|
Name |
Accession |
Description |
Interval |
E-value |
| TBC |
smart00164 |
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and ... |
116-324 |
3.65e-83 |
|
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and Gyp7, thereby giving rise to the notion that it performs a GTP-activator activity on Rab-like GTPases.
Pssm-ID: 214540 [Multi-domain] Cd Length: 216 Bit Score: 263.78 E-value: 3.65e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 116 VHKGIPHHFRAIVWQLLCSAQSMPI---KDQYSELLKMTSPCEKL----IRRDIARTYPEHNFFKEKDSLGQEVLFNVMK 188
Cdd:smart00164 1 VRKGVPPSLRGVVWKLLLNAQPMDTsadKDLYSRLLKETAPDDKSivhqIEKDLRRTFPEHSFFQDKEGPGQESLRRVLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 189 AYSLVDREVGYCQGSAFIVGLLLMQMP-EEEAFCVFVKLMQDYRLReLFKPSMAELGLCMYQFECMIQEHLPELFVHFQS 267
Cdd:smart00164 81 AYALYNPEVGYCQGMNFLAAPLLLVMEdEEDAFWCLVKLMERYGPN-FYLPDMSGLQLDLLQLDRLVKEYDPDLYKHLKD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1785914762 268 QSFHTSMYASSWFLTIFLTTFPLPIATRIFDIFMSEGLEIVFRVGLALLQMNQAELM 324
Cdd:smart00164 160 LGITPSLYALRWFLTLFARELPLEIVLRIWDVLFAEGSDFLFRVALALLKLHRDVLL 216
|
|
| RabGAP-TBC |
pfam00566 |
Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are ... |
156-324 |
2.74e-55 |
|
Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are GTPase activator proteins of yeast Ypt6 and Ypt7, implies that these domains are GTPase activator proteins of Rab-like small GTPases.
Pssm-ID: 459855 Cd Length: 178 Bit Score: 187.85 E-value: 2.74e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 156 KLIRRDIARTYPEHNFFKEKDslGQEVLFNVMKAYSLVDREVGYCQGSAFIVGLLLMQ-MPEEEAFCVFVKLMQDYRLRE 234
Cdd:pfam00566 10 EQIEKDVPRTFPHSFFFDNGP--GQNSLRRILKAYSIYNPDVGYCQGMNFIAAPLLLVyLDEEDAFWCFVSLLENYLLRD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 235 LFKPSMAELGLCMYQFECMIQEHLPELFVHFQSQSFHTSMYASSWFLTIFLTTFPLPIATRIFDIFMSEGLEIV-FRVGL 313
Cdd:pfam00566 88 FYTPDFPGLKRDLYVFEELLKKKLPKLYKHLKELGLDPDLFASQWFLTLFAREFPLSTVLRIWDYFFLEGEKFVlFRVAL 167
|
170
....*....|.
gi 1785914762 314 ALLQMNQAELM 324
Cdd:pfam00566 168 AILKRFREELL 178
|
|
| COG5210 |
COG5210 |
GTPase-activating protein [General function prediction only]; |
87-333 |
1.71e-43 |
|
GTPase-activating protein [General function prediction only];
Pssm-ID: 227535 [Multi-domain] Cd Length: 496 Bit Score: 164.59 E-value: 1.71e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 87 EEDSWILWGRIVN-EWEDVRKKKEKQVKELVHKGIPHHFRAIVWQLLCSAQSM--PIKDQYSELLKM-------TSPCEK 156
Cdd:COG5210 179 ELAADKLWISYLDpNPLSFLPVQLSKLRELIRKGIPNELRGDVWEFLLGIGFDldKNPGLYERLLNLhreakipTQEIIS 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 157 LIRRDIARTYPEHNFFKEKDSLGQEVLFNVMKAYSLVDREVGYCQGSAFIVGLLLMQMPEEE-AFCVFVKLMQDYRLREL 235
Cdd:COG5210 259 QIEKDLSRTFPDNSLFQTEISIRAENLRRVLKAYSLYNPEVGYVQGMNFLAAPLLLVLESEEqAFWCLVKLLKNYGLPGY 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 236 FKPSMAELGLCMYQFECMIQEHLPELFVHFQSQSFHTSMYASSWFLTIFLTTFPLPIATRIFDIFMSEGLEIVFRVGLAL 315
Cdd:COG5210 339 FLKNLSGLHRDLKVLDDLVEELDPELYEHLLREGVVLLMFAFRWFLTLFVREFPLEYALRIWDCLFLEGSSMLFQLALAI 418
|
250
....*....|....*...
gi 1785914762 316 LQMNQAELMQLDMEGMLQ 333
Cdd:COG5210 419 LKLLRDKLLKLDSDELLD 436
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
362-642 |
7.16e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 78.83 E-value: 7.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 362 KKMKKLEKEYTTIKTKEMEEQVEIKRLRTENRLLKQRIETLEKESASLADRLIQGQVTRAQEAEENYLIKRELATIKQQS 441
Cdd:COG1196 260 AELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 442 DEASAKLEQAENTIRKLQHQQQWLEKELVQARLSEAESQCALKEMQDKVLDIEKRNNSLpdENNIARLQEELIAVKLREA 521
Cdd:COG1196 340 EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL--AAQLEELEEAEEALLERLE 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 522 EAIMGLKELRQQVKDLEEhwqrhlarttgrwkdppkknAMNELQDELMTIRLREAETQAEIREIKQRMMEMETQNQINSN 601
Cdd:COG1196 418 RLEEELEELEEALAELEE--------------------EEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA 477
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1785914762 602 HLRRAEQEVISLQEKVQYLSAQNKGLLTQLSEAKRKQAEIE 642
Cdd:COG1196 478 ALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAG 518
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
380-673 |
7.49e-13 |
|
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: 72.40 E-value: 7.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 380 EEQVEIKRLRTENRLLKQRIETLEKESASLADRLIQGQvtraqeaEENYLIKRELATIKQQSDEASAKLEQAENTIRKLQ 459
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELE-------EELEQLRKELEELSRQISALRKDLARLEAEVEQLE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 460 HQQQWLEKELVQARLSEAESQCALKEMQDKVLDIEKRNNSLpdENNIARLQEELIAVKLREAEAIMGLKELRQQVKDLEE 539
Cdd:TIGR02168 747 ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEEL--EAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 540 HWQRHLARTTGrwkdppKKNAMNELQDELMTIRLREAETQAEIREIKQRMMEMETQNQINSNHLRRAEQEVISLQEKVQY 619
Cdd:TIGR02168 825 RLESLERRIAA------TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEE 898
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1785914762 620 LSAQNKGLLTQLSEAKRKQaeIECKKEEGKLQGQLNKSDSNqyIGELKDQIAEL 673
Cdd:TIGR02168 899 LSEELRELESKRSELRREL--EELREKLAQLELRLEGLEVR--IDNLQERLSEE 948
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
402-678 |
2.57e-12 |
|
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: 70.87 E-value: 2.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 402 LEKESASLADRLiqgqvtRAQEAEENYLIKrELATIKQQSDEASAKLEQAENTIRKLQHQQQWLEKELVQARLSEAESQC 481
Cdd:TIGR02169 672 EPAELQRLRERL------EGLKRELSSLQS-ELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEE 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 482 ALKEMQDKVLDIEKRNNSLpdENNIARLQEELIAVKLREAE-----AIMGLKELRQQVKDLEEHWQR------HLARTTG 550
Cdd:TIGR02169 745 DLSSLEQEIENVKSELKEL--EARIEELEEDLHKLEEALNDlearlSHSRIPEIQAELSKLEEEVSRiearlrEIEQKLN 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 551 RwKDPPKKNA---MNELQDELMTIRLREAETQAEIREIKQRMMEMETQnqinsnhLRRAEQEVISLQEKVQYLSAQNKGL 627
Cdd:TIGR02169 823 R-LTLEKEYLekeIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE-------LEELEAALRDLESRLGDLKKERDEL 894
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1785914762 628 LTQLSEAKRKQAEIECKKEEGKlqgqLNKSDSNQYIGELKDQIAELNHELR 678
Cdd:TIGR02169 895 EAQLRELERKIEELEAQIEKKR----KRLSELKAKLEALEEELSEIEDPKG 941
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
363-683 |
3.25e-12 |
|
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: 70.47 E-value: 3.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 363 KMKKLEKEYTTIKTKEMEEQVEikRLRTEnrlLKQRIETLEKEsASLADRLiqgqvtRAQEAEENYLikrELATIKQQSD 442
Cdd:TIGR02168 171 KERRKETERKLERTRENLDRLE--DILNE---LERQLKSLERQ-AEKAERY------KELKAELREL---ELALLVLRLE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 443 EASAKLEQAENTIRKLQHQQQWLEKELVQARLSEAESQCALKEMQDKVLDIEKRNNSLPD-----ENNIARLQEELIAVK 517
Cdd:TIGR02168 236 ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANeisrlEQQKQILRERLANLE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 518 LREAEAIMGLKELRQQVKDLEE---HWQRHLARTTGRWKDppKKNAMNELQDELMTIRLREAETQAEIREIKQRMMEMET 594
Cdd:TIGR02168 316 RQLEELEAQLEELESKLDELAEelaELEEKLEELKEELES--LEAELEELEAELEELESRLEELEEQLETLRSKVAQLEL 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 595 QNQINSNHLRRAEQEVISLQEKVQYLSAQNKGLLTQLSEAKRKQAEIEC-KKEEGKLQGQLNKSDSNQYIGELKDQIAEL 673
Cdd:TIGR02168 394 QIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELeELEEELEELQEELERLEEALEELREELEEA 473
|
330
....*....|
gi 1785914762 674 NHELRCLKGQ 683
Cdd:TIGR02168 474 EQALDAAERE 483
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
379-635 |
1.89e-10 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 64.27 E-value: 1.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 379 MEEQVEIKRLRTENRL--LKQRIETLEKesasladrliqgQVTRAQEAEENYLIKRELATIKQQSDEASAKLEQaentir 456
Cdd:COG3206 162 LEQNLELRREEARKALefLEEQLPELRK------------ELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSE------ 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 457 klqhqqqwLEKELVQARLSEAESQCALKEMQDKVLDIEKRNNSLPDENNIARLQEELIAVKLREAEAIMGL-------KE 529
Cdd:COG3206 224 --------LESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYtpnhpdvIA 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 530 LRQQVKDLEEHWQRHLARttgrwkdppkknAMNELQDELMTIRLREAETQAEIREIKQRMMEmetqnqinsnhLRRAEQE 609
Cdd:COG3206 296 LRAQIAALRAQLQQEAQR------------ILASLEAELEALQAREASLQAQLAQLEARLAE-----------LPELEAE 352
|
250 260
....*....|....*....|....*.
