|
Name |
Accession |
Description |
Interval |
E-value |
| KIP1 |
pfam07765 |
KIP1-like protein; This is a family of sequences found exclusively in plants. They are similar ... |
23-95 |
4.74e-38 |
|
KIP1-like protein; This is a family of sequences found exclusively in plants. They are similar to kinase interacting protein 1 (KIP1), which has been found to interact with the kinase domain of PRK1, a receptor-like kinase. This particular region contains two coiled-coils, which are described as motifs involved in protein-protein interactions. It has also been suggested that the protein's coiled- coils allow it to dimerize in vivo.
Pssm-ID: 429647 [Multi-domain] Cd Length: 74 Bit Score: 134.33 E-value: 4.74e-38
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063741969 23 WWWDSHIGLKNSKWLENNLDEMDRSVKRMVKLIEEDADSFAKKAEMYYQSRPELIALVDEFHRMYRALAERYE 95
Cdd:pfam07765 2 WWWDSHIRPKQSKWLQENLSEMDEKVKAMLKLIEEDGDSFAKRAEMYYKKRPELINLVEEFYRSYRSLAERYD 74
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
192-526 |
2.80e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.53 E-value: 2.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 192 SIGSDFQSLSKRIMDLEIELREAKERLRmQLEGNTESLLPRVKSETKFVDFPAKLAACEQELKDVNEKLQNSEDQIYILK 271
Cdd:PRK03918 235 ELKEEIEELEKELESLEGSKRKLEEKIR-ELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 272 SQLARYlpsglddeqSEGAASTQEL--DIETLSEELRITSLRLREAEKQNGIMRKEVEKSKSDDAKLKSLQDM------- 342
Cdd:PRK03918 314 KRLSRL---------EEEINGIEERikELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLkkrltgl 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 343 -LESAQKEAAAWKSKASADKREVVKLLDRISMLKSSLAGRDHEIRDLKTA----------LSDAEEKIFpeKAQVKADIA 411
Cdd:PRK03918 385 tPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAkgkcpvcgreLTEEHRKEL--LEEYTAELK 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 412 KLLEEKIHRDDQFKELEANVRYLEDERRK-----VNNEKIEEEEKLKSEIEVLTLEKVE-KGRCIETLSRKVSELESEIS 485
Cdd:PRK03918 463 RIEKELKEIEEKERKLRKELRELEKVLKKeseliKLKELAEQLKELEEKLKKYNLEELEkKAEEYEKLKEKLIKLKGEIK 542
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1063741969 486 RLGSEIKarddRTMEMEKEVEKQRRELEEVAEEKREVIRQL 526
Cdd:PRK03918 543 SLKKELE----KLEELKKKLAELEKKLDELEEELAELLKEL 579
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
250-514 |
3.25e-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: 53.52 E-value: 3.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 250 EQELKDVNEKLQNSEDQIYILKSQLARYLPSGLDDEQSEGAASTQELDIETLSEELRITSLRLREAEKQNGIMRKEVEKS 329
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 330 KSD-DAKLKSLQDMLESAQKEAAAWKSKASADKREVVKLLDRISMLKSSLAGRDHEIRDLKTALSDAEEKIFPEKAQVkA 408
Cdd:TIGR02168 756 LTElEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI-A 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 409 DIAKLLEEkihRDDQFKELEANVRYLEDERrkvnNEKIEEEEKLKSEIEVLTLEKVEKGRCIETLSRKVSELESEISRLG 488
Cdd:TIGR02168 835 ATERRLED---LEEQIEELSEDIESLAAEI----EELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE 907
|
250 260
....*....|....*....|....*.
gi 1063741969 489 SEIKARDDRTMEMEKEVEKQRRELEE 514
Cdd:TIGR02168 908 SKRSELRRELEELREKLAQLELRLEG 933
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
243-498 |
6.68e-07 |
|
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: 51.69 E-value: 6.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 243 PAKLAACEQELKDVNEKLQNSEDQIYILKSQLARYLpsgLDDEQSEGAASTQELDIETLSEELRITSLRLREAEKQNGIM 322
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALL---KQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 323 RKEVEKSKsddaklKSLQDMLESAQKEAAAWKSKASADKREVVKLLDRISMLKSSLAGRDHEIRDLK---TALSDAEEKI 399
Cdd:COG4942 96 RAELEAQK------EELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRadlAELAALRAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 400 FPEKAQVKADIAKLLEEKihrddqfKELEAnvryLEDERRKVNNEkieeeeklkseievLTLEKVEKGRCIETLSRKVSE 479
Cdd:COG4942 170 EAERAELEALLAELEEER-------AALEA----LKAERQKLLAR--------------LEKELAELAAELAELQQEAEE 224
|
250
....*....|....*....
