|
Name |
Accession |
Description |
Interval |
E-value |
| LRRFIP |
pfam09738 |
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the ... |
138-492 |
6.36e-99 |
|
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the GC-rich consensus sequence (5'- AGCCCCCGGCG-3') and may regulate expression of TNF, EGFR and PDGFA. LRRFIP2 may function as activator of the canonical Wnt signalling pathway, in association with DVL3, upstream of CTNNB1/beta-catenin.
Pssm-ID: 462869 [Multi-domain] Cd Length: 303 Bit Score: 302.39 E-value: 6.36e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 138 LDEKSDKQYAENYT---------RPSSRNSASATTPLSGNSSRRGSGDTSSLIDPDTSLSELRDiydlkdqihdvegrym 208
Cdd:pfam09738 30 VEENADRVFDMSSSsgadtasgsPTASTTSAGTLNSLGGTSSRRSSEDSSISLEDEGSLRDIKH---------------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 209 qglkelkeSLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKM 288
Cdd:pfam09738 94 --------ELKEVEEKYRKAMISNAQLDNEKSNLMYQVDLLKDKLEEMEESLAELQRELREKNKELERLKRNLRRLQFQL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 289 DELKEGLRQRDELIeenqrlqqkvdtmtkevfdlqetllwkdktigalekqkehiaclrnerdvlreeladlqqtvktaE 368
Cdd:pfam09738 166 AELKEQLKQRDELI-----------------------------------------------------------------E 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 369 KHGLVIIPESTPNGDVNHEPVVGAITAVSQEAAQVLESAGEGPLDVRLRKLAEEKDELLSQIRKLKLQLEEERQ-KCSRN 447
Cdd:pfam09738 181 KHGLVIVPDENTNGEEENSPADAKRALVSVEAAEVLESAGEGSLDVRLKKLADEKEELLDEVRKLKLQLEEEKSkRNSTR 260
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1958795722 448 DGMSGDLAGLQNGSDLqfIEMQRDANRQISEYKFKLSKAEQDIAT 492
Cdd:pfam09738 261 SSQSPDGFGLENGSHV--IEVQREANKQISDYKFKLQKAEQEITT 303
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
211-542 |
4.46e-10 |
|
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: 62.77 E-value: 4.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 211 LKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHkmdE 290
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK---E 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 291 LKEGLRQRDELIEENQRLQQKVDTMTKEVFDLQETLlwkDKTIGALEKQKEHIACLRNERDVLREELADLQQTVKTAEKh 370
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQI---EQLKEELKALREALDELRAELTLLNEEAANLRERLESLER- 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 371 glviipestpngdvNHEPVVGAITAVSQEAAQVLESAGEgpLDVRLRKLAEEKDELLSQI-RKLKLQLEEERQKCSRNDG 449
Cdd:TIGR02168 832 --------------RIAATERRLEDLEEQIEELSEDIES--LAAEIEELEELIEELESELeALLNERASLEEALALLRSE 895
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 450 MSgDLAGLQNGSDLQFIEMQRD---ANRQISEYKFKLSKAEQDIATLEQSISRlegqvlRYKTAAENAEKIEDELKAEKR 526
Cdd:TIGR02168 896 LE-ELSEELRELESKRSELRREleeLREKLAQLELRLEGLEVRIDNLQERLSE------EYSLTLEEAEALENKIEDDEE 968
|
330
....*....|....*.
gi 1958795722 527 KLQRELRTAQDKIEEM 542
Cdd:TIGR02168 969 EARRRLKRLENKIKEL 984
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
188-542 |
2.61e-08 |
|
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: 56.99 E-value: 2.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 188 SELRDIYDLKDQIHDVEGRYMQGLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYREN 267
Cdd:TIGR02168 705 KELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEI 784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 268 EEKSKELERQKHMCSVLQHKMDELKEGLRqrdELIEENQRLQQKVDTMTKEVFDLQETLLWKDKTIgalEKQKEHIACLR 347
Cdd:TIGR02168 785 EELEAQIEQLKEELKALREALDELRAELT---LLNEEAANLRERLESLERRIAATERRLEDLEEQI---EELSEDIESLA 858
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 348 NERDVLREELADLQQTVKTAEKhglviipestpngdvnhepvvgaITAVSQEAAQVLESAGEGpLDVRLRKLAEEKDELL 427
Cdd:TIGR02168 859 AEIEELEELIEELESELEALLN-----------------------ERASLEEALALLRSELEE-LSEELRELESKRSELR 914
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 428 SQIRKLKLQLEEERQKCSrndGMSGDLAGLQNGSDLQFIEMQRDANRQISEYKFKLSKAEQDIATLEQSISRLEGQVLRY 507
Cdd:TIGR02168 915 RELEELREKLAQLELRLE---GLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAA 991
|
330 340 350
....*....|....*....|....*....|....*
gi 1958795722 508 KTAAENAEKIEDELKAEKRKLQRELRTAQDKIEEM 542
Cdd:TIGR02168 992 IEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEI 1026
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
165-543 |
3.38e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.53 E-value: 3.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 165 LSGNSSRRGSGDTSSLIDPDTSLSELRDIYDLKDQIHDVegryMQGLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIY 244
Cdd:TIGR02169 655 MTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSL----QSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQ 730
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 245 QVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMDELKEGLR--QRDELIEENQRLQQKVDTMTKEVFDL 322
Cdd:TIGR02169 731 EEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNdlEARLSHSRIPEIQAELSKLEEEVSRI 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 323 QETLLWKDKTIGALEKQKEHIACLRNERDVLREELaDLQQTVKTAEKHGLVIIPESTPngdvnhepvvgaiTAVSQEAAQ 402
