|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
33-296 |
1.12e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.72 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 33 EKVRQDLSQQLELVSSEKSSLQ*ELEDLHQELGFAREQIQRAKQTIYEKESKLQEVEK-------LEIAVGDLKAQLASA 105
Cdd:COG1196 245 EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQdiarleeRRRELEERLEELEEE 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 106 SESKEELELKHEAEVTNYKIKLEMLEREKDAVLDRMAEsQEAELERLRTQLLFSHEEELSKLKDDLQQEHRINTENLKDN 185
Cdd:COG1196 325 LAELEEELEELEEELEELEEELEEAEEELEEAEAELAE-AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLE 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 186 LVIQHKQQLDQLQKEMSKKIEALQFENDNLLTKQNQLTLEISRLKDLQQSIVNSKSEEMMLQIHELQKEIEILRQEEKEK 265
Cdd:COG1196 404 ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELL 483
|
250 260 270
....*....|....*....|....*....|.
gi 401833395 266 GTLEQEVQELQLKTELLEKQMKEREDSLKEK 296
Cdd:COG1196 484 EELAEAAARLLLLLEAEADYEGFLEGVKAAL 514
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
36-303 |
2.00e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.95 E-value: 2.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 36 RQDLSQQLELVSSEKSSLQ*ELEDLHQELGFAREQIQRAKQTIYEKESKLQEVEKLEiavgdlkaQLASASESKEELELK 115
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE--------YELLAELARLEQDIA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 116 HEAE-VTNYKIKLEMLEREKDAVLDRMAESQEAELERLRTQLLFSHEEELSKLKDDLQQEHRINTENLKDNLVIQHKQQL 194
Cdd:COG1196 306 RLEErRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 195 DQLQKEMSKKIEALQfENDNLLTKQNQLTLEISRLKDLQQSIVNSKSEEMMLQIHELQKEIEILR---QEEKEKGTLEQE 271
Cdd:COG1196 386 EELLEALRAAAELAA-QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEeeaELEEEEEALLEL 464
|
250 260 270
....*....|....*....|....*....|..
gi 401833395 272 VQELQLKTELLEKQMKEREDSLKEKCSLLETQ 303
Cdd:COG1196 465 LAELLEEAALLEAALAELLEELAEAAARLLLL 496
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
39-375 |
1.27e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.39 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 39 LSQQLELVSSEKSSLQ*ELEDLHQELGFAREQIQRAKQTIYEKESKLQEVEK-LEIAVGDLKAQLASASESKEELELKhE 117
Cdd:TIGR02169 672 EPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKeIEQLEQEEEKLKERLEELEEDLSSL-E 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 118 AEVTNYKIKLEMLEREKDAvLDRMAESQEAELERLRTQLLFSHEEELSKLKDDLQQEHRINTENLKDnlVIQHKQQLDQL 197
Cdd:TIGR02169 751 QEIENVKSELKELEARIEE-LEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLRE--IEQKLNRLTLE 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 198 QKEMSKKIEALQFENDNLLTKQNQLTLEISRLKDLQQSIvNSKSEEMMLQIHELQKEIEILRQE----EKEKGTLEQEVQ 273
Cdd:TIGR02169 828 KEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEL-EEELEELEAALRDLESRLGDLKKErdelEAQLRELERKIE 906
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 274 ELQLKTELLEKQMKEredsLKEKCSLLETQNNIFEDEMNTLKE---------KLKKyAVTNMEESLIFIDDVSSKSQD-- 342
Cdd:TIGR02169 907 ELEAQIEKKRKRLSE----LKAKLEALEEELSEIEDPKGEDEEipeeelsleDVQA-ELQRVEEEIRALEPVNMLAIQey 981
|
330 340 350
....*....|....*....|....*....|...
gi 401833395 343 SDLLKRIENLIAENEKLVKQDTELKEEIEKLNN 375
Cdd:TIGR02169 982 EEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
147-434 |
9.65e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.56 E-value: 9.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 147 AELERLRTQLLFSHEEELSKLKDDLQQEHRINTENLKdnlviQHKQQLDQLQKEMSKKIEALQFENDNLLTKQNQLTLEI 226
Cdd:COG1196 220 EELKELEAELLLLKLRELEAELEELEAELEELEAELE-----ELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 227 SRLKDLQQsivnskseemmlqihELQKEIEILRQEEKEKGTLEQEVQELQLKTELLEKQMKEREDSLKEKCSLLETQNNI 306
Cdd:COG1196 295 AELARLEQ---------------DIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 307 FEDEMNTLKEKLKKYAVTNMEESLIFIDDVSSKSQDSDLLKRIENLIAENEKLVKQDTELKEEIEKLNNSLSFAEMKFEH 386
Cdd:COG1196 360 LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 401833395 387 NYQELQEKYTSLVKIKSDLEESKNKQEAEyKAKLQTLMDEIQHLQGDI 434
Cdd:COG1196 440 EEEALEEAAEEEAELEEEEEALLELLAEL-LEEAALLEAALAELLEEL 486
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
54-411 |
1.65e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.91 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 54 Q*ELEDLHQELGFAREQIQRAKQTIYEKESKLQEVEKLEIAVGDLKAQLASASESKEELELKHEAEVTNYKIKLEMLERE 133
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 134 kDAVLDRMAESQEAELERLRTQLLfSHEEELSKLKDDLQQeHRINTENLKDNLVIQHKqQLDQLQKEMSKKIEALQFEND 213
Cdd:TIGR02168 756 -LTELEAEIEELEERLEEAEEELA-EAEAEIEELEAQIEQ-LKEELKALREALDELRA-ELTLLNEEAANLRERLESLER 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 214 NLLTKQNQLTLEISRLKDLQQSIVNSKS--EEMMLQIHELQKEIEILrqeEKEKGTLEQEVQELQLKTELLEKQMKERED 291
Cdd:TIGR02168 832 RIAATERRLEDLEEQIEELSEDIESLAAeiEELEELIEELESELEAL---LNERASLEEALALLRSELEELSEELRELES 908
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 292 SLKEKCSLLETQNnifeDEMNTLKEKLKKYAVTNMEesliFIDDVSSKSQDSdllkrIENLIAENEKLVKQDTELKEEIE 371
Cdd:TIGR02168 909 KRSELRRELEELR----EKLAQLELRLEGLEVRIDN----LQERLSEEYSLT-----LEEAEALENKIEDDEEEARRRLK 975
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 401833395 372 KLNNSLSF---AEMKFEHNYQELQEKYTSLVKIKSDLEESKNK 411
Cdd:TIGR02168 976 RLENKIKElgpVNLAAIEEYEELKERYDFLTAQKEDLTEAKET 1018
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
39-311 |
2.36e-07 |
|
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: 53.20 E-value: 2.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 39 LSQQLELVSSEKSslq*eLEDLHQELGFAREQIQRAKQtiyEKESKLQEVEKleiavgdlKAQLASAsESKEELELKHEA 118
Cdd:pfam17380 271 LNQLLHIVQHQKA-----VSERQQQEKFEKMEQERLRQ---EKEEKAREVER--------RRKLEEA-EKARQAEMDRQA 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 119 EVTNYKIKLEMlEREKDavLDRM-AESQEAELERLRTQLLFSHEEELSKLkDDLQQEHRINTENLKDNLVIQHKQQLdqL 197
Cdd:pfam17380 334 AIYAEQERMAM-ERERE--LERIrQEERKRELERIRQEEIAMEISRMREL-ERLQMERQQKNERVRQELEAARKVKI--L 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 198 QKEMSKKIEALQFENDNLLTKQ-NQLTLEISRLKDLQQSIVNSKSEEMMlqihELQKEIEILRQEEKE----KGTLEQEV 272
Cdd:pfam17380 408 EEERQRKIQQQKVEMEQIRAEQeEARQREVRRLEEERAREMERVRLEEQ----ERQQQVERLRQQEEErkrkKLELEKEK 483
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 401833395 273 QELQLKTEL----LEKQMKEREDSLKEKcsllETQNNIFEDEM 311
Cdd:pfam17380 484 RDRKRAEEQrrkiLEKELEERKQAMIEE----ERKRKLLEKEM 522
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
37-363 |
5.31e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.37 E-value: 5.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 37 QDLSQQLELVSSEKSSLQ*ELEDLHQELGFAREQIQRAKQTIYEKESKLQEVEK----LEIAVGDLKAQLASASESKEEL 112
Cdd:TIGR02168 235 EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKelyaLANEISRLEQQKQILRERLANL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 113 ELKHEAevtnYKIKLEMLEREKDAVLDRMAEsQEAELERLRTQLLfSHEEELSKLKDDLQQEHRINTE-----NLKDNLV 187
Cdd:TIGR02168 315 ERQLEE----LEAQLEELESKLDELAEELAE-LEEKLEELKEELE-SLEAELEELEAELEELESRLEEleeqlETLRSKV 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 188 IQHKQQLDQLQKE---MSKKIEALQFENDNLLTKQNQLTleiSRLKDLQQSIVNSKSEEMMLQIHELQKEIEILRQEEKE 264
Cdd:TIGR02168 389 AQLELQIASLNNEierLEARLERLEDRRERLQQEIEELL---KKLEEAELKELQAELEELEEELEELQEELERLEEALEE 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 265 KGTLEQEVQELQLKTELLEKQMKEREDSLKekcSLLETQNNIFEDEMNTLKEKLKKYAVTNMEESLIFIDDVSSKSQDSD 344
Cdd:TIGR02168 466 LREELEEAEQALDAAERELAQLQARLDSLE---RLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAA 542
|
330
....*....|....*....
