAQK 824
Cdd:COG4372 205 AEKLIESLPRELAEELLEAKDSLEAKLGLALS-ALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAAL 283
|
....*...
gi 1720383800 825 WKEAEEKE 832
Cdd:COG4372 284 ELEALEEA 291
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
563-708 |
9.98e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.00 E-value: 9.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 563 IVDYQTREWERIRNDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEEKmAQQRQRLAAVKR 642
Cdd:COG1196 623 LGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLA-EEELELEEALLA 701
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720383800 643 ELEIKEIHLQDAARRRLLKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKR 708
Cdd:COG1196 702 EEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELER 767
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
572-714 |
1.14e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 572 ERIRNDELDFLRERQTVENMQAEVDEQRAKDEawyQKQELLRRAEEtrREILLQEEEKMAQQRQRLAavKRELEIKEIHl 651
Cdd:COG1579 48 EAAKTELEDLEKEIKRLELEIEEVEARIKKYE---EQLGNVRNNKE--YEALQKEIESLKRRISDLE--DEILELMERI- 119
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720383800 652 qDAARRRLLKLQQdqremELRRLEDEIERKVQMRDQEIAATAKDLEirqlELEAQKRLYEKDL 714
Cdd:COG1579 120 -EELEEELAELEA-----ELAELEAELEEKKAELDEELAELEAELE----ELEAEREELAAKI 172
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
582-886 |
1.19e-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: 43.02 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 582 LRERQTVENMQAEVDEQRAKdeawyqkqelLRRAEETRREilLQEEEKMAQQRQRLAavkrELEIKEIHLQDAARRRLLK 661
Cdd:COG3096 343 LRQQEKIERYQEDLEELTER----------LEEQEEVVEE--AAEQLAEAEARLEAA----EEEVDSLKSQLADYQQALD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 662 LQQD---QREMELRRLE--------DEI------ERKVQMRDQEIAATAKDLEIRQ-LEL-EAQKRLYEKDL-------- 714
Cdd:COG3096 407 VQQTraiQYQQAVQALEkaralcglPDLtpenaeDYLAAFRAKEQQATEEVLELEQkLSVaDAARRQFEKAYelvckiag 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 715 -TTSQEA--VAKEIREDTDAHRRKAALEEHMFQKL-----LENSQmggRRAQRVMEDnLAKAEQACLNADWQIQTLHKQK 786
Cdd:COG3096 487 eVERSQAwqTARELLRRYRSQQALAQRLQQLRAQLaeleqRLRQQ---QNAERLLEE-FCQRIGQQLDAAEELEELLAEL 562
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 787 CADQQRSQGYYDVATLLRENRRKEVEVLNAMMEEEAQK---WKEAEEKEFHL-----QSAKKASALSDAsRKWFLRQETS 858
Cdd:COG3096 563 EAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARapaWLAAQDALERLreqsgEALADSQEVTAA-MQQLLERERE 641
|
330 340
....*....|....*....|....*...