Cdd:TIGR02169 811 EARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDL-KEQIKSIEKEIENLNGKKEELE-------------EELEELEAA 876
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 403 VLEsagegpLDVRLRKLAEEKDELLSQIRKLKL---QLEEERQKcsRNDGMSGDLAGLQNGSD-LQFIEMQRDANRQISE 478
Cdd:TIGR02169 877 LRD------LESRLGDLKKERDELEAQLRELERkieELEAQIEK--KRKRLSELKAKLEALEEeLSEIEDPKGEDEEIPE 948
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958795722 479 YKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAEKRKLQRELRTAQDKIEEME 543
Cdd:TIGR02169 949 EELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYE 1013
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
234-543 |
8.85e-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: 51.98 E-value: 8.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 234 QLDNEKNNLiyqvDTLKDVIEEQEEQM---------AEFYRE--NEEKS--------------KELERQKHMCSVLQHKM 288
Cdd:TIGR02168 180 KLERTRENL----DRLEDILNELERQLkslerqaekAERYKElkAELRElelallvlrleelrEELEELQEELKEAEEEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 289 DELKEGLRQRDELIEENQRLQQKVDtmtKEVFDLQETLLWKDKTIGALEKQKEHI----ACLRNERDVLREELADLQQTV 364
Cdd:TIGR02168 256 EELTAELQELEEKLEELRLEVSELE---EEIEELQKELYALANEISRLEQQKQILrerlANLERQLEELEAQLEELESKL 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 365 KTAEKHgLVIIPESTPNGDVNHEPVVGAITAvSQEAAQVLESAGEGpLDVRLRKLAEEKDELLSQIRKLKLQLEEERQKC 444
Cdd:TIGR02168 333 DELAEE-LAELEEKLEELKEELESLEAELEE-LEAELEELESRLEE-LEEQLETLRSKVAQLELQIASLNNEIERLEARL 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 445 SRndgmsgdlaglQNGSDLQFIEMQRDANRQISEYKFKLSKAEqdIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAE 524
Cdd:TIGR02168 410 ER-----------LEDRRERLQQEIEELLKKLEEAELKELQAE--LEELEEELEELQEELERLEEALEELREELEEAEQA 476
|
330
....*....|....*....
gi 1958795722 525 KRKLQRELRTAQDKIEEME 543
Cdd:TIGR02168 477 LDAAERELAQLQARLDSLE 495
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
182-558 |
1.67e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.19 E-value: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 182 DPDTSLSELRDIYDLKDQ--IHDVEGRYMQGLKELKESLSEVEEKYKKAMVSNAQLD---NEKNNLIYQVDTLKDVIEEQ 256
Cdd:PRK02224 184 DQRGSLDQLKAQIEEKEEkdLHERLNGLESELAELDEEIERYEEQREQARETRDEADevlEEHEERREELETLEAEIEDL 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 257 EEQMAEFYRENEEKSKELERQKHMCSVLQHKMDELKEGLRQRDELIEenqRLQQKVDTMTKEVFDLQETLLWKDKTIGAL 336
Cdd:PRK02224 264 RETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAE---AVEARREELEDRDEELRDRLEECRVAAQAH 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 337 EKQ----KEHIACLRNERDVLREELADLQQTVKTAEkhglviipestpngdVNHEPVVGAITAVSQEAAQVLESAGEGPL 412
Cdd:PRK02224 341 NEEaeslREDADDLEERAEELREEAAELESELEEAR---------------EAVEDRREEIEELEEEIEELRERFGDAPV 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 413 DV-----RLRKLAEEKDELLSQIRKLKLQLEEERQKCSRNDGMsgdLAGLQNGSDLQFIEMQRDANRqISEYKFKLSKAE 487
Cdd:PRK02224 406 DLgnaedFLEELREERDELREREAELEATLRTARERVEEAEAL---LEAGKCPECGQPVEGSPHVET-IEEDRERVEELE 481
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958795722 488 QDIATLEQSISRLEGQVLRYKTAAENAEKIEDelKAEKRKLQRELR-TAQDKIEEMEMTNSHLAKRLEKMKA 558
Cdd:PRK02224 482 AELEDLEEEVEEVEERLERAEDLVEAEDRIER--LEERREDLEELIaERRETIEEKRERAEELRERAAELEA 551
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
265-514 |
3.25e-06 |
|
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: 49.38 E-value: 3.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 265 RENEEKSKELERQkhmcsvLQHKMDELKEGLRQRDELIEENQRLQQKVDTMTKEVFDLQETLLWKDKTIGALEKQKEHia 344
Cdd:COG4942 23 AEAEAELEQLQQE------IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 345 cLRNERDVLREELADLqqtVKTAEKHG-----LVIIPESTPNGDVNHEPVVGAITAVSQEAAQVLESAGEgpldvRLRKL 419
Cdd:COG4942 95 -LRAELEAQKEELAEL---LRALYRLGrqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA-----ELAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 420 AEEKDELLSQIRKLKLQLEEERQKcsrndgmsgdLAGLQNGSDlqfiEMQRDANRQISEYKFKLSKAEQDIATLEQSISR 499
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAA----------LEALKAERQ----KLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
250
....*....|....*
gi 1958795722 500 LEGQVLRYKTAAENA 514
Cdd:COG4942 232 LEAEAAAAAERTPAA 246
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
189-555 |
9.14e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 9.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 189 ELRDIYDLKDQIHDVEGRYMQGLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIE--EQEEQMAEFYRE 266
Cdd:COG4717 54 EADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEklEKLLQLLPLYQE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 267 NEEKSKELERqkhmcsvLQHKMDELKEGLRQRDELIEENQRLQQKVDTMTKEVFDLQETLLWkdKTIGALEKQKEHIACL 346
Cdd:COG4717 134 LEALEAELAE-------LPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSL--ATEEELQDLAEELEEL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 347 RNERDVLREELADLQQTVKTAEK--HGLVIIPESTPNGDVNHEP-----VVGAITAVSQEAAQVLESAGE---------G 410
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEelEQLENELEAAALEERLKEArllllIAAALLALLGLGGSLLSLILTiagvlflvlG 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 411 PLDVRLRKLAEEKDELLSQIRKLKLQLEEERqkcSRNDGMSGDLAGLQNGSDLQfIEMQRDANRQISEYKFKLSKAEQDI 490