gi 401833395 345 LLKRIENLIAENEKLVKQD 363
Cdd:TIGR02168 543 LGGRLQAVVVENLNAAKKA 561
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
8-296 |
4.10e-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: 49.28 E-value: 4.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 8 EDQIHLMNIAINELNQMVQDANYQREKVRQDLSQQLELVSSEKSSLQ----------*ELEDLHQELGFAREQIQRAKQT 77
Cdd:TIGR02168 690 EEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLArleaeveqleERIAQLSKELTELEAEIEELEER 769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 78 IYEKESKLQEVE----KLEIAVGDLKAQLASASESKEELELKHEA---EVTNYKIKLEMLEREKDAVLDRMAESQEaELE 150
Cdd:TIGR02168 770 LEEAEEELAEAEaeieELEAQIEQLKEELKALREALDELRAELTLlneEAANLRERLESLERRIAATERRLEDLEE-QIE 848
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 151 RLRTQLlfsheEELSKLKDDLQQEHRintenlkdnlviQHKQQLDQLQKEMSKKIEALQFENDNLLTKQNQLTLEISRLK 230
Cdd:TIGR02168 849 ELSEDI-----ESLAAEIEELEELIE------------ELESELEALLNERASLEEALALLRSELEELSEELRELESKRS 911
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 401833395 231 DLQQSI--VNSKSEEMMLQIHELQKEIEILRQEEKEKGTLE-QEVQELQLKTELLEKQMKEREDSLKEK 296
Cdd:TIGR02168 912 ELRRELeeLREKLAQLELRLEGLEVRIDNLQERLSEEYSLTlEEAEALENKIEDDEEEARRRLKRLENK 980
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
100-393 |
4.62e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 49.30 E-value: 4.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 100 AQLASASESKEELELKHEaevtnykikLEMLEREKDAVLDRMAEsQEAELERLRTQLLFSHEE--ELSKLKDDLQQEHRI 177
Cdd:TIGR02169 665 GILFSRSEPAELQRLRER---------LEGLKRELSSLQSELRR-IENRLDELSQELSDASRKigEIEKEIEQLEQEEEK 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 178 NTENLKdnlviqhkqQLDQLQKEMSKKIEALQFENDNLLTKQNQLTLEISRLKDLQQSIVNSKSEEMMLQIH-ELQKEIE 256
Cdd:TIGR02169 735 LKERLE---------ELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQaELSKLEE 805
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 257 ILRQEEKEKGTLEQEVQELQLKTELLEKQMKEREDSLKEkcslLETQNNIFEDEMNTLKEKLKKYAvTNMEESLIFIDDV 336
Cdd:TIGR02169 806 EVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRID----LKEQIKSIEKEIENLNGKKEELE-EELEELEAALRDL 880
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 401833395 337 SSKSqdSDLLKRIENLIAENEKLVKQDTELKEEIEKLNNSLSFAEMKFEHNYQELQE 393
Cdd:TIGR02169 881 ESRL--GDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSE 935
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
50-288 |
6.73e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.47 E-value: 6.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 50 KSSLQ*ELEDLHQELGFAREQIQRAKQTIYEKESKLQEVeKLEIAVGDLKAQLASASESKEELElkheAEVTNYKIKLEM 129
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEF-RQKNGLVDLSEEAKLLLQQLSELE----SQLAEARAELAE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 130 LEREKDAVLDRMAESQEAELERLRTQLLFSHEEELSKLKDDLQQEHRINTENLKDnlVIQHKQQLDQLQKEMSKKIEALq 209
Cdd:COG3206 238 AEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPD--VIALRAQIAALRAQLQQEAQRI- 314
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 401833395 210 fendnLLTKQNQLTLEISRLKDLQQsivnskseemmlQIHELQKEIEILRQEEKEKGTLEQEVQELQLKTELLEKQMKE 288
Cdd:COG3206 315 -----LASLEAELEALQAREASLQA------------QLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEE 376
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
33-434 |
7.00e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.50 E-value: 7.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 33 EKVRQDLSQQLELVSSEKSSLQ*ELEDLHQELGFAREQIQRAKQTIYEKESKLQEVEKLEIAVGDLKAQLASASESKEEL 112
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREEL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 113 elkhEAEVTNYKIKLEMLEREKDAVLDrmaesqEAELERLRTQLLFSHEEELSKLKDDLQ----------QEHRINTENL 182
Cdd:PRK02224 278 ----AEEVRDLRERLEELEEERDDLLA------EAGLDDADAEAVEARREELEDRDEELRdrleecrvaaQAHNEEAESL 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 183 KDNlVIQHKQQLDQLQKEMSKKIEALQFENDNLLTKQNQLTLEISRLKDLQQSIVNSKSEEMMLQIH--ELQKEIEILRQ 260
Cdd:PRK02224 348 RED-ADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFleELREERDELRE 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 261 EEKEKGTLEQEVQELQLKTELLEKQMK--------------EREDSLKEKCSLLETQNNIFEDEMNTLKEKLkkyavtNM 326
Cdd:PRK02224 427 REAELEATLRTARERVEEAEALLEAGKcpecgqpvegsphvETIEEDRERVEELEAELEDLEEEVEEVEERL------ER 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 327 EESLIFIDDVSSKSQDSdlLKRIENLIAENEKLVKQDTE----LKEEIEKLNNSLSFAEMKFEHNYQELQEKYTSLVKIK 402
Cdd:PRK02224 501 AEDLVEAEDRIERLEER--REDLEELIAERRETIEEKREraeeLRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELN 578
|
410 420 430
....*....|....*....|....*....|..