gi 1785914762 610 VISLQEKVQYLSAQNKGLLTQLSEAK 635
Cdd:COG3206 353 LRRLEREVEVARELYESLLQRLEEAR 378
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
361-649 |
8.61e-10 |
|
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: 62.39 E-value: 8.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 361 SKKMKKLEKEYTTIKTKEMEEQVEIKRLRTENRLLKQRIETLEKESASLADRLIQGQVTRAQEAEENYLIKRELATIKQQ 440
Cdd:TIGR02169 680 RERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSE 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 441 SDEASAKLEQAENTIRKLQHQQQWLEKELVQARLSEAESQcaLKEMQDKVLDIEKRNNSLPDENNiARLQEELIAVKLRE 520
Cdd:TIGR02169 760 LKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAE--LSKLEEEVSRIEARLREIEQKLN-RLTLEKEYLEKEIQ 836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 521 aeaimglkELRQQVKDLEEhwqrhlarttgrwkdppkKNAMNELQDELMTIRLRE-----AETQAEIREIKQRMMEMETQ 595
Cdd:TIGR02169 837 --------ELQEQRIDLKE------------------QIKSIEKEIENLNGKKEEleeelEELEAALRDLESRLGDLKKE 890
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1785914762 596 NQINSNHLRRAEQEVISLQEKVQYLSAQNKGLLTQLSEAKRKQAEIECKKEEGK 649
Cdd:TIGR02169 891 RDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDE 944
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
362-670 |
4.95e-09 |
|
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: 60.07 E-value: 4.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 362 KKMKKLEKEYTTIKTKEMEEQVEIKRLRTENRLLKQRIETLEKESASLADrliqgqvtraqeaeenylikrELATIKQQS 441
Cdd:TIGR02168 274 LEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEA---------------------QLEELESKL 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 442 DEASAKLEQaentirkLQHQQQWLEKELVQARLSEAESQCALKEMQDKVLDIEKRNNSLPDENNIARLQEELIAVKLREA 521
Cdd:TIGR02168 333 DELAEELAE-------LEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERL 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 522 EAimglkelrqQVKDLEEHWQRHLARTTGRWKDpPKKNAMNELQDELMTIRLREAETQAEIREIKQRMMEMETQnqinsn 601
Cdd:TIGR02168 406 EA---------RLERLEDRRERLQQEIEELLKK-LEEAELKELQAELEELEEELEELQEELERLEEALEELREE------ 469
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1785914762 602 hLRRAEQEVISLQEKVQYLSAQNKGLLTQLSEAKRKQaeieckkeEGKLQGQLNKSDSNQYIGELKDQI 670
Cdd:TIGR02168 470 -LEEAEQALDAAERELAQLQARLDSLERLQENLEGFS--------EGVKALLKNQSGLSGILGVLSELI 529
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
348-681 |
1.76e-08 |
|
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: 58.11 E-value: 1.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 348 DKLIQAAYQVKYNSKKMKKLEKEYTTIKTKEMEEQVEIKRLRTENRLLKQRIETLEKESASLAdrliqgqvtraQEAEEN 427
Cdd:TIGR04523 239 QEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLN-----------NQKEQD 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 428 YL--IKRELATIKQQSDEASAKLEQAENTIRKLQHQQQWLEKELVQARLSEAESQCALKEMQDKVLDIEKRNNSLPDE-- 503
Cdd:TIGR04523 308 WNkeLKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEik 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 504 ---NNIARLQEELIAVKLREAEAIMGLKELRQQVKDLEEHWQRHLARTT---GRWKDPPKKNAMNELQDELMTIRLREAE 577
Cdd:TIGR04523 388 nleSQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIknnSEIKDLTNQDSVKELIIKNLDNTRESLE 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 578 TQAEIREIKQRmmEMETQNQINSNHLRRAEQEVISLQEKVQYLSAQNKGLLTQLSEAKRKQAEIECKKEE-----GKLQG 652
Cdd:TIGR04523 468 TQLKVLSRSIN--KIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEkeskiSDLED 545
|
330 340
....*....|....*....|....*....
gi 1785914762 653 QLNKSDSNQYIGELKDQIAELNHELRCLK 681
Cdd:TIGR04523 546 ELNKDDFELKKENLEKEIDEKNKEIEELK 574
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
356-676 |
2.00e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.13 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 356 QVKYNSKKMKKLEKEYTTIKTKEMEEQVEIKRLRTENRLLKQRIETLEKESASLADRLIQGQVTRAQEAEENYLIKRELA 435
Cdd:PRK02224 343 EAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 436 TIKQQSDEASAKLEQAENTIRKlqhQQQWLEK----ELVQArLSEAESQCALKEMQDKVLDIEKRNNSLPDEnnIARLQE 511
Cdd:PRK02224 423 ELREREAELEATLRTARERVEE---AEALLEAgkcpECGQP-VEGSPHVETIEEDRERVEELEAELEDLEEE--VEEVEE 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 512 EL-IAVKLREAEAimGLKELRQQVKDLEEHWQRHLARTTG-RWKDPPKKNAMNELQDELMTIRLREAETQAEIREIKQRM 589
Cdd:PRK02224 497 RLeRAEDLVEAED--RIERLEERREDLEELIAERRETIEEkRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEV 574
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 590 MEMETQNQINSNHLRR-------------AEQEVISLQEKVQYLSAQNKGLLTQLSEAKRKQAEIECKKEEGKLQG-QLN 655
Cdd:PRK02224 575 AELNSKLAELKERIESlerirtllaaiadAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARIEEaRED 654
|
330 340
....*....|....*....|.
gi 1785914762 656 KSDSNQYIGELKDQIAELNHE 676
Cdd:PRK02224 655 KERAEEYLEQVEEKLDELREE 675
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
358-678 |
2.29e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.64 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 358 KYNSKK---MKKLEKeyttikTKEMEEQVEIkrLRTEnrlLKQRIETLEKEsaslADRLIQGQVTRAQEAE-ENYLIKRE 433
Cdd:COG1196 169 KYKERKeeaERKLEA------TEENLERLED--ILGE---LERQLEPLERQ----AEKAERYRELKEELKElEAELLLLK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 434 LATIKQQSDEASAKLEQAENTIRKLQHQQQWLEKELVQARLSEAESQCALKEMQDKVLDIEKRnnslpdennIARLQEEL 513
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE---------LARLEQDI 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 514 IAVKLREAEAimglkelrqqvkdleehwqrhlarttgrwkdppkKNAMNELQDELMTIRLREAETQAEIREIKQRMMEME 593
Cdd:COG1196 305 ARLEERRREL----------------------------------EERLEELEEELAELEEELEELEEELEELEEELEEAE 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 594 TQNQINSNHLRRAEQEVISLQEKVQYLSAQNKGLLTQLSEAKRKQAEIECKKEEGKLQGQLNKSDSNQYIGELKDQIAEL 673
Cdd:COG1196 351 EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
|
....*
gi 1785914762 674 NHELR 678
Cdd:COG1196 431 AELEE 435
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
444-656 |
5.00e-08 |
|
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: 55.93 E-value: 5.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 444 ASAKLEQAENTIRKLQHQQQWLEKELVQARLSEAESQCALKEMQDKVLDIEKRNNSLpdENNIARLQEELIAVKLREAEA 523
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAL--EQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 524 IMGLKELRQQVKDLEEHWQRHLARTTGRW----KDPPKKNAMNELQDELMTIRLREAEtqaEIREIKQRMMEMETQNQIN 599
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLGRQPPLALllspEDFLDAVRRLQYLKYLAPARREQAE---ELRADLAELAALRAELEAE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1785914762 600 SNHLRRAEQEVISLQEKVQYLSAQNKGLLTQL-SEAKRKQAEI-ECKKEEGKLQGQLNK 656
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLeKELAELAAELaELQQEAEELEALIAR 231
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
349-651 |
7.48e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.30 E-value: 7.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 349 KLIQAAYQVKYNSKKMKKLEKEYTTIKTKEMEEQVEIKRLRTENRLLKQRIETLEKESASL--ADRLIQG--QVTRAQEA 424
Cdd:PTZ00121 1357 DEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKkkADEAKKKaeEKKKADEA 1436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 425 EENYLIKRELATIKQQSDEAsaklEQAENTIRKLQHQQQW--LEKELVQARLSEaESQCALKEMQDKVLDIEKRNNSLPD 502
Cdd:PTZ00121 1437 KKKAEEAKKADEAKKKAEEA----KKAEEAKKKAEEAKKAdeAKKKAEEAKKAD-EAKKKAEEAKKKADEAKKAAEAKKK 1511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 503 ENNIARLQEELIAVKLREAEAIMGLKELR--QQVKDLEEHWQRHLARTTGRWKDPPKKNAMNElqDELMTIRLREAETQA 580
Cdd:PTZ00121 1512 ADEAKKAEEAKKADEAKKAEEAKKADEAKkaEEKKKADELKKAEELKKAEEKKKAEEAKKAEE--DKNMALRKAEEAKKA 1589
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1785914762 581 EIREIKQRMMEMETQNQINSNHLRRAEQEVISLQE--KVQYLSAQNKGLLTQLSEAKRKQAEIECKKEEGKLQ 651
Cdd:PTZ00121 1590 EEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEElkKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIK 1662