Cdd:COG4717 285 LLALLFLLLAREKASLGKEAEELQALPALEE---LEEEELEELLAALGLPPDLS-PEELLELLDRIEELQELLREAEELE 360
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958795722 491 ATLEQSISRLEGQVLRYKTAAENAEKIED--ELKAEKRKLQRELRTAQDKIEEMEMTNSHLAKRLEK 555
Cdd:COG4717 361 EELQLEELEQEIAALLAEAGVEDEEELRAalEQAEEYQELKEELEELEEQLEELLGELEELLEALDE 427
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
249-567 |
1.23e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.39 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 249 LKDVIEEQEEQM---------AEFYRENEEKSKELERQkhmcsVLQHKMDELKEGLRQRDELIEENQRlqqkvdtmtkev 319
Cdd:COG1196 191 LEDILGELERQLeplerqaekAERYRELKEELKELEAE-----LLLLKLRELEAELEELEAELEELEA------------ 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 320 fdlqetllwkdktigALEKQKEHIACLRNERDVLREELADLQQTVKTAEkhglviipestpngdvnhepvvGAITAVSQE 399
Cdd:COG1196 254 ---------------ELEELEAELAELEAELEELRLELEELELELEEAQ----------------------AEEYELLAE 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 400 AAQVLEsagegpldvRLRKLAEEKDELLSQIRKLKLQLEEERQKcsrndgmsgdlaglqngsdlqfiemQRDANRQISEY 479
Cdd:COG1196 297 LARLEQ---------DIARLEERRRELEERLEELEEELAELEEE-------------------------LEELEEELEEL 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 480 KFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAEKRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKAN 559
Cdd:COG1196 343 EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422
|
....*...
gi 1958795722 560 RTALLAQQ 567
Cdd:COG1196 423 LEELEEAL 430
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
412-558 |
1.68e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 412 LDVRLRKLAEEKDELLSQIRKLKLQLEEERQKCsrnDGMSGDLAGlQNGSDLQFIEMQ-RDANRQISEYKFKLSKAEQDI 490
Cdd:COG4913 293 LEAELEELRAELARLEAELERLEARLDALREEL---DELEAQIRG-NGGDRLEQLEREiERLERELEERERRRARLEALL 368
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958795722 491 ATLEQSI-----------SRLEGQVLRYKTAAENAEKIEDELKAEKRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKA 558
Cdd:COG4913 369 AALGLPLpasaeefaalrAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRD 447
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
336-566 |
2.64e-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: 46.68 E-value: 2.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 336 LEKQKEHIACLRNERDVLREELADLQQTVKTAEKhglviipestpngdvnhepvvgAITAVSQEAAQvlesagegpLDVR 415
Cdd:COG4942 36 IAELEKELAALKKEEKALLKQLAALERRIAALAR----------------------RIRALEQELAA---------LEAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 416 LRKLAEEKDELLSQIRKLKLQLEEERQKCSRNdGMSGDLAGLQNGSDLQFIEMQRDANRQISEYKfklskaEQDIATLEQ 495
Cdd:COG4942 85 LAELEKEIAELRAELEAQKEELAELLRALYRL-GRQPPLALLLSPEDFLDAVRRLQYLKYLAPAR------REQAEELRA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958795722 496 SISRLEGQVLRYKTAAENAEKIEDELKAEKRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKANRTALLAQ 566
Cdd:COG4942 158 DLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
261-558 |
3.85e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.60 E-value: 3.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 261 AEFYRENEEKSKELERQKHMCSVLQHKMDELKEGL----RQRDELIEENQRLQQKVDTMTKE-VFDLQETLLWKDKTIGA 335
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLerlrREREKAERYQALLKEKREYEGYElLKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 336 LEKQKEHIACLRNERDVLREELADLQQTVKTAEKHglviIPESTPNGDVNHEPVVGAITA-VSQEAAQVLESAGE-GPLD 413
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEIEQLLEELNKK----IKDLGEEEQLRVKEKIGELEAeIASLERSIAEKERElEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 414 VRLRKLAEEKDELLSQIRKLKLQLEEERQkcsRNDGMSGDLAGLQNGSDLQFIEMQ------RDANRQISEYKFKLSKAE 487
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAEIEELEREIEEERK---RRDKLTEEYAELKEELEDLRAELEevdkefAETRDELKDYREKLEKLK 398
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958795722 488 QDIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAEKRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKA 558
Cdd:TIGR02169 399 REINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQ 469
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
191-460 |
6.61e-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: 6.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 191 RDIYDLKDQIHDVEGRymqgLKELKESLSEVEEKYkkamvsnAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEK 270
Cdd:TIGR02168 253 EELEELTAELQELEEK----LEELRLEVSELEEEI-------EELQKELYALANEISRLEQQKQILRERLANLERQLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 271 SKELERQKHMCSVLQHKMDELKEglrQRDELIEENQRLQQKVDTMTKEVFDLQETLLWKDKtigALEKQKEHIACLRNER 350
Cdd:TIGR02168 322 EAQLEELESKLDELAEELAELEE---KLEELKEELESLEAELEELEAELEELESRLEELEE---QLETLRSKVAQLELQI 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 351 DVLREELADLQQTVKTAEKHGLVIIPESTPNGDVNHEPVVGAITAVSQEAAQVLESAGEGPLDV--RLRKLAEEKDELLS 428
Cdd:TIGR02168 396 ASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLeeALEELREELEEAEQ 475
|
250 260 270
....*....|....*....|....*....|..
