|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
235-535 |
1.05e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 81.14 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 235 EQLRRQ--HLEKMV------HTLQSHLLEYQQRISVAieVDRSKDAALTEAEQTVQSLNYEVQHLRDAVHRLEADRGESQ 306
Cdd:COG1196 196 GELERQlePLERQAekaeryRELKEELKELEAELLLL--KLRELEAELEELEAELEELEAELEELEAELAELEAELEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 307 SRFDALQNELSQAVNLATRFQEKNDKLERELDHCRQDAKQWEERLEQLEMQLNSSKRAEELSHAELNKLRDKFAKVDYQQ 386
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 387 EKLKARIEELEKENNTLTNQKEMLQEYHQKQKARADSLESHRKSLQETLANLTETETNLKKKLDIQQKSLKQYYQQQMEn 466
Cdd:COG1196 354 EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE- 432
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442629624 467 vVAKKMQEFQDQLDKNEEHLKNEARERERLIAERAVKQLEmiNEKNNQELNLIQEKHNEEVELYRLQLA 535
Cdd:COG1196 433 -LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE--AALLEAALAELLEELAEAAARLLLLLE 498
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
232-510 |
2.52e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 79.98 E-value: 2.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 232 LKEEQLRRQHLEKMVH--TLQSHLLEYQQRISVAIEVDRSKDAALTEAEQTVQSLNYEVQHLRDAVHRLEADRGESQSRF 309
Cdd:COG1196 218 LKEELKELEAELLLLKlrELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 310 DALQNELSQAVNLATRFQEKNDKLERELDHCRQDAKQWEERLEQLEMQLNSSKRAEELSHAELNKLRDKFAKVDYQQEKL 389
Cdd:COG1196 298 ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 390 KARIEELEKENNTLTNQKEMLQEYHQKQKARADSLESHRKSLQETLANLTETETNLKKKLDIQQKSLKQYYQQQMENVVA 469
Cdd:COG1196 378 EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 442629624 470 KKMQEFQDQLDKNEEHLKNEARERERLIAERAVKQLEMINE 510
Cdd:COG1196 458 EEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
241-544 |
3.63e-15 |
|
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: 79.72 E-value: 3.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 241 HLEKMVHTLQSHLLEYQQRISVAIEVDRSKDAALTEAEQTVQSLNYEVQHLRDAVHRLEADRGESQSRFDALQNELSQAV 320
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 321 NLATRFQEKNDKLERELDHCRQDAKQWEERLEQLEMQLNSSKRAEELSHAELNKLRDKFAKVDYQQEKLKARIEELEKEN 400
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRL 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 401 NTLTNQKEMLQEyhqkqkaRADSLESHRKSLQETLANLTET---ETNLKKKLDIQQKSLKQYYQQQME--NVVAKKMQEF 475
Cdd:TIGR02168 841 EDLEEQIEELSE-------DIESLAAEIEELEELIEELESEleaLLNERASLEEALALLRSELEELSEelRELESKRSEL 913
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442629624 476 QDQLDKNEEHLKNEARERERLIAERAvKQLEMINEKNNQELNLIQEKHNE---EVELYRLQLANASKKIDEM 544
Cdd:TIGR02168 914 RRELEELREKLAQLELRLEGLEVRID-NLQERLSEEYSLTLEEAEALENKiedDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
287-545 |
8.20e-14 |
|
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: 75.10 E-value: 8.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 287 EVQHLRDAVHRLEADRGESQSRFDALQNELSQAVNLATRFQEKNDKLERELDHCRQDAKQWEERLEQLEMQLNSSKRAEE 366
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIE 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 367 LSHAELNKLRDKFAKVDYQQEKLKARIEELEKENN-----TLTNQKEMLQEYHQKQKARADSLESHRKSLQETLANLTET 441
Cdd:TIGR02169 755 NVKSELKELEARIEELEEDLHKLEEALNDLEARLShsripEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKE 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 442 ETNLKKK---LDIQQKSLkqyyQQQMENVVAKK------MQEFQDQLDKNEEHLKNEARERERLIAERAVKQlemineKN 512
Cdd:TIGR02169 835 IQELQEQridLKEQIKSI----EKEIENLNGKKeeleeeLEELEAALRDLESRLGDLKKERDELEAQLRELE------RK 904
|
250 260 270
....*....|....*....|....*....|...
gi 442629624 513 NQELNLIQEKHNEEVELYRLQLANASKKIDEMD 545
Cdd:TIGR02169 905 IEELEAQIEKKRKRLSELKAKLEALEEELSEIE 937
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
234-533 |
8.97e-14 |
|
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: 75.09 E-value: 8.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 234 EEQLRRQHLEKMVHTLQSHLLEYQQRISVAIEVDRSKDAALTEAEQtvqslnyEVQHLRDAVHRLEADRGESQSRFDALQ 313
Cdd:TIGR02168 222 LRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEE-------KLEELRLEVSELEEEIEELQKELYALA 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 314 NELSqavnlatrfqekndKLERELDHCRQDAKQWEERLEQLEMQLNSSKRAEELSHAELNKLRDKFAKVDYQQEKLKARI 393
Cdd:TIGR02168 295 NEIS--------------RLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 394 EELEKENNTLTNQKEMLQEYHQKQKARADSLESHRKSLQETLANLTETETNLKKKLDIQQKSLKQYYQQQMENvvakKMQ 473
Cdd:TIGR02168 361 EELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA----ELK 436
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442629624 474 EFQDQLDKNEEHLKNEARERERLIA--ERAVKQLEMINEKNNQELNLIQEKHNEEVELYRLQ 533
Cdd:TIGR02168 437 ELQAELEELEEELEELQEELERLEEalEELREELEEAEQALDAAERELAQLQARLDSLERLQ 498
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
308-547 |
3.34e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.05 E-value: 3.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 308 RFDALQNELSQAVNLATRFQEKNDKLERELDHCRQDAKQWEERLEQLEMQLNSSKRAEELSHAELNKLRDKFAKVDYQQE 387
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 388 KLKARIEELEKENNTLTNQKEMLQEYHQKQKARADSLESHRKSLQETLANLTETETNLKKKLDIQQKSLKQYYQQQMEnv 467
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE-- 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 468 VAKKMQEFQDQLDKNEEHLKNEARERERLIAERAVKQLEmINEKNNQELNLIQEKHNEEVELYRLQLANASKKIDEMDLK 547
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA-LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
231-515 |
4.97e-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: 69.70 E-value: 4.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 231 SLKEEQLRRQHLEKMVHTLQSHLLEYQQRISVAIEVDRSKDAALTEAEQTVQSLNYEVQHLRDAVHRLEADRGESQSRFD 310
Cdd:TIGR02168 734 DLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT 813
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 311 ALQNELSQAVNLATRFQEKNDKLERELDHCRQDAKQWEERLEQLEMQLNSSKRAEELSHAELNKLRDKFAKVDYQ----- 385
Cdd:TIGR02168 814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAlallr 893
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 386 --QEKLKARIEELEKENNTLTNQKEMLQEYHQKQKARADSLESHRKSLQETLANLTETE-----------TNLKKKLDIQ 452
Cdd:TIGR02168 894 seLEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTleeaealenkiEDDEEEARRR 973
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442629624 453 QKSLKQYYqQQMENVVAKKMQEFQDQldknEEHLKNEARERERLiaERAVKQLEMINEKNNQE 515
Cdd:TIGR02168 974 LKRLENKI-KELGPVNLAAIEEYEEL----KERYDFLTAQKEDL--TEAKETLEEAIEEIDRE 1029
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
343-598 |
3.99e-11 |
|
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: 66.63 E-value: 3.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 343 DAKQWEERLEQLEMQLNSSKRaeelshaELNKLRDKFAKVDYQQEKLKARIEELEKENNTLTNQKEMLQEYHQKQKARAD 422
Cdd:TIGR02169 668 FSRSEPAELQRLRERLEGLKR-------ELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLE 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 423 SLESHRKSLQETLANLTETETNLKKKLDIQQKSLKQYyQQQMENVVAK----KMQEFQDQLDK-NEEHLKNEAR------ 491
Cdd:TIGR02169 741 ELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKL-EEALNDLEARlshsRIPEIQAELSKlEEEVSRIEARlreieq 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 492 -------ERERLIAERAVKQLEMINEKNN---------------QELNLIQEKHNEEVELYRLQLANASKKIDEMDLKLS 549
Cdd:TIGR02169 820 klnrltlEKEYLEKEIQELQEQRIDLKEQiksiekeienlngkkEELEEELEELEAALRDLESRLGDLKKERDELEAQLR 899
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 442629624 550 CYKTKRADIAEKLHGVMEAQWQQALAILTTPSQNSIIQSSDTEASESPE 598
Cdd:TIGR02169 900 ELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPE 948
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
334-573 |
1.26e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.08 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 334 ERELDHCRQDAKQWEERLEQLEMQLN--------------SSKRAEELSHAELNKLRDKFAKVDYQQEKLKARIEELEKE 399
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAelrkeleeleeeleQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 400 NNTLTNQKEMLQEYHQKQKARADSLESHRKSLQETLANLTETETNLKKKLDIQQKSL---------KQYYQQQMENVVAK 470
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELtllneeaanLRERLESLERRIAA 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 471 KMQEFQD---QLDKNEEHLKNEARERERLIAERAVKQLEMINEKNnqelnlIQEKHNEEVELYRLQLANASKKIDEMDLK 547
Cdd:TIGR02168 836 TERRLEDleeQIEELSEDIESLAAEIEELEELIEELESELEALLN------ERASLEEALALLRSELEELSEELRELESK 909
|
250 260
....*....|....*....|....*.