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
396-678 |
2.71e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.54 E-value: 2.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 396 KQRIETLEKESASLADRL--IQGQVTRAQEAEENYLIKRELATIKQQSDEASAKLEQAENTIRKLQHQQQWLEK-----E 468
Cdd:COG4913 609 RAKLAALEAELAELEEELaeAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDAssddlA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 469 LVQARLSEAESQcaLKEMQDKVLDIEKRNNSLpdENNIARLQEELIAVKLREAEAIMGLKElrQQVKDLEEHWQRHLART 548
Cdd:COG4913 689 ALEEQLEELEAE--LEELEEELDELKGEIGRL--EKELEQAEEELDELQDRLEAAEDLARL--ELRALLEERFAAALGDA 762
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 549 TGRwkdppkkNAMNELQDELMTIRLREAETQAEIREIKQRmmemetqnqinsnHLRRAEQEVISLQEKVQYLSAQNKgLL 628
Cdd:COG4913 763 VER-------ELRENLEERIDALRARLNRAEEELERAMRA-------------FNREWPAETADLDADLESLPEYLA-LL 821
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1785914762 629 TQLS-------EAKRKQAEIECKKEE-GKLQGQLNKSdsnqyIGELKDQIAELNHELR 678
Cdd:COG4913 822 DRLEedglpeyEERFKELLNENSIEFvADLLSKLRRA-----IREIKERIDPLNDSLK 874
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
446-642 |
3.58e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.87 E-value: 3.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 446 AKLEQAENTIrklqhqqQWLEKEL--VQARLSEAESqcALKEMQDK--VLDIEKRNNSLpdENNIARLQEELIAVKLREA 521
Cdd:COG3206 168 LRREEARKAL-------EFLEEQLpeLRKELEEAEA--ALEEFRQKngLVDLSEEAKLL--LQQLSELESQLAEARAELA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 522 EAIMGLKELRQQvkdleehwqrhLARTTGRWKDPPKKNAMNELQDELMTIRLREAETQA-------EIREIKQRMMEMET 594
Cdd:COG3206 237 EAEARLAALRAQ-----------LGSGPDALPELLQSPVIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRA 305
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1785914762 595 Q-NQINSNHLRRAEQEVISLQEKVQYLSAQNKGLLTQLSEAKRKQAEIE 642
Cdd:COG3206 306 QlQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELR 354
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
317-646 |
4.36e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 53.58 E-value: 4.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 317 QMNQAELMQLDMEGMLQHFQKVIphqfdgvpdkliqaayqVKYNSKKMKKLEKE--YTTIKTKEMEEQVE--IKRLRTEN 392
Cdd:pfam15921 171 QIEQLRKMMLSHEGVLQEIRSIL-----------------VDFEEASGKKIYEHdsMSTMHFRSLGSAISkiLRELDTEI 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 393 RLLKQRI-------ETLEKESASLADRLIQGQVTRAQEaeenyLIKRELATIKQQSDEASAKLEQAENTIRKLQHQQQwl 465
Cdd:pfam15921 234 SYLKGRIfpvedqlEALKSESQNKIELLLQQHQDRIEQ-----LISEHEVEITGLTEKASSARSQANSIQSQLEIIQE-- 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 466 ekelvQARLSEAESQCALKEMQDKV--LDIEKRNNSLPDENNIARLQEELIAVKLREAEAIMGLKELRQQVKDLEEHWQR 543
Cdd:pfam15921 307 -----QARNQNSMYMRQLSDLESTVsqLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQK 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 544 HLArttgrwkdppkknamnelqdelmTIRLREAETQAEiREIKQRMMEMETQNQINSNHLRRaeqEVISLQEKVQYLSAQ 623
Cdd:pfam15921 382 LLA-----------------------DLHKREKELSLE-KEQNKRLWDRDTGNSITIDHLRR---ELDDRNMEVQRLEAL 434
|
330 340
....*....|....*....|....
gi 1785914762 624 NKGLLTQLS-EAKRKQAEIECKKE 646
Cdd:pfam15921 435 LKAMKSECQgQMERQMAAIQGKNE 458
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
431-686 |
5.02e-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: 5.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 431 KRELATIKQQSDEASAKLEQAENTIRKLQHQQQWLEK-ELVQARLSEAESQCALKEMQDKVLDIEKRNNSLPD-ENNIAR 508
Cdd:TIGR02169 176 LEELEEVEENIERLDLIIDEKRQQLERLRREREKAERyQALLKEKREYEGYELLKEKEALERQKEAIERQLASlEEELEK 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 509 LQEELIAVKLREAEAIMGLKELRQQVKDLEEHWQRHLARTTGRWKDPPK--KNAMNELQDELMTIRLREAETQAEIREIK 586
Cdd:TIGR02169 256 LTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIAslERSIAEKERELEDAEERLAKLEAEIDKLL 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 587 QRMMEMETQNQINSNHLRRAEQEVISLQEKVQYLSAQNKGLLTQLSEAKRKQAEIECKKEegklqgqlnksDSNQYIGEL 666
Cdd:TIGR02169 336 AEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLE-----------KLKREINEL 404
|
250 260
....*....|....*....|
gi 1785914762 667 KDQIAELNHELRCLKGQRGF 686
Cdd:TIGR02169 405 KRELDRLQEELQRLSEELAD 424
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
352-536 |
5.11e-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: 5.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 352 QAAYQVKYNSKK--MKKLEKEYTTIKTKEMEEQVEIKRLRTENRLLKQRIETLEKESASLADRLIQGQVTRAQEAEENYL 429
Cdd:TIGR02169 324 LAKLEAEIDKLLaeIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINE 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 430 IKRELATIKQQSDEASAKLEQAENTIRKLQHQQQWLEKELVQARLSEAESQCALKEMQDKVLDIEKRNNSLpdENNIARL 509
Cdd:TIGR02169 404 LKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDL--KEEYDRV 481
|
170 180
....*....|....*....|....*..
gi 1785914762 510 QEELIAVKLREAEAIMGLKELRQQVKD 536
Cdd:TIGR02169 482 EKELSKLQRELAEAEAQARASEERVRG 508
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
494-684 |
8.38e-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: 52.75 E-value: 8.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 494 EKRNNSLPDENNIARLQEELIAVKLREAEAIMGLKELRQQVKDLEEhwQRHLARTTGRWKDPPKKNAMNELQDELMTIRL 573
Cdd:TIGR02168 667 KTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEE--ELEQLRKELEELSRQISALRKDLARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 574 RE---AETQAEIREIKQRMMEMETQNQINSNHLRRAEQEVISLQEKVQYLSAQNKGLLTQLSEAKRKQAEIE---CKKEE 647
Cdd:TIGR02168 745 LEeriAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNeeaANLRE 824
|
170 180 190
....*....|....*....|....*....|....*..
gi 1785914762 648 GKLQGQLNKSDSNQYIGELKDQIAELNHELRCLKGQR 684
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEI 861
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
362-683 |
1.34e-06 |
|
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: 51.94 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 362 KKMKKLEKEYTTIKTKEMEEQVEIKRLRTENRLLKQRIETLEKESASLADRL--IQGQV--TRAQEAEENYLIKrELATI 437
Cdd:TIGR04523 131 KQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKlnIQKNIdkIKNKLLKLELLLS-NLKKK 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 438 KQQSDEASAKLEQAENTIRKLQHQQQWLEKELVQ--ARLSEAESQC---------ALKEMQDKVLDIEKRNNSLPD-ENN 505
Cdd:TIGR04523 210 IQKNKSLESQISELKKQNNQLKDNIEKKQQEINEktTEISNTQTQLnqlkdeqnkIKKQLSEKQKELEQNNKKIKElEKQ 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 506 IARLQEELIAVKLREAEAIMglKELRQQVKDleehwqrhlarttgrwkdppKKNAMNELQDELMTIRLREAETQAEIREI 585
Cdd:TIGR04523 290 LNQLKSEISDLNNQKEQDWN--KELKSELKN--------------------QEKKLEEIQNQISQNNKIISQLNEQISQL 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 586 KQRMMEMETQNQINSNHLRRAEQEVISLQEKVQYLSAQNKGLLTQLSEAKRK--QAEIECKKEEGKLQG-QLNKSDSNQY 662
Cdd:TIGR04523 348 KKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKiqNQEKLNQQKDEQIKKlQQEKELLEKE 427
|
330 340
....*....|....*....|.
gi 1785914762 663 IGELKDQIAELNHELRCLKGQ 683
Cdd:TIGR04523 428 IERLKETIIKNNSEIKDLTNQ 448
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
352-601 |
1.64e-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: 51.98 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 352 QAAYQVKYNSKKMKKLEKEYTTIKTKEMEEQVEIKRLRTENRLLKQRIETLEKESASLADRL--IQGQVTRAQEAEENyl 429
Cdd:TIGR02168 793 QLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIesLAAEIEELEELIEE-- 870
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 430 IKRELATIKQQSDEASAKLEQAENTIRKLQHQQQWLEKELVQARLseaesqcALKEMQDKVLDIEKRNNSLpdENNIARL 509
Cdd:TIGR02168 871 LESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRR-------ELEELREKLAQLELRLEGL--EVRIDNL 941
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 510 QEELIAVKLREAEAIMGLKELrqqVKDLEEHWQRHLARTTGRWKD--PPKKNAMNELQDElmTIRLREAETQAE------ 581
Cdd:TIGR02168 942 QERLSEEYSLTLEEAEALENK---IEDDEEEARRRLKRLENKIKElgPVNLAAIEEYEEL--KERYDFLTAQKEdlteak 1016
|
250 260
....*....|....*....|....*...