gi 401833395 403 SDLEEskNKQEAEYKAKLQTLMDEIQHLQGDI 434
Cdd:PRK02224 579 SKLAE--LKERIESLERIRTLLAAIADAEDEI 608
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
62-209 |
7.84e-06 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 48.21 E-value: 7.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 62 QELGFAREQIQRAKQTIYEKESKLQEV-EKLEIAVGDLKAQLASASESKEELELKHEaevtNYKIKLEMLEREKDAVLDR 140
Cdd:COG1193 493 RRLGLPEEIIERARELLGEESIDVEKLiEELERERRELEEEREEAERLREELEKLRE----ELEEKLEELEEEKEEILEK 568
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 401833395 141 MAESQEAELERLRTQLlfshEEELSKLKDDLQQEHRIntenlkdnlvIQHKQQLDQLQKEMSKKIEALQ 209
Cdd:COG1193 569 AREEAEEILREARKEA----EELIRELREAQAEEEEL----------KEARKKLEELKQELEEKLEKPK 623
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
41-322 |
1.02e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 47.97 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 41 QQLELVSSEKSSLQ*ELEDLHQE----------LGFAREQ-IQRAKQTIYEKESKLQEVEKLEIAVGDLKAQLASASESK 109
Cdd:PLN02939 114 EQQTNSKDGEQLSDFQLEDLVGMiqnaeknillLNQARLQaLEDLEKILTEKEALQGKINILEMRLSETDARIKLAAQEK 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 110 EELELKHEAEVtnyKIKLEMLEREKDAVLDRMAESQEAELERlrtqllfshEEELSkLKDDLQ--QEHRINTENLKDNLV 187
Cdd:PLN02939 194 IHVEILEEQLE---KLRNELLIRGATEGLCVHSLSKELDVLK---------EENML-LKDDIQflKAELIEVAETEERVF 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 188 IQHKQQ--LDQLQKEMSKKIEALQFENDNLLTKQNQLTLE-ISRLKDLQQSIVNSKSEEMML--QIHELQKEIEILRQEE 262
Cdd:PLN02939 261 KLEKERslLDASLRELESKFIVAQEDVSKLSPLQYDCWWEkVENLQDLLDRATNQVEKAALVldQNQDLRDKVDKLEASL 340
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 401833395 263 KEKGTLE---QEVQELQLKTELLEKQMKEREDSLKEKCSLLETQNNIFEDEMNTLKEKLKKYA 322
Cdd:PLN02939 341 KEANVSKfssYKVELLQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQDTLSKLKEESKKRS 403
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
21-285 |
2.49e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.93 E-value: 2.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 21 LNQMVQDANYQREKVRQDLSQQLELVSSEKSS-LQ*ELEDLHQELGfarEQIQRAKQTIYEKESKLQEVEKLEIAVGDLK 99
Cdd:COG3206 105 LDEDPLGEEASREAAIERLRKNLTVEPVKGSNvIEISYTSPDPELA---AAVANALAEAYLEQNLELRREEARKALEFLE 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 100 AQLASASESKEELElkheAEVTNYKIK--LEMLEREKDAVLDRMAESqEAELERLRTQLLfSHEEELSKLKDDLQQEHRI 177
Cdd:COG3206 182 EQLPELRKELEEAE----AALEEFRQKngLVDLSEEAKLLLQQLSEL-ESQLAEARAELA-EAEARLAALRAQLGSGPDA 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 178 NTENLKDNLVIQHKQQLDQLQKEMSKKIEALQFENDNLLTKQNQL-TLEISRLKDLQQSIVNSKSEEMMLQIHE--LQKE 254
Cdd:COG3206 256 LPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIaALRAQLQQEAQRILASLEAELEALQAREasLQAQ 335
|
250 260 270
....*....|....*....|....*....|.
gi 401833395 255 IEILRQEEKEKGTLEQEVQELQLKTELLEKQ 285
Cdd:COG3206 336 LAQLEARLAELPELEAELRRLEREVEVAREL 366
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
227-434 |
2.88e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.30 E-value: 2.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 227 SRLKDLQQSIVNSKSEemmlqIHELQKEIEILRQEEKEkgtLEQEVQELQLKTELLEKQMKEREDSLKEKCSLLETQNNI 306
Cdd:COG4942 27 AELEQLQQEIAELEKE-----LAALKKEEKALLKQLAA---LERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 307 FEDEMNTLKEKLKKYAVTNMEESLIFIDDVSSKSQDSDLLKRIENLIAENEKLVKQDTELKEEIEKLNNSLSFAEMKFEH 386
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 401833395 387 NYQELQEKYTSLVKIKSD---LEESKNKQEAEYKAKLQTLMDEIQHLQGDI 434
Cdd:COG4942 179 LLAELEEERAALEALKAErqkLLARLEKELAELAAELAELQQEAEELEALI 229
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
47-296 |
4.31e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.53 E-value: 4.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 47 SSEKSSLQ*ELEDLHQELGFAREQIQRAKQtiyEKESKLQEVEKLEIAVGDLKAQLASASESKEELELkheaevtnykiK 126
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKK---EEKALLKQLAALERRIAALARRIRALEQELAALEA-----------E 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 127 LEMLEREKDAVLDRMAESQEAELERLRTQLLFSHEEELSKLkddlqqehrINTENLKDnlVIQHKQQLDQLQKEMSKKIE 206
Cdd:COG4942 85 LAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALL---------LSPEDFLD--AVRRLQYLKYLAPARREQAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 207 ALQFENDNLLTKQNQLTLEISRLKDLQQSIVNSKsEEMMLQIHELQKEIEILRQEEKEkgtLEQEVQELQLKTELLEKQM 286
Cdd:COG4942 154 ELRADLAELAALRAELEAERAELEALLAELEEER-AALEALKAERQKLLARLEKELAE---LAAELAELQQEAEELEALI 229
|
250
....*....|
gi 401833395 287 KEREDSLKEK 296
Cdd:COG4942 230 ARLEAEAAAA 239
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
56-301 |
4.38e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 4.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 56 ELEDLHQELGFAREQ------IQRAKQTIYEKESKLQEVEKLEIAVGDLKAQLASASESKEELELKHE-----AEVTNYK 124
Cdd:COG4913 236 DLERAHEALEDAREQiellepIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAElarleAELERLE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 125 IKLEMLEREKDAVLDRMAESQEAELERLRTQLLfSHEEELSKLKDDLQQ-EHRINTENLKDNLviqHKQQLDQLQKEMSK 203
Cdd:COG4913 316 ARLDALREELDELEAQIRGNGGDRLEQLEREIE-RLERELEERERRRARlEALLAALGLPLPA---SAEEFAALRAEAAA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 204 KIEALQFENDNLltkQNQLTLEISRLKDLQQsivnskseemmlQIHELQKEIEILRQeekEKGTLEQEVQELQlktELLE 283
Cdd:COG4913 392 LLEALEEELEAL---EEALAEAEAALRDLRR------------ELRELEAEIASLER---RKSNIPARLLALR---DALA 450
|
250
....*....|....*...