gi 1720383800 859 AALEHEEMPwLQRQYMDSaylpQTSRLH 886
Cdd:COG3096 642 ATVERDELA-ARKQALES----QIERLS 664
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
575-708 |
1.29e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 42.32 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 575 RNDELDFLRER-----QTVENMQAEVDE-----QRAKDEAWYQKQELLRRAEETRR-----EILLQEEEKMAQ-QR---- 634
Cdd:pfam05667 333 REEELEELQEQledleSSIQELEKEIKKlessiKQVEEELEELKEQNEELEKQYKVkkktlDLLPDAEENIAKlQAlvda 412
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720383800 635 --QRLAAVKRELEIKEIHLQDAARRrlLKLQQDQREMELRRLEDEIER-KVQMRDQEIAATAKDLEIRQLELEAQKR 708
Cdd:pfam05667 413 saQRLVELAGQWEKHRVPLIEEYRA--LKEAKSNKEDESQRKLEEIKElREKIKEVAEEAKQKEELYKQLVAEYERL 487
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
574-866 |
1.34e-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: 42.64 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 574 IRNDELDFLRERQTVENMQAEVD------EQRA--KDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELE 645
Cdd:COG5185 231 IEEALKGFQDPESELEDLAQTSDkleklvEQNTdlRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKA 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 646 IKEIHLQDAARRRLLKLQQDQRE--MELRRLEDEIERKVqmRDQEIAATAKDLEIRQLELEAQKRLYEKDL---TTSQEA 720
Cdd:COG5185 311 TESLEEQLAAAEAEQELEESKREteTGIQNLTAEIEQGQ--ESLTENLEAIKEEIENIVGEVELSKSSEELdsfKDTIES 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 721 VAKEIREDTDAHRRKA-----ALEEHMFQKLLENSQMGG--RRAQRVMED--NLAKAEQACLNadwQIQTLHKQKcADQQ 791
Cdd:COG5185 389 TKESLDEIPQNQRGYAqeilaTLEDTLKAADRQIEELQRqiEQATSSNEEvsKLLNELISELN---KVMREADEE-SQSR 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 792 RSQGYYDVATLLRENRRKEVEVLNaMMEEEAQKWKEAEEK-----EFHLQSAKKASALSDASRKWFLRQETSAALEHEEM 866
Cdd:COG5185 465 LEEAYDEINRSVRSKKEDLNEELT-QIESRVSTLKATLEKlraklERQLEGVRSKLDQVAESLKDFMRARGYAHILALEN 543
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
572-741 |
1.46e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 572 ERIRNDELDFLRER-QTVENMQAEVDEQRAKDEAWYQKQELLRRAEEtRREILLQEEEKMAQQRQRLAAVKRELEIKEIH 650
Cdd:COG4717 49 ERLEKEADELFKPQgRKPELNLKELKELEEELKEAEEKEEEYAELQE-ELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 651 LQDAARRRLLKLQQDQREMELRRLEDEIERKVQMRDQeiaatakdleIRQLELEAQK------RLYEKDLTTSQEAVAKE 724
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEERLEELRELEEE----------LEELEAELAElqeeleELLEQLSLATEEELQDL 197
|
170
....*....|....*..
gi 1720383800 725 IREDTDAHRRKAALEEH 741
Cdd:COG4717 198 AEELEELQQRLAELEEE 214
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
1-32 |
1.73e-03 |
|
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: 36.91 E-value: 1.73e-03
10 20 30
....*....|....*....|....*....|...
gi 1720383800 1 MRGHESSVCSISVHASGRYAITTSSD-TAQLWD 32
Cdd:smart00320 8 LKGHTGPVTSVAFSPDGKYLASGSDDgTIKLWD 40
|
|
| Nop53 |
pfam07767 |
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ... |
593-712 |
1.95e-03 |
|
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ribosomal biogenesis. They are specifically involved in the processing beyond the 27S stage of 25S rRNA maturation. This family contains sequences that bear similarity to the glioma tumour suppressor candidate region gene 2 protein (p60). This protein has been found to interact with herpes simplex type 1 regulatory proteins.
Pssm-ID: 462259 [Multi-domain] Cd Length: 353 Bit Score: 41.51 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 593 AEVDEQRAKDEAwyQKQELLRRAEETRREILLQEEEKMAQQrQRLAAVKRELEIKEihlqdAARRRLLKLQQDQremeLR 672
Cdd:pfam07767 205 VEAEKKRLKEEE--KLERVLEKIAESAATAEAREEKRKTKA-QRNKEKRRKEEERE-----AKEEKALKKKLAQ----LE 272
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1720383800 673 RLEdEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEK 712
Cdd:pfam07767 273 RLK-EIAKEIAEKEKEREEKAEARKREKRKKKKEEKKLRP 311
|
|
| Fibrinogen_BP |
pfam08017 |
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family ... |
592-795 |
1.97e-03 |
|
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: 41.77 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 592 QAEVDEQRAKDEAWYQKQELLRRAEetrREILLQEEEKMAQQRQRLAAVKRELEIKEIHLQDAARRRLLK-LQQDQREME 670
Cdd:pfam08017 27 QGNVLERRQRDAENRSQGNVLERRQ---RDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNvLERRQRDAE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 671 LRRLEDEIERKvqMRDQEIAATAKDLEIRQLELEAQkrlyekdlttSQEAVAKEIREDTDAHRRKAALEEHmfQKLLENS 750