gi 442629624 548 LScYKTKRADIAEKLHGVMEAQWQQA 573
Cdd:TIGR02168 910 RS-ELRRELEELREKLAQLELRLEGL 934
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
232-432 |
1.64e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.57 E-value: 1.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 232 LKEEQLRRQHLEKMVHTLQSHLLEYQQRISVAIEVDRSKDAALTEAEQTVQSLNYEVQHLRDAVHRLEADRGESQSRFDA 311
Cdd:COG1196 304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 312 LQNELSQAVNLATRFQEKNDKLERELDHCRQDAKQWEERLEQLEMQLNSSKRAEELSHAELNKLRDKFAKVDYQQEKLKA 391
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 442629624 392 RIEELEKENNTLTNQKEMLQEYHQKQKARADSLESHRKSLQ 432
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
229-437 |
5.58e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.65 E-value: 5.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 229 SSSLKEEQLRRQHLEKMVHTLQSHLLEYQQRISVAIEVDRSKDAALTEAEQTVQSLNYEVQHLRDAVHRLEADRGESQSR 308
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 309 FDALQNELSQAVNLATRFQEKNDKLERELDHCRQDAKQWEERLEQLEMQLNSSKRAEELSHAELNKLRDKFAKVDYQQEK 388
Cdd:COG1196 374 LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 442629624 389 LKARIEELEKENNTLTNQKEMLQEYHQKQKARADSLESHRKSLQETLAN 437
Cdd:COG1196 454 LEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
288-499 |
2.06e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.08 E-value: 2.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 288 VQHLRDAVHRLEADRGESQSRFDALQNELSQAVNLATRFQEKNDKLERELdhcrqDAKQWEERLEQLEMQLnsskRAEEL 367
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEI-----DVASAEREIAELEAEL----ERLDA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 368 SHAELNKLRDkfakvdyQQEKLKARIEELEKENNTLTNQKEMLQEyhqkqkaRADSLESHRKSLQETLANLTETEtnlkk 447
Cdd:COG4913 683 SSDDLAALEE-------QLEELEAELEELEEELDELKGEIGRLEK-------ELEQAEEELDELQDRLEAAEDLA----- 743
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 442629624 448 KLDIQQKSLKQYYQQQMENVVAKKMQEFQDQLDKNEEHLKNEARERERLIAE 499
Cdd:COG4913 744 RLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRA 795
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
232-407 |
5.98e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.54 E-value: 5.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 232 LKEEQLRRQHLEKMVhTLQSHLLEYQQRISVAIEVDRSkdAALTEAEQTVQSLNYEVQHLRDAVHRLEADRGESQSRFDA 311
Cdd:COG4913 244 LEDAREQIELLEPIR-ELAERYAAARERLAELEYLRAA--LRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDA 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 312 LQNELSQAVNLA--------TRFQEKNDKLERELDHCRQDAKQWEERLEQLEMQLNSS-----------KRAEELSHAEL 372
Cdd:COG4913 321 LREELDELEAQIrgnggdrlEQLEREIERLERELEERERRRARLEALLAALGLPLPASaeefaalraeaAALLEALEEEL 400
|
170 180 190
....*....|....*....|....*....|....*
gi 442629624 373 NKLRDKFAKVDYQQEKLKARIEELEKENNTLTNQK 407
Cdd:COG4913 401 EALEEALAEAEAALRDLRRELRELEAEIASLERRK 435
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
229-458 |
6.22e-09 |
|
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: 58.62 E-value: 6.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 229 SSSLKEEQLRRQHLEKMVHTLQSHLLEYQQRISVAIEVDRSKDAALTEAEQTVQSLNYEVQHLRDAVHRLEADRGESQSR 308
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 309 FDALQNELSQAVNLATRFqekndklereldhcrqdakqweERLEQLEMQLNSSKRAEELSHAELNKlrdKFAKVDYQQ-E 387
Cdd:COG4942 99 LEAQKEELAELLRALYRL----------------------GRQPPLALLLSPEDFLDAVRRLQYLK---YLAPARREQaE 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442629624 388 KLKARIEELEKENNTLTNQKEMLQEYHQKQKARADSLESHRKSLQETLANLTETETNLKKKLDIQQKSLKQ 458
Cdd:COG4942 154 ELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
229-516 |
1.22e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.54 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 229 SSSLKEEQLRRQHLEKMVHTLQSHLLEYQQRISVAIEVDRSKDAALTEAEQTVQSLNYEVQ-HLRDAVHRLEADRGESQS 307
Cdd:TIGR02169 229 LKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQlRVKEKIGELEAEIASLER 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 308 RFDALQNELSQAVNLATRFQEKNDKLERELDHCRQDAKQWEERLEQLEMQLNSSKRAEELSHAELNKLRDKFAKVDYQQE 387
Cdd:TIGR02169 309 SIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELK 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 388 KLKARIEELEKENNTLTNQKEMLQEYHQKQKARADSLESHRKSLQETLANLTETETNLKKKLDIQQKSLKQyyQQQMENV 467
Cdd:TIGR02169 389 DYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQ--LAADLSK 466
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 442629624 468 VAKKMQEFQDQLDKNEEHLKNEARERERLIAERAVKQLEMINEKNNQEL 516
Cdd:TIGR02169 467 YEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEV 515
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
286-456 |
2.45e-08 |
|
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: 55.32 E-value: 2.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 286 YEVQHLRDAVHRLEADRGESQSRFDALQNELSQAVNLATRFQEKNDKLERELDHCRQDAKQWEERLEQLEMQLNSSKRAE 365
Cdd:COG1579 10 LDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 366 ELSHAELnklrdkfakvdyQQEKLKARIEELEKE----NNTLTNQKEMLQEYHQKQKARADSLESHRKSLQETLANLTET 441
Cdd:COG1579 90 EYEALQK------------EIESLKRRISDLEDEilelMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE 157
|
170
....*....|....*
gi 442629624 442 ETNLKKKLDIQQKSL 456
Cdd:COG1579 158 LEELEAEREELAAKI 172
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
228-448 |
2.98e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.37 E-value: 2.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 228 CSSSLKEEQLRRQHLEKMVHTLQSHLLEYQQRISVAIEVDRSKDAALTEAEQTVQSLNYEVQH-------LRDAVHRLEA 300
Cdd:TIGR02168 265 LEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEEleskldeLAEELAELEE 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 301 DRGESQSRFDALQNELS----QAVNLATRFQEKNDKLE---RELDHCRQDAKQWEERLEQLEMQLNSSKRAEELSHAELN 373
Cdd:TIGR02168 345 KLEELKEELESLEAELEeleaELEELESRLEELEEQLEtlrSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIE 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 374 KLRDK-----FAKVDYQQEKLKARIEELEKENNTLTNQKEMLQE--------------YHQKQKARADSLEshrkSLQET 434
Cdd:TIGR02168 425 ELLKKleeaeLKELQAELEELEEELEELQEELERLEEALEELREeleeaeqaldaaerELAQLQARLDSLE----RLQEN 500
|
250
....*....|....
gi 442629624 435 LANLTETETNLKKK 448
Cdd:TIGR02168 501 LEGFSEGVKALLKN 514
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
272-505 |
8.93e-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: 54.77 E-value: 8.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 272 AALTEAEQTVQSLNYEVQHLRDAVHRLEADRGESQSRFDALQNELSQAvnlatrfQEKNDKLERELDHCRQDAKQWEERL 351
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAAL-------ARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 352 EQLEMQLNSSKR--AEELSHAELNKLRDK----------------FAKVDYQQEKLKARIEELEKENNTLTNQKEMLQEY 413
Cdd:COG4942 93 AELRAELEAQKEelAELLRALYRLGRQPPlalllspedfldavrrLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 414 HQKQKARADSLESHRKSLQETLANLTETETNLKKKLDIQQKSLKQyyqqqmenvvakkMQEFQDQLDKNEEHLKNEARER 493
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAE-------------LQQEAEELEALIARLEAEAAAA 239
|
250
....*....|..
gi 442629624 494 ERLIAERAVKQL 505
Cdd:COG4942 240 AERTPAAGFAAL 251
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
272-565 |
1.42e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.05 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 272 AALTEAEQTVQSLNYEVQHLRDAVHRLEADRGESQSRFDALQNELSQAVN----LATRFQEKNDKLER------------ 335
Cdd:PRK02224 377 EAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREreaeLEATLRTARERVEEaealleagkcpe 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 336 ------------ELDHCRQDAKQWEERLEQLEMQLNSSK----RAEELSHAE--LNKLRDKFAKVDYQQEKLKARIEELE 397
Cdd:PRK02224 457 cgqpvegsphveTIEEDRERVEELEAELEDLEEEVEEVEerleRAEDLVEAEdrIERLEERREDLEELIAERRETIEEKR 536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 398 KENNTLTNQKEMLQEYHQKQKARADSLESHRKSLQETLANLTETETNLKKKLDiqqkslkqyyqqQMENVVakkmqEFQD 477
Cdd:PRK02224 537 ERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIE------------SLERIR-----TLLA 599
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 478 QLDKNEEHLKnEARERERLIAERAVKQLEMINEKNNQELNLIQEKHNEEVELYRLQLANASKKIDEMDLKLSCYKTKRAD 557
Cdd:PRK02224 600 AIADAEDEIE-RLREKREALAELNDERRERLAEKRERKRELEAEFDEARIEEAREDKERAEEYLEQVEEKLDELREERDD 678
|
....*...
gi 442629624 558 IAEKLHGV 565
Cdd:PRK02224 679 LQAEIGAV 686
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
232-540 |
2.08e-07 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 54.59 E-value: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 232 LKEEQLRRQHLEKMVHTLQ-SHLLEYQQRISVAIEVDRSKDAALTEAEQTVQSLNYEVQHLRDAVHRLEADRgesQSRFD 310
Cdd:pfam02463 178 LIEETENLAELIIDLEELKlQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDE---QEEIE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 311 ALQNELSQAVNLATRFQEKNDKLERELDHCRQDAKQWEERLEQLEMQLNSSKRAEELSHAELNKLRDKFAKVDYQQEKLK 390
Cdd:pfam02463 255 SSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEK 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 391 ARIEELEKENNTLTNQK--------EMLQEYHQKQKARADSLESHRKSLQETLANLTETETNLKKKLDIQQKSLKQYYQQ 462
Cdd:pfam02463 335 EEIEELEKELKELEIKReaeeeeeeELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELA 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 463 QMENVVAKKMQEFQDQLDKNEEHLKNEARERERLIAERAVKQLEMINEKNNQEL---NLIQEKHNEEVELYRLQLANASK 539
Cdd:pfam02463 415 RQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKkseDLLKETQLVKLQEQLELLLSRQK 494
|
.
gi 442629624 540 K 540
Cdd:pfam02463 495 L 495
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
324-562 |
3.19e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.91 E-value: 3.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 324 TRFQEKNDKLERELDHCRQDAKQWEERLEQLEMQLNS----SKRAE-------ELSHAEL-------------------- 372
Cdd:TIGR02168 168 SKYKERRKETERKLERTRENLDRLEDILNELERQLKSlerqAEKAErykelkaELRELELallvlrleelreeleelqee 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 373 -NKLRDKFAKVDYQQEKLKARIEELEKENNTLTNQKEMLQEYHQKQKARADSLESH-------RKSLQETLANLTETETN 444
Cdd:TIGR02168 248 lKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQkqilrerLANLERQLEELEAQLEE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 445 LKKKLDIQQKSLKQyyQQQMENVVAKKMQEFQDQLDKNEEHLKN-----EARERERLIAERAVKQLEMINEKNNQEL--- 516
Cdd:TIGR02168 328 LESKLDELAEELAE--LEEKLEELKEELESLEAELEELEAELEElesrlEELEEQLETLRSKVAQLELQIASLNNEIerl 405
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 442629624 517 ------------NLIQEKHNEEVELYRLQLANASKKIDEMDLKLSCYKTKRADIAEKL 562
Cdd:TIGR02168 406 earlerledrreRLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEAL 463
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
271-471 |
5.92e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.14 E-value: 5.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 271 DAALTEAEQTVQSLNYEVQHLRDAVHRLEADRGESQSRFDALQNELSQAVNLATRFQEKNDKLERELDHCRQDAKQW--- 347
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERara 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 348 ----EERLEQLEMQLNSSKRAEELSHAE-LNKLRDKFAKVdyqQEKLKARIEELEKENNTLTNQKEMLQEYHQKQKARAD 422
Cdd:COG3883 95 lyrsGGSVSYLDVLLGSESFSDFLDRLSaLSKIADADADL---LEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 442629624 423 SLESHRKSLQETLANLTETETNLKKKLDIQQKSLKQYYQQQMENVVAKK 471
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAA 220
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
234-496 |
6.20e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 53.04 E-value: 6.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 234 EEQLRRQHLEkmVHTLQSHLLEYQQRISV----AIEVDRSKdAALTEAEQTVQSLNYEVQHLRDAVHRLEADRGESQSRF 309
Cdd:PRK04863 382 EARAEAAEEE--VDELKSQLADYQQALDVqqtrAIQYQQAV-QALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEEL 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 310 DALQNELSQAVNLATRFqEKNDKLEREL--DHCRQDAKQW--------------EERLEQLEMQLNSSKRAEELsHAELN 373
Cdd:PRK04863 459 LSLEQKLSVAQAAHSQF-EQAYQLVRKIagEVSRSEAWDVarellrrlreqrhlAEQLQQLRMRLSELEQRLRQ-QQRAE 536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 374 KLRDKFAKV---------DYQQ--EKLKARIEELEKENNTLtNQKEMLQEYHQKQ-KARADSLESHRKSLQETLANLTET 441
Cdd:PRK04863 537 RLLAEFCKRlgknlddedELEQlqEELEARLESLSESVSEA-RERRMALRQQLEQlQARIQRLAARAPAWLAAQDALARL 615
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 442629624 442 ETNLKKKLDIQQkSLKQYYQQQMENVVAKKMQEfqDQLDKNEEHLKneaRERERL 496
Cdd:PRK04863 616 REQSGEEFEDSQ-DVTEYMQQLLERERELTVER--DELAARKQALD---EEIERL 664
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
230-567 |
1.03e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.99 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 230 SSLKEEQLRRQHLEKMVHTLQSHLLEYQQRIsvaievdRSKDAALTEAEQTVQSLNyEVQHLRDAVHRLEADRGESQSRF 309
Cdd:PRK03918 238 EEIEELEKELESLEGSKRKLEEKIRELEERI-------EELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDEL 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 310 DALQNELSQAVNLATRFQEKNDKLE---RELDHCRQDAKQWEERLEQLEMQLNSSKRAEELShAELNKLRDKFAkvDYQQ 386
Cdd:PRK03918 310 REIEKRLSRLEEEINGIEERIKELEekeERLEELKKKLKELEKRLEELEERHELYEEAKAKK-EELERLKKRLT--GLTP 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 387 EKLKARIEELEKEnntltnqKEMLQEYHQKQKARADSLESHRKSLQETLANLTETETN---LKKKLDIQ-QKSLKQYYQQ 462
Cdd:PRK03918 387 EKLEKELEELEKA-------KEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvCGRELTEEhRKELLEEYTA 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 463 QMENvVAKKMQEFQD---QLDKNEEHLKNEARERERLIAERAV-KQLEMINEK----NNQELnliqEKHNEEVELYRLQL 534
Cdd:PRK03918 460 ELKR-IEKELKEIEEkerKLRKELRELEKVLKKESELIKLKELaEQLKELEEKlkkyNLEEL----EKKAEEYEKLKEKL 534
|
330 340 350
....*....|....*....|....*....|....*.