gi 401833395 284 KQMKEREDSLKEKCSLLE 301
Cdd:COG4913 451 EALGLDEAELPFVGELIE 468
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
41-415 |
4.64e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 4.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 41 QQLELVSSEKSSLQ*ELEDLHQELGFAREQIQRAKQTIYEKESKLQEVEKLEIAVGDLKAQLASASESKEELELKHE--- 117
Cdd:PRK03918 200 KELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEele 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 118 ------AEVTNYKIKLEMLEREKDAVLDRMAESqEAELERLRTQL------------LFSHEEELSKLKDDLQQE-HRIN 178
Cdd:PRK03918 280 ekvkelKELKEKAEEYIKLSEFYEEYLDELREI-EKRLSRLEEEIngieerikeleeKEERLEELKKKLKELEKRlEELE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 179 TENLKDNLVIQHKQQLDQLQKEMS-KKIEALQFENDNLLTKQNQLTLEISRLKDLQQSIvNSKSEEMMLQIHELQK---- 253
Cdd:PRK03918 359 ERHELYEEAKAKKEELERLKKRLTgLTPEKLEKELEELEKAKEEIEEEISKITARIGEL-KKEIKELKKAIEELKKakgk 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 254 ------------EIEILRQEEKEKGTLEQEVQELQLKTELLEKQMKEREDSLKEKCSLLetQNNIFEDEMNTLKEKLKKY 321
Cdd:PRK03918 438 cpvcgrelteehRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELI--KLKELAEQLKELEEKLKKY 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 322 AVTNMEESLIFIDDVSSKSQD--------SDLLKRIENLIAENEKLVKQDTELKEEIEKLNNSLS-FAEMKFEHNYQELQ 392
Cdd:PRK03918 516 NLEELEKKAEEYEKLKEKLIKlkgeikslKKELEKLEELKKKLAELEKKLDELEEELAELLKELEeLGFESVEELEERLK 595
|
410 420
....*....|....*....|....*....
gi 401833395 393 E------KYTSLVKIKSDLEESKNKQEAE 415
Cdd:PRK03918 596 ElepfynEYLELKDAEKELEREEKELKKL 624
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
124-382 |
5.51e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 45.69 E-value: 5.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 124 KIKLEMLEREKDAVLDRMAESQEAELERL-------RTQLLFSH----EEELSKLKDDLQQEHRIntenlKDNLVIQHKQ 192
Cdd:PRK05771 8 KVLIVTLKSYKDEVLEALHELGVVHIEDLkeelsneRLRKLRSLltklSEALDKLRSYLPKLNPL-----REEKKKVSVK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 193 QLDQLQKEMSKKIEALQFENDNLLTKQNQLTLEISRLKDLQQSI-------------------------VNSKSEEMMLQ 247
Cdd:PRK05771 83 SLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLepwgnfdldlslllgfkyvsvfvgtVPEDKLEELKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 248 IHELQKEIEIlrQEEKEKGTL--------EQEVQELQLKTELLEKQMKErEDSLKEKCSLLETQNNIFEDEMNTLKEKLK 319
Cdd:PRK05771 163 ESDVENVEYI--STDKGYVYVvvvvlkelSDEVEEELKKLGFERLELEE-EGTPSELIREIKEELEEIEKERESLLEELK 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 401833395 320 KYAVTNMEESLIFIDDVSSKSQDSDLLKRienlIAENEKLV--------KQDTELKEEIEKLNNSLSFAEM 382
Cdd:PRK05771 240 ELAKKYLEELLALYEYLEIELERAEALSK----FLKTDKTFaiegwvpeDRVKKLKELIDKATGGSAYVEF 306
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
144-432 |
6.08e-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: 45.82 E-value: 6.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 144 SQEAELERLRTQLLFShEEELSKLKDDLQqEHRINTENLKDNLViqhkqQLDQLQKEMSKKIEALQFENDNLLTKQNQLT 223
Cdd:TIGR02168 674 ERRREIEELEEKIEEL-EEKIAELEKALA-ELRKELEELEEELE-----QLRKELEELSRQISALRKDLARLEAEVEQLE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 224 LEISRLKDLQQSIvnskSEEMMLQIHELQKEIEILRQEEKEKGTLEQEVQELQLKTELLEKQMKEREDSLKEKCSLLETQ 303
Cdd:TIGR02168 747 ERIAQLSKELTEL----EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANL 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 304 NNIFEDEMNTLKEKLKKYAVTNmeeslifiddvsskSQDSDLLKRIENLIAENEKLVKQDTELKEEIEKLNNSLSFAE-- 381
Cdd:TIGR02168 823 RERLESLERRIAATERRLEDLE--------------EQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEea 888
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 401833395 382 -MKFEHNYQELQEKYTSLVKIKSDLE---ESKNKQEAEYKAKLQTLMDEIQHLQG 432
Cdd:TIGR02168 889 lALLRSELEELSEELRELESKRSELRrelEELREKLAQLELRLEGLEVRIDNLQE 943
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
26-236 |
1.07e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 26 QDANYQREKVRQDLSQ---QLELVSSEKSSLQ*ELEDLHQELGFAREQIQRAKQTIYEKESKLQEVEKLEIAvgdLKAQL 102
Cdd:COG4942 23 AEAEAELEQLQQEIAElekELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE---LRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 103 AsasESKEEL-ELKHEAEVTNYKIKLEMLEREKDA--------VLDRMAESQEAELERLRTQLlfsheEELSKLKDDLQQ 173
Cdd:COG4942 100 E---AQKEELaELLRALYRLGRQPPLALLLSPEDFldavrrlqYLKYLAPARREQAEELRADL-----AELAALRAELEA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 401833395 174 EHrinteNLKDNLVIQHKQQLDQLQKEMSKKIEALQFENDNLLTKQNQLTLEISRLKDLQQSI 236
Cdd:COG4942 172 ER-----AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
93-317 |
2.01e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.60 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 93 IAVGDLKAQLASASESKEELElKHEAEVTNYKIKLEMLEREKDAVLDRMAEsQEAELERLrTQLLFSHEEELSKLKDDLQ 172
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELE-QLQQEIAELEKELAALKKEEKALLKQLAA-LERRIAAL-ARRIRALEQELAALEAELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 173 Q-EHRINtenlkdnlviQHKQQLDQLQKEMSKKIEALQFENDN----LLTKQNQLTLEISRLKDLQQsiVNSKSEEMMLQ 247
Cdd:COG4942 87 ElEKEIA----------ELRAELEAQKEELAELLRALYRLGRQpplaLLLSPEDFLDAVRRLQYLKY--LAPARREQAEE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 401833395 248 IHELQKEIEILRQE-EKEKGTLEQEVQELQLKTELLEKQMKEREDSLKEkcslLETQNNIFEDEMNTLKEK 317
Cdd:COG4942 155 LRADLAELAALRAElEAERAELEALLAELEEERAALEALKAERQKLLAR----LEKELAELAAELAELQQE 221
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
56-168 |
2.31e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 43.69 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 56 ELEDLHQELGFAREQIQRAKQTIYEKESKLQE-VEKLEIAVGDLKAQLASASESKEELELK-------------HEAEVT 121
Cdd:COG2433 389 ELPEEEPEAEREKEHEERELTEEEEEIRRLEEqVERLEAEVEELEAELEEKDERIERLERElsearseerreirKDREIS 468
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 401833395 122 NYKIKLEMLEREKDAvLDRMAESQEAELERLRTQLLFSHEEELSKLK 168
Cdd:COG2433 469 RLDREIERLERELEE-ERERIEELKRKLERLKELWKLEHSGELVPVK 514
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
37-318 |
2.67e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 43.50 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 37 QDLSQQLELVSSEkssLQ*ELEDLHQELGFARE----------QIQRAKQTIYEKESKLQEVEKLEIAVGdlKAQLASAs 106
Cdd:PRK10929 105 DALEQEILQVSSQ---LLEKSRQAQQEQDRAREisdslsqlpqQQTEARRQLNEIERRLQTLGTPNTPLA--QAQLTAL- 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 107 eskeelelkhEAEVTNYKIKLEMLErekdavLDRMAESQEAELERLRTQLlfsHEEELSKLKDDLQQehrintenLKDNL 186
Cdd:PRK10929 179 ----------QAESAALKALVDELE------LAQLSANNRQELARLRSEL---AKKRSQQLDAYLQA--------LRNQL 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 187 VIQHKQQLDQlqkeMSKKIEALQFENDNL---LTKQNQLTLEISRLKDlQQS----IVNSKSEEMMLQIHELQKEIEILR 259
Cdd:PRK10929 232 NSQRQREAER----ALESTELLAEQSGDLpksIVAQFKINRELSQALN-QQAqrmdLIASQQRQAASQTLQVRQALNTLR 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 260 QEEKEKG-------TLEQEVQEL-------QLKTE-------------LLEKQMKEREDSLKEKCSLLETQNNIFEDEMN 312
Cdd:PRK10929 307 EQSQWLGvsnalgeALRAQVARLpempkpqQLDTEmaqlrvqrlryedLLNKQPQLRQIRQADGQPLTAEQNRILDAQLR 386
|
....*.