Cdd:pfam08017 104 NRSQGNVLERR--QRDAENKSQGNVLERRQRDAENR----------SQGNVLERRQRDAENRSQGNVLERR--QRDAENR 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1720383800 751 QMGG--RRAQRVMED----NLAKAEQACLNADWQIQTLHKQKCADQQRSQG 795
Cdd:pfam08017 170 SQGNvlERRQRDAENksqgNVLERRQRDAENRSQGNVLERRQRDAENRSQG 220
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
586-727 |
2.16e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.77 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 586 QTVENMQAEVDEQRAKDEAwyQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELEiKEIHLQDAARRRL---LKL 662
Cdd:COG2433 376 LSIEEALEELIEKELPEEE--PEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELE-AELEEKDERIERLereLSE 452
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720383800 663 QQDQREMELRRledeiERKVQMRDQEIAATAKDLE-----IRQLE--LEAQKRLYEKDLttSQEAVA-KEIRE 727
Cdd:COG2433 453 ARSEERREIRK-----DREISRLDREIERLERELEeererIEELKrkLERLKELWKLEH--SGELVPvKVVEK 518
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
594-748 |
2.29e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 594 EVDEQRAKDEAWYQKQELLRRAE---ETRREILLQEEEKMAQQRQRLAAVKRELEIKEIHLQDA-----------ARRRL 659
Cdd:PRK03918 589 ELEERLKELEPFYNEYLELKDAEkelEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELekkyseeeyeeLREEY 668
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 660 LKLqqdqrEMELRRLEDEIERKVQMRDqEIAATAKDLEiRQLELEAQKRLYEKDLTTSQEAVaKEIREDTdaHRRKAALE 739
Cdd:PRK03918 669 LEL-----SRELAGLRAELEELEKRRE-EIKKTLEKLK-EELEEREKAKKELEKLEKALERV-EELREKV--KKYKALLK 738
|
....*....
gi 1720383800 740 EHMFQKLLE 748
Cdd:PRK03918 739 ERALSKVGE 747
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
569-852 |
2.32e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.88 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 569 REWERIRNDELDFLRERQTVENMQAEVDEQRAKDEAwYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELEIKE 648
Cdd:TIGR00618 615 HALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHA-LQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLT 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 649 IHLQDAARRRLLKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEKDLTTSQEAVAKE--IR 726
Cdd:TIGR00618 694 YWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEvtAA 773
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 727 EDTDAHRRKAALEEHMFQKLLEnsqmggrraQRVMEDNLAKAE-QACLNADWQIQTLhkqkcADQQRSQGYYDVATLLRE 805
Cdd:TIGR00618 774 LQTGAELSHLAAEIQFFNRLRE---------EDTHLLKTLEAEiGQEIPSDEDILNL-----QCETLVQEEEQFLSRLEE 839
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1720383800 806 NRRKEVEVlnammeeeAQKWKEAEEKEFHLQSAKKASA-LSDASRKWF 852
Cdd:TIGR00618 840 KSATLGEI--------THQLLKYEECSKQLAQLTQEQAkIIQLSDKLN 879
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
594-841 |
2.47e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.56 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 594 EVDEQR-----AKDEAwyqkQELLRRAEETRREILLQEEEkMAQQRQRLAAVKRELEIKEIHLQDaARRRLLKLQQDQRE 668
Cdd:PRK02224 224 RYEEQReqareTRDEA----DEVLEEHEERREELETLEAE-IEDLRETIAETEREREELAEEVRD-LRERLEELEEERDD 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 669 M----ELRRLEDEI---------ERKVQMRD----QEIAAT------------AKDLEIRQLELEAQKRLYEKDLTTSQE 719
Cdd:PRK02224 298 LlaeaGLDDADAEAvearreeleDRDEELRDrleeCRVAAQahneeaeslredADDLEERAEELREEAAELESELEEARE 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 720 AVAK------EIREDTDAHRRKAA--------LEEHMFQKLLENSQMGGRRAQ-----RVMEDNLAKAEqaclnadwqiQ 780
Cdd:PRK02224 378 AVEDrreeieELEEEIEELRERFGdapvdlgnAEDFLEELREERDELREREAEleatlRTARERVEEAE----------A 447
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720383800 781 TLHKQKCAD-QQRSQGYYDVATLlrENRRKEVEVLNAMMEEEAQKWKEAEEKEFHLQSAKKA 841
Cdd:PRK02224 448 LLEAGKCPEcGQPVEGSPHVETI--EEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEA 507
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
657-770 |
2.62e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.68 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 657 RRLLKLQQ-DQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLE---LEAQKRLYEKDLTTSQEAVA---------- 722
Cdd:COG1579 7 RALLDLQElDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTEledLEKEIKRLELEIEEVEARIKkyeeqlgnvr 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1720383800 723 --KEI----REDTDAHRRKAALEEHMFQKLLENSQMggRRAQRVMEDNLAKAEQ 770
Cdd:COG1579 87 nnKEYealqKEIESLKRRISDLEDEILELMERIEEL--EEELAELEAELAELEA 138
|
|
| DUF4200 |
pfam13863 |
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ... |
619-712 |
2.77e-03 |
|
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.