gi 1958795722 429 QIRKLKLQLEEERQKCSRNDGMSGDLAGLQNG 460
Cdd:TIGR02168 476 ALDAAERELAQLQARLDSLERLQENLEGFSEG 507
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
334-567 |
7.91e-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: 7.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 334 GALEKQKEHIACLRNERDVLREELADLQQTVKTAEKhglviipestpngdvnhepvvgAITAVSQEAAQVLESAgegpld 413
Cdd:TIGR02168 663 GGSAKTNSSILERRREIEELEEKIEELEEKIAELEK----------------------ALAELRKELEELEEEL------ 714
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 414 VRLRKLAEEKDELLSQIRKLKLQLEEERQKCSrndgmsgDLAGLQNGSDLQFIEMQRDANRQISEYKFKLSKAEQDIATL 493
Cdd:TIGR02168 715 EQLRKELEELSRQISALRKDLARLEAEVEQLE-------ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEEL 787
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958795722 494 EQSISRLEGQVLRYKTAAENAEKIEDELKAEKRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKANRTALLAQQ 567
Cdd:TIGR02168 788 EAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEI 861
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
400-567 |
1.53e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.66 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 400 AAQVLESAGEG--PLDVRLRKLAEEKDELLSQIRKLKLQLEEERQKCSRndgMSGDLAGLQnGSDLQFIEMQRDANRQIS 477
Cdd:TIGR02168 230 LVLRLEELREEleELQEELKEAEEELEELTAELQELEEKLEELRLEVSE---LEEEIEELQ-KELYALANEISRLEQQKQ 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 478 EYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAEKRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMK 557
Cdd:TIGR02168 306 ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLR 385
|
170
....*....|
gi 1958795722 558 ANRTALLAQQ 567
Cdd:TIGR02168 386 SKVAQLELQI 395
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
215-563 |
2.24e-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: 44.29 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 215 KESLSEVEEKYKKAMVsnaqLDNEKNNliyQVDTLKDvieeqEEQMAEFYRENEEKSKELERQKHMCSVLQHKmDELKEG 294
Cdd:TIGR02169 176 LEELEEVEENIERLDL----IIDEKRQ---QLERLRR-----EREKAERYQALLKEKREYEGYELLKEKEALE-RQKEAI 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 295 LRQRDELIEENQRLQQKVDTMTKEVFDLQETLLWKDKTIGALEKQ-----KEHIACLRNERDVLREELADLQQTVKTAEK 369
Cdd:TIGR02169 243 ERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEeqlrvKEKIGELEAEIASLERSIAEKERELEDAEE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 370 HgLVIIPESTPNGDVNHEPVVGAITAVSQEAAQVLEsagegpldvRLRKLAEEKDELLSQIRKLKLQLEEERQKCSRndg 449
Cdd:TIGR02169 323 R-LAKLEAEIDKLLAEIEELEREIEEERKRRDKLTE---------EYAELKEELEDLRAELEEVDKEFAETRDELKD--- 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 450 MSGDLAGLQNGSDlqfiEMQRDANRQISEykfkLSKAEQDIATLEQSISRLEGQVLRYKTAAENA----EKIEDELK--- 522
Cdd:TIGR02169 390 YREKLEKLKREIN----ELKRELDRLQEE----LQRLSEELADLNAAIAGIEAKINELEEEKEDKaleiKKQEWKLEqla 461
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1958795722 523 AEKRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKANRTAL 563
Cdd:TIGR02169 462 ADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARAS 502
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
336-563 |
2.53e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.28 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 336 LEKQKEHIACLRNERDVLREELADLQQTVKTA--EKHGLVIIPESTPNGDVNHEPVVGAITA-VSQEAAQVLESAGE-GP 411
Cdd:TIGR02168 686 IEELEEKIAELEKALAELRKELEELEEELEQLrkELEELSRQISALRKDLARLEAEVEQLEErIAQLSKELTELEAEiEE 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 412 LDVRLRKLAEEKDELLSQIRKLKLQLEEERQKCSRNDGMSGDL---AGLQNGSDLQFIEMQRDANRQISEYKFKLSKAEQ 488
Cdd:TIGR02168 766 LEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELraeLTLLNEEAANLRERLESLERRIAATERRLEDLEE 845
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958795722 489 DIATLEQSISRLEGQVLRYKTAAEnaeKIEDELKA---EKRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKANRTAL 563
Cdd:TIGR02168 846 QIEELSEDIESLAAEIEELEELIE---ELESELEAllnERASLEEALALLRSELEELSEELRELESKRSELRRELEEL 920
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
184-540 |
2.82e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.18 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 184 DTSLSELRDIYDLKDQIHDVEGRY---MQGLKELKESLSEVEEKYKKA-----MVSNAQLDNEKNNLiYQVDTLKdvIEE 255
Cdd:PRK04863 286 EEALELRRELYTSRRQLAAEQYRLvemARELAELNEAESDLEQDYQAAsdhlnLVQTALRQQEKIER-YQADLEE--LEE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 256 QEEQMAEFYRENEEKSKELERQKhmcSVLQHKMDELKEGLRQRDELIEENQR----LQQKVDTmtkevfdLQETLLWKDK 331
Cdd:PRK04863 363 RLEEQNEVVEEADEQQEENEARA---EAAEEEVDELKSQLADYQQALDVQQTraiqYQQAVQA-------LERAKQLCGL 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 332 TIGALEKQKEHIACLRNERDVLREELADLQQTVKTAEkhglviipestpngdvnhepvvgAITAVSQEAAQVLESAGeGP 411
Cdd:PRK04863 433 PDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQ-----------------------AAHSQFEQAYQLVRKIA-GE 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 412 LDvrlRKLAEEkdellsQIRKLKLQLEEERQKCSRNDGMSGDLAGLQngsdlQFIEMQRDANRQISEYKFKLSKAEQDIA 491
Cdd:PRK04863 489 VS---RSEAWD------VARELLRRLREQRHLAEQLQQLRMRLSELE-----QRLRQQQRAERLLAEFCKRLGKNLDDED 554
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958795722 492 TLEQSISRLEGQVLRYKTAAENA-------EKIEDELKAEKRKLQR---ELRTAQDKIE 540
Cdd:PRK04863 555 ELEQLQEELEARLESLSESVSEArerrmalRQQLEQLQARIQRLAArapAWLAAQDALA 613
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
195-543 |
3.61e-04 |
|
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: 43.47 E-value: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 195 DLKDQIHDVEGRymqgLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKEL 274