gi 442629624 535 ANASKKID--EMDL-KLSCYKTKRADIAEKLHGVME 567
Cdd:PRK03918 535 IKLKGEIKslKKELeKLEELKKKLAELEKKLDELEE 570
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
316-561 |
1.36e-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: 50.92 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 316 LSQAVNLATRFQEKNDKLERELDHCRQDAKQWEERLEQLEMQLNSSKRAEELSHAELNKLRDKFAKVDYQQEKLKARIEE 395
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 396 LEKENNTLTNQ-KEMLQEYHQKQKARADSLESHRKSLQETLANLTetetnlkkkldiqqkSLKQYYQQQMENvvAKKMQE 474
Cdd:COG4942 95 LRAELEAQKEElAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQ---------------YLKYLAPARREQ--AEELRA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 475 FQDQLDKNEEHLKNEARERERLIAERAVKQLEMINEKNNQELNLiqEKHNEEVELYRLQLANASKKIDEMDLKLSCYKTK 554
Cdd:COG4942 158 DLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLL--ARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
....*..
gi 442629624 555 RADIAEK 561
Cdd:COG4942 236 AAAAAER 242
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
297-560 |
2.59e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 50.29 E-value: 2.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 297 RLEADRGESQSRFDALQNELSQAVNLATRFQEKNDKLERELDHCRQDAKQWEERLEQLEMQLNSSKRAEELSHAELNKLR 376
Cdd:COG4372 14 SLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 377 DKFAKVDYQQEKLKARIEELEKENNTLTNQKEMLQEYHQKQKARADSLESHRKSLQETLANLTETETNLKKKLDIQQKSL 456
Cdd:COG4372 94 AELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQEL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 457 KQYYQQQMENVVAKKMQEFQDQLDKNEEHLKNEARERERLIAERAVKQLEMINEKNNQELNLIQEKHNEEVELYRLQLAN 536
Cdd:COG4372 174 QALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLE 253
|
250 260
....*....|....*....|....
gi 442629624 537 ASKKIDEMDLKLSCYKTKRADIAE 560
Cdd:COG4372 254 EVILKEIEELELAILVEKDTEEEE 277
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
233-567 |
2.89e-06 |
|
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: 50.49 E-value: 2.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 233 KEEQLRRQHLEKMVHTLQshLLEYQQRISVAIEVDRSKDAALTEAEQTVQSLNYEVQHLRDAVHRLEADRGESQSRFDAL 312
Cdd:pfam05483 333 KEAQMEELNKAKAAHSFV--VTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEEL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 313 QNELSQAVNLATRfQEKNDKLERELDHCRQDA----KQWEERLEQLEMQLNSSKRAEELSHAELNKLRDKFAKVDYQQEK 388
Cdd:pfam05483 411 KKILAEDEKLLDE-KKQFEKIAEELKGKEQELifllQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIE 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 389 LKARIEELEKENNTLTNQKEMLQEYHQKQKARADSLESHRKSLQETLANLTETETNLKKKLDIQQKSLKQyyqqqmenvv 468
Cdd:pfam05483 490 LTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQ---------- 559
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 469 akKMQEFQDQLDKNEEHLKNEARERERLIAERAVKQLEMINEKNNQE--LNLIQEKHNEEVELYRLQLANASK------K 540
Cdd:pfam05483 560 --KGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIEnkNKNIEELHQENKALKKKGSAENKQlnayeiK 637
|
330 340
....*....|....*....|....*..
gi 442629624 541 IDEMDLKLSCYKTKRADIAEKLHGVME 567
Cdd:pfam05483 638 VNKLELELASAKQKFEEIIDNYQKEIE 664
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
312-549 |
3.15e-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: 50.40 E-value: 3.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 312 LQNELSQAVNLATRFQEKNDKLERELDHCRQDAKQWEERLEQLEMQLNSSKRAEELSHAEL-------NKLRDKFAKVDY 384
Cdd:TIGR04523 326 IQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIknlesqiNDLESKIQNQEK 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 385 QQEKLKARIEELEKENNTLTNQKEMLQEYHQKQKARADSLESHRKSLQETLANLTETETNLKKKLDIQQKSLKQYYQQQM 464
Cdd:TIGR04523 406 LNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLE 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 465 ENV--VAKKMQEFqDQLDKNEEHLKNEARERERLIAERAVKQLEMINEKNNQELNLIQEKHNEEVELYRLQLANASKKID 542
Cdd:TIGR04523 486 QKQkeLKSKEKEL-KKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEID 564
|
....*..
gi 442629624 543 EMDLKLS 549
Cdd:TIGR04523 565 EKNKEIE 571
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
232-493 |
9.37e-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: 9.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 232 LKEEQLRRQHLEKMVHTLQSHLLEYQQRISVAIEVD---------RSKDAALTEAEQTVQSL---NYEVQHLRDAVHRLE 299
Cdd:COG4913 619 LAELEEELAEAEERLEALEAELDALQERREALQRLAeyswdeidvASAEREIAELEAELERLdasSDDLAALEEQLEELE 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 300 ADRGESQSRFDALQNELSQAVNLATRFQEKNDKLERELDHCRQDAKQW-EERLEQlemqlnssKRAEELSHAELNKLRDK 378
Cdd:COG4913 699 AELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLElRALLEE--------RFAAALGDAVERELREN 770
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 379 FAKvdyQQEKLKARIEELEKEnntLTNQkemLQEYHQKQKARADSLESHRKSLQETLANLTE-TETNLKKKldiqQKSLK 457
Cdd:COG4913 771 LEE---RIDALRARLNRAEEE---LERA---MRAFNREWPAETADLDADLESLPEYLALLDRlEEDGLPEY----EERFK 837
|
250 260 270
....*....|....*....|....*....|....*.
gi 442629624 458 QYYQQQMENVVAkkmqEFQDQLDKNEEhlknEARER 493
Cdd:COG4913 838 ELLNENSIEFVA----DLLSKLRRAIR----EIKER 865
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
268-549 |
1.59e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.14 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 268 RSKDAALTEAEQTVQSLNYEVQHLRDAVHRLEadrgESQSRFDALQNELSQAvnlatrfQEKNDKLERELDHCRQDAKQW 347
Cdd:PRK03918 196 KEKEKELEEVLREINEISSELPELREELEKLE----KEVKELEELKEEIEEL-------EKELESLEGSKRKLEEKIREL 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 348 EERLEQLEMQLNS-SKRAEELShaELNKLRDKFAKVDYQQEKLKARIEELEKENNTLTNQKEMLQEYHQKQKARADSLES 426
Cdd:PRK03918 265 EERIEELKKEIEElEEKVKELK--ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 427 HRKSLQETLANLTETETNLKKKLDIQQKslkqyyQQQMENVVAKKMQEFQDQLDKNEEHLKNEARERERLIAERAVKQLE 506
Cdd:PRK03918 343 LKKKLKELEKRLEELEERHELYEEAKAK------KEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGE 416
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 507 MINEKNNQELNLIQ----------------EKHNEEV-ELYRLQLANASKKIDEMDLKLS 549
Cdd:PRK03918 417 LKKEIKELKKAIEElkkakgkcpvcgreltEEHRKELlEEYTAELKRIEKELKEIEEKER 476
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
232-562 |
2.94e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.34 E-value: 2.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 232 LKEEQLRRQHLEkmvhTLQSHLLEYQQRISvaiEVDRSKDA---ALTEAEQTVQSLNYEVQHLRD-------AVHRLEAD 301
Cdd:PRK02224 243 LEEHEERREELE----TLEAEIEDLRETIA---ETEREREElaeEVRDLRERLEELEEERDDLLAeaglddaDAEAVEAR 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 302 RGESQSRFDALQNELSQ-------AVNLATRFQEKNDKLERELDHCRQDAKQWEERLEQLEMQLNSSKRAEELSHAELNK 374
Cdd:PRK02224 316 REELEDRDEELRDRLEEcrvaaqaHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEE 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 375 LRDKFAKVDYQQEKLKARIEELEKENN-----------TLTNQKEMLQEYHQKQKA--------------RADSLESHRK 429
Cdd:PRK02224 396 LRERFGDAPVDLGNAEDFLEELREERDelrereaeleaTLRTARERVEEAEALLEAgkcpecgqpvegspHVETIEEDRE 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 430 ---SLQETLANLTETETNLKKKLDiqqkslkqyyqqqmenvVAKKMQEFQDQLDKneehLKNEARERERLIAERAvkqlE 506
Cdd:PRK02224 476 rveELEAELEDLEEEVEEVEERLE-----------------RAEDLVEAEDRIER----LEERREDLEELIAERR----E 530
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 442629624 507 MINEKNNQ--ELNLIQEKHNEEVELYRLQLANASKKIDEMDLKLSCYKTKRADIAEKL 562
Cdd:PRK02224 531 TIEEKRERaeELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERI 588
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
310-516 |
3.46e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 3.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 310 DALQNELSQAVNLATRFQEKNDKLERELDHCRQDAKQWEERLEQLEMQLNSSKRAEELSHAELNKLRDKFAKVDyQQEKL 389
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE-KLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 390 KARIEELEKENNTLTNQKEMLQEYHQKQKARADsleshrksLQETLANLTETETNLKKKLDIQQKSLKQYYQQQMENvVA 469
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEERLEELRE--------LEEELEELEAELAELQEELEELLEQLSLATEEELQD-LA 198
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 442629624 470 KKMQEFQDQLDKNEEHLKNEARERERLIAERAVKQLEMINEKNNQEL 516
Cdd:COG4717 199 EELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERL 245
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
263-433 |
4.64e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 4.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 263 AIEVDRSKDAALTEAEQTVQSLNYEVQHLRDAVHRLEADRGESQSRFDALQNELsQAVNLATRFQEKNDKLE---RELDH 339
Cdd:COG4717 72 ELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL-QLLPLYQELEALEAELAelpERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 340 CRQDAKQWEERLEQLEMQLNSSKRAEElshaELNKLRDKFAKVDYQQ-EKLKARIEELEKENNTLTNQKEMLQEYHQKQK 418
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQE----ELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELEELE 226
|
170
....*....|....*
gi 442629624 419 ARADSLESHRKSLQE 433
Cdd:COG4717 227 EELEQLENELEAAAL 241
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
294-568 |
5.40e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 5.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 294 AVHRLEADRGESQSRFDALQNELSQAVNLATRFQEKNDKLE-------------RELDHCRQDAKQWEERLEQLEMQLNS 360
Cdd:PRK03918 163 AYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEevlreineisselPELREELEKLEKEVKELEELKEEIEE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 361 SKRAEELSHAELNKLRDKFAKVDYQQEKLKARIEELEKENNTLTNQKEMLQEYHQKQKARADSLESHRKsLQETLANLTE 440
Cdd:PRK03918 243 LEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELRE-IEKRLSRLEE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 441 TETNLKKKLdiqqkslkqyyqqqmenvvaKKMQEFQDQLDKNEEHLKNEARERERLiaERAVKQLEMINEKNNQELNLIQ 520
Cdd:PRK03918 322 EINGIEERI--------------------KELEEKEERLEELKKKLKELEKRLEEL--EERHELYEEAKAKKEELERLKK 379
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 442629624 521 EKHNEEVELYRLQLANASKKIDEMDLKLSCYKTKRADIAEKLHGVMEA 568
Cdd:PRK03918 380 RLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKA 427
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
251-492 |
5.75e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 46.48 E-value: 5.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 251 SHLLEYQQRISVAievdrskDAALTEAEQTVQSlnyeVQHLRDAVHRLEADrgesqsrfdalqnelSQAVNLATRFqekn 330
Cdd:COG3096 455 EEVLELEQKLSVA-------DAARRQFEKAYEL----VCKIAGEVERSQAW---------------QTARELLRRY---- 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 331 dkleRELDHCRQDAKQWEERLEQLEMQLNSSKRAEELShAELNKL----RDKFAKVDYQQEKLKARIEELEKENNTLTNQ 406
Cdd:COG3096 505 ----RSQQALAQRLQQLRAQLAELEQRLRQQQNAERLL-EEFCQRigqqLDAAEELEELLAELEAQLEELEEQAAEAVEQ 579
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 407 KEMLQEYHQKQKARADSLES---HRKSLQETLANL-TETETNLKKKLDIQqkslkQYYQQQMENVVAKKMQEfqDQLDKN 482
Cdd:COG3096 580 RSELRQQLEQLRARIKELAArapAWLAAQDALERLrEQSGEALADSQEVT-----AAMQQLLEREREATVER--DELAAR 652
|
250
....*....|
gi 442629624 483 EEHLKNEARE 492
Cdd:COG3096 653 KQALESQIER 662
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
322-533 |
5.80e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 5.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 322 LATRFQEKNDKLEReldhcrQDAKQWEERLEQLEmQLNSSKRAEELSHAELNKLRDKFAKVDYQQEKLKARIEELEKENN 401
Cdd:COG4717 47 LLERLEKEADELFK------PQGRKPELNLKELK-ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 402 TLTNQKEMLQEYHQKQKARA--DSLESHRKSLQETLANLTETETNLKKKLDiQQKSLKQYYQQQMENVVAKKMQEFQDQL 479
Cdd:COG4717 120 KLEKLLQLLPLYQELEALEAelAELPERLEELEERLEELRELEEELEELEA-ELAELQEELEELLEQLSLATEEELQDLA 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 442629624 480 DKNEEHlknearERERLIAERAVKQLEMINEKNNQELNLIQEKHNEEVELYRLQ 533
Cdd:COG4717 199 EELEEL------QQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLK 246
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
325-510 |
6.70e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 45.86 E-value: 6.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 325 RFQEKNDKLERELDHCRQDAkQWEERLEQLEMQLNSSKRAEELSHAELNKLRDKFAKVDYQQEKLKARIEELEKENNTLT 404
Cdd:PRK12705 23 VLLKKRQRLAKEAERILQEA-QKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 405 NQKEMLQEYHQKQKARADSLESHRKSLQETL---ANLTETETN--LKKKLDIQQKSLKQYYQQQMENvvakkmqEFQDQL 479
Cdd:PRK12705 102 NLENQLEEREKALSARELELEELEKQLDNELyrvAGLTPEQARklLLKLLDAELEEEKAQRVKKIEE-------EADLEA 174
|
170 180 190
....*....|....*....|....*....|...