Pssm-ID: 464003 [Multi-domain] Cd Length: 119 Bit Score: 38.70 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 619 RREI-LLQEE-----EKMAQQRQRLAAVKRELEIKEIHLQDAARR--RLLKLQQDQREMELRRLEDEIERKVQmRDQEIA 690
Cdd:pfam13863 5 KREMfLVQLAldakrEEIERLEELLKQREEELEKKEQELKEDLIKfdKFLKENDAKRRRALKKAEEETKLKKE-KEKEIK 83
|
90 100
....*....|....*....|..
gi 1720383800 691 ATAKDLEIRQLELEAQKRLYEK 712
Cdd:pfam13863 84 KLTAQIEELKSEISKLEEKLEE 105
|
|
| DegS |
pfam05384 |
Sensor protein DegS; This is small family of Bacillus DegS proteins. The DegS-DegU ... |
587-682 |
3.08e-03 |
|
Sensor protein DegS; This is small family of Bacillus DegS proteins. The DegS-DegU two-component regulatory system of Bacillus subtilis controls various processes that characterize the transition from the exponential to the stationary growth phase, including the induction of extracellular degradative enzymes, expression of late competence genes and down-regulation of the sigma D regulon. The family also contains one sequence Swiss:Q8R9D3 from Thermoanaerobacter tengcongensis which are described as sensory transduction histidine kinases.
Pssm-ID: 428449 [Multi-domain] Cd Length: 159 Bit Score: 39.39 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 587 TVENMQAEVDE--QRAKDEAWYQKQELlrraEETRREIL--------LQEEEKMAqqRQRLAAVKR------ELEIKEIH 650
Cdd:pfam05384 10 TIENSKEEIFEiaENARQEYERLKQEL----EELKEEVSetikevdkLEKKERRA--RQRLMEVSRdfnrysEEDIKEAY 83
|
90 100 110
....*....|....*....|....*....|...