Cdd:TIGR04523 311 ELKSELKNQEKK----LEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEI 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 275 ERQKHMCSVLQHKMDELKEGLRQRDELIEEnqrLQQKVDTMTKEVFDLQETLLWKDKTIGALEKQ----KEHIACLRNER 350
Cdd:TIGR04523 387 KNLESQINDLESKIQNQEKLNQQKDEQIKK---LQQEKELLEKEIERLKETIIKNNSEIKDLTNQdsvkELIIKNLDNTR 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 351 DVLREELADLQQTVKTAEKhglviipestpngdvNHEPVVGAITAVSQEAAQVLESAGEgpLDVRLRKLAEEKDELLSQI 430
Cdd:TIGR04523 464 ESLETQLKVLSRSINKIKQ---------------NLEQKQKELKSKEKELKKLNEEKKE--LEEKVKDLTKKISSLKEKI 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 431 RKLKLQLEEERQKCSRndgMSGDLAGLQNGSDLQFIEMQRDA-NRQISEYKF-------KLSKAEQDIATLEQSISRLEG 502
Cdd:TIGR04523 527 EKLESEKKEKESKISD---LEDELNKDDFELKKENLEKEIDEkNKEIEELKQtqkslkkKQEEKQELIDQKEKEKKDLIK 603
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1958795722 503 QVLRYKTAAENAEKIEDELKAEKRKLQRELRTAQDKIEEME 543
Cdd:TIGR04523 604 EIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLK 644
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
195-459 |
5.23e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.12 E-value: 5.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 195 DLKDQIHDVEGR-YMQGLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDvieeqeeQMAEFYRENEEKSKE 273
Cdd:TIGR02168 217 ELKAELRELELAlLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRL-------EVSELEEEIEELQKE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 274 L------------------ERQKHMCSVLQHKMDELKEGLRQRDELIEENQRLQQKVDTMTKEVFDLQETLlwkDKTIGA 335
Cdd:TIGR02168 290 LyalaneisrleqqkqilrERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL---EELEAE 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 336 LEKQKEHIACLRNERDVLREELADLQQTVKTAEKHgLVIIPESTPNGDVNHEPVVGAITAVSQEAAQVLESAGEGPLDVR 415
Cdd:TIGR02168 367 LEELESRLEELEEQLETLRSKVAQLELQIASLNNE-IERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEEL 445
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1958795722 416 LRKLAEEKDELLSQIRKLKLQLEEERQKCSRNDGMSGDLAGLQN 459
Cdd:TIGR02168 446 EEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQA 489
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
412-566 |
9.70e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 9.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 412 LDVRLRKLAEEKDELLSQIRKLKLQLEEERQKCSRNDGMSGDLAglqngSDLQFIEMQ-RDANRQISEYKFKLSKA---- 486
Cdd:COG1579 15 LDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLE-----KEIKRLELEiEEVEARIKKYEEQLGNVrnnk 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 487 -----EQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAEKRKLQRELRTAQDKIEEMEmtnSHLAKRLEKMKANRT 561
Cdd:COG1579 90 eyealQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEEL---AELEAELEELEAERE 166
|
....*
gi 1958795722 562 ALLAQ 566
Cdd:COG1579 167 ELAAK 171
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
192-411 |
1.06e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 192 DIYDLKDQIHDVEGRYMQGLKELKESLSEVEEKYKKAMVSNAQLD---NEKNNLIYQVDTLKDVIEEQEEQMAEFYRENE 268
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEalqAEIDKLQAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 269 EKSKE----------------LERQKHMCSVLQHKMDELKEGLRQRDELIEENQRLQQKVDTMTKEVFDLQETllwKDKT 332
Cdd:COG3883 97 RSGGSvsyldvllgsesfsdfLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA---KAEL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958795722 333 IGALEKQKEHIACLRNERDVLREELADLQQTVKTAEKHGLVIIPESTPNGDVNHEPVVGAITAVSQEAAQVLESAGEGP 411
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAA 252
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
346-542 |
1.29e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.54 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 346 LRNERDVLREELADLQQTVKTAE--------KHGLVIIPESTpngdvnhEPVVGAITAVSQE--AAQVLESAGEGPLDVR 415
Cdd:COG3206 173 ARKALEFLEEQLPELRKELEEAEaaleefrqKNGLVDLSEEA-------KLLLQQLSELESQlaEARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 416 LRKLAEEKD------------ELLSQIRKLKLQLEEERQKCSRNDgmsgdlaglqngSDLQFIEMQRDANRQI--SEYKF 481
Cdd:COG3206 246 RAQLGSGPDalpellqspviqQLRAQLAELEAELAELSARYTPNH------------PDVIALRAQIAALRAQlqQEAQR 313
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958795722 482 KLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELkaekRKLQRELRTAQDKIEEM 542
Cdd:COG3206 314 ILASLEAELEALQAREASLQAQLAQLEARLAELPELEAEL----RRLEREVEVARELYESL 370
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
238-556 |
1.49e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 238 EKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERqkhmcsvLQHKMDELKEGLRQRDELIEENQRLQQKVDTMTK 317
Cdd:PRK03918 180 RLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPE-------LREELEKLEKEVKELEELKEEIEELEKELESLEG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 318 EVFDLQEtllwkdkTIGALEKQkehIACLRNERDVLREELADLQQTVKTAEKHglVIIPESTPNGDVNHEPVVGAITAVS 397
Cdd:PRK03918 253 SKRKLEE-------KIRELEER---IEELKKEIEELEEKVKELKELKEKAEEY--IKLSEFYEEYLDELREIEKRLSRLE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 398 QEAAQVLESAGEGPLDV-RLRKLAEEKDELLSQIRKLK---LQLEEERQKCSRNDGMSGDLAGLQNGSDLQFIEMQRDAN 473
Cdd:PRK03918 321 EEINGIEERIKELEEKEeRLEELKKKLKELEKRLEELEerhELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 474 RQISEykfKLSKAEQDIATLEQSISRLEGQVLRYKTAAE-----NAEKIEDELKAEKRKLQRELRTAQDKIEEMEMTNSH 548
Cdd:PRK03918 401 EEIEE---EISKITARIGELKKEIKELKKAIEELKKAKGkcpvcGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERK 477
|
....*...