gi 442629624 480 DKNEEHLKNEARER--ERLIAERAVKQLEMINE 510
Cdd:PRK12705 175 ERKAQNILAQAMQRiaSETASDLSVSVVPIPSD 207
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
239-547 |
6.81e-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: 6.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 239 RQHLEKMVHTLQSHLLEYQQRISVAIEVDRSKDAALTEAEQTVQSLNYEVQHLRDAVhrLEADRGESQSRFDaLQNELSQ 318
Cdd:pfam15921 73 KEHIERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAM--ADIRRRESQSQED-LRNQLQN 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 319 AVN-LATRFQEKNDKLE---RELDHCRQDAKQWEERLEQL-----EMQLNSSKRAEE---LSHAELNKLRDKFAKV---- 382
Cdd:pfam15921 150 TVHeLEAAKCLKEDMLEdsnTQIEQLRKMMLSHEGVLQEIrsilvDFEEASGKKIYEhdsMSTMHFRSLGSAISKIlrel 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 383 DYQQEKLKARIEELEKENNTL----TNQKEMLQEYHQkqkaraDSLESHRKSLQETLANLTETETNLKKKLDIQQKSLkQ 458
Cdd:pfam15921 230 DTEISYLKGRIFPVEDQLEALksesQNKIELLLQQHQ------DRIEQLISEHEVEITGLTEKASSARSQANSIQSQL-E 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 459 YYQQQMENVVAKKMQEFQDqLDKNEEHLKNEARERERLIA---ERAVKQLEMIN----EKNNQELNLIQEKHNEEVELYR 531
Cdd:pfam15921 303 IIQEQARNQNSMYMRQLSD-LESTVSQLRSELREAKRMYEdkiEELEKQLVLANseltEARTERDQFSQESGNLDDQLQK 381
|
330
....*....|....*.
gi 442629624 532 LqLANASKKIDEMDLK 547
Cdd:pfam15921 382 L-LADLHKREKELSLE 396
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
332-506 |
1.14e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.72 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 332 KLERELDHCRQDAKQWEERLEQLEMQLNSSKRAEELSHAELNKLRDKFAKVD---YQQEKLKARIEELEKENNTLTNQKE 408
Cdd:PRK04863 290 ELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQtalRQQEKIERYQADLEELEERLEEQNE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 409 MLQEYHQKQ---KARADSLESHRKSLQETLANLTEtetnlkkKLDIQQKSLKQYYQ--QQMENV---------VAKKMQE 474
Cdd:PRK04863 370 VVEEADEQQeenEARAEAAEEEVDELKSQLADYQQ-------ALDVQQTRAIQYQQavQALERAkqlcglpdlTADNAED 442
|
170 180 190
....*....|....*....|....*....|....
gi 442629624 475 FQDQLDKNEEHLKNEARERERL--IAERAVKQLE 506
Cdd:PRK04863 443 WLEEFQAKEQEATEELLSLEQKlsVAQAAHSQFE 476
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
232-506 |
1.40e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 45.33 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 232 LKEEQLRRQHLEKMVHTLQSHLLEYQQRIsvaievdrskdAALTEAEQTVQSLNYEVQHLRDAVHrleadrgesQSRFDA 311
Cdd:COG3096 838 LAALRQRRSELERELAQHRAQEQQLRQQL-----------DQLKEQLQLLNKLLPQANLLADETL---------ADRLEE 897
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 312 LQNELSQAvNLATRFQEKNDK----LERELDHCRQDAKQWEE---RLEQLEMQLNSSK-RAEELShaELNKLRDKFAKVD 383
Cdd:COG3096 898 LREELDAA-QEAQAFIQQHGKalaqLEPLVAVLQSDPEQFEQlqaDYLQAKEQQRRLKqQIFALS--EVVQRRPHFSYED 974
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 384 YQQ---------EKLKARIEELEKENNTLTNQKEMLQEYHQKQKARADSLESHRKSLQETLANLTETETNLKKKLDiqqk 454
Cdd:COG3096 975 AVGllgensdlnEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQAD---- 1050
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 442629624 455 slkqyyqQQMENVVAKKMQEFQDQLDKNEEHlKNEArERERLIAERAVKQLE 506
Cdd:COG3096 1051 -------AEAEERARIRRDELHEELSQNRSR-RSQL-EKQLTRCEAEMDSLQ 1093
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
305-500 |
1.44e-04 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 44.84 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 305 SQSRFDALQNELSQAVNLATRF-----QEKNDKLERELDHCRQDAKQWEERLEQLemqlnssKRAEELSHAELNKLRDKF 379
Cdd:pfam06160 58 VTKSLPDIEELLFEAEELNDKYrfkkaKKALDEIEELLDDIEEDIKQILEELDEL-------LESEEKNREEVEELKDKY 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 380 AKVdyqQEKLKAR-------IEELEKEnntLTNQKEMLQEYHQKQ------KAR--ADSLESHRKSLQETLANLTETETN 444
Cdd:pfam06160 131 REL---RKTLLANrfsygpaIDELEKQ---LAEIEEEFSQFEELTesgdylEARevLEKLEEETDALEELMEDIPPLYEE 204
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442629624 445 LKKKLDIQQKSLKQYYQQQME-------NVVAKKMQEFQDQLDKNEEHLKN----EARERERLIAER 500
Cdd:pfam06160 205 LKTELPDQLEELKEGYREMEEegyalehLNVDKEIQQLEEQLEENLALLENleldEAEEALEEIEER 271
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
260-548 |
1.68e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 260 ISVAIEVDRSKDAALTEAEQTVQSLNYEVQHLRDAVHRLEADRGESQSRFDALQNELSQAVNLATRFQEKNDKLERELDH 339
Cdd:COG4372 26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELES 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 340 CRQDAKQWEERLEQLEMQLNSSKRAEELSHAELNKLRDKFAKVDYQQEKLKARIEELEKENNTLTNQKEMLQEYHQKQKa 419
Cdd:COG4372 106 LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQA- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 420 radsLESHRKSLQETLANLTETETNLKKKLDIQQKSLKQYYQQQMENVVAKKMQEFQDQLDKNEEHLKNEARERERLIAE 499
Cdd:COG4372 185 ----LDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEI 260
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 442629624 500 RAVKQLEMINEKNNQELNLIQEKHNEEVELYRLQLANASKKIDEMDLKL 548
Cdd:COG4372 261 EELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSL 309
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
232-561 |
1.91e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 232 LKEEQLRRQHLEKMVHTLQSHLLEYQQRIsvaiEVDRSKDAALTEAEQTVQSLNYEVQHLRDAVHRLEADRGESQsrfda 311
Cdd:COG4717 120 KLEKLLQLLPLYQELEALEAELAELPERL----EELEERLEELRELEEELEELEAELAELQEELEELLEQLSLAT----- 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 312 lQNELSQAVNLATRFQEKNDKLERELDHCRQDAKQWEERLEQLEMQLNSSKRAEELSHAE-------------------- 371
Cdd:COG4717 191 -EEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARlllliaaallallglggsll 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 372 ---------------------LNKLRDKFAKVDYQQE-KLKARIEELEKENntltnQKEMLQEYHQKQKARADSLESHRK 429
Cdd:COG4717 270 sliltiagvlflvlgllallfLLLAREKASLGKEAEElQALPALEELEEEE-----LEELLAALGLPPDLSPEELLELLD 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 430 SLQETLANLTETETnLKKKLDIQQ--------------KSLKQYYQQQMEnvvAKKMQEFQDQLDKNEEHLKNEARERER 495
Cdd:COG4717 345 RIEELQELLREAEE-LEEELQLEEleqeiaallaeagvEDEEELRAALEQ---AEEYQELKEELEELEEQLEELLGELEE 420
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442629624 496 LIAERAVKQLEMINEKNNQELNLIQEKHNEEVE-----LYRLQLANASKKIDEMDLKLSCYKTKRADIAEK 561
Cdd:COG4717 421 LLEALDEEELEEELEELEEELEELEEELEELREelaelEAELEQLEEDGELAELLQELEELKAELRELAEE 491
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
326-442 |
2.09e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.38 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 326 FQEKNDKLERELDHCRQDAKQWEERLEQLEMQLNSskraeelshaELNKLRDKFAKVDYQQEKLKARIEELEKenntltn 405
Cdd:PRK12704 66 IHKLRNEFEKELRERRNELQKLEKRLLQKEENLDR----------KLELLEKREEELEKKEKELEQKQQELEK------- 128
|
90 100 110
....*....|....*....|....*....|....*..