gi 401833395 313 TLKEKL 318
Cdd:PRK10929 387 TQRELL 392
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
30-296 |
2.81e-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: 2.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 30 YQREKVRQDLSQQLELVSSEKSSLQ*ELEDLH---QELGFAREQIQRAKQTIYEKESKLQEVEKLEIA--VGDLKAQLAS 104
Cdd:TIGR02169 226 YELLKEKEALERQKEAIERQLASLEEELEKLTeeiSELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKekIGELEAEIAS 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 105 ASESKEELEL---KHEAEVTNYKIKLEMLEREKDAvLDRMAESQEAELERLRTQLLfSHEEELSKLKDDLQQEHRINTEn 181
Cdd:TIGR02169 306 LERSIAEKEReleDAEERLAKLEAEIDKLLAEIEE-LEREIEEERKRRDKLTEEYA-ELKEELEDLRAELEEVDKEFAE- 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 182 LKDNLViQHKQQLDQLQKEMskkiEALQFENDNLLTKQNQLTLEISRLKDLQQSI---VNSKSEEMMLQIHELQKEIEIL 258
Cdd:TIGR02169 383 TRDELK-DYREKLEKLKREI----NELKRELDRLQEELQRLSEELADLNAAIAGIeakINELEEEKEDKALEIKKQEWKL 457
|
250 260 270
....*....|....*....|....*....|....*...
gi 401833395 259 RQEEKEKGTLEQEVQELQLKTELLEKQMKEREDSLKEK 296
Cdd:TIGR02169 458 EQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEA 495
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
180-420 |
3.16e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 43.35 E-value: 3.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 180 ENLKDNLVIQHKQQLDQLQKEMSKKIEALQFENDNLL---------TKQNQLTLEISRLKDLQQSivnsksEEMMLQIHE 250
Cdd:PLN02939 94 DDDHNRASMQRDEAIAAIDNEQQTNSKDGEQLSDFQLedlvgmiqnAEKNILLLNQARLQALEDL------EKILTEKEA 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 251 LQKEIEILRQEEKEKGTLEQEVQELQLKTELLEKQMKER--------------EDSLKEKCSLLETQNNIFEDEMNTLKE 316
Cdd:PLN02939 168 LQGKINILEMRLSETDARIKLAAQEKIHVEILEEQLEKLrnellirgateglcVHSLSKELDVLKEENMLLKDDIQFLKA 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 317 KLKKyaVTNMEESLIFIDDVSSKSQDSdlLKRIE-NLIAENEKLVKQDTE----LKEEIEKLNNSLSFAEMKFEH----- 386
Cdd:PLN02939 248 ELIE--VAETEERVFKLEKERSLLDAS--LRELEsKFIVAQEDVSKLSPLqydcWWEKVENLQDLLDRATNQVEKaalvl 323
|
250 260 270
....*....|....*....|....*....|....*
gi 401833395 387 -NYQELQEKytsLVKIKSDLEESKNKQEAEYKAKL 420
Cdd:PLN02939 324 dQNQDLRDK---VDKLEASLKEANVSKFSSYKVEL 355
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
32-276 |
3.92e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.98 E-value: 3.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 32 REKVRQDLS--QQLELVSSEKSSLQ*ELEDLHQELgfarEQIQRAKQtiyekesklqEVEKLEIAVGDLKAQLASASESK 109
Cdd:PRK11281 38 EADVQAQLDalNKQKLLEAEDKLVQQDLEQTLALL----DKIDRQKE----------ETEQLKQQLAQAPAKLRQAQAEL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 110 EEL--ELKHEAEVTNYKIKLEMLEREKDAVLDRMAESQEA------ELERLRTQLlfshEEELSKLKDDLQQEHRINTE- 180
Cdd:PRK11281 104 EALkdDNDEETRETLSTLSLRQLESRLAQTLDQLQNAQNDlaeynsQLVSLQTQP----ERAQAALYANSQRLQQIRNLl 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 181 -NLKDNLVIQHKQQLDQLQKEMSkkieALqfendNLLTKQNQLTLE-ISRLKDLQQSivnsKSEEMMLQIHELQKEIEIL 258
Cdd:PRK11281 180 kGGKVGGKALRPSQRVLLQAEQA----LL-----NAQNDLQRKSLEgNTQLQDLLQK----QRDYLTARIQRLEHQLQLL 246
|
250 260
....*....|....*....|.
gi 401833395 259 rQE---EKEKGTLEQEVQELQ 276
Cdd:PRK11281 247 -QEainSKRLTLSEKTVQEAQ 266
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
8-318 |
4.21e-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: 43.13 E-value: 4.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 8 EDQIHLMNIAINELNQMVQDANYQREKVRQDLSQQLELVSSEKSSLQ*ELEDLHQELGFAREQIQRAKQTIYEKESKLQE 87
Cdd:TIGR02169 183 EENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 88 VEK-LEIAVGDLKAQLASASESKEELELKHEAEVTNYKIKLEMLEREKDAVLDRM--AESQEAELERLRTQLLFSHE--- 161
Cdd:TIGR02169 263 LEKrLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELedAEERLAKLEAEIDKLLAEIEele 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 162 ---EELSKLKDDLQQEHRINTENLkdNLVIQHKQQLDQLQKEMSKKIEALQFENDNLLTKQNQLTLEISRLKDLqqsivn 238
Cdd:TIGR02169 343 reiEEERKRRDKLTEEYAELKEEL--EDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEE------ 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 239 skSEEMMLQIHELQKEIEILRQEEKEkgtLEQEVQELQLKTELLE---KQMKEREDSLKEKCSLLETQNNIFEDEMNTLK 315
Cdd:TIGR02169 415 --LQRLSEELADLNAAIAGIEAKINE---LEEEKEDKALEIKKQEwklEQLAADLSKYEQELYDLKEEYDRVEKELSKLQ 489
|
...