gi 1785914762 582 ------IREIKQRMME--METQNQINSN 601
Cdd:TIGR02168 1017 etleeaIEEIDREARErfKDTFDQVNEN 1044
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
357-685 |
1.79e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.60 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 357 VKYNSKKMKKLEKEYTTIKTKEMEEQVEIKRLRTENRLLKQRIETLEKESASLADRLiqGQVTRAQEAEENYL-IKRELA 435
Cdd:PRK03918 226 LEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKV--KELKELKEKAEEYIkLSEFYE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 436 TIKQQSDEASAKLEQAENTIRKLQHQQQWLEKElvQARLSEAESQcaLKEMQDKVLDIEKRNNSLPD------------- 502
Cdd:PRK03918 304 EYLDELREIEKRLSRLEEEINGIEERIKELEEK--EERLEELKKK--LKELEKRLEELEERHELYEEakakkeelerlkk 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 503 ---ENNIARLQEELIAVKLREAEAIMGLKELRQQVKDLE-EHWQRHLA-----------RTTGR-WKDPPKKNAMNELQD 566
Cdd:PRK03918 380 rltGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKkEIKELKKAieelkkakgkcPVCGReLTEEHRKELLEEYTA 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 567 ELMTIRLREAETQAEIREIKQRMMEMETqnqinsnhLRRAEQEVISLQEKVQYL-SAQNKGLLTQLSEAKRKQAEIECKK 645
Cdd:PRK03918 460 ELKRIEKELKEIEEKERKLRKELRELEK--------VLKKESELIKLKELAEQLkELEEKLKKYNLEELEKKAEEYEKLK 531
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1785914762 646 EE-GKLQGQL-NKSDSNQYIGELKDQIAELNHELRCLKGQRG 685
Cdd:PRK03918 532 EKlIKLKGEIkSLKKELEKLEELKKKLAELEKKLDELEEELA 573
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
395-650 |
4.32e-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: 49.76 E-value: 4.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 395 LKQRIETLEKESASLADRLIQgqvtraqeaeenylIKRELATIKQQSDEASAKLEQAENTIRKLQHQQQWLEKELVQARL 474
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAA--------------LKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 475 SEAESQCALKEMQDkvlDIEKRNNSLPDENNIARLQEELIAVKLREAE-AIMGLKELRQQVKDLEEHWQRHLARTTGrwk 553
Cdd:COG4942 91 EIAELRAELEAQKE---ELAELLRALYRLGRQPPLALLLSPEDFLDAVrRLQYLKYLAPARREQAEELRADLAELAA--- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 554 dppKKNAMNELQDELMTIRlreAETQAEIREIKQRMMEMETQNQINSNHLRRAEQEVISLQEKVQYLSAQNKGLLTQLSE 633
Cdd:COG4942 165 ---LRAELEAERAELEALL---AELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
250
....*....|....*..
gi 1785914762 634 AKRKQAEIECKKEEGKL 650
Cdd:COG4942 239 AAERTPAAGFAALKGKL 255
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
385-684 |
4.44e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.42 E-value: 4.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 385 IKRLR--TENRLLKQRIETLEKESASLADRL--IQGQVTRAQEAEENYLIKRELAtiKQQSDEASAKLEQAENTIRKLQH 460
Cdd:PRK02224 178 VERVLsdQRGSLDQLKAQIEEKEEKDLHERLngLESELAELDEEIERYEEQREQA--RETRDEADEVLEEHEERREELET 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 461 QQQWLEKelVQARLSEAESQC-----ALKEMQDKVLDIEKRNNSLPDENNIARLQEELIAVKL-----REAEAIMGLKEL 530
Cdd:PRK02224 256 LEAEIED--LRETIAETEREReelaeEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARReeledRDEELRDRLEEC 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 531 RQQVKDLEEHWQRHLARTT---GRWKDppKKNAMNELQDELMTIRLREAETQAEIREIKQRMMEMETQNQINSNHLRRAE 607
Cdd:PRK02224 334 RVAAQAHNEEAESLREDADdleERAEE--LREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAE 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 608 QEVISLQEKVQYLSAQNKGLLTQLSEAKRKQAEIECKKEEGKLQ--GQ-LNKSDSNQYIGELKDQIAELNHELRCLKGQR 684
Cdd:PRK02224 412 DFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPecGQpVEGSPHVETIEEDRERVEELEAELEDLEEEV 491
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
360-539 |
9.51e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 9.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 360 NSKKMKKLEKEYTTIKTKEMEEQVEIKRLRTenrlLKQRIETLEKESASLADRLiqGQVTRAQEAEENYLIKRELATIKQ 439
Cdd:COG4717 69 NLKELKELEEELKEAEEKEEEYAELQEELEE----LEEELEELEAELEELREEL--EKLEKLLQLLPLYQELEALEAELA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 440 QSDEASAKLEQAENTIRKLQHQQQWLEKELVQARlseaesqcalkemqdKVLDIEKRNNSLPDENNIARLQEELIAVKLR 519
Cdd:COG4717 143 ELPERLEELEERLEELRELEEELEELEAELAELQ---------------EELEELLEQLSLATEEELQDLAEELEELQQR 207
|
170 180
....*....|....*....|
gi 1785914762 520 EAEAIMGLKELRQQVKDLEE 539
Cdd:COG4717 208 LAELEEELEEAQEELEELEE 227
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
377-588 |
9.93e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 9.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 377 KEMEEQVEIKRLRTENRLLKQRIETLEKESASLADrliqgqvtraqeaeenylikrELATIKQQSDEASAKLEQAENTIR 456
Cdd:COG4913 275 EYLRAALRLWFAQRRLELLEAELEELRAELARLEA---------------------ELERLEARLDALREELDELEAQIR 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 457 KLQHQQqwleKELVQARLSEAESQcaLKEMQDKVldiekrnnslpdenniARLQEELIAVKLREAEAIMGLKELRQQVKD 536
Cdd:COG4913 334 GNGGDR----LEQLEREIERLERE--LEERERRR----------------ARLEALLAALGLPLPASAEEFAALRAEAAA 391
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1785914762 537 LEEHWQRHLARTTgrwkdppkkNAMNELQDELMTIRLREAETQAEIREIKQR 588
Cdd:COG4913 392 LLEALEEELEALE---------EALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
366-647 |
2.60e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 366 KLEKEYTTIKTKEMEEQVEIKRLRTENRLLKQRIETLEK-----ESASLADRLIQGQVTRAQEAE--ENYL-----IKRE 433
Cdd:PRK03918 388 KLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKaieelKKAKGKCPVCGRELTEEHRKEllEEYTaelkrIEKE 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 434 LATIKQQSDEASAKLEQAENTI---------RKLQHQQQWLEKELVQARLSEAESQCA-LKEMQDKVLDIEKRNNSLPDE 503
Cdd:PRK03918 468 LKEIEEKERKLRKELRELEKVLkkeseliklKELAEQLKELEEKLKKYNLEELEKKAEeYEKLKEKLIKLKGEIKSLKKE 547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 504 -NNIARLQEELIAV--KLREAEAIMG-------------LKELRQQVKDLEEHWQRHLARTTGRWKDPPKKNAMNELQDE 567
Cdd:PRK03918 548 lEKLEELKKKLAELekKLDELEEELAellkeleelgfesVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEE 627
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 568 LMTIRLREAETQAEIREIKQRMMEMEtqNQINSNHLRRAEQEVISLQEKVQYLSAQNKGLLTQLSEAKRKQAEIECKKEE 647
Cdd:PRK03918 628 LDKAFEELAETEKRLEELRKELEELE--KKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEE 705
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
348-529 |
2.94e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 2.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 348 DKLIQAAYQVKYNSKKMKKLEKEYTTIKTKEMEEQVEIKRLRTENRLLKQRIETLEKESASLADRLIQGQVTRAQEAEEN 427
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 428 Y--------------------LIKReLATIKQQSDEASAKLEQAENTIRKLQHQQQWLEKELVQARLSEAESQCALKEMQ 487
Cdd:COG3883 96 YrsggsvsyldvllgsesfsdFLDR-LSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1785914762 488 DKVLDIEKRNNSLPDENNIARLQEELIAVKLREAEAIMGLKE 529
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
361-667 |
7.75e-05 |
|
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: 46.26 E-value: 7.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 361 SKKMKKLEKEYT----TIKTKEMEEQVE-----IKRLRTENRLLKQRIETLEKESASLADRLIQGQVTRAQEAEENYLIK 431
Cdd:pfam15921 486 AKKMTLESSERTvsdlTASLQEKERAIEatnaeITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIE 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 432 relaTIKQQSDEASAKLEQAENTIRKLQHQQQWLEKELVQARLSEAESQcALKEMQD-KVLDIEKRNNSLpdenniarlq 510
Cdd:pfam15921 566 ----ILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFK-ILKDKKDaKIRELEARVSDL---------- 630
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 511 eELIAVKLREA--EAIMGLKELRQQVKDL--EEHWQRHLARTTGRWKDPPKKNAMNELQDELMT---IRLREAETQAEIR 583
Cdd:pfam15921 631 -ELEKVKLVNAgsERLRAVKDIKQERDQLlnEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTtnkLKMQLKSAQSELE 709
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 584 EIKQRMMEME------------TQNQINSNhlrraEQEVISLQEKVQYLSaqnkgllTQLSEAKRKQAEIecKKEEGKLQ 651
Cdd:pfam15921 710 QTRNTLKSMEgsdghamkvamgMQKQITAK-----RGQIDALQSKIQFLE-------EAMTNANKEKHFL--KEEKNKLS 775
|
330
....*....|....*...