gi 442629624 406 QKEMLQEYHQKQKARadsLEShrkslqetLANLTETE 442
Cdd:PRK12704 129 KEEELEELIEEQLQE---LER--------ISGLTAEE 154
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
273-578 |
2.11e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.94 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 273 ALTEAEQTVQSLNYEVQHLRDAVHRLEADRGESQSRFDALQNelsqavnlATRFQEKndklereLDHCRQDAKQWEERLE 352
Cdd:COG3096 300 QLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQT--------ALRQQEK-------IERYQEDLEELTERLE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 353 QLEMQLNSSK----RAEELSHA---ELNKLRDKFAkvDYQQ--EKLKARIEELEKENNTLTNQKEMLQEYHQKQKARADS 423
Cdd:COG3096 365 EQEEVVEEAAeqlaEAEARLEAaeeEVDSLKSQLA--DYQQalDVQQTRAIQYQQAVQALEKARALCGLPDLTPENAEDY 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 424 LESHRKSLQEtlanLTETETNLKKKLDIQQKSLKQYYQ--QQMENVVA---------------KKMQEFQDQLDkNEEHL 486
Cdd:COG3096 443 LAAFRAKEQQ----ATEEVLELEQKLSVADAARRQFEKayELVCKIAGeversqawqtarellRRYRSQQALAQ-RLQQL 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 487 KNEARERERLIAE--RAVKQLEMINEKNNQELN------LIQEKHNEEVELYRLQLANASKKIDEMDLKLSCYKTKRADI 558
Cdd:COG3096 518 RAQLAELEQRLRQqqNAERLLEEFCQRIGQQLDaaeeleELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKEL 597
|
330 340
....*....|....*....|
gi 442629624 559 AEKlhgvmEAQWQQALAILT 578
Cdd:COG3096 598 AAR-----APAWLAAQDALE 612
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
321-626 |
2.19e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 321 NLATRFQEKNDKLE--RELDHCRQDAKQWEERLEQLEMQLNSSKRAEELSHAELNKLRDKFAKVDYQQEKLKAriEELEK 398
Cdd:PTZ00121 1577 NMALRKAEEAKKAEeaRIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKA--EELKK 1654
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 399 ENNTLTNQKEMLQEYHQKQKARADSL---ESHRKSLQETLANLTETE---TNLKKKLDIQQKSLKQYYQQQMENVV-AKK 471
Cdd:PTZ00121 1655 AEEENKIKAAEEAKKAEEDKKKAEEAkkaEEDEKKAAEALKKEAEEAkkaEELKKKEAEEKKKAEELKKAEEENKIkAEE 1734
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 472 MQEFQDQLDKNEEHLKNEARERERlIAERAVKQLEMINEKNNQELNLIQEKHNEEVELYRLQLANASKKIDEmDLKLSCY 551
Cdd:PTZ00121 1735 AKKEAEEDKKKAEEAKKDEEEKKK-IAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFD-NFANIIE 1812
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442629624 552 KTKRADIAEKLHGVMEAQWQQALAIlttpSQNSIIQSSDTEASESPELNNarmypETPKSSKSQRSNNTEKNNLD 626
Cdd:PTZ00121 1813 GGKEGNLVINDSKEMEDSAIKEVAD----SKNMQLEEADAFEKHKFNKNN-----ENGEDGNKEADFNKEKDLKE 1878
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
230-440 |
2.39e-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: 44.67 E-value: 2.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 230 SSLKEEQLRRQHLEKMVHTLQSHLLEYQQRI-SVAIEVD------RSKDAALTEAEQTVQSLNYEVQHLRDAVHRLEADR 302
Cdd:TIGR02169 819 QKLNRLTLEKEYLEKEIQELQEQRIDLKEQIkSIEKEIEnlngkkEELEEELEELEAALRDLESRLGDLKKERDELEAQL 898
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 303 GEsqsrfdalqnelsqavnlatrFQEKNDKLERELDHCRQDAKQWEERLEQLEMQLNS---SKRAEELSHAELNKLRDkf 379
Cdd:TIGR02169 899 RE---------------------LERKIEELEAQIEKKRKRLSELKAKLEALEEELSEiedPKGEDEEIPEEELSLED-- 955
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442629624 380 akVDYQQEKLKARIEELEKENNTLTNQKEMLQEYHQKQKARADSLESHRKSLQETLANLTE 440
Cdd:TIGR02169 956 --VQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
316-479 |
2.45e-04 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 44.36 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 316 LSQAVNLATRFQEKNDKLERELDHCRQDAKQWEERLEQLEMQLNSSKRAEELSHAELNKLRDKFAKVDYQQEKLKARIEE 395
Cdd:pfam07111 61 LSQQAELISRQLQELRRLEEEVRLLRETSLQQKMRLEAQAMELDALAVAEKAGQAEAEGLRAALAGAEMVRKNLEEGSQR 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 396 LEKENNTLtnQKEMLQEYHQKQKARADSLESHRKSLQETLANLtetetNLKKKLDIQQKSLKQYYQQQMENVVAKKMQEF 475
Cdd:pfam07111 141 ELEEIQRL--HQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSL-----ETKRAGEAKQLAEAQKEAELLRKQLSKTQEEL 213
|
....
gi 442629624 476 QDQL 479
Cdd:pfam07111 214 EAQV 217
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
238-549 |
2.56e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 44.24 E-value: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 238 RRQHLEKMVHTLQSHLLEYQQRIsvaievdRSKDAALTEAEQTVQSLNYEVQHLRDAVHRLEADRGESQSRFDALQNELS 317
Cdd:TIGR04523 34 EEKQLEKKLKTIKNELKNKEKEL-------KNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 318 qavnlatrfqekndKLERELDHCRQDAKQWEERLEQLEMQLNSSKRAEELSHAELNKLRDKFAKVDYQQEKLKARIEELE 397
Cdd:TIGR04523 107 --------------KINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 398 KENNTLTNQKEMLQEYHQKQKARADSLE----------SHRKSLQETLANLTETETNLKKKLDIQQKSLKQyyQQQMENV 467
Cdd:TIGR04523 173 NELNLLEKEKLNIQKNIDKIKNKLLKLElllsnlkkkiQKNKSLESQISELKKQNNQLKDNIEKKQQEINE--KTTEISN 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 468 VAKKMQEFQDQLDKNEEHLKNEARERERliAERAVKQLE-MINEKNNQELNLIQEKHNEEVELYRLQLANASKKIDEMDL 546
Cdd:TIGR04523 251 TQTQLNQLKDEQNKIKKQLSEKQKELEQ--NNKKIKELEkQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQN 328
|
...
gi 442629624 547 KLS 549
Cdd:TIGR04523 329 QIS 331
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
265-422 |
2.77e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 265 EVDRSKDAALTEAeqtvqslNYEVQHLRdavHRLEADRGESQSRFDALQNELSQAVNLATRFQEKNDKLERELDHCRQDA 344
Cdd:PRK12704 50 EAEAIKKEALLEA-------KEEIHKLR---NEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKEL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 345 KQWEERLEQLEmqlnssKRAEELSHAELNKLrDKFAKvdYQQEKLKARI-EELEKEnntLTNQK-EMLQEYHQKQKARAD 422
Cdd:PRK12704 120 EQKQQELEKKE------EELEELIEEQLQEL-ERISG--LTAEEAKEILlEKVEEE---ARHEAaVLIKEIEEEAKEEAD 187
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
235-499 |
3.56e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.01 E-value: 3.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 235 EQLRR--QHLEKMVHTLQSHLLEYQQRIsvaievdRSKDAALTEAEQTVQSLNYEVQHLRDAVHRLEADRGESQSRFDAL 312
Cdd:pfam01576 366 EQAKRnkANLEKAKQALESENAELQAEL-------RTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKL 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 313 QNELSQAVNLATRFQEKNDKLERELDhcrqdakQWEERLEQLEMQLNSSKRAEELSHAELNKLRDKFAKVDYQQEKLKAR 392
Cdd:pfam01576 439 QSELESVSSLLNEAEGKNIKLSKDVS-------SLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEA 511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 393 IEELEKENNTLTNQKEMLQEYHQKQKARADSLESHRKSLQETLANLT---ETETNLKKKLDIQQKSLKQYY--------- 460
Cdd:pfam01576 512 KRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTqqlEEKAAAYDKLEKTKNRLQQELddllvdldh 591
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 442629624 461 QQQMENVVAKKMQEFqDQLDKNEEHLKNE-ARERERLIAE 499
Cdd:pfam01576 592 QRQLVSNLEKKQKKF-DQMLAEEKAISARyAEERDRAEAE 630
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
352-533 |
3.91e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.85 E-value: 3.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 352 EQLEMQLNSSKRAEELSHAELNKLRDKFAKVDYQQEKLKAR--IEELEKENNTLTNQKEMLQEYHQKQKARADSLESHRK 429
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 430 SLQETLANLTETETNLKKKLDIQQksLKQYYQQ---QMENVVAK------KMQEFQDQLDKNEEHLKNEAR------ERE 494
Cdd:COG3206 244 ALRAQLGSGPDALPELLQSPVIQQ--LRAQLAEleaELAELSARytpnhpDVIALRAQIAALRAQLQQEAQrilaslEAE 321
|
170 180 190
....*....|....*....|....*....|....*....
gi 442629624 495 RLIAERAVKQLEMINEKNNQELNLIQEKhneEVELYRLQ 533
Cdd:COG3206 322 LEALQAREASLQAQLAQLEARLAELPEL---EAELRRLE 357
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
273-562 |
4.82e-04 |
|
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.
Pssm-ID: 427715 [Multi-domain] Cd Length: 360 Bit Score: 43.15 E-value: 4.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 273 ALTEAEQTVQSLNYEVQHLRDAVHRLEADRGESQSRFDALQNELSQAVNLATRFQEKNDKLERELDHCRQDAK----QWE 348
Cdd:pfam04108 1 SLSSAQDLCRWANELLTDARSLLEELVVLLAKIAFLRRGLSVQLANLEKVREGLEKVLNELKKDFKQLLKDLDaaleRLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 349 ERLEQLEMQLNSSKRAEE----------LSHAELNKLRDKFAKvdyQQEKLKARIEELEKENNTLTNQKEMLQEYHQKQK 418
Cdd:pfam04108 81 ETLDKLRNTPVEPALPPGeekqktlldfIDEDSVEILRDALKE---LIDELQAAQESLDSDLKRFDDDLRDLQKELESLS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 419 ARADSLESHRKSLQETLANLTETETNLkkkldiqqKSLKQYYQQQMENVvakkmQEFQDQLDKNEEHLKNEARERERLIA 498
Cdd:pfam04108 158 SPSESISLIPTLLKELESLEEEMASLL--------ESLTNHYDQCVTAV-----KLTEGGRAEMLEVLENDARELDDVVP 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442629624 499 ERAVKQLEMinEKNNQELNLIQEKHNEEVElyrlQLANASKKIDEMDLKLSCYKTKRADIAEKL 562
Cdd:pfam04108 225 ELQDRLDEM--ENNYERLQKLLEQKNSLID----ELLSALQLIAEIQSRLPEYLAALKEFEERW 282
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
301-501 |
6.05e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 6.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 301 DRGESQSRFDALQN---ELSQAVNLATRFQEKNDKLERELDHCRQDAKQWEeRLEQLEmqlnsskraeelshAELNKLRD 377
Cdd:COG4913 219 EEPDTFEAADALVEhfdDLERAHEALEDAREQIELLEPIRELAERYAAARE-RLAELE--------------YLRAALRL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 378 KFAKVDYQQekLKARIEELEKENNTLTNQKEMLQEYHQKQKARADSLE-SHRKSLQETLANLTETETNLKKKLDIQQKSL 456
Cdd:COG4913 284 WFAQRRLEL--LEAELEELRAELARLEAELERLEARLDALREELDELEaQIRGNGGDRLEQLEREIERLERELEERERRR 361
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 442629624 457 KQyYQQQMENV---VAKKMQEFQDQLDKNEEHLKNEARERERLIAERA 501
Cdd:COG4913 362 AR-LEALLAALglpLPASAEEFAALRAEAAALLEALEEELEALEEALA 408
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
271-523 |
6.11e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 42.90 E-value: 6.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 271 DAALTEAEQTVQSLNYEVQHLRDAVHRLEADRGESQSRFDALQNELsqavnLATRFQ--EKNDKLERELDhcrqdakQWE 348
Cdd:PRK04778 111 ESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRKSL-----LANRFSfgPALDELEKQLE-------NLE 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 349 ERLEQLEmQLNSSKRAEElSHAELNKLRDKFAKVDYQQEKLKARIEELEKE-----NNTLTNQKEMLQE-YHQKQKARAD 422
Cdd:PRK04778 179 EEFSQFV-ELTESGDYVE-AREILDQLEEELAALEQIMEEIPELLKELQTElpdqlQELKAGYRELVEEgYHLDHLDIEK 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 423 SLESHRKSLQETLANLTETE-TNLKKKLDIQQKSLKQYYqQQME------NVVAKKMQEFQDQLDKNEEHLKNEARERER 495
Cdd:PRK04778 257 EIQDLKEQIDENLALLEELDlDEAEEKNEEIQERIDQLY-DILErevkarKYVEKNSDTLPDFLEHAKEQNKELKEEIDR 335
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 442629624 496 L-----IAERAV-------KQLEMINEKNNQELNLIQEKH 523
Cdd:PRK04778 336 VkqsytLNESELesvrqleKQLESLEKQYDEITERIAEQE 375
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
230-560 |
6.86e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.09 E-value: 6.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 230 SSLKEEqlrRQHLEKMVHTLQSHLLEYQQRISVAIEVDRSKDAALTEAEQTVQSLNYEVQH-------LRDAVHRLEADR 302
Cdd:TIGR04523 345 SQLKKE---LTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNqeklnqqKDEQIKKLQQEK 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 303 GESQSRFDALQNELSQAVNLATRFQEKNDKLERELDHCRQDAKQWEERLEQLEMQLNSSKRAEELSHAELNKLRDKFAKV 382
Cdd:TIGR04523 422 ELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKL 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 383 DYQQEKLKARIEELEKENNTLTNQKEMLQEYHQKQKARADSLESHRKSLQETLanlteTETNLKKKLDIQQKSLKQYYQQ 462
Cdd:TIGR04523 502 NEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFEL-----KKENLEKEIDEKNKEIEELKQT 576
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 463 QMENVVA-KKMQEFQDQLDKNEEHLKNEARERERLIA--ERAVKQLEMINEKNNQELNLIQEKHN---EEVELYRLQLAN 536
Cdd:TIGR04523 577 QKSLKKKqEEKQELIDQKEKEKKDLIKEIEEKEKKISslEKELEKAKKENEKLSSIIKNIKSKKNklkQEVKQIKETIKE 656
|
330 340
....*....|....*....|....