gi 1958795722 549 LAKRLEKM 556
Cdd:PRK03918 478 LRKELREL 485
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
253-558 |
1.53e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 41.63 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 253 IEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMDELKEGLRQRDELIEENQRLQQKVDTMTKEVFDLQETLLWKDKT 332
Cdd:pfam05483 372 LEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKE 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 333 IGALEKQkehIACLRNERDVLREELADLQQTVKTAEKHGLVIIPEST----PNGDVNHEPVVGAITAVSQEAAQVLESAG 408
Cdd:pfam05483 452 IHDLEIQ---LTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDklllENKELTQEASDMTLELKKHQEDIINCKKQ 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 409 EGPLDVRLRKLAEEKDELLSQIRKLKLQLEEERQKCSRNDGMSGDLAGLQNGSDLQFIEMQRDANRQISEYKFKLSKAEQ 488
Cdd:pfam05483 529 EERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNK 608
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958795722 489 DIATLEQsisrlEGQVLRYKTAAENAE---------KIEDELKAEKRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKA 558
Cdd:pfam05483 609 NIEELHQ-----ENKALKKKGSAENKQlnayeikvnKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKA 682
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
201-557 |
1.68e-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: 41.26 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 201 HDVEgryMQGLKELKESL-SEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKH 279
Cdd:pfam15921 276 HEVE---ITGLTEKASSArSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLV 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 280 MCSvlqhkmDELKEGLRQRDELIEENQRLQqkvDTMTKEVFDLQEtllwKDKTIgALEKQKEHIACLRNER-----DVLR 354
Cdd:pfam15921 353 LAN------SELTEARTERDQFSQESGNLD---DQLQKLLADLHK----REKEL-SLEKEQNKRLWDRDTGnsitiDHLR 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 355 EELADLQQTVKTAEKHGLVIIPESTPNGDVNHEPVVG---AITAVSQEAAQvLESAGEgpldvRLRKLAEE----KDELL 427
Cdd:pfam15921 419 RELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGkneSLEKVSSLTAQ-LESTKE-----MLRKVVEEltakKMTLE 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 428 SQIRKLKLQLEEERQKCSRNDGMSGDLAGLQNGSDLQFIEMQ---------RDANRQISEYKFKLSKAEQDIATLEQSI- 497
Cdd:pfam15921 493 SSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQhlknegdhlRNVQTECEALKLQMAEKDKVIEILRQQIe 572
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958795722 498 --SRLEGQVLRyKTAAENAEKIEDELKAEKRKLQ-RELRTAQD----KIEEMEMTNSHLakRLEKMK 557
Cdd:pfam15921 573 nmTQLVGQHGR-TAGAMQVEKAQLEKEINDRRLElQEFKILKDkkdaKIRELEARVSDL--ELEKVK 636
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
470-558 |
1.69e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.38 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 470 RDANRQISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELkaekRKLQRELRTAQDKIEEMEMTNSHL 549
Cdd:COG2433 416 RRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDREI----SRLDREIERLERELEEERERIEEL 491
|
....*....
gi 1958795722 550 AKRLEKMKA 558
Cdd:COG2433 492 KRKLERLKE 500
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
412-566 |
1.69e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 412 LDVRLRKLAEEKDELLSQIRKLKLQLEEERQkcsrndgmsgdlaglqngsdlqfiemQRDANRQISEYKFklskAEQDIA 491
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQE--------------------------RREALQRLAEYSW----DEIDVA 664
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958795722 492 TLEQSISRLEGQvlryKTAAENAEKIEDELKAEKRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKANRTALLAQ 566
Cdd:COG4913 665 SAEREIAELEAE----LERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR 735
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
209-559 |
1.96e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 40.96 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 209 QGLKELKESLSEVEEKykkamvsNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHM-------C 281
Cdd:pfam10174 324 QHIEVLKESLTAKEQR-------AAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMldvkerkI 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 282 SVLQHKMDELKEGLRQRDELIEENQR----LQQKVDTMTKEVFDLQETLLWKDKTIGALEKQKEhiaclrNERDVLREEL 357
Cdd:pfam10174 397 NVLQKKIENLQEQLRDKDKQLAGLKErvksLQTDSSNTDTALTTLEEALSEKERIIERLKEQRE------REDRERLEEL 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 358 ADLQQTVKTAEKHGLVIIPESTPNGDVNHEpvvgaitavSQEAAQVLESAGEgpldvrlrklaeEKDellSQIRKLKLQL 437
Cdd:pfam10174 471 ESLKKENKDLKEKVSALQPELTEKESSLID---------LKEHASSLASSGL------------KKD---SKLKSLEIAV 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 438 EEERQKCSRndgMSGDLAGLQNgsdlqfIEMQRDANRQISEykfklskaeqdiatleqSISRLEGQVLRYKTAAENAEKI 517
Cdd:pfam10174 527 EQKKEECSK---LENQLKKAHN------AEEAVRTNPEIND-----------------RIRLLEQEVARYKEESGKAQAE 580
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1958795722 518 EDELKAEKRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKAN 559
Cdd:pfam10174 581 VERLLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVAN 622
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
209-369 |
2.17e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.52 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 209 QGLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVL---- 284
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELlral 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 285 --QHKMDELKEGLRQRD--ELIEENQRLQQKVDTMTKEVFDLQETLLWKDKTIGALEKQKEHIACLRNERDVLREELADL 360
Cdd:COG4942 114 yrLGRQPPLALLLSPEDflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEAL 193
|
....*....