gi 1720383800 651 LQ-DAARRRLLKLQQdqREMELRRLEDEIERKV 682
Cdd:pfam05384 84 EEaKDLQVELALLRE--REKQLRERRDELERRL 114
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
614-744 |
3.21e-03 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 39.25 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 614 RAEETRReiLLQEEEKMA-QQRQRLAAVKRELEIKEIHLQDAARRRLLKLQQDQREmELRRLEDeiERKVQMRDQEIAAT 692
Cdd:pfam05672 8 DAEEAAR--ILAEKRRQArEQREREEQERLEKEEEERLRKEELRRRAEEERARREE-EARRLEE--ERRREEEERQRKAE 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1720383800 693 AKDLEIRQLELEAQKRLYEKdlttSQEAVAKEiREdtDAHRRKAALEEHMFQ 744
Cdd:pfam05672 83 EEAEEREQREQEEQERLQKQ----KEEAEAKA-RE--EAERQRQEREKIMQQ 127
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
578-836 |
3.58e-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: 3.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 578 ELDFLRErQTVENMQAEVDEQRAKDEAwyQKQELLRRAEETRREilLQEE-EKMAQQRQRLAAVKRELEIKEIHLQDAAR 656
Cdd:pfam01576 320 ELRSKRE-QEVTELKKALEEETRSHEA--QLQEMRQKHTQALEE--LTEQlEQAKRNKANLEKAKQALESENAELQAELR 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 657 rrllKLQQDQREMELRRledeieRKVQMRDQEIAATAKDLEIRQLELE--AQKRLYEKDLTTS--QEAVAKEIREDTDA- 731
Cdd:pfam01576 395 ----TLQQAKQDSEHKR------KKLEGQLQELQARLSESERQRAELAekLSKLQSELESVSSllNEAEGKNIKLSKDVs 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 732 ------HRRKAALEEHMFQKLLENSQMGGRRAQRV-MEDNLAKAEQACLNADWQIQTLHKQKCADQQRSQGYYDVATLLR 804
Cdd:pfam01576 465 slesqlQDTQELLQEETRQKLNLSTRLRQLEDERNsLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALE 544
|
250 260 270
....*....|....*....|....*....|....*
gi 1720383800 805 ENRRK---EVEVLNAMMEEEAQKWKEAEEKEFHLQ 836
Cdd:pfam01576 545 EGKKRlqrELEALTQQLEEKAAAYDKLEKTKNRLQ 579
|
|
| G_path_suppress |
pfam15991 |
G-protein pathway suppressor; This family of proteins inhibits G-protein- and ... |
583-669 |
3.58e-03 |
|
G-protein pathway suppressor; This family of proteins inhibits G-protein- and mitogen-activated protein kinase-mediated signal transduction.
Pssm-ID: 464961 [Multi-domain] Cd Length: 272 Bit Score: 40.29 E-value: 3.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 583 RERQTVEnMQAEVDEQRAKDEAWYQKQELLRRAEETRREIlLQEEEKMAQQRQRlaavKREL--EIKEIHLQDAARRRLL 660
Cdd:pfam15991 22 RERKKQE-QEAKMEEERLRREREEREKEDRMTLEETKEQI-LKLEKKLADLKEE----KHQLflQLKKVLHEDETRKRQL 95
|
....*....
gi 1720383800 661 KLQQDQREM 669
Cdd:pfam15991 96 KEQSELFAL 104
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
617-850 |
3.73e-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: 41.11 E-value: 3.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 617 ETRREILLQEEEKMAQQRQRLAAVKRELEIKEIHLQdaaRRRLLKlQQDQREMELRRLEDEIERKVQMRDQE-----IAA 691
Cdd:TIGR00618 222 QVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLK---KQQLLK-QLRARIEELRAQEAVLEETQERINRArkaapLAA 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 692 TAKDL-EIRQ------LELEAQKRLYEKDLTTSQEAVAKE--IREDTDAHRRKAALEEHMFQkllENSQMGGRRAQRVME 762
Cdd:TIGR00618 298 HIKAVtQIEQqaqrihTELQSKMRSRAKLLMKRAAHVKQQssIEEQRRLLQTLHSQEIHIRD---AHEVATSIREISCQQ 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 763 DNLA---KAEQACLNADWQIQTLHKQKCADQQRSQGyyDVATLLRENRRKEVEVLNAMMEEEAQKwKEAEEKEFH----L 835
Cdd:TIGR00618 375 HTLTqhiHTLQQQKTTLTQKLQSLCKELDILQREQA--TIDTRTSAFRDLQGQLAHAKKQQELQQ-RYAELCAAAitctA 451
|
250
....*....|....*
gi 1720383800 836 QSAKKASALSDASRK 850
Cdd:TIGR00618 452 QCEKLEKIHLQESAQ 466
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
631-872 |
4.15e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 40.60 E-value: 4.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 631 AQQRQRLAAVKreleikeihlQDAARR---RLLKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKDLE-IRQLELEAQ 706
Cdd:TIGR02794 49 AQQANRIQQQK----------KPAAKKeqeRQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEqAAKQAEEKQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 707 KrlyekdlttsQEAVAKEIREDtdahRRKAALEEHMFQKLLENSQmggRRAQrvmEDNLAKAEQAClnadwqiqtlhKQK 786
Cdd:TIGR02794 119 K----------QAEEAKAKQAA----EAKAKAEAEAERKAKEEAA---KQAE---EEAKAKAAAEA-----------KKK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 787 CADQQRSQGYYDVATLLRENRRKEVEvlnAMMEEEAQKWKEAEEKEFHLQSAKKASALSDASRK-WFLRQETSAALEHEE 865
Cdd:TIGR02794 168 AEEAKKKAEAEAKAKAEAEAKAKAEE---AKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKaDEAELGDIFGLASGS 244
|
....*..