gi 442629624 537 ASKKIDEMDLKLSCYKTKRADIAE 560
Cdd:TIGR04523 657 IRNKWPEIIKKIKESKTKIDDIIE 680
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
233-547 |
7.20e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 7.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 233 KEEQLRRQHLEKMVHT--LQSHLLEYQQRISVAIEVDRSKDAALTEAEQTVQSlnyevQHLRDAVHRLEADRGESQSRFD 310
Cdd:PTZ00121 1576 KNMALRKAEEAKKAEEarIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA-----EEEKKKVEQLKKKEAEEKKKAE 1650
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 311 ALQNELSQAVNLATRFQEKNDKLERELDHCRQDAKQWEERLEQLEMQLNSSKRAEELSHAELNKLRdKFAKVDYQQEKLK 390
Cdd:PTZ00121 1651 ELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKK-KAEELKKAEEENK 1729
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 391 ARIEELEKENNTLTNQKEMLQ-EYHQKQKARADSLESHRKSLQETLANLTETETNLKKK-------LDIQQKSLKQYYQQ 462
Cdd:PTZ00121 1730 IKAEEAKKEAEEDKKKAEEAKkDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEdekrrmeVDKKIKDIFDNFAN 1809
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 463 QME-----NVVAKKMQEFQDQLDKNEEHLKNEARERERLIAERAVKQLEMINEKNNQELNLIQEKHNEEVELYRLQLANA 537
Cdd:PTZ00121 1810 IIEggkegNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADE 1889
|
330
....*....|
gi 442629624 538 SKKIDEMDLK 547
Cdd:PTZ00121 1890 IEKIDKDDIE 1899
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
332-532 |
8.36e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.02 E-value: 8.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 332 KLERELDHCRQDAKQWEERLEQLEMQLNSSKRAEELSHAELNKLRDKFAKVD---YQQEKLKARIEELEKENNTLTNQKE 408
Cdd:COG3096 289 ELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQtalRQQEKIERYQEDLEELTERLEEQEE 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 409 ML---QEYHQKQKARADSLESHRKSLQETLAnltetetNLKKKLDIQQKSLKQYYQ--QQMENvvAKKMQEFQDQLDKNE 483
Cdd:COG3096 369 VVeeaAEQLAEAEARLEAAEEEVDSLKSQLA-------DYQQALDVQQTRAIQYQQavQALEK--ARALCGLPDLTPENA 439
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 442629624 484 EHLKNEARERERLIAERaVKQLEmineknnQELNLIQEKHNEEVELYRL 532
Cdd:COG3096 440 EDYLAAFRAKEQQATEE-VLELE-------QKLSVADAARRQFEKAYEL 480
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
248-447 |
8.78e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.64 E-value: 8.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 248 TLQSHLLEYQQRISVAIEVDRSKD---AALTEAEQTVQSLNYEVQH---LRDAVHRLEADRGESQSRFDAL--------- 312
Cdd:PRK04863 891 TLADRVEEIREQLDEAEEAKRFVQqhgNALAQLEPIVSVLQSDPEQfeqLKQDYQQAQQTQRDAKQQAFALtevvqrrah 970
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 313 ------QNELSQAVNLATRFQEKNDKLERELDHCRQDAKQWEERL---EQLEMQLNSSKRAEELSHAELNKLRDKFAkVD 383
Cdd:PRK04863 971 fsyedaAEMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLaqyNQVLASLKSSYDAKRQMLQELKQELQDLG-VP 1049
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442629624 384 YQQ---EKLKARIEELEKENNTLTNQKEMLQEYHQKQKARADSLESHRKSLQETLANLTETETNLKK 447
Cdd:PRK04863 1050 ADSgaeERARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNAKA 1116
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
236-474 |
9.14e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.80 E-value: 9.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 236 QLRRQHLEKMVHTLQSHLLEYQqrisvaIEVDRsKDAALTEAEQTVQSLNYEVQHLRDA-VHRLEADRGESQSRfDALQN 314
Cdd:pfam15921 589 QVEKAQLEKEINDRRLELQEFK------ILKDK-KDAKIRELEARVSDLELEKVKLVNAgSERLRAVKDIKQER-DQLLN 660
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 315 ELSQAVNLATRFQEKNDKLERELdhcRQDAKQWEERLEQLEMQLNSSKRAEELSHAELNKL--------------RDKFA 380
Cdd:pfam15921 661 EVKTSRNELNSLSEDYEVLKRNF---RNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMegsdghamkvamgmQKQIT 737
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 381 KVDYQQEKLKARIEELEKENNTLTNQKEMLQEYHQKQKARADSLESHRKSLQETLANLTETETNLKKKLDIQQKSLKQYY 460
Cdd:pfam15921 738 AKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKAS 817
|
250
....*....|....*.
gi 442629624 461 QQ--QMENVVAKKMQE 474
Cdd:pfam15921 818 LQfaECQDIIQRQEQE 833
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
271-440 |
9.48e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.64 E-value: 9.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 271 DAALTEAEQTVQSLNYEVQHLRDAVHRLEADRGES--------QSRFDALQNELSQAVNlATRFQEKNDK----LERELD 338
Cdd:PRK04863 850 ERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLnlladetlADRVEEIREQLDEAEE-AKRFVQQHGNalaqLEPIVS 928
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 339 HCRQDAKQWE---ERLEQLEMQLNSSK-RAEELShaELNKLRDKFAKVDYQQ---------EKLKARIEELEKENNTLTN 405
Cdd:PRK04863 929 VLQSDPEQFEqlkQDYQQAQQTQRDAKqQAFALT--EVVQRRAHFSYEDAAEmlaknsdlnEKLRQRLEQAEQERTRARE 1006
|
170 180 190
....*....|....*....|....*....|....*
gi 442629624 406 QKEMLQEYHQKQKARADSLESHRKSLQETLANLTE 440
Cdd:PRK04863 1007 QLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQ 1041
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
244-443 |
1.15e-03 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 41.17 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 244 KMVHTLQSHLLEYQQRISVAIEVDRSKDAALTEAEQTVQSLNYEVQhlrdavhRLEADRGESQSRFDALQNELSQAvnla 323
Cdd:pfam00261 1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQ-------LLEEELERTEERLAEALEKLEEA---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 324 trfQEKNDKLERELDHCRQDAKQWEERLEQLEMQLNSSKRAEE--------------LSHAELNKLRDKfakvdyqQEKL 389
Cdd:pfam00261 70 ---EKAADESERGRKVLENRALKDEEKMEILEAQLKEAKEIAEeadrkyeevarklvVVEGDLERAEER-------AELA 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 442629624 390 KARIEELEKENNTLTNQKEMLQEYHQKQKARADSLESHRKSLQEtlaNLTETET 443
Cdd:pfam00261 140 ESKIVELEEELKVVGNNLKSLEASEEKASEREDKYEEQIRFLTE---KLKEAET 190
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
304-493 |
1.33e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 304 ESQSRFDALQNELSQAVNLATRFQEKNDKLERELDHCR-QDAKQWEERLEQLE------MQLNSSKRAEELSHAELNKLR 376
Cdd:PRK03918 546 KELEKLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEpfyneyLELKDAEKELEREEKELKKLE 625
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 377 DKFAKVDYQQEKLKARIEELEKENNTLtnQKEMLQEYHQKQKARADSLESHRKSLQETLANLTETETNLKKKLDIQQKSL 456
Cdd:PRK03918 626 EELDKAFEELAETEKRLEELRKELEEL--EKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEEL 703
|
170 180 190
....*....|....*....|....*....|....*..
gi 442629624 457 KQYYQQQMENVVAKKMQEFQDQLDKNEEHLKNEARER 493
Cdd:PRK03918 704 EEREKAKKELEKLEKALERVEELREKVKKYKALLKER 740
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
327-549 |
1.58e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 41.70 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 327 QEKNDKLERELDHCRQDAKQWEERLEQLEMQLnsskRAEELSHAELNKLRDKFAKVDYQQEK----LKARIEELEKENNT 402
Cdd:pfam01576 18 KERQQKAESELKELEKKHQQLCEEKNALQEQL----QAETELCAEAEEMRARLAARKQELEEilheLESRLEEEEERSQQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 403 LTNQKEMLQEYHQKQKARADSLESHRKSLQ----ETLANLTETETNLKKKLDIQQKSLKQyyQQQMENVVAkkmqEFQDQ 478
Cdd:pfam01576 94 LQNEKKKMQQHIQDLEEQLDEEEAARQKLQlekvTTEAKIKKLEEDILLLEDQNSKLSKE--RKLLEERIS----EFTSN 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442629624 479 LDKNEEHLKNEARER---ERLIAERAVKQLEmiNEKNNQELNLIQEKHNEEVELYRLQLANASKKIDEMDLKLS 549
Cdd:pfam01576 168 LAEEEEKAKSLSKLKnkhEAMISDLEERLKK--EEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLA 239
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
332-511 |
1.59e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.68 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 332 KLERELDHCRQDAKQWEERLEQLEMQLNSSKRAEELSHAELNKLRDKFAKVDYQQEKLKARIEELEKENNTLTNQKEMlq 411
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEY-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 412 EYHQKQKaraDSLESHRKSLQETLANLTETETNLKKKLDiqqkslkqyyqqqmenvvakkmqEFQDQLDKNEEHLKNEAR 491
Cdd:COG1579 92 EALQKEI---ESLKRRISDLEDEILELMERIEELEEELA-----------------------ELEAELAELEAELEEKKA 145
|
170 180
....*....|....*....|
gi 442629624 492 ERERLIAERAvKQLEMINEK 511
Cdd:COG1579 146 ELDEELAELE-AELEELEAE 164
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
273-561 |
1.61e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 273 ALTEAEQTVQSLNYEVQHLRDAVHRLEADRGESQSRFDALQNElsQAVNLATRFQEKNDKLERELDHCRQDAKQWEERLE 352
Cdd:PRK03918 406 EISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEE--HRKELLEEYTAELKRIEKELKEIEEKERKLRKELR 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 353 QLEMQLNSSKR-------AEELSHAE--LNKLRDKFAKVDYQQ-EKLKARIEELEKENNTLTNQKEMLQEYHQKQKARAD 422
Cdd:PRK03918 484 ELEKVLKKESEliklkelAEQLKELEekLKKYNLEELEKKAEEyEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEK 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 423 SLESHRKSLQETLANLTETETNLKKKLDIQQKSLKQYYQQQMENVVAKK-MQEFQDQLDKNEEHLKNEARERERLIA--E 499
Cdd:PRK03918 564 KLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKeLEREEKELKKLEEELDKAFEELAETEKrlE 643
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442629624 500 RAVKQLEMINEKNNQE--LNLIQEKHNEEVELYRL--QLANASKKIDEMDLKLSCYKTKRADIAEK 561
Cdd:PRK03918 644 ELRKELEELEKKYSEEeyEELREEYLELSRELAGLraELEELEKRREEIKKTLEKLKEELEEREKA 709
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
297-548 |
1.79e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 41.70 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 297 RLEADRGESQSRFDALQNELSQAVNLATRFQEKNDKLERELDHCRQD--------------AKQWEERLEQLEMQLNSSK 362
Cdd:pfam01576 774 KLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASrdeilaqskesekkLKNLEAELLQLQEDLAASE 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 363 RAEELSHAELNKLRDKFA-----KVDYQQEK--LKARIEELEKENNTLTNQKEMLQEYHQKQKARADSLESHRKSLQETL 435
Cdd:pfam01576 854 RARRQAQQERDELADEIAsgasgKSALQDEKrrLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTS 933
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 436 ANLteteTNLKKKLDIQQKSLKQYYqQQMENVVAKK----MQEFQDQLDKNEEHLKNEARERErlIAERAVKQlemiNEK 511
Cdd:pfam01576 934 QKS----ESARQQLERQNKELKAKL-QEMEGTVKSKfkssIAALEAKIAQLEEQLEQESRERQ--AANKLVRR----TEK 1002
|
250 260 270
....*....|....*....|....*....|....*..