gi 401833395 316 EKL 318
Cdd:TIGR02169 490 REL 492
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
38-320 |
4.53e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.02 E-value: 4.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 38 DLSQQLELVSSEKSSLQ*ELEDLHQELGFAREQIQRAKQTI-----YEKESKLQEVEKLEIAVGDLKAQLASASESKeel 112
Cdd:PRK04863 834 DPEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLsalnrLLPRLNLLADETLADRVEEIREQLDEAEEAK--- 910
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 113 elkheAEVTNYKIKLEMLEREKDAVldrmaESQEAELERLRTQLLFShEEELSKLK------DDLQQ-------EHRINT 179
Cdd:PRK04863 911 -----RFVQQHGNALAQLEPIVSVL-----QSDPEQFEQLKQDYQQA-QQTQRDAKqqafalTEVVQrrahfsyEDAAEM 979
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 180 ENLKDNLVIQHKQQLDQLQKEMSKKIEALQfendnllTKQNQLTLEISRLKDLQQSIvnskseemmlqihelqkeiEILR 259
Cdd:PRK04863 980 LAKNSDLNEKLRQRLEQAEQERTRAREQLR-------QAQAQLAQYNQVLASLKSSY-------------------DAKR 1033
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 401833395 260 QEEKEkgtLEQEVQELQLK-TELLEKQMKEREDSL-------KEKCSLLETQNNIFEDEMNTLKEKLKK 320
Cdd:PRK04863 1034 QMLQE---LKQELQDLGVPaDSGAEERARARRDELharlsanRSRRNQLEKQLTFCEAEMDNLTKKLRK 1099
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
4-291 |
6.81e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 6.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 4 GNTNEDQIHLMNIAINELNQMVQDAnyqrEKVRQDLSQQLELVSSEKSSLQ*eledlHQELGFAREQIQRAKQTIYEKES 83
Cdd:COG4913 605 GFDNRAKLAALEAELAELEEELAEA----EERLEALEAELDALQERREALQR-----LAEYSWDEIDVASAEREIAELEA 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 84 KLQEVEKLEIAVGDLKAQLASASESKEElelkheaevtnykiklemLEREKDAVLDRMAEsQEAELERLRTQLLfSHEEE 163
Cdd:COG4913 676 ELERLDASSDDLAALEEQLEELEAELEE------------------LEEELDELKGEIGR-LEKELEQAEEELD-ELQDR 735
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 164 LSKLKDDLQQEHRINTENLKDNLVIQhkQQLDQLQKEMSKKIEALQFENDNLltkQNQLTLEISRLK-----DLQQSIVN 238
Cdd:COG4913 736 LEAAEDLARLELRALLEERFAAALGD--AVERELRENLEERIDALRARLNRA---EEELERAMRAFNrewpaETADLDAD 810
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 401833395 239 SKSEEMMLQIHELQKEIEILRQEEKEKGTLEQevQELQLKTELLEKQMKERED 291
Cdd:COG4913 811 LESLPEYLALLDRLEEDGLPEYEERFKELLNE--NSIEFVADLLSKLRRAIRE 861
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
81-434 |
6.99e-04 |
|
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: 42.41 E-value: 6.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 81 KESKLQEVEKLEIAVGDLKAQLASASESKEELELKHEAEVTNYKIKLEMLEREKDAVLD-RMAESQEAELERLRTQLLFS 159
Cdd:pfam15921 73 KEHIERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADiRRRESQSQEDLRNQLQNTVH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 160 HEEELSKLKDDLQQEHRINTENLKdNLVIQHKQQLDQLQKEMSKKIEALQ---FENDNLLTKQ-NQLTLEISR-LKDLQQ 234
Cdd:pfam15921 153 ELEAAKCLKEDMLEDSNTQIEQLR-KMMLSHEGVLQEIRSILVDFEEASGkkiYEHDSMSTMHfRSLGSAISKiLRELDT 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 235 SIVNSKSeemmlQIHELQKEIEILRQEEKEKgtLEQEVQELQLKTELLEKQMKEREDSLKEKCSLLETQNNIFEDEMNTL 314
Cdd:pfam15921 232 EISYLKG-----RIFPVEDQLEALKSESQNK--IELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEII 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 315 KEKLKKyavtnmeeslifiddvssksqdsdllkrienliaENEKLVKQDTELKEEIEKLNNSLSFAEMKFEHNYQELQEK 394
Cdd:pfam15921 305 QEQARN----------------------------------QNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQ 350
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 401833395 395 ytsLVKIKSDLEESKNKQEaEYKAKLQTLMDEIQHLQGDI 434
Cdd:pfam15921 351 ---LVLANSELTEARTERD-QFSQESGNLDDQLQKLLADL 386
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
87-259 |
1.27e-03 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 41.28 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 87 EVEKLEIAVGDLKAQLASASEskEELELKHEAEVTNYKIKLEMLEREKDAVLDRMAESQEAELERLRtqllfshEEELSK 166
Cdd:pfam09731 295 EIDQLSKKLAELKKREEKHIE--RALEKQKEELDKLAEELSARLEEVRAADEAQLRLEFEREREEIR-------ESYEEK 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 167 LKDDLQQEHRINTENLKDNLVIQHKQQLDQLQKEMSKKIEAlqfENDNLLTKQNQLTleiSRLKDLQQSIV-NSKSEEMM 245
Cdd:pfam09731 366 LRTELERQAEAHEEHLKDVLVEQEIELQREFLQDIKEKVEE---ERAGRLLKLNELL---ANLKGLEKATSsHSEVEDEN 439
|
170
....*....|....
gi 401833395 246 LQIHELQKEIEILR 259
Cdd:pfam09731 440 RKAQQLWLAVEALR 453
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
82-265 |
1.43e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.92 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 82 ESKLQEVEKLeiAVGDLKAQLASASESKEELELKHEAEVTNYKIKLEMLEREKdavldrmaesqEAELERLRTQLLfSHE 161
Cdd:PRK12704 30 EAKIKEAEEE--AKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRER-----------RNELQKLEKRLL-QKE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 162 EELSKLKDDLQQehrintenlKDNLVIQHKQQLDQLQKEMSKKIEALqfenDNLLTKQNQLTLEISRL--KDLQQSIVNS 239
Cdd:PRK12704 96 ENLDRKLELLEK---------REEELEKKEKELEQKQQELEKKEEEL----EELIEEQLQELERISGLtaEEAKEILLEK 162
|
170 180
....*....|....*....|....*.