gi 1720383800 866 MPWLQRQ 872
Cdd:TIGR02794 245 NAEKQGG 251
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
596-731 |
4.17e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 40.98 E-value: 4.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 596 DEQRAKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELEIKEIHLQDAarRRLLKlqqdQREMELRRLE 675
Cdd:pfam12128 586 DLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFA--RTALK----NARLDLRRLF 659
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720383800 676 DEiERKVQMRDQEIAATAKDLEIRQL-ELEAQKRLYEKDLTTSQEAVAKEIREDTDA 731
Cdd:pfam12128 660 DE-KQSEKDKKNKALAERKDSANERLnSLEAQLKQLDKKHQAWLEEQKEQKREARTE 715
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
579-776 |
4.83e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.09 E-value: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 579 LDFLRERQT---VENMQAEVDEQRAKDEAWYQKqelLRRAEETR---REILLQEEEKMAQQRQRLAAVKRELeikeihlq 652
Cdd:COG3096 960 LSEVVQRRPhfsYEDAVGLLGENSDLNEKLRAR---LEQAEEARreaREQLRQAQAQYSQYNQVLASLKSSR-------- 1028
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 653 DAARRRLLKLQQDQREMELrRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKrlyekdltTSQEAvakEIREdtdAH 732
Cdd:COG3096 1029 DAKQQTLQELEQELEELGV-QADAEAEERARIRRDELHEELSQNRSRRSQLEKQL--------TRCEA---EMDS---LQ 1093
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1720383800 733 RRKAALEEHMFQ--KLLENSQMGGRRAQRVMEDN-----LAKAEQACLNAD 776
Cdd:COG3096 1094 KRLRKAERDYKQerEQVVQAKAGWCAVLRLARDNdverrLHRRELAYLSAD 1144
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
610-708 |
5.60e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.13 E-value: 5.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 610 ELLRRAEETRREILlqeeEKMAQQRQRLAAVKRELEIKEIHLQD-----AARRRLLKLQQDQREMELRRLEDEIERKvQM 684
Cdd:COG4942 139 QYLKYLAPARREQA----EELRADLAELAALRAELEAERAELEAllaelEEERAALEALKAERQKLLARLEKELAEL-AA 213
|
90 100
....*....|....*....|....*.
gi 1720383800 685 RDQEIAATAKDLE--IRQLELEAQKR 708
Cdd:COG4942 214 ELAELQQEAEELEalIARLEAEAAAA 239
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
593-822 |
5.81e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.54 E-value: 5.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 593 AEVDEQRAKDEAwyQKQELLR---------RAEETRREILLQEEEKMAQQ--------------RQRLAAVKRELEIKEI 649
Cdd:pfam01576 57 AEAEEMRARLAA--RKQELEEilhelesrlEEEEERSQQLQNEKKKMQQHiqdleeqldeeeaaRQKLQLEKVTTEAKIK 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 650 HLQDaaRRRLLKLQQDQREMELRRLEDEI-ERKVQMRDQE------------IAATAKDLEIR-------QLELEAQKRL 709
Cdd:pfam01576 135 KLEE--DILLLEDQNSKLSKERKLLEERIsEFTSNLAEEEekakslsklknkHEAMISDLEERlkkeekgRQELEKAKRK 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 710 YEKDLTTSQEAVAKEIREDTDAHRRKAALEEHMFQKLLENSQMGGRRAQRVMEDNLAKAEQACLNADWQIQTLHKQKCAD 789
Cdd:pfam01576 213 LEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEK 292
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1720383800 790 QQRSQGYYDVA-------TL--------LRENRRKEVEVLNAMMEEEA 822
Cdd:pfam01576 293 QRRDLGEELEAlkteledTLdttaaqqeLRSKREQEVTELKKALEEET 340
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
627-820 |
6.02e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 40.71 E-value: 6.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 627 EEKMAQQRQRLAAVKRELEIKEIHLQ------DAARRRLLKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQ 700
Cdd:COG3096 835 EAELAALRQRRSELERELAQHRAQEQqlrqqlDQLKEQLQLLNKLLPQANLLADETLADRLEELREELDAAQEAQAFIQQ 914
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 701 -----LELEAQKRLYEKDlTTSQEAVAKEIREDTDAHRR-KA---ALEE-----HMF------QKLLENSQMGGRRAQRv 760
Cdd:COG3096 915 hgkalAQLEPLVAVLQSD-PEQFEQLQADYLQAKEQQRRlKQqifALSEvvqrrPHFsyedavGLLGENSDLNEKLRAR- 992