gi 1958795722 361 QQTVKTAEK 369
Cdd:COG4942 194 KAERQKLLA 202
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
197-563 |
2.47e-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: 40.77 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 197 KDQIHDVEgrymQGLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELER 276
Cdd:TIGR04523 116 KEQKNKLE----VELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDK 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 277 QKHMCSVLQHKMDELKEGLRQRDELIEENQRLQQKVDTMTKEVFDLQETLlwkDKTIGALEKQKEHIACLRNERDVLREE 356
Cdd:TIGR04523 192 IKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEI---NEKTTEISNTQTQLNQLKDEQNKIKKQ 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 357 LADLQQTVKTAEKhglVIIPESTPNGDVNHEpvvgaITAVSQEAAQVLesagegpldvrLRKLAEEKDELLSQIRKLKLQ 436
Cdd:TIGR04523 269 LSEKQKELEQNNK---KIKELEKQLNQLKSE-----ISDLNNQKEQDW-----------NKELKSELKNQEKKLEEIQNQ 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 437 LEEERQKCSRNDGMSGDLAGLQNGSDLQFIEMQrdanRQISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEK 516
Cdd:TIGR04523 330 ISQNNKIISQLNEQISQLKKELTNSESENSEKQ----RELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEK 405
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1958795722 517 IEDELKAEKRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKANRTAL 563
Cdd:TIGR04523 406 LNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVK 452
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
420-566 |
3.61e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 3.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 420 AEEKDELLSQIRKLKLQLEEERQKCSRNDGmsgdlagLQNGSDLQFIEMQRDANRQiseykfKLSKAEQDIATLEQSISR 499
Cdd:COG4913 247 AREQIELLEPIRELAERYAAARERLAELEY-------LRAALRLWFAQRRLELLEA------ELEELRAELARLEAELER 313
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958795722 500 LEGQvlryktaaenaekiEDELKAEKRKLQRELRTAQ-DKIEEMEMTNSHLAKRLEKMKANRTALLAQ 566
Cdd:COG4913 314 LEAR--------------LDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEAL 367
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
235-531 |
3.76e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.00 E-value: 3.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 235 LDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSkelerqkhmcsvlqhkmdelkeglrqrDELIEENQRLQQKVDT 314
Cdd:PHA02562 186 LDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKY---------------------------DELVEEAKTIKAEIEE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 315 MTKEVFDLQETllwkdktigaLEKQKEHIACLRNERDVLREELADLQQTVKTAEKHGlvIIPESTpngdvnhepvvgait 394
Cdd:PHA02562 239 LTDELLNLVMD----------IEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKGG--VCPTCT--------------- 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 395 avsqeaaQVLESAGEgpldvRLRKLAEEKDELLSQIRKLKLQLEEERQKCSrndgmsgdlaglqngsdlQFIEMQR---D 471
Cdd:PHA02562 292 -------QQISEGPD-----RITKIKDKLKELQHSLEKLDTAIDELEEIMD------------------EFNEQSKkllE 341
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 472 ANRQISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAEKRKLQRE 531
Cdd:PHA02562 342 LKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKE 401
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
184-443 |
4.68e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.92 E-value: 4.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 184 DTSLSELRD-IYDLKDQIHDVEGRYMqglkELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAE 262
Cdd:COG1196 266 EAELEELRLeLEELELELEEAQAEEY----ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 263 fyrENEEKSKELERQKHMCSVLQHKMDELKEGLRQRDELIEENQRLQQKVDTMTKEVFDLQETLLWKDKTIGALEKQKEH 342
Cdd:COG1196 342 ---LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 343 iacLRNERDVLREELADLQQTVKTAEKhglviipestpngdvnhepvvgAITAVSQEAAQVLESAGEgpLDVRLRKLAEE 422
Cdd:COG1196 419 ---LEEELEELEEALAELEEEEEEEEE----------------------ALEEAAEEEAELEEEEEA--LLELLAELLEE 471
|
250 260
....*....|....*....|.