gi 1785914762 652 GQLNK--SDSNQYIGELK 667
Cdd:pfam15921 776 QELSTvaTEKNKMAGELE 793
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
391-683 |
2.35e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.95 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 391 ENRL--LKQRIETLEKESASLA-------------DRLIQGQVTRAQEAEENylikRELATIKQQSDEASAKLEQAENTI 455
Cdd:PRK04863 785 EKRIeqLRAEREELAERYATLSfdvqklqrlhqafSRFIGSHLAVAFEADPE----AELRQLNRRRVELERALADHESQE 860
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 456 RklQHQQQW-------------------LEKELVQARLSEAESQcaLKEMQDKVLDIEKRNNSLPD-ENNIARLQ---EE 512
Cdd:PRK04863 861 Q--QQRSQLeqakeglsalnrllprlnlLADETLADRVEEIREQ--LDEAEEAKRFVQQHGNALAQlEPIVSVLQsdpEQ 936
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 513 LIAVKLREAEAIMGLKELRQQVKDLEEHWQR--HLArttgrWKDPPKK-NAMNELQDELMTiRLREAETQAeiREIKQRM 589
Cdd:PRK04863 937 FEQLKQDYQQAQQTQRDAKQQAFALTEVVQRraHFS-----YEDAAEMlAKNSDLNEKLRQ-RLEQAEQER--TRAREQL 1008
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 590 MEMETQnqinsnhLRRAEQEVISLQEkvqylSAQNKglLTQLSEAKRK----------QAEIECKKEEGKLQGQLNKSDS 659
Cdd:PRK04863 1009 RQAQAQ-------LAQYNQVLASLKS-----SYDAK--RQMLQELKQElqdlgvpadsGAEERARARRDELHARLSANRS 1074
|
330 340
....*....|....*....|....
gi 1785914762 660 NqyIGELKDQIAELNHELRCLKGQ 683
Cdd:PRK04863 1075 R--RNQLEKQLTFCEAEMDNLTKK 1096
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
363-641 |
3.47e-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: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 363 KMKKLEKEYTTIKTKEMEEQVEIKR-----LRTENRLLKQRIETLEKESASLADRLIQGQVTRAQEAEENYLIKRELATI 437
Cdd:TIGR02169 773 DLHKLEEALNDLEARLSHSRIPEIQaelskLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSI 852
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 438 KQQSDEASAKLEQAENTIRKLQHQQQWLEKELV--QARLSEAESQcaLKEMQDKVLDIEKrnnslpdENNIARLQEELIA 515
Cdd:TIGR02169 853 EKEIENLNGKKEELEEELEELEAALRDLESRLGdlKKERDELEAQ--LRELERKIEELEA-------QIEKKRKRLSELK 923
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 516 VKLREAEaimglkelrQQVKDLEehwqrhlarttgrwkdpPKKNAMNELQDELMTIRlreaETQAEIREIKQRMMEMETQ 595
Cdd:TIGR02169 924 AKLEALE---------EELSEIE-----------------DPKGEDEEIPEEELSLE----DVQAELQRVEEEIRALEPV 973
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1785914762 596 NQINSNHLRRAEQEVISLQEKVQYLSAQNKGLLTQLSEAKRKQAEI 641
Cdd:TIGR02169 974 NMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
347-539 |
3.83e-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: 3.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 347 PDKLIQAAYQVKYNSKKMKKLEKEYTTIKTKEMEEQVEIKRLRTENRLLKQRIETLEKESASLADRL----IQGQVTRAQ 422
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELaeleKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 423 EAEENYLIKRELATIKQQSDEASAKLEQAENTIRKLQHQQQWLeKELVQARLSEAESQCA-LKEMQDKVLDIEKRNNSLp 501
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYL-KYLAPARREQAEELRAdLAELAALRAELEAERAEL- 176
|
170 180 190
....*....|....*....|....*....|....*...
gi 1785914762 502 dENNIARLQEELIAVKLREAEAIMGLKELRQQVKDLEE 539
Cdd:COG4942 177 -EALLAELEEERAALEALKAERQKLLARLEKELAELAA 213
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
439-612 |
4.08e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 4.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 439 QQSDEASAKLEQAENTIRKLQHQQQwlEKELVQARLSEAESQcaLKEMQDKVLDIEKRNNSLPDENNIARLQEELIAVKL 518
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQE--ELEELEEELEELEAE--LEELREELEKLEKLLQLLPLYQELEALEAELAELPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 519 REAEAIMGLKELRQQVKDLE------EHWQRHLARTTGRWkDPPKKNAMNELQDELMTIRLREAETQAEIREIKQRMMEM 592
Cdd:COG4717 147 RLEELEERLEELRELEEELEeleaelAELQEELEELLEQL-SLATEEELQDLAEELEELQQRLAELEEELEEAQEELEEL 225
|
170 180
....*....|....*....|.
gi 1785914762 593 ETQ-NQINSNHLRRAEQEVIS 612
Cdd:COG4717 226 EEElEQLENELEAAALEERLK 246
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
377-690 |
5.15e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 43.81 E-value: 5.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 377 KEMEEQVEIKRLRTENRLLKQRIETLEKESASLADRLIQGQVTRAQEAEENYLIK-----------RELATIKQQSDEAS 445
Cdd:pfam02463 177 KLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYlklneeridllQELLRDEQEEIESS 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 446 AKLEQAENTIRKLQHQQQWLEKELVQARLSEAESQCALKEMQDKVLDIEKRNNSLPDEnniaRLQEELIAVKLREAEAIM 525
Cdd:pfam02463 257 KQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEE----KLKESEKEKKKAEKELKK 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 526 GLKELRQQVKDLEEHWQRHLARTTGRWKDPPKKNAMNELQDELMTIRLREAETQAEIREIKQRMMEM--ETQNQINSNHL 603
Cdd:pfam02463 333 EKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELksEEEKEAQLLLE 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 604 RRAEQEVISLQEKVQYLS----AQNKGLLTQLSEAKRKQAEIECKKEEGKLQGQLNKSDSN-QYIGELKDQIAELNHELR 678
Cdd:pfam02463 413 LARQLEDLLKEEKKEELEileeEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLlKETQLVKLQEQLELLLSR 492
|
330
....*....|..
gi 1785914762 679 CLKGQRGFSGQP 690
Cdd:pfam02463 493 QKLEERSQKESK 504
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
380-539 |
5.18e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.77 E-value: 5.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 380 EEQVEIKRLRTENRLLKQRIETLEKESASLADRLIQGQVTRAQEAEENYLIKRELATIKQQSDEASAKLEQAENTIRKLQ 459
Cdd:COG1196 624 GRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEE 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 460 HQQQWLEKELVQARLSEAEsqcalKEMQDKVLDIEKRNnslpDENNIARLQEELIAVKLREAEAIMGLKELRQQVKDLEE 539
Cdd:COG1196 704 EEERELAEAEEERLEEELE-----EEALEEQLEAEREE----LLEELLEEEELLEEEALEELPEPPDLEELERELERLER 774
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
429-613 |
5.33e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 5.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 429 LIKRELATIKQQSDEASAKLEQAENTIRKLQHQQQwlEKELVQARLSEAESQCALKEMQDKVLDIEKRNNSLpdENNIAR 508
Cdd:COG4717 68 LNLKELKELEEELKEAEEKEEEYAELQEELEELEE--ELEELEAELEELREELEKLEKLLQLLPLYQELEAL--EAELAE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 509 LQEELIAVKLREA---EAIMGLKELRQQVKDLEEHWQRHLARTTGRWKDPPKKNA--MNELQDELMTIRLREAETQAEIR 583
Cdd:COG4717 144 LPERLEELEERLEelrELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAeeLEELQQRLAELEEELEEAQEELE 223
|
170 180 190
....*....|....*....|....*....|
gi 1785914762 584 EIKQRMMEMETQNQINSNHLRRAEQEVISL 613
Cdd:COG4717 224 ELEEELEQLENELEAAALEERLKEARLLLL 253
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
390-676 |
5.58e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.49 E-value: 5.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 390 TENRLLKQRIETLEKESASLADRLIQGQVTRAQEAEENYLIKRELATIKQQSDEASAKL-------EQAENTIRKLQHQQ 462
Cdd:PRK02224 244 EEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAglddadaEAVEARREELEDRD 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 463 QWLEKELVQARLSEAESQCALKEMQDKVLDIEKRNNSLPDEnnIARLQEELIAVKLREAEAIMGLKELRQQVKDLEEhwq 542
Cdd:PRK02224 324 EELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREE--AAELESELEEAREAVEDRREEIEELEEEIEELRE--- 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 543 rhlaRTTGRWKDPPKKNAMNE-LQDELMTIRLREAETQAEIREIKQRMMEMET-----------QNQINSNHLRRAE--- 607
Cdd:PRK02224 399 ----RFGDAPVDLGNAEDFLEeLREERDELREREAELEATLRTARERVEEAEAlleagkcpecgQPVEGSPHVETIEedr 474
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1785914762 608 QEVISLQEKVQYLSAQNKGL---LTQLSEAKRKQAEIECKKEEGKLQGQLnKSDSNQYIGELKDQIAELNHE 676
Cdd:PRK02224 475 ERVEELEAELEDLEEEVEEVeerLERAEDLVEAEDRIERLEERREDLEEL-IAERRETIEEKRERAEELRER 545
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
506-684 |
5.64e-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: 5.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 506 IARLQEELIAVKLREAEAIMGLKELRQQVKDLE---EHWQRHLA-----RTTGRWKDPPKKNAM----NELQDELMTIRL 573
Cdd:TIGR02169 172 KEKALEELEEVEENIERLDLIIDEKRQQLERLRrerEKAERYQAllkekREYEGYELLKEKEALerqkEAIERQLASLEE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 574 REAETQAEIREIKQRMMEME-TQNQINSNHLRRAEQEVISLQEKVQYLSAqnkglltQLSEAKRKQAeiECKKEEGKLQG 652
Cdd:TIGR02169 252 ELEKLTEEISELEKRLEEIEqLLEELNKKIKDLGEEEQLRVKEKIGELEA-------EIASLERSIA--EKERELEDAEE 322
|
170 180 190
....*....|....*....|....*....|..