gi 442629624 512 NNQELNLIQEKHNEEVELYRLQLANASKKIDEMDLKL 548
Cdd:pfam01576 1003 KLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQL 1039
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
313-501 |
2.23e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 313 QNELSQAVNLATRF-QEKNDKLERELDHCRQDAKQ-WEERLEQLEMQLNSskRAEELSHAElNKLRDKfakvdyqQEKLK 390
Cdd:PRK12704 30 EAKIKEAEEEAKRIlEEAKKEAEAIKKEALLEAKEeIHKLRNEFEKELRE--RRNELQKLE-KRLLQK-------EENLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 391 ARIEELEKENNtltnqkemlqeyhqkqkaradSLESHRKSLQETLANLTETETNLKKKLDIQQKSLKQYYQQQMENvvAK 470
Cdd:PRK12704 100 RKLELLEKREE---------------------ELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEE--AK 156
|
170 180 190
....*....|....*....|....*....|.
gi 442629624 471 KMqefqdQLDKNEEHLKNEARERERLIAERA 501
Cdd:PRK12704 157 EI-----LLEKVEEEARHEAAVLIKEIEEEA 182
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
279-501 |
2.73e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 40.65 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 279 QTVQSLNYEVQHLRDAVHRLEADRGESQSRFDALQNELSQAVNLATRFQEKNDKLERELDHCRQDAKQWEERLEQLEMQL 358
Cdd:pfam07888 143 QRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKL 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 359 NSSKRAE---ELSHAELNKLRDKFAKVDYQQEKLKARIEELekenntltnqkemlqeyhQKQKARADSlESHRKSLQETL 435
Cdd:pfam07888 223 TTAHRKEaenEALLEELRSLQERLNASERKVEGLGEELSSM------------------AAQRDRTQA-ELHQARLQAAQ 283
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442629624 436 ANLTETETNLKKKLDIQQKSLKQYYQQQMENVVAKKMQEFQDQLDKNEEHLKNEARERERLIAERA 501
Cdd:pfam07888 284 LTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELG 349
|
|
| IFT57 |
pfam10498 |
Intra-flagellar transport protein 57; Eukaryotic cilia and flagella are specialized organelles ... |
341-456 |
2.77e-03 |
|
Intra-flagellar transport protein 57; Eukaryotic cilia and flagella are specialized organelles found at the periphery of cells of diverse organizms. Intra-flagellar transport (IFT) is required for the assembly and maintenance of eukaryotic cilia and flagella, and consists of the bidirectional movement of large protein particles between the base and the distal tip of the organelle. IFT particles contain multiple copies of two distinct protein complexes, A and B, which contain at least 6 and 11 protein subunits. IFT57 is part of complex B but is not, however, required for the core subunits to stay associated. This protein is known as Huntington-interacting protein-1 in humans.
Pssm-ID: 463118 [Multi-domain] Cd Length: 360 Bit Score: 40.71 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 341 RQDAKQWEERLEQleMQLNSSKRAEEL--SHAELNKLRDKFAKvdyQQEKLKARieelEKennTLTNQ-KEMLQEYHQKQ 417
Cdd:pfam10498 214 KADAKDWRAHLEQ--MKQHKKSIEESLpdTKSQLDKLHTDISK---TLEKIESR----EK---YINSQlEPLIQEYREAQ 281
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 442629624 418 KARADSLESHR------KSLQETLANLTETETNLKKKLDIQQKSL 456
Cdd:pfam10498 282 DELSEVQEKYKqlsegvTERTRELAEITEELEKVKQEMEERGSSM 326
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
229-543 |
3.04e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 229 SSSLKEEQLRRQHLEKMVHTLQSHLLEYQQRISVAIEVDRSKDAALTEAEQTVQSLNYEVQHLRDAVHRLEADRGESQSR 308
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 309 FDALQNELSQAVNLATRFQEKNDKLERELDHCRQDAKQWEERLEQLEMQLNSSKRAEELSHAELNKLrdkfakvdyQQEK 388
Cdd:COG4372 110 AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAL---------SEAE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 389 LKARIEELEKENNTLTNQKEMLQEYHQKQKARADSLESHRKSLQETLANLTETETNLKKKLDIQQKSLKQYYQQQMENVV 468
Cdd:COG4372 181 AEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEI 260
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442629624 469 AKKMQEFQDQLDKNEEHLKNEARERERLIAERAVKQLEMINEKNNQELNLIQEKHNEEVELYRLQLANASKKIDE 543
Cdd:COG4372 261 EELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAIL 335
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
238-438 |
3.42e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 3.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 238 RRQHLEKMVHTLQSHLLEYQQRISVAIEVDRSKDAALTEAEQTVQSLNYEVQHLRDAVHRLEADRGESQSRFDALQN--- 314
Cdd:PRK02224 517 RREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERirt 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 315 ELSQAVNLATRFQEKNDKLEreldhcrQDAKQWEERLEQLEmQLNSSKR--AEELSHAELNKLRDKFAKVDYQQEKLKAR 392
Cdd:PRK02224 597 LLAAIADAEDEIERLREKRE-------ALAELNDERRERLA-EKRERKRelEAEFDEARIEEAREDKERAEEYLEQVEEK 668
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 442629624 393 IEELEKENNTLTNQKEMLQEyhqkQKARADSLESHRKSLQETLANL 438
Cdd:PRK02224 669 LDELREERDDLQAEIGAVEN----ELEELEELRERREALENRVEAL 710
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
315-569 |
3.76e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 3.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 315 ELSQAVNLATRFQEKNDKLE--RELDHCRQDAKQWEERLEQLEMQLNSSKRAEELSHAELNKLRDKFAKVDYQQEKLKAR 392
Cdd:PTZ00121 1461 EAKKKAEEAKKADEAKKKAEeaKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAK 1540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 393 IEELEKENNTLTNQKEM-----LQEYHQKQKARADSLESHRKSlqETLANLTETETNLKKKLDIQQKSLK--QYYQQQME 465
Cdd:PTZ00121 1541 KAEEKKKADELKKAEELkkaeeKKKAEEAKKAEEDKNMALRKA--EEAKKAEEARIEEVMKLYEEEKKMKaeEAKKAEEA 1618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 466 NVVAKKMQEFQDQLDKNEEHLKNEARERERliAERAVKQLEMINEKNNQELNLIQEKHNEEVELYRLQ-----LANASKK 540
Cdd:PTZ00121 1619 KIKAEELKKAEEEKKKVEQLKKKEAEEKKK--AEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEedekkAAEALKK 1696
|
250 260
....*....|....*....|....*....
gi 442629624 541 IDEMDLKLSCYKTKRADIAEKLHGVMEAQ 569
Cdd:PTZ00121 1697 EAEEAKKAEELKKKEAEEKKKAEELKKAE 1725
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
278-492 |
4.02e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 40.49 E-value: 4.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 278 EQTVQSLNYEVQHLRDAVHRLEADRGESQSRFDALQnelSQAVNLATRFQEKNDKLERELDHCRQDAKQ----WEERLEQ 353
Cdd:pfam15921 270 EQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQ---EQARNQNSMYMRQLSDLESTVSQLRSELREakrmYEDKIEE 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 354 LEMQLNSSKRAEELSHAELNKLRDKFAKVDYQQEKLKARIEELEKEnntLTNQKEMLQEYHQKQKARADSLESHRKSLQE 433
Cdd:pfam15921 347 LEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKE---LSLEKEQNKRLWDRDTGNSITIDHLRRELDD 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 434 TLANLTETETNLKK-KLDIQQKSLKQYYQQQMENVVAKKMQEFQDQLDKNEEHLKNEARE 492
Cdd:pfam15921 424 RNMEVQRLEALLKAmKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEE 483
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
234-596 |
4.77e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 40.34 E-value: 4.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 234 EEQLRRQHLEKMvHTLQSHLLEYQQRISVAIEVDRSKDAALTEAEQTVQSLNYEVQHLRDAVHRLEADRGESQSRfdaLQ 313
Cdd:TIGR00618 363 VATSIREISCQQ-HTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQ---QR 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 314 NELSQAVNLATRFQEKNDKlERELDHCRQDAKQWEERLEQLEMQLNSSKRAEELSHAELNKLRDKFAKVDYQQEKLKARI 393
Cdd:TIGR00618 439 YAELCAAAITCTAQCEKLE-KIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPAR 517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 394 EELEKENNTLTNQKEMLQEYHQKQKARADsLESHRKSLQETLANLTETETNLKKKLDIqQKSLKQYYQQQMENVVaKKMQ 473
Cdd:TIGR00618 518 QDIDNPGPLTRRMQRGEQTYAQLETSEED-VYHQLTSERKQRASLKEQMQEIQQSFSI-LTQCDNRSKEDIPNLQ-NITV 594
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 474 EFQDQLDKNEEHLKNEARERERLIAERAVKQLEMinEKNNQELNLIQEKHNEEVELYRLQLANASKKIDEMDLKLSCYKT 553
Cdd:TIGR00618 595 RLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQ--DVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPK 672
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 442629624 554 KRADIAEKLHGVMEAQWQQALAILTT-PSQNSIIQSSDTEASES 596
Cdd:TIGR00618 673 ELLASRQLALQKMQSEKEQLTYWKEMlAQCQTLLRELETHIEEY 716
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
271-369 |
4.88e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 40.23 E-value: 4.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 271 DAALTEAEQTVQSLNYEVQHLRDAVHRLEADRGESQSRFDALQNELSQAVNLA----------TRFQEKNDKLERELDHC 340
Cdd:COG2433 405 ERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEErreirkdreiSRLDREIERLERELEEE 484
|
90 100
....*....|....*....|....*....
gi 442629624 341 RQDAKQWEERLEQLemqlnssKRAEELSH 369
Cdd:COG2433 485 RERIEELKRKLERL-------KELWKLEH 506
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
318-507 |
4.93e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 40.34 E-value: 4.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 318 QAVNLATRFQEKNDKLERELDHcRQDAKQWEERLEQLEMQLNSSKRAEELSHAELNKLRDKFAKVDyQQEKLKARIEELE 397
Cdd:TIGR00618 308 QAQRIHTELQSKMRSRAKLLMK-RAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISC-QQHTLTQHIHTLQ 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 398 KENNTLTNQKEMLQ---EYHQKQKARADSLESHRKSLQETLANLTETETNLKKKLDIQQK-SLKQYYQQQMENVVAKKMQ 473
Cdd:TIGR00618 386 QQKTTLTQKLQSLCkelDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAaITCTAQCEKLEKIHLQESA 465
|
170 180 190
....*....|....*....|....*....|....
gi 442629624 474 EFQDQLDKNEEHLKNEARERERLIAERAVKQLEM 507
Cdd:TIGR00618 466 QSLKEREQQLQTKEQIHLQETRKKAVVLARLLEL 499
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
232-396 |
5.00e-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: 5.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 232 LKEEQLRRQHLEKMVHTLQSHLLEYQQRISvAIEVDRSKDAA--LTEAEQTVQSLNYEVQHLRDAVHRLEADRGESQSRF 309
Cdd:COG4913 304 LARLEAELERLEARLDALREELDELEAQIR-GNGGDRLEQLEreIERLERELEERERRRARLEALLAALGLPLPASAEEF 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 310 DALQNELSQAVNLATRFQEKNDKLERELdhcRQDAKQWEERLEQLEMQLNSSKRAEELSHAELNKLRDKFAkvdyqqEKL 389
Cdd:COG4913 383 AALRAEAAALLEALEEELEALEEALAEA---EAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALA------EAL 453
|
....*..