gi 401833395 240 KSEEMMLQIHELQKEIEILRQEEKEK 265
Cdd:PRK12704 163 VEEEARHEAAVLIKEIEEEAKEEADK 188
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
139-269 |
1.43e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.92 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 139 DRMAESQEAELERLRTQLLFSHEEELSKLKDDLQQEHRINTENLKD--NLVIQHKQQLDQLQKEMSKKIEALQFENDNLL 216
Cdd:PRK12704 41 KRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKleKRLLQKEENLDRKLELLEKREEELEKKEKELE 120
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 401833395 217 TKQNQLTLEISRLKDLQQsivnsKSEEMMLQIHELQKE--IEILRQEEKEKGTLE 269
Cdd:PRK12704 121 QKQQELEKKEEELEELIE-----EQLQELERISGLTAEeaKEILLEKVEEEARHE 170
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
231-431 |
1.62e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 231 DLQQSIVNSKSEEMMLQIHELQKEIEILRQEEKEkgtLEQEVQELQLKTELLEKQMKEREDSLKEKcslletqnnifEDE 310
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEE---LNEEYNELQAELEALQAEIDKLQAEIAEA-----------EAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 311 MNTLKEKLKKYAVTNMEE--SLIFIDDVSSKSQDSDLLKRIENLiaenEKLVKQDTELKEEIEKLNNSLSFAEMKFEHNY 388
Cdd:COG3883 81 IEERREELGERARALYRSggSVSYLDVLLGSESFSDFLDRLSAL----SKIADADADLLEELKADKAELEAKKAELEAKL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 401833395 389 QELQEKYTSLVKIKSDLEESKNKQEAEY---KAKLQTLMDEIQHLQ 431
Cdd:COG3883 157 AELEALKAELEAAKAELEAQQAEQEALLaqlSAEEAAAEAQLAELE 202
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
8-275 |
2.32e-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: 40.59 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 8 EDQIHLMNIAINELNQMVQDANYQREKVRQDL------SQQLEL-----VSSEKSSLQ*ELEDLHQELGFAREQIQRAKQ 76
Cdd:pfam12128 624 EEQLVQANGELEKASREETFARTALKNARLDLrrlfdeKQSEKDkknkaLAERKDSANERLNSLEAQLKQLDKKHQAWLE 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 77 TIYE--KESKLQEVEKLEIAVGDLKAQLASASESKEELELKHEAEV----TNYKIKLEML--EREKDAVLDRMAESQEAE 148
Cdd:pfam12128 704 EQKEqkREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELkaleTWYKRDLASLgvDPDVIAKLKREIRTLERK 783
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 149 LERLRTQllfshEEELSKLKDDLQQEHRINTENLKDNL------VIQHKQQLDQLQKEMSKKIEALQFENDNLLTKQNQL 222
Cdd:pfam12128 784 IERIAVR-----RQEVLRYFDWYQETWLQRRPRLATQLsnieraISELQQQLARLIADTKLRRAKLEMERKASEKQQVRL 858
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 401833395 223 TLEISRLKDLQQSI----VNSKSEEMMLQIHELQKEIE-ILRQEEKEKGTLEQEVQEL 275
Cdd:pfam12128 859 SENLRGLRCEMSKLatlkEDANSEQAQGSIGERLAQLEdLKLKRDYLSESVKKYVEHF 916
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
9-374 |
2.41e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.39 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 9 DQIHLMNIAINELNQMVQdanyQREKVRQDLSQQLELVSSEKSSLQ*ELEDLHQELGFAREQIQRAKQTIYEKESKlqeV 88
Cdd:TIGR04523 384 QEIKNLESQINDLESKIQ----NQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELI---I 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 89 EKLEIAVGDLKAQLASASESKEELELKHEAEVTNYKIKLEMLEREKDAVLDrmAESQEAELERlRTQLLFSHEEELSKLK 168
Cdd:TIGR04523 457 KNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKE--LEEKVKDLTK-KISSLKEKIEKLESEK 533
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 169 DDLQQEHRINTENLKDNLVIQHKQQLDQLQKEMSKKIEALQFENDNLLTKQNQLTLEISRLKDLQQSIvNSKSEEMMLQI 248
Cdd:TIGR04523 534 KEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDL-IKEIEEKEKKI 612
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 249 HELQKEIEILRQEEKEKGTLEQEVQELQLKTELLEKQMKEREDSLKEKCSLLETQNNIFEDEMNTLKEKLKKYavtNMEE 328
Cdd:TIGR04523 613 SSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDW---LKEL 689
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 401833395 329 SLIFIDDVSSKSQDSDLLK---RIENLIAENEKLVKQDTELKEEIEKLN 374
Cdd:TIGR04523 690 SLHYKKYITRMIRIKDLPKleeKYKEIEKELKKLDEFSKELENIIKNFN 738
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
53-202 |
3.06e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 39.36 E-value: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 53 LQ*ELEDLHQELGFAREQIQRAKQTIYEKESKLQEVE--------KLEIAVGDLKAQLASASESKEELELKHEAEVTNYK 124
Cdd:pfam09787 45 LTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEaqqqeeaeSSREQLQELEEQLATERSARREAEAELERLQEELR 124
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 401833395 125 IKLEMLEREKDAVLDRMAEsQEAELERLRTQLLFSHEEELSklKDDLQQEHRINTENLkdnlvIQHKQQLDQLQKEMS 202
Cdd:pfam09787 125 YLEEELRRSKATLQSRIKD-REAEIEKLRNQLTSKSQSSSS--QSELENRLHQLTETL-----IQKQTMLEALSTEKN 194
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
17-427 |
3.32e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 17 AINELNQMVQDANYQREKVRQdLSQQLELVSSEKSSLQ*ELEDLHQELGFArEQIQRAKQTIYEKESKLQEVEKLEIAVG 96
Cdd:COG4717 72 ELKELEEELKEAEEKEEEYAE-LQEELEELEEELEELEAELEELREELEKL-EKLLQLLPLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 97 DLKAQLASASESKEELElKHEAEVTNYKIKLEMLEREKDAVLDRMAESQEAELERLRTQLLfSHEEELSKLKDDLQQEHR 176
Cdd:COG4717 150 ELEERLEELRELEEELE-ELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLA-ELEEELEEAQEELEELEE 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 177 INTENLKDNLVIQHKQQLDQLQ-------------------------------------------KEMSKKIEALQFEND 213
Cdd:COG4717 228 ELEQLENELEAAALEERLKEARlllliaaallallglggsllsliltiagvlflvlgllallfllLAREKASLGKEAEEL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 214 NLLTKQNQLT-LEISRLKDLQQSIVNSKSEEMMLQIHELQKEIEILRQEEKEKGTLEQEVQELQLKTELLEKQMKEREDs 292
Cdd:COG4717 308 QALPALEELEeEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEE- 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 293 LKEKCSLLETQNNIfEDEMNTLKEKLKKYAvTNMEESLIFIDDVSSKSQDSDLLKRIENLIAENEKLVKQDTELKEEIEK 372
Cdd:COG4717 387 LRAALEQAEEYQEL-KEELEELEEQLEELL-GELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQ 464
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 373 LNNSLSFAEMKFEHNY-----QELQEKYTSLVKIKSDLEESKNKQEAEYKAKLQTLMDEI 427
Cdd:COG4717 465 LEEDGELAELLQELEElkaelRELAEEWAALKLALELLEEAREEYREERLPPVLERASEY 524
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
17-320 |
3.45e-03 |
|
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: 40.05 E-value: 3.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 17 AINELNQMVQDANYQ---REKVRQDLSQQLELVSSEKSSLQ*ELEDLHQELGFAREQIQRAKQTIYEKESKLqevEKLEI 93
Cdd:TIGR02169 703 RLDELSQELSDASRKigeIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDL---HKLEE 779
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 94 AVGDLKAQLasaSESKEELELKHEAEVTNYKIKLEMLEREKDAVLDRmaESQEAELERLRTQLLFSHEEELSKLKDDLQQ 173
Cdd:TIGR02169 780 ALNDLEARL---SHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNR--LTLEKEYLEKEIQELQEQRIDLKEQIKSIEK 854
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 174 E-HRINTENLKDNLVIQHKQ----QLDQLQKEMSKKIEALQFENDNLLTKQNQLTLEISRLKDLQQSIVNSKS--EEMML 246
Cdd:TIGR02169 855 EiENLNGKKEELEEELEELEaalrDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEalEEELS 934
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 247 QIHELQKEIEILRQEEKEKGTLEQEVQELQLKTELLE----------KQMKEREDSLKEKCSLLETQNNIFEDEMNTLKE 316
Cdd:TIGR02169 935 EIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEpvnmlaiqeyEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
....