gi 1785914762 653 QLNKSDSNqyIGELKDQIAELNHELRCLKGQR 684
Cdd:TIGR02169 323 RLAKLEAE--IDKLLAEIEELEREIEEERKRR 352
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
352-642 |
5.69e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.79 E-value: 5.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 352 QAAYQVKYNSKKMKKLEKEYTTIKTKEMEEQVEIKRLRTENRLLKQRIETLEKESASLADRL--------IQGQVTRAQE 423
Cdd:PRK04863 276 RHANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLnlvqtalrQQEKIERYQA 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 424 AEENYLIKRE-----LATIKQQSDEASAKLEQAENTIRKLQHQ----QQWLE---------KELVQArLSEAESQCAL-- 483
Cdd:PRK04863 356 DLEELEERLEeqnevVEEADEQQEENEARAEAAEEEVDELKSQladyQQALDvqqtraiqyQQAVQA-LERAKQLCGLpd 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 484 -----------------KEMQDKVLDIEKRNNSLPDenniARLQEELIAVKLREAEAIMGLKELRQQVKDLEEHW--QRH 544
Cdd:PRK04863 435 ltadnaedwleefqakeQEATEELLSLEQKLSVAQA----AHSQFEQAYQLVRKIAGEVSRSEAWDVARELLRRLreQRH 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 545 LARTTgrwkdPPKKNAMNELQDELMtirlREAETQAEIREIKQRMMEMETQNQINSNHLRRAEQEVISLQEKVQYLSAQN 624
Cdd:PRK04863 511 LAEQL-----QQLRMRLSELEQRLR----QQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERR 581
|
330
....*....|....*...
gi 1785914762 625 KGLLTQLSEAKRKQAEIE 642
Cdd:PRK04863 582 MALRQQLEQLQARIQRLA 599
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
384-539 |
6.52e-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: 42.22 E-value: 6.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 384 EIKRLRTENRLLKQRIETLEKESASLADRLIQGQVTRAQEAEENYLIKRELATIKQQSDEASAKLEQAENT--IRKLQHq 461
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNkeYEALQK- 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1785914762 462 qqwlEKELVQARLSEAESQcaLKEMQDKVLDIEKRNNSLpdENNIARLQEELIAVKlREAEAImgLKELRQQVKDLEE 539
Cdd:COG1579 97 ----EIESLKRRISDLEDE--ILELMERIEELEEELAEL--EAELAELEAELEEKK-AELDEE--LAELEAELEELEA 163
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
368-462 |
7.77e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.92 E-value: 7.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 368 EKEYTTIKTKEMEEQV-----EIKRLRTENRLLKQRIETLEKESASLADRLIQGQVTRAQEA----------EENYLIKR 432
Cdd:COG2433 400 EKEHEERELTEEEEEIrrleeQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIrkdreisrldREIERLER 479
|
90 100 110
....*....|....*....|....*....|
gi 1785914762 433 ELATIKQQSDEASAKLEQAEnTIRKLQHQQ 462
Cdd:COG2433 480 ELEEERERIEELKRKLERLK-ELWKLEHSG 508
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
384-506 |
9.11e-04 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 39.93 E-value: 9.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 384 EIKRLRTENRLLKQRIETLEKESASLADRLiQGQVTRAQEAEENYliKREL---ATIKQQSDEASAKLEQAENTIRKLQH 460
Cdd:pfam07926 2 ELSSLQSEIKRLKEEAADAEAQLQKLQEDL-EKQAEIAREAQQNY--ERELvlhAEDIKALQALREELNELKAEIAELKA 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1785914762 461 QQQWLEKELVQARLSEAESQcalKEMQDKVLDIEKRNNSLPDENNI 506
Cdd:pfam07926 79 EAESAKAELEESEESWEEQK---KELEKELSELEKRIEDLNEQNKL 121
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
342-642 |
1.12e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 342 QFDGVPDKLIQAAYQVKYNSKKMKKLEKEYTTIKTKEMEEQVEIKRLRTENRLLKQRIETLEKESASLADRliqgqvtRA 421
Cdd:COG4372 60 ELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQ-------RK 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 422 QEAEENYLIKRELATIKQQSDEASAKLEQAENTIRKLQHQQQWLEKELVQARLSEAESQCALKEMQDKVLDIEKRNNSLP 501
Cdd:COG4372 133 QLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESL 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 502 DENNIARLQEELIAVKLREAEAIMGLK----ELRQQVKDLEEHWQRHLARTTGRWKDPPKKNAMNELQDELMTIRLREAE 577
Cdd:COG4372 213 PRELAEELLEAKDSLEAKLGLALSALLdaleLEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAA 292
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1785914762 578 TQAEIREIKQRMMEMETQNQINSNHLRRAEQEVISLQEKVQYLSAQNKGLLTQLSEAKRKQAEIE 642
Cdd:COG4372 293 LELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLE 357
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
363-684 |
1.20e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 363 KMKKLEKEYTTIKtkemEEQVEIKRLRTENRLLKQRIETLEKESASLADRLIQGQVTRAQEAEENY-LIKRELATIKQQS 441
Cdd:COG4717 147 RLEELEERLEELR----ELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLaELEEELEEAQEEL 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 442 DEASAKLEQAENTIRKLQHQQQWLEKELVQARLSEAesqCALKEMQDKVLDIEKRNN--------SLPDENNIARLQEEL 513
Cdd:COG4717 223 EELEEELEQLENELEAAALEERLKEARLLLLIAAAL---LALLGLGGSLLSLILTIAgvlflvlgLLALLFLLLAREKAS 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 514 IAVKLREAEAIMGLKELRQQVkdleehWQRHLARTTGRWKDPPKK-----NAMNELQDELMtiRLREAETQAEIREIKQR 588
Cdd:COG4717 300 LGKEAEELQALPALEELEEEE------LEELLAALGLPPDLSPEEllellDRIEELQELLR--EAEELEEELQLEELEQE 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 589 MMEMETQNQINS----NHLRRAEQEVISLQEKVQYLSAQNKGLLTQLSEAKRKQAEIECKKEEGKLQGQLNKSDSNqyIG 664
Cdd:COG4717 372 IAALLAEAGVEDeeelRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEE--LE 449
|
330 340
....*....|....*....|
gi 1785914762 665 ELKDQIAELNHELRCLKGQR 684
Cdd:COG4717 450 ELREELAELEAELEQLEEDG 469
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
348-677 |
1.21e-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: 42.31 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 348 DKLIQAAYQVKYNSKKMKKLEKEYTTIKTKEMEEQVEIKRLRTENRLL-------KQRIETLEKESASLAdrliqgqvtr 420
Cdd:TIGR04523 61 KNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKInseikndKEQKNKLEVELNKLE---------- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 421 aQEAEENyliKRELATIKQQSDEASAKLEQAENTIRKLQHQQQWLEKELvqarlseaesqcalKEMQDKVLDIEKRNNSL 500
Cdd:TIGR04523 131 -KQKKEN---KKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENEL--------------NLLEKEKLNIQKNIDKI 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 501 pdENNIARLQEELIAVKLREAEAimglKELRQQVKDLEEhwqrhlarttgrwKDPPKKNAMNELQDELmtirlreAETQA 580
Cdd:TIGR04523 193 --KNKLLKLELLLSNLKKKIQKN----KSLESQISELKK-------------QNNQLKDNIEKKQQEI-------NEKTT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 581 EIREIKQRMMEMETQNQINSNHLRRAEQEVISLQEKVQYLSAQNKGLLTQLSEAKRKQAEIECKKEEGKLQGQLNK---- 656
Cdd:TIGR04523 247 EISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKleei 326
|
330 340
....*....|....*....|....*
gi 1785914762 657 ----SDSNQYIGELKDQIAELNHEL 677
Cdd:TIGR04523 327 qnqiSQNNKIISQLNEQISQLKKEL 351
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
387-534 |
1.25e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.38 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 387 RLRTEN-------RLLKQRIETLEKESASLADRLIQGQVTRAQEaeenylIKRELATIKQQSDEASAKLEQAENTIRKLQ 459
Cdd:COG0542 401 RVRMEIdskpeelDELERRLEQLEIEKEALKKEQDEASFERLAE------LRDELAELEEELEALKARWEAEKELIEEIQ 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 460 HQQQWLEKELVQARLSEAEsqcaLKEMQDKVLDIEKRNNSLPDENNIA------------RLQEEliavklrEAEAIMGL 527
Cdd:COG0542 475 ELKEELEQRYGKIPELEKE----LAELEEELAELAPLLREEVTEEDIAevvsrwtgipvgKLLEG-------EREKLLNL 543
|
....*...