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 761 mednLAKAEQACLNADWQIQTlhkqkcADQQRSQgYYDVATLLRENRRKEVEVLNAMMEE 820
Cdd:COG3096 993 ----LEQAEEARREAREQLRQ------AQAQYSQ-YNQVLASLKSSRDAKQQTLQELEQE 1041
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
596-771 |
6.57e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.31 E-value: 6.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 596 DEQRAKDEAWYQKQELLRRAE---------------------ETRREILLQEEEKMAQQRQRLAAVKRELEIKEIHLQDA 654
Cdd:COG1196 555 DDEVAAAAIEYLKAAKAGRATflpldkiraraalaaalargaIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEA 634
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 655 ARRRLLKLQQDQREMELRRlEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEKDLTTSQEAVAKEIREDTDAHRR 734
Cdd:COG1196 635 ALRRAVTLAGRLREVTLEG-EGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAE 713
|
170 180 190
....*....|....*....|....*....|....*..
gi 1720383800 735 KAALEEHMFQKLLENSQMGGRRAQRVMEDNLAKAEQA 771
Cdd:COG1196 714 EERLEEELEEEALEEQLEAEREELLEELLEEEELLEE 750
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
607-721 |
6.89e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 40.32 E-value: 6.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 607 QKQELLRRAEETRREiLLQEEEKMAQQRQRLAAVKRELEIK---EIHLQ---DAARRRLLKLQQDQREMElrrledeier 680
Cdd:COG3096 279 ERRELSERALELRRE-LFGARRQLAEEQYRLVEMARELEELsarESDLEqdyQAASDHLNLVQTALRQQE---------- 347
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1720383800 681 KVQMRDQEIAATAKDLEIRQLELEA---QKRLYEKDLTTSQEAV 721
Cdd:COG3096 348 KIERYQEDLEELTERLEEQEEVVEEaaeQLAEAEARLEAAEEEV 391
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
577-711 |
7.10e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 39.52 E-value: 7.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 577 DELDFLRERQTVENMQAEVDEQRAKDEAWYQKQELL----RRAEETRREILLQEEEKMAQQ-RQRLAAVKRELEIKEIHL 651
Cdd:pfam13868 201 AERDELRAKLYQEEQERKERQKEREEAEKKARQRQElqqaREEQIELKERRLAEEAEREEEeFERMLRKQAEDEEIEQEE 280
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720383800 652 QDAARRRLLKLQQD-QREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYE 711
Cdd:pfam13868 281 AEKRRMKRLEHRRElEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKKLKE 341
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
578-833 |
8.10e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.03 E-value: 8.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 578 ELDFLRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEEKM-------------AQQRQRLAAVKREL 644
Cdd:TIGR00606 814 KLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTnelkseklqigtnLQRRQQFEEQLVEL 893
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 645 ---------EIKEIHLQDAARRRLLKLQQDQREMELRRLEDEiERKVQMRDQEIAATAKDLEIRQLELEAQ----KRLYE 711
Cdd:TIGR00606 894 stevqslirEIKDAKEQDSPLETFLEKDQQEKEELISSKETS-NKKAQDKVNDIKEKVKNIHGYMKDIENKiqdgKDDYL 972
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 712 KDLTTSQEAVAKEIREDtdaHRRKAALEEHMfqKLLENSQMGGRRAQRVMEDNLA--KAEQACLNADWQIQTLHKQKCAD 789
Cdd:TIGR00606 973 KQKETELNTVNAQLEEC---EKHQEKINEDM--RLMRQDIDTQKIQERWLQDNLTlrKRENELKEVEEELKQHLKEMGQM 1047
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1720383800 790 Q--QRSQGYYDVATLLRENRRKEVEVLNAMMEEEAQKW---KEAEEKEF 833
Cdd:TIGR00606 1048 QvlQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKhfkKELREPQF 1096
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
585-693 |
8.27e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 39.75 E-value: 8.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 585 RQTVENMQAEVDEQRAKdeawYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELEIKEIHLQ---DAARRRLLK 661
Cdd:COG4942 142 KYLAPARREQAEELRAD----LAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEkelAELAAELAE 217
|
90 100 110
....*....|....*....|....*....|..