gi 442629624 390 KARIEEL 396
Cdd:COG4913 454 GLDEAEL 460
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
318-504 |
5.33e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.81 E-value: 5.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 318 QAVNLATRFQEKNDKLERELDHCRQDAKQWEERLEQLEMQLNSSKRAEELSHAELNKLRDKFAK----VDYQQEKLKARI 393
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEaeaeIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 394 EELEKENNTLTN-----QKEMLQEYHQKQKARADSLESHRK---SLQETLANLTETETNLKKKLDIQQKSLKQyyQQQME 465
Cdd:COG3883 93 RALYRSGGSVSYldvllGSESFSDFLDRLSALSKIADADADlleELKADKAELEAKKAELEAKLAELEALKAE--LEAAK 170
|
170 180 190
....*....|....*....|....*....|....*....
gi 442629624 466 NVVAKKMQEFQDQLDKNEEHLKNEARERERLIAERAVKQ 504
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAE 209
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
199-433 |
5.52e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 40.27 E-value: 5.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 199 NKIISLSE-LWGKSSLTKTVLDNNSPNRPLCSSSLKEEQLRRQHLEKMVHTLQSHLL---EYQQRISVAIEVDRSKDAAL 274
Cdd:PLN02939 159 EKILTEKEaLQGKINILEMRLSETDARIKLAAQEKIHVEILEEQLEKLRNELLIRGAtegLCVHSLSKELDVLKEENMLL 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 275 TEAEQTVQSLNYEVQHLRDAVHRLEADRG-------ESQSRFDALQNELSQAVNLATR-FQEKNDKLERELDHCRQDAKQ 346
Cdd:PLN02939 239 KDDIQFLKAELIEVAETEERVFKLEKERSlldaslrELESKFIVAQEDVSKLSPLQYDcWWEKVENLQDLLDRATNQVEK 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 347 WEERLEQLEMQLNSSKRAEElSHAELNKLRDKFAKVDYQQEKLKARIEELEKENNTLTNQKEMLQEYHQKQKARADSL-- 424
Cdd:PLN02939 319 AALVLDQNQDLRDKVDKLEA-SLKEANVSKFSSYKVELLQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQDTLSKLke 397
|
....*....
gi 442629624 425 ESHRKSLQE 433
Cdd:PLN02939 398 ESKKRSLEH 406
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
232-448 |
5.65e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 5.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 232 LKEEQLRRQHLEKMVHTLQSHLLEYQQRISVAIEVDRSKDAALTEAEQTVQslnyEVQHLRDAVHRLEADrgESQSRFDA 311
Cdd:COG4717 294 AREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLD----RIEELQELLREAEEL--EEELQLEE 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 312 LQNELSQAvnLATRFQEKNDKLERELDHCRQdAKQWEERLEQLEMQLNSSKRAEELS---------HAELNKLRDKFAKV 382
Cdd:COG4717 368 LEQEIAAL--LAEAGVEDEEELRAALEQAEE-YQELKEELEELEEQLEELLGELEELlealdeeelEEELEELEEELEEL 444
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442629624 383 DYQQEKLKARIEELEKENNTLTNQK---EMLQEYHQKqKARADSLESHRKSLQETLANLTETETNLKKK 448
Cdd:COG4717 445 EEELEELREELAELEAELEQLEEDGelaELLQELEEL-KAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
304-496 |
6.20e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 39.68 E-value: 6.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 304 ESQSRFDALQNELSQAVNLATRFQEKNDKLERELdhcrqdAKQWEERLEQ-----LEMQLN--SSKRAEELshaelnklr 376
Cdd:PRK11637 93 ETQNTLNQLNKQIDELNASIAKLEQQQAAQERLL------AAQLDAAFRQgehtgLQLILSgeESQRGERI--------- 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 377 dkFAKVDYQQEKLKARIEELEKENNTLTNQKEMLQEYHQKQK-------ARADSLESHRKSLQETLANLtetETNLKKkl 449
Cdd:PRK11637 158 --LAYFGYLNQARQETIAELKQTREELAAQKAELEEKQSQQKtllyeqqAQQQKLEQARNERKKTLTGL---ESSLQK-- 230
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 442629624 450 DIQQKSLKQYYQQQMENVVAKKMQEFQDQLDKneehlknEARERERL 496
Cdd:PRK11637 231 DQQQLSELRANESRLRDSIARAEREAKARAER-------EAREAARV 270
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
452-573 |
6.92e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 39.40 E-value: 6.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 452 QQKSLKQYYQQQMENVVAKKMQEFQDQLDKNEEHLKneARERERLIAERAVKQLEmineknnQELNLIQEKHNEEVELYR 531
Cdd:PRK09510 69 QQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLK--QLEKERLAAQEQKKQAE-------EAAKQAALKQKQAEEAAA 139
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 442629624 532 LQLANASKKIDEMDLKLSCYKTKRADIAEKLHGVmEAQWQQA 573
Cdd:PRK09510 140 KAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEA-EAAKKAA 180
|
|
| Rootletin |
pfam15035 |
Ciliary rootlet component, centrosome cohesion; |
231-406 |
8.22e-03 |
|
Ciliary rootlet component, centrosome cohesion;
Pssm-ID: 464459 [Multi-domain] Cd Length: 190 Bit Score: 38.10 E-value: 8.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 231 SLKEEQLRRQHLEKMVHTLQSHLLEYQQRISvaievdrskdaaltEAEQTVQSLNYEVQHLrdavhRLEADRGESQSRFD 310
Cdd:pfam15035 3 KLQAYQEAQQRQAQLVQKLQAKVLQYKKRCS--------------ELEQQLLEKTSELEKT-----ELLLRKLTLEPRLQ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 311 ALQNELSQAVNLATRfqekndKLEREldhcRQDAKQWEERLEQLEMQLNSSKRAEELSHAELNKLRDKFAKVdyqQEKLK 390
Cdd:pfam15035 64 RLEREHSADLEEALI------RLEEE----RQRSESLSQVNSLLREQLEQASRANEALREDLQKLTNDWERA---REELE 130
|
170
....*....|....*.
gi 442629624 391 ARIEELEKENNTLTNQ 406
Cdd:pfam15035 131 QKESEWRKEEEAFNEY 146
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
303-500 |
8.76e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 39.43 E-value: 8.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 303 GESQSRFDALQNE---------------LSQAVNLATRFQEKndKLERELDHCRQDAKQWEERLEQLEMQLNSSKRAEEL 367
Cdd:PRK04778 60 GQSEEKFEEWRQKwdeivtnslpdieeqLFEAEELNDKFRFR--KAKHEINEIESLLDLIEEDIEQILEELQELLESEEK 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 368 SHAELNKLRDKFAKVdyqQEKLKAR-------IEELEKEnntLTNQKEMLQEY--------HQKQKARADSLESHRKSLQ 432
Cdd:PRK04778 138 NREEVEQLKDLYREL---RKSLLANrfsfgpaLDELEKQ---LENLEEEFSQFveltesgdYVEAREILDQLEEELAALE 211
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442629624 433 ETLANLTETETNLKKKLDIQQKSLKQYYQQ-QMENV------VAKKMQEFQDQLDKNEEHLKN----EARERERLIAER 500
Cdd:PRK04778 212 QIMEEIPELLKELQTELPDQLQELKAGYRElVEEGYhldhldIEKEIQDLKEQIDENLALLEEldldEAEEKNEEIQER 290
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
319-521 |
8.83e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 38.81 E-value: 8.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 319 AVNLATRFQEKNDKLERELDHCRQDAKQWEERLEQLEMQLNSSKRAEELSHAELNKLRDKFAKVDYQQEKLKARIEELEK 398
Cdd:pfam02841 83 AVFMKRSFKDENQEFQKELVELLEAKKDDFLKQNEEASSKYCSALLQDLSEPLEEKISQGTFSKPGGYKLFLEERDKLEA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 399 ENNTLTNQ----KEMLQEYHQKQKARADSLESHRKSLQE---TLANLTETETNLKKKLDIQQKSLKQYyQQQMENvvakK 471
Cdd:pfam02841 163 KYNQVPRKgvkaEEVLQEFLQSKEAVEEAILQTDQALTAkekAIEAERAKAEAAEAEQELLREKQKEE-EQMMEA----Q 237
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 442629624 472 MQEFQDQLDKNEEHLKNE----ARERERLIAERAVKQLEMINEKNNQELNLIQE 521
Cdd:pfam02841 238 ERSYQEHVKQLIEKMEAEreqlLAEQERMLEHKLQEQEELLKEGFKTEAESLQK 291
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
380-499 |
8.94e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 39.29 E-value: 8.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 380 AKVDYQQEKLKARIEELEKENNTLTNQKEML-QEYHQKQKARADSLESHRKSLQETLANLT---ETETNLKKKLDIQQKS 455
Cdd:COG0542 400 ARVRMEIDSKPEELDELERRLEQLEIEKEALkKEQDEASFERLAELRDELAELEEELEALKarwEAEKELIEEIQELKEE 479
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 442629624 456 LKQYYQQQMEnvVAKKMQEFQDQLDKNEEHLKNEARERErlIAE 499
Cdd:COG0542 480 LEQRYGKIPE--LEKELAELEEELAELAPLLREEVTEED--IAE 519
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
234-527 |
9.52e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 39.51 E-value: 9.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 234 EEQLRRQHLEKMVHTL------QSHLLEYQQRISVA--------IEVDRSKDAALTEAEQTVQSLNyevqhlrdaVHRLE 299
Cdd:PRK11281 57 EDKLVQQDLEQTLALLdkidrqKEETEQLKQQLAQApaklrqaqAELEALKDDNDEETRETLSTLS---------LRQLE 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 300 ADRGESQSRFDALQNEL----SQAVNLATRfqekndkLER---ELDHCRQdakqweeRLEQLEMQLNSSKRAEE-LSHAE 371
Cdd:PRK11281 128 SRLAQTLDQLQNAQNDLaeynSQLVSLQTQ-------PERaqaALYANSQ-------RLQQIRNLLKGGKVGGKaLRPSQ 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 372 LNKLRDKFA----KVDYQQEKLK-----------------ARIEELEKENNTL---TNQK---------EMLQEYHQKQK 418
Cdd:PRK11281 194 RVLLQAEQAllnaQNDLQRKSLEgntqlqdllqkqrdyltARIQRLEHQLQLLqeaINSKrltlsektvQEAQSQDEAAR 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 419 ARADSL---ES---HRKS---LQET----------------LANLTETETNLKKKLDIQQKSL---KQYYQQQmenvvak 470
Cdd:PRK11281 274 IQANPLvaqELeinLQLSqrlLKATeklntltqqnlrvknwLDRLTQSERNIKEQISVLKGSLllsRILYQQQ------- 346
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442629624 471 kmQEF-QDQLDKNeehLKNEarererlIAERAVKQLEmINEKNNQELNL------IQEKHNEEV 527
Cdd:PRK11281 347 --QALpSADLIEG---LADR-------IADLRLEQFE-INQQRDALFQPdayidkLEAGHKSEV 397
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
314-477 |
9.68e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.28 E-value: 9.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 314 NELSQAVNLATRFQEKNDKLERELDHCRQDAKQWEERLEQLEMQLNSSKRaeELSHAELNKLRDKFAKVDYQQEKLKARI 393
Cdd:PRK03918 605 LELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEK--KYSEEEYEELREEYLELSRELAGLRAEL 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 394 EELEKENNTLTNQKEMLQEYHQKQKARADSLESHRKSLQETlanlteteTNLKKKLDIQQKSLKQYYQQQMENVVAKKMQ 473
Cdd:PRK03918 683 EELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERV--------EELREKVKKYKALLKERALSKVGEIASEIFE 754
|
....
gi 442629624 474 EFQD 477
Cdd:PRK03918 755 ELTE 758
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
230-426 |
9.96e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 38.66 E-value: 9.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 230 SSLKEEQLRRQHLEKMVHTLQSHLLEYQQRISVAIEVDRSKDAALTEAEQTVQSLNYEVQHLRDAVHRLEAD-------- 301
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREElgeraral 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629624 302 --RGESQSRFDALQN-----ELSQAVNLATRFQEKNDKLERELDHCRQDAKQWEERLEQLEMQLNSSKRAEELSHAELNK 374
Cdd:COG3883 96 yrSGGSVSYLDVLLGsesfsDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 442629624 375 LRDkfakvdyQQEKLKARieeLEKENNTLTNQKEMLQEYHQKQKARADSLES 426
Cdd:COG3883 176 QQA-------EQEALLAQ---LSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| |