gi 1785914762 528 -KELRQQV 534
Cdd:COG0542 544 eEELHERV 551
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
378-637 |
1.34e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.23 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 378 EMEEQVEIKRLRTENRLLKQRIETLEKESASLADRLIQGQVTRAQEAEENYLIKRELATIKQQSDEASAKLEQAENTIRK 457
Cdd:COG1196 597 IGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLE 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 458 LQHQQQWLEKELVQARLSEAESQCALKEMQDKVLDIEKRnnslpdenniaRLQEELIAVKLREAEAIMGLKELRQQVKDL 537
Cdd:COG1196 677 AEAELEELAERLAEEELELEEALLAEEEEERELAEAEEE-----------RLEEELEEEALEEQLEAEREELLEELLEEE 745
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 538 EEhwqrhlarttgrwkdppkknaMNELQDELMTIRLREAETQAEIREIKQRMMEMETQNQinsnhlrRAEQEVISLQEKV 617
Cdd:COG1196 746 EL---------------------LEEEALEELPEPPDLEELERELERLEREIEALGPVNL-------LAIEEYEELEERY 797
|
250 260
....*....|....*....|
gi 1785914762 618 QYLSAQnkglLTQLSEAKRK 637
Cdd:COG1196 798 DFLSEQ----REDLEEARET 813
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
349-677 |
1.66e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 349 KLIQAAYQVKynsKKMKKLEKEYTTIKTKEMEEQVEIKRLRTENRLLKQRIETLEKesasladrliqgqvtRAQEAEEny 428
Cdd:PRK03918 183 KFIKRTENIE---ELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEE---------------LKEEIEE-- 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 429 lIKRELATIKQQSDEASAKLEQAENTIRKLQHQQQWLEKelVQARLSE----AESQCALKEMQDKVLD----IEKRNNSL 500
Cdd:PRK03918 243 -LEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEE--KVKELKElkekAEEYIKLSEFYEEYLDelreIEKRLSRL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 501 PDE-NNIARLQEELIAVKLREAEAIMGLKELRQQVKDLEEHWQ-----RHLARTTGRWKDPPKKNAMNELQDELMTIRLR 574
Cdd:PRK03918 320 EEEiNGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHElyeeaKAKKEELERLKKRLTGLTPEKLEKELEELEKA 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 575 EAETQAEIREIKQRMMEMET---QNQINSNHLRRAEQEV------ISLQEKVQYLSAQNKGLLTQLSEAKR-KQAEIECK 644
Cdd:PRK03918 400 KEEIEEEISKITARIGELKKeikELKKAIEELKKAKGKCpvcgreLTEEHRKELLEEYTAELKRIEKELKEiEEKERKLR 479
|
330 340 350
....*....|....*....|....*....|...
gi 1785914762 645 KEEGKLQGQLNKSDSNQYIGELKDQIAELNHEL 677
Cdd:PRK03918 480 KELRELEKVLKKESELIKLKELAEQLKELEEKL 512
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
362-681 |
1.80e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.81 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 362 KKMKKLEKEYTTIKTKEMEEQVEIKRLRTenrlLKQRIETLEKESASLADRLIQGQVTRAQEAEEnylIKRELATIKQQS 441
Cdd:PRK01156 346 SRYDDLNNQILELEGYEMDYNSYLKSIES----LKKKIEEYSKNIERMSAFISEILKIQEIDPDA---IKKELNEINVKL 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 442 DEASAKLEQAENTIRKLQHQQQWLEK--ELVQAR---------LSEAESQCALKEMQDKVLDIEKRNNSLpdENNIARLQ 510
Cdd:PRK01156 419 QDISSKVSSLNQRIRALRENLDELSRnmEMLNGQsvcpvcgttLGEEKSNHIINHYNEKKSRLEEKIREI--EIEVKDID 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 511 EELIAVKLREAEAIMG-----------LKELRQQVKDLEEHWQR------------------HLARTTGRWKDPPKKNAM 561
Cdd:PRK01156 497 EKIVDLKKRKEYLESEeinksineynkIESARADLEDIKIKINElkdkhdkyeeiknrykslKLEDLDSKRTSWLNALAV 576
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 562 NELQDeLMTIRLREAETQAEIREIKQRMMEMETQ----NQINSNHLRRAEQEVIS-----------------LQEKVQYL 620
Cdd:PRK01156 577 ISLID-IETNRSRSNEIKKQLNDLESRLQEIEIGfpddKSYIDKSIREIENEANNlnnkyneiqenkiliekLRGKIDNY 655
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1785914762 621 ---SAQNKGLLTQLSEAKRKQAEIECKKEegKLQGQLNKSDSNQY------------IGELKDQIAELNHELRCLK 681
Cdd:PRK01156 656 kkqIAEIDSIIPDLKEITSRINDIEDNLK--KSRKALDDAKANRArlestieilrtrINELSDRINDINETLESMK 729
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
384-542 |
2.67e-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: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 384 EIKRLRTENRLLKQRIETLEKESASLADRLIQGQVTRAQEAEENYLIKRELATIKQQSDEASAKLEQAENTIRklqhqqq 463
Cdd:COG4913 339 RLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAE------- 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 464 wlekelvqARLSEAESQcaLKEMQDKVLDIEKRNNSLPDEnnIARLQEELI-AVKLREAEA-IMGlkELrQQVKDLEEHW 541
Cdd:COG4913 412 --------AALRDLRRE--LRELEAEIASLERRKSNIPAR--LLALRDALAeALGLDEAELpFVG--EL-IEVRPEEERW 476
|
.
gi 1785914762 542 Q 542
Cdd:COG4913 477 R 477
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
391-647 |
2.70e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.50 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 391 ENRLLKQRIETLEKESASLADRLIQgqVTRAQEAEENYLIKRELATIKQQSDEASAKLEQAENTIRKLQHQQQWlEKELV 470
Cdd:pfam02463 167 LKRKKKEALKKLIEETENLAELIID--LEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEER-IDLLQ 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 471 QARLSEAESQCALKEMQDKVLDIEKRNNSLPDENN-IARLQEELIAVK-LREAEAIMGLKELRQQVKDLEEHWQRHLART 548
Cdd:pfam02463 244 ELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEkEKKLQEEELKLLaKEEEELKSELLKLERRKVDDEEKLKESEKEK 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 549 TGRWKDPPK-KNAMNELQDELMTIRLREAETQAEIREIKQRMMEMET-QNQINSNHLRRAEQEVISLQEKVQYLSAQNKG 626
Cdd:pfam02463 324 KKAEKELKKeKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQlEEELLAKKKLESERLSSAAKLKEEELELKSEE 403
|
250 260
....*....|....*....|.
gi 1785914762 627 LLTQLSEAKRKQAEIECKKEE 647
Cdd:pfam02463 404 EKEAQLLLELARQLEDLLKEE 424
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
338-654 |
2.83e-03 |
|
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: 41.26 E-value: 2.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 338 VIPHQFDGVPDKLiqAAYQVKYNSKKMKKLEKEYTTIkTKEMEEQVEIKRLrTENRLLKQRIEtlekesasladrLIQGQ 417
Cdd:pfam17380 218 VAPKEVQGMPHTL--APYEKMERRKESFNLAEDVTTM-TPEYTVRYNGQTM-TENEFLNQLLH------------IVQHQ 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 418 VTRAQEAEENYLIKRELATIKQQSDEASAKLEQAENTIRKLQHQQQWLEKELV----QARLS-EAESQCALKEMQDKVLD 492
Cdd:pfam17380 282 KAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAiyaeQERMAmERERELERIRQEERKRE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 493 IEK-RNNSLPDENNIARLQEELIAVKLREAEAIMGLKELRQQVKDLEEHWQRHLARTTGRWKDPPKKnamnelQDELMTI 571
Cdd:pfam17380 362 LERiRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAE------QEEARQR 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 572 RLREAETQAEIREIKQRMMEMETQNQI-----NSNHLRRAEQEVISLQEKVQYLSAQNKGLLTQLSEAkRKQAEIECKKE 646
Cdd:pfam17380 436 EVRRLEEERAREMERVRLEEQERQQQVerlrqQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEE-RKQAMIEEERK 514
|
....*...
gi 1785914762 647 EGKLQGQL 654
Cdd:pfam17380 515 RKLLEKEM 522
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
362-678 |
2.86e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 362 KKMKKLEKEYTTIKTKEMEEQVEIKRLRTENRLLKQRIETLEKESASLADRLiqgqvTRAQEAEENYLIKRELATIKQQS 441
Cdd:PTZ00121 1476 KKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEA-----KKAEEAKKADEAKKAEEKKKADE 1550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 442 DEASAKLEQAENtIRKLQHQQQWLEKELVQARLSEAESQCALKEMQDKVLDIEKRNNSLPDENNIARlQEELIAVKLREA 521
Cdd:PTZ00121 1551 LKKAEELKKAEE-KKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAE-EAKIKAEELKKA 1628
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 522 EAImglKELRQQVKDLEEHWQRHLARTTGRWKDPPKKNAMNELQDELMTIRLREAETQAEIREIKQRMMEMETQNQINSN 601
Cdd:PTZ00121 1629 EEE---KKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAE 1705
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 602 HLRRAEQEVISLQEKVQYLSAQNKGLLTQL----SEAKRKQAEIECKKEEGKLQGQLNKSDSNQYIGELKDQIAELNHEL 677
Cdd:PTZ00121 1706 ELKKKEAEEKKKAEELKKAEEENKIKAEEAkkeaEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEEL 1785
|
.
gi 1785914762 678 R 678
Cdd:PTZ00121 1786 D 1786
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
348-523 |
3.20e-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: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 348 DKLIQAAYQVKYNSKKMKKLEKEyttIKTKEMEEQVEIKRLRTENRLLKQRIETLEKESASLADRLIQGQVTRAQEAEEN 427
Cdd:COG4942 62 RRIAALARRIRALEQELAALEAE---LAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 428 YLIKRELATIKQQSDEASAKLEQAENTIRKLQHQQQWLEKELVQARLSEAESQCALKEMQDKVLDIEKRNNSLPDE---- 503
Cdd:COG4942 139 QYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAElael 218
|
170 180
....*....|....*....|.