gi 1720383800 662 LQQDQRemELRRLEDEIERKVQMRDQEIAATA 693
Cdd:COG4942 218 LQQEAE--ELEALIARLEAEAAAAAERTPAAG 247
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
603-751 |
8.50e-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: 38.92 E-value: 8.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 603 EAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRE--LEIKEihlQDAARRRLLKLQQDQREMELRRLeDEIER 680
Cdd:pfam13904 58 ENWLAAKQRQRQKELQAQKEEREKEEQEAELRKRLAKEKYQewLQRKA---RQQTKKREESHKQKAAESASKSL-AKPER 133
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720383800 681 KVQMRdqEIAATAKDLEIRQLELEAQKRLYEKDlttsqeavAKEIREDTDAHRRKAAleEHMFQKLLENSQ 751
Cdd:pfam13904 134 KVSQE--EAKEVLQEWERKKLEQQQRKREEEQR--------EQLKKEEEEQERKQLA--EKAWQKWMKNVK 192
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
583-771 |
8.79e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 39.36 E-value: 8.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 583 RERQTVENMQAEVDEQRAKDEAwyQKQELLRRAEETRREILLQE------EEKMAQQRQRLAAV---KRELEIKEIHLQD 653
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKK--EEKALLKQLAALERRIAALArriralEQELAALEAELAELekeIAELRAELEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 654 AARRRLLKLQQDQREMEL-------------RRLE--DEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEKDLTTsQ 718
Cdd:COG4942 105 ELAELLRALYRLGRQPPLalllspedfldavRRLQylKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAE-L 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1720383800 719 EAVAKEIREDTDAHRRKAALEEHMFQKLLENSQMGGRRAQRvMEDNLAKAEQA 771
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE-LEALIARLEAE 235
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
572-772 |
9.40e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.66 E-value: 9.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 572 ERIRNDELDF---LRERQTVENMQAEVDEQRAKDEAWYQKQELLR-RAEETRREILLQE------EEKMAQQRQRLAAVK 641
Cdd:PRK03918 193 ELIKEKEKELeevLREINEISSELPELREELEKLEKEVKELEELKeEIEELEKELESLEgskrklEEKIRELEERIEELK 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 642 REL--------EIKEIHLQDAARRRLLKLQQDQREmELRRLEDEIER------KVQMRDQEIAATAKDL-EIRQLELEAQ 706
Cdd:PRK03918 273 KEIeeleekvkELKELKEKAEEYIKLSEFYEEYLD-ELREIEKRLSRleeeinGIEERIKELEEKEERLeELKKKLKELE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383800 707 KRL--YEKDLTTSQEAVAKE------------------IREDTDAHRRKAALEEHMFQKLLENSQMGGRRAQR---VMEd 763
Cdd:PRK03918 352 KRLeeLEERHELYEEAKAKKeelerlkkrltgltpeklEKELEELEKAKEEIEEEISKITARIGELKKEIKELkkaIEE- 430
|
....*....
gi 1720383800 764 nLAKAEQAC 772
Cdd:PRK03918 431 -LKKAKGKC 438
|
|
| |