gi 1958795722 423 KDELLSQIRKLKLQLEEERQK 443
Cdd:COG1196 472 AALLEAALAELLEELAEAAAR 492
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
191-413 |
5.25e-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: 39.67 E-value: 5.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 191 RDIYDLKDQIHDVEGRYMQGLKELKESLSEVEE---KYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYREN 267
Cdd:TIGR02169 308 RSIAEKERELEDAEERLAKLEAEIDKLLAEIEElerEIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDEL 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 268 EEKSKELERQKHMCSVLQHKMDELKEGLRQRDELIEE-NQRL------QQKVDTMTKEVFDLQETLLWKDKTIGA-LEKQ 339
Cdd:TIGR02169 388 KDYREKLEKLKREINELKRELDRLQEELQRLSEELADlNAAIagieakINELEEEKEDKALEIKKQEWKLEQLAAdLSKY 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 340 KEHIACLRNERDVLREELADLQQTVKTAEKHGLVIIPESTPNGDV------NHEPVVGAIT---AVSQEAAQVLESAGEG 410
Cdd:TIGR02169 468 EQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVeevlkaSIQGVHGTVAqlgSVGERYATAIEVAAGN 547
|
...
gi 1958795722 411 PLD 413
Cdd:TIGR02169 548 RLN 550
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
393-567 |
5.30e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.43 E-value: 5.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 393 ITAVSQEAAQVLESAGEgpLDVRLRKLAEEKDELLSQIRKLKLQLEEERQKCS-------RNDGMSGDLAGLQNGSDLQ- 464
Cdd:COG3883 39 LDALQAELEELNEEYNE--LQAELEALQAEIDKLQAEIAEAEAEIEERREELGeraralyRSGGSVSYLDVLLGSESFSd 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 465 FIE-------MQRDANRQISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAEKRKLQRELRTAQD 537
Cdd:COG3883 117 FLDrlsalskIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEA 196
|
170 180 190
....*....|....*....|....*....|
gi 1958795722 538 KIEEMEMTNSHLAKRLEKMKANRTALLAQQ 567
Cdd:COG3883 197 QLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
472-541 |
5.54e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.43 E-value: 5.54e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 472 ANRQISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAEKRKLQRELRTAQDKIEE 541
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEE 83
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
255-566 |
7.63e-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: 39.33 E-value: 7.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 255 EQEEQMAEFYRENEEKSKelerqkhmCSVLQHKMDELKEGLRQrdeLIEENQRLQQKVDTMTKEVFDLQETLLWKDKtig 334
Cdd:pfam15921 445 QMERQMAAIQGKNESLEK--------VSSLTAQLESTKEMLRK---VVEELTAKKMTLESSERTVSDLTASLQEKER--- 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 335 ALEKQKEHIACLRNERDVLREELadlqQTVKTAEKHGLVIIPE------STPNGDVNHEPVVGAITAVSQEAAQVLESAG 408
Cdd:pfam15921 511 AIEATNAEITKLRSRVDLKLQEL----QHLKNEGDHLRNVQTEcealklQMAEKDKVIEILRQQIENMTQLVGQHGRTAG 586
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 409 egpldvrlrKLAEEKDELLSQIRKLKLQLEEERQKCSRNDGMSGDLAGLQNGSDLQFIEMQRDANRQISEYKFKLSKAEQ 488
Cdd:pfam15921 587 ---------AMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQ 657
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 489 DIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAEKRKLQRELRTAQDKIEE-------MEMTNSHLAKRLEKMKANRT 561
Cdd:pfam15921 658 LLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQtrntlksMEGSDGHAMKVAMGMQKQIT 737
|
....*
gi 1958795722 562 ALLAQ 566
Cdd:pfam15921 738 AKRGQ 742
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
211-555 |
8.01e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 39.11 E-value: 8.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 211 LKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKhmcsvlqhkmDE 290
Cdd:pfam07888 89 LRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMK----------ER 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 291 LKEGLRQRDELIEENQRLQQKVDTMTKEVFDLQETLlwkdktigalEKQKEHIACLRNERDVLREELADLQQTVKTAEKH 370
Cdd:pfam07888 159 AKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEF----------QELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRK 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 371 glviipestpngDVNHEPVVGAIT------AVSQEAAQVLESAGEGPLDVRLRKLAE------EKDELLSQIRKLKLQLE 438
Cdd:pfam07888 229 ------------EAENEALLEELRslqerlNASERKVEGLGEELSSMAAQRDRTQAElhqarlQAAQLTLQLADASLALR 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 439 EERQKcsrndgMSGDLAGLQngsdlQFIEMQRDANRQISEYKFKLSKAEQDiatleqsiSRLEGQVLRYKTAAE------ 512
Cdd:pfam07888 297 EGRAR------WAQERETLQ-----QSAEADKDRIEKLSAELQRLEERLQE--------ERMEREKLEVELGREkdcnrv 357
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1958795722 513 ---NAEKIEDELKAEKRKLQRELRTAQDKIEEMEMTNSHLAKRLEK 555
Cdd:pfam07888 358 qlsESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLET 403
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
472-567 |
8.83e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 38.59 E-value: 8.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 472 ANRQISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAEKRKLQRELRTAQDKIEEMEMTNSHLAK 551
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90
....*....|....*.
gi 1958795722 552 RLEKMKAnrtaLLAQQ 567
Cdd:COG4942 98 ELEAQKE----ELAEL 109
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
284-493 |
9.98e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 38.74 E-value: 9.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 284 LQHKMDELKEGLRQRDELIEENQRLQQKVDTMTKEVFDLQ--ETLLWKDKTIGALEKQkehIACLRNERDVLRE---ELA 358
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQrlAEYSWDEIDVASAERE---IAELEAELERLDAssdDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795722 359 DLQQTVKTAEKhglviipestpngdvnhepvvgAITAVSQEAAQvlesagegpLDVRLRKLAEEKDELLSQIRKLKLQLE 438
Cdd:COG4913 689 ALEEQLEELEA----------------------ELEELEEELDE---------LKGEIGRLEKELEQAEEELDELQDRLE 737
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1958795722 439 EERQKCSRNDGMSGDLAGLQNGSDLQFIEMQRDANRQISEYKFKLSKAEQDIATL 493
Cdd:COG4913 738 AAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERA 792
|
|
| |