gi 1785914762 504 -NNIARLQEELIAVKLREAEA 523
Cdd:COG4942 219 qQEAEELEALIARLEAEAAAA 239
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
477-642 |
3.44e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.91 E-value: 3.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 477 AESQCALKEMQD---KVLDIEKRNNSLPDEnnIARLQEELIAVKLREAEAIMGLKELRQQVKDLE---EHWQRHLARTTG 550
Cdd:COG1579 3 PEDLRALLDLQEldsELDRLEHRLKELPAE--LAELEDELAALEARLEAAKTELEDLEKEIKRLEleiEEVEARIKKYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 551 RWKDPPKKNAMNELQDELMTIRLREAETQAEIREIKQRMMEMETQNQINSNHLRRAEQEvisLQEKVQYLSAQNKGLLTQ 630
Cdd:COG1579 81 QLGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAE---LEEKKAELDEELAELEAE 157
|
170
....*....|..
gi 1785914762 631 LSEAKRKQAEIE 642
Cdd:COG1579 158 LEELEAEREELA 169
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
382-679 |
4.28e-03 |
|
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular sites as centrioles, basal bodies, and along ciliary and flagellar doublet microtubules. Tektins form unique protofilaments, organized as longitudinal polymers of tektin heterodimers with axial periodicity matching tubulin. Tektin polypeptides consist of several alpha-helical regions that are predicted to form coiled coils. Indeed, tektins share considerable structural similarities with intermediate filament proteins. Possible functional roles for tektins are: stabilization of tubulin protofilaments; attachment of A and B-tubules in ciliary/flagellar microtubule doublets and C-tubules in centrioles; binding of axonemal components.
Pssm-ID: 460827 [Multi-domain] Cd Length: 383 Bit Score: 40.22 E-value: 4.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 382 QVEIKRLRTENRLLKQRIETLEKESASLADRL---IQGQVTRAQ---------EAEENylIKRELATIKQQSDEASAKLE 449
Cdd:pfam03148 63 EKELEELDEEIELLLEEKRRLEKALEALEEPLhiaQECLTLREKrqgidlvhdEVEKE--LLKEVELIEGIQELLQRTLE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 450 QAENTIRKLQHQQQWLEKELvqARLSEA----ESQCALKEMQDKVL---DIEK--RNNSLPDE------NNIARLQEELI 514
Cdd:pfam03148 141 QAWEQLRLLRAARHKLEKDL--SDKKEAleidEKCLSLNNTSPNISykpGPTRipPNSSTPEEwekftqDNIERAEKERA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 515 A-VKLREAeaimgLKELRQQV-KDLEEHWQ-------RHLARTtgrwkdppkKNAMNELQDELMTIRLREAETQAEIREI 585
Cdd:pfam03148 219 AsAQLREL-----IDSILEQTaNDLRAQADavnfalrKRIEET---------EDAKNKLEWQLKKTLQEIAELEKNIEAL 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 586 KQRMMEMETQNQIN----SNHLRRAEQEVIslQEKVQYlsaqnkGLltqLSEAKRKQAEIECkkeegkLQGQLNKSDSNq 661
Cdd:pfam03148 285 EKAIRDKEAPLKLAqtrlENRTYRPNVELC--RDEAQY------GL---VDEVKELEETIEA------LKQKLAEAEAS- 346
|
330
....*....|....*...
gi 1785914762 662 yIGELKDQIAELNHELRC 679
Cdd:pfam03148 347 -LQALERTRLRLEEDIAV 363
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
372-646 |
6.40e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.51 E-value: 6.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 372 TTIKTKEMEEQVE--IKRLRTENRLLKQRIETLEKESASLADRL------IQGQVTRAQEAEENY-LIKRELATIKQQSD 442
Cdd:COG1340 2 KTDELSSSLEELEekIEELREEIEELKEKRDELNEELKELAEKRdelnaqVKELREEAQELREKRdELNEKVKELKEERD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 443 EASAKLEQAENTIRKLQHQQqwleKELVQARLSEAESQCAL----KEMQDKVLDIEKRNNsLPDEnnIARLQEELIAVK- 517
Cdd:COG1340 82 ELNEKLNELREELDELRKEL----AELNKAGGSIDKLRKEIerleWRQQTEVLSPEEEKE-LVEK--IKELEKELEKAKk 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 518 -LREAEAIMGLK-----------ELRQQVKDLEEHWQRHlarttgrwkdppkKNAMNELQDELMTIRLREAETQAEIREI 585
Cdd:COG1340 155 aLEKNEKLKELRaelkelrkeaeEIHKKIKELAEEAQEL-------------HEEMIELYKEADELRKEADELHKEIVEA 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1785914762 586 KQRmmemetqnqinsnhLRRAEQEVISLQEKVQYLSAQNKGLLTQLSEAKRKQAEIECKKE 646
Cdd:COG1340 222 QEK--------------ADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEK 268
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
505-656 |
6.41e-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: 6.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 505 NIARLQEELIavKLREAEAIMglKELRQQVKDLE---EHWQRHLArttgrwkdppKKNAMNELQDELMTIRLREAET--- 578
Cdd:COG4913 226 AADALVEHFD--DLERAHEAL--EDAREQIELLEpirELAERYAA----------ARERLAELEYLRAALRLWFAQRrle 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 579 --QAEIREIKQRMMEMETQNQINSNHLRRAEQEVISLQEKVQYLSAQNKGLLTQLSEAKRKQAEiECKKEEGKLQGQLNK 656
Cdd:COG4913 292 llEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELE-ERERRRARLEALLAA 370
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
358-657 |
8.85e-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: 39.70 E-value: 8.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 358 KYNSKKMKKLEKEYTTIKTKEMEEQVEIKRLRTENRLLKQRIETLEKESASLADRLIQG---------QVTRAQEAEENy 428
Cdd:pfam05483 467 EHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCkkqeermlkQIENLEEKEMN- 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 429 lIKRELATI----KQQSDEASAKLEQAENTIRKLQHQQQWLEKelvQARLSEAESQCALKEMQDKVLDIE---KRNNSLP 501
Cdd:pfam05483 546 -LRDELESVreefIQKGDEVKCKLDKSEENARSIEYEVLKKEK---QMKILENKCNNLKKQIENKNKNIEelhQENKALK 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 502 DENNIARLQEELIAVKLREAEaiMGLKELRQQVKDLEEHWQRHLARttgrwKDPPKKNAMNELQDELMTIRlREAETQAE 581
Cdd:pfam05483 622 KKGSAENKQLNAYEIKVNKLE--LELASAKQKFEEIIDNYQKEIED-----KKISEEKLLEEVEKAKAIAD-EAVKLQKE 693
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 582 I-----REIKQRMMEMETQNQINSNHLRRAEQEVISLQEKVQYLSAQNKGLLTQLSEAK------RKQAEIEC-KKEEGK 649
Cdd:pfam05483 694 IdkrcqHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKaellslKKQLEIEKeEKEKLK 773
|
....*...
gi 1785914762 650 LQGQLNKS 657
Cdd:pfam05483 774 MEAKENTA 781
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
348-693 |
9.20e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 39.57 E-value: 9.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 348 DKLIQAAYQVKYNSKKMK-KLEKEyttiktkemEEQVEIKRLRTENRL--LKQRIETLEKESASLADRLIQGQVTRAQ-- 422
Cdd:TIGR00618 176 DQYTQLALMEFAKKKSLHgKAELL---------TLRSQLLTLCTPCMPdtYHERKQVLEKELKHLREALQQTQQSHAYlt 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 423 ----EAEENYLIKRELATIKQQSDEASAKLEQAENTIRKLQHQQQWLEKELVQARLSEAESQC--ALKEMQDKVLDIEK- 495
Cdd:TIGR00618 247 qkreAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAqrIHTELQSKMRSRAKl 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 496 ---RNNSLPDENNIARL---------QEELIAvklREAEAIMGLKELRQQVKDLEEH---WQRHLarTTGRWKDPPKKNA 560
Cdd:TIGR00618 327 lmkRAAHVKQQSSIEEQrrllqtlhsQEIHIR---DAHEVATSIREISCQQHTLTQHihtLQQQK--TTLTQKLQSLCKE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 561 MNELQDELMTIrlrEAETQAEiREIKQRMMEMETQNQINsnhLRRAEQEVISLQEKVQYLSAQNKgLLTQLSEAKRKQAE 640
Cdd:TIGR00618 402 LDILQREQATI---DTRTSAF-RDLQGQLAHAKKQQELQ---QRYAELCAAAITCTAQCEKLEKI-HLQESAQSLKEREQ 473
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1785914762 641 IECKKEEGKLQGQLNKSDSNQYIGELKDQIAELNHELRCLKGQRGFSGQPPFD 693
Cdd:TIGR00618 474 QLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPL 526
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
317-492 |
9.28e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 39.61 E-value: 9.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 317 QMNQAELMQLDMEGMLQHFQKVIPHQFDGVPDKLIQAAYQVKynSKKMKKLEKEYTTIKTKEMEEQVEIKRLRTENRLLK 396
Cdd:COG3206 227 QLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQL--RAQLAELEAELAELSARYTPNHPDVIALRAQIAALR 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785914762 397 QRIETLEKEsaSLADRLIQGQVTRAQEAEenylIKRELATIKQQSDEASAKLEQAENTIRKLQHQQQWLekELVQARLSE 476
Cdd:COG3206 305 AQLQQEAQR--ILASLEAELEALQAREAS----LQAQLAQLEARLAELPELEAELRRLEREVEVARELY--ESLLQRLEE 376
|
170
....*....|....*.
gi 1785914762 477 AESQCALKEMQDKVLD 492
Cdd:COG3206 377 ARLAEALTVGNVRVID 392
|
|
| |