gi 401833395 317 KLKK 320
Cdd:TIGR02169 1015 KKRE 1018
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
31-411 |
4.23e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.53 E-value: 4.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 31 QREKVRQDLSQQLELVSSEKSSLQ*ELEDLHQELGFAREQIQRAKQTIYEKESKLQEVEKLEIAVGDLKAQLASASESKE 110
Cdd:COG1196 418 RLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 111 ELELKHEAEVTNYKIKLEMLEREKDA--------VLDRMAESQEAELERLRTQLLFSHEEELSKLKDDLQQE-----HRI 177
Cdd:COG1196 498 EAEADYEGFLEGVKAALLLAGLRGLAgavavligVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAkagraTFL 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 178 NTENLKDNLVIQHKQQLDQLQKEMSKKIEALQFENDNLLTKQNQLTLEISRLKDLQQSIVNSKSEEMMLQIHELQKEI-- 255
Cdd:COG1196 578 PLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGgs 657
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 256 ----EILRQEEKEKGTLEQEVQELQLKTELLEKQMKEREDSLKEKCSLLETQNNIFEDEMNTLKEKLKKYAVTNMEESLI 331
Cdd:COG1196 658 aggsLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREEL 737
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 332 FIDDVSSKSQDSDLLKRIENLIAENEKLVKQDTELKEEIEKLN--NSLSFAEmkfehnYQELQEKYTSLVKIKSDLEESK 409
Cdd:COG1196 738 LEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALGpvNLLAIEE------YEELEERYDFLSEQREDLEEAR 811
|
..
gi 401833395 410 NK 411
Cdd:COG1196 812 ET 813
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
191-373 |
6.21e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.13 E-value: 6.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 191 KQQLDQLQKEMSKKIEALQfENDNLLTKQNQLTLEISRLKDLQQSIVNSKSEEmmLQIHELQKEIEILRQEEKEKGTLEQ 270
Cdd:COG4913 616 EAELAELEEELAEAEERLE-ALEAELDALQERREALQRLAEYSWDEIDVASAE--REIAELEAELERLDASSDDLAALEE 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 271 EVQELQLKTELLEKQMKEredsLKEKCSLLETQNNIFEDEMNTLKEKLKKYAVTNMEESLIFIDDVSSKSQDSDLLKRI- 349
Cdd:COG4913 693 QLEELEAELEELEEELDE----LKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELr 768
|
170 180
....*....|....*....|....
gi 401833395 350 ENLIAENEKLVKQDTELKEEIEKL 373
Cdd:COG4913 769 ENLEERIDALRARLNRAEEELERA 792
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
20-290 |
6.77e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 39.29 E-value: 6.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 20 ELNQMVQDANYQREKVRQDLSQQLELVSSEKSSLQ*ELEDLHQELGFAREQIQRA--------KQTIYEKESKLQEVE-K 90
Cdd:COG5022 886 ELKIDVKSISSLKLVNLELESEIIELKKSLSSDLIENLEFKTELIARLKKLLNNIdleegpsiEYVKLPELNKLHEVEsK 965
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 91 LEIAVGDLKAQLASASESKEELeLKHEAEVTNYKIKLEMLEREKDAVldrMAESQEAELERLRTQLLFSHEEELSKLKDD 170
Cdd:COG5022 966 LKETSEEYEDLLKKSTILVREG-NKANSELKNFKKELAELSKQYGAL---QESTKQLKELPVEVAELQSASKIISSESTE 1041
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 171 LQQEHRIntenlkDNLVIQHKQQLDQLQKE---MSKKIEALQFENDNLLTKQNQLTLEIS-RLKDLQQSIVNSKSEEMML 246
Cdd:COG5022 1042 LSILKPL------QKLKGLLLLENNQLQARykaLKLRRENSLLDDKQLYQLESTENLLKTiNVKDLEVTNRNLVKPANVL 1115
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 401833395 247 QIHELQKEIEILRQEEKEkgTLEQEVQELQLKTELLEKQMKERE 290
Cdd:COG5022 1116 QFIVAQMIKLNLLQEISK--FLSQLVNTLEPVFQKLSVLQLELD 1157
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
10-410 |
6.87e-03 |
|
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: 38.95 E-value: 6.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 10 QIHLMNIAINELNQMVQDANYQREKVRQDLSQQLELVSSEKSSLQ*ELEDLHQELGFAREQIQRAKQTIYEKESKLQ-EV 88
Cdd:pfam15921 318 QLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSlEK 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 89 EKLEIAVGDLKAQLASASESKEELELKHeAEVTNYKIKLEMLEREKDAVLDRMAESQEAELERLR-----TQLLFSHEEE 163
Cdd:pfam15921 398 EQNKRLWDRDTGNSITIDHLRRELDDRN-MEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEkvsslTAQLESTKEM 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 164 LSKLKDDLQQEhRINTENLKDNLviqhkQQLDQLQKEMSKKIEALQFENDNLLTKQNQLTLEISRLKDLQQSIVNSKSE- 242
Cdd:pfam15921 477 LRKVVEELTAK-KMTLESSERTV-----SDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTEc 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 243 -EMMLQIHELQKEIEILRQEEKEK----GTLEQEVQELQLKTELLEKQMKEREDSLKEKcslletqnNIFEDEMNTLKEK 317
Cdd:pfam15921 551 eALKLQMAEKDKVIEILRQQIENMtqlvGQHGRTAGAMQVEKAQLEKEINDRRLELQEF--------KILKDKKDAKIRE 622
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 318 LKKyAVTNMEeslifIDDVSSKSQDSDLLKRIENLIAENEKLVKQDTELKEEIEKLNNSLSFAEMKFEHNYQELQEKYT- 396
Cdd:pfam15921 623 LEA-RVSDLE-----LEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNk 696
|
410
....*....|....*..
gi 401833395 397 ---SLVKIKSDLEESKN 410
Cdd:pfam15921 697 lkmQLKSAQSELEQTRN 713
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
343-436 |
7.66e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 38.69 E-value: 7.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 343 SDLLKRIENLIAENEKLVKQDTELKEEIEKLNNSLSFA------EMKFEHNYQELQEKYTSLvkiKSDLEESKNKQEaEY 416
Cdd:COG2433 416 RRLEEQVERLEAEVEELEAELEEKDERIERLERELSEArseerrEIRKDREISRLDREIERL---ERELEEERERIE-EL 491
|
90 100
....*....|....*....|..
gi 401833395 417 KAKLQTL--MDEIQHLQGDIPV 436
Cdd:COG2433 492 KRKLERLkeLWKLEHSGELVPV 513
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
37-227 |
8.45e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 38.27 E-value: 8.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 37 QDLSQQLELVSSEKSSLQ*ELEDLHQELGFAREQIQRAKQTIYEKESKLQEVE-KLEIAVGDLKAQLASASESKeelelk 115
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEaEIEERREELGERARALYRSG------ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401833395 116 heaEVTNYkikLEMLEREKD--------AVLDRMAESQEAELERLRTQllfshEEELSKLKDDLQQEHRINTENLKDnlV 187
Cdd:COG3883 100 ---GSVSY---LDVLLGSESfsdfldrlSALSKIADADADLLEELKAD-----KAELEAKKAELEAKLAELEALKAE--L 166
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 401833395 188 IQHKQQLDQLQKEMSKKIEALQFENDNLLTKQNQLTLEIS 227
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELA 206
|
|
| |