gi 1063741969 480 LESEISRLGSEIKARDDRT 498
Cdd:COG4942 225 LEALIARLEAEAAAAAERT 243
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
250-526 |
7.32e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.25 E-value: 7.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 250 EQELKDVNEKLQNSEDQIYILKSQL----------ARY--LPSGLDDEQSEGAAS---TQELDIETLSEELRITSLRLRE 314
Cdd:COG1196 178 ERKLEATEENLERLEDILGELERQLeplerqaekaERYreLKEELKELEAELLLLklrELEAELEELEAELEELEAELEE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 315 AEKQNGIMRKEVEKSKsddAKLKSLQDMLESAQKEAAAWKSKASADKREVVKLLDRISMLKSSLAGRDHEIRDLKTALSD 394
Cdd:COG1196 258 LEAELAELEAELEELR---LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 395 AEEkifpEKAQVKADIAKLLEEKIHRDDQFKELEANvryLEDERRKVNNEKIEEEEKLKSEIEVLTLEKVEKGRcIETLS 474
Cdd:COG1196 335 LEE----ELEELEEELEEAEEELEEAEAELAEAEEA---LLEAEAELAEAEEELEELAEELLEALRAAAELAAQ-LEELE 406
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1063741969 475 RKVSELESEISRLGSEIKARDDRTMEMEKEVEKQRRELEEVAEEKREVIRQL 526
Cdd:COG1196 407 EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE 458
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
193-519 |
9.40e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.98 E-value: 9.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 193 IGSDFQSLSKRIMDLEIELREAKERLRMQLEGNTESLLPRVKSETKFVDFPAKLAACEQELKDVNEKLQNSEDQIYILKS 272
Cdd:TIGR02168 689 LEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEE 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 273 QLarylpsglddEQSEGAASTQELDIETLSEELRITSLRLREAEKQNGIMRKEVEKSKSDDAKLKSLQDMLESAQKEAaa 352
Cdd:TIGR02168 769 RL----------EEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAAT-- 836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 353 wkskasadKREVVKLLDRISMLKSSLAGRDHEIRDLKTALSDAEEKI---FPEKAQVKADIAKLLEEKIHRDDQFKELEA 429
Cdd:TIGR02168 837 --------ERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELealLNERASLEEALALLRSELEELSEELRELES 908
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 430 NVRYLEDERRKVNNEkieeeeklkseievltlekvekgrcIETLSRKVSELESEISRLGSEIKARDDRTMEMEKEVEKQR 509
Cdd:TIGR02168 909 KRSELRRELEELREK-------------------------LAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKI 963
|
330
....*....|
gi 1063741969 510 RELEEVAEEK 519
Cdd:TIGR02168 964 EDDEEEARRR 973
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
290-521 |
1.10e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.61 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 290 AASTQELDIETLSEELRITSLRLREAEKQNGIMRKEVEKSKSD----DAKLKSLQDMLESAQKEAAAWKSKASADKREVV 365
Cdd:TIGR02169 661 APRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRldelSQELSDASRKIGEIEKEIEQLEQEEEKLKERLE 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 366 KLLDRISMLKSSLAGRDHEIRDLKTALSDAEEKIFPEKAQVKADIAKLLEEKIHR--------DDQFKELEANVRYLEDE 437
Cdd:TIGR02169 741 ELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEiqaelsklEEEVSRIEARLREIEQK 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 438 RRKVNNEKI---EEEEKLKSEIEVLTLEKVEKGRCIETLSRKVSELESEISRLGSEIKARDDRTMEMEKEVEKQRRELEE 514
Cdd:TIGR02169 821 LNRLTLEKEyleKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRE 900
|
....*..
gi 1063741969 515 VAEEKRE 521
Cdd:TIGR02169 901 LERKIEE 907
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
297-541 |
9.98e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.53 E-value: 9.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 297 DIETLSEELRITSLRLREAEKQNGIMRKEVEKSKSDDAKLKSLQdmlESAQKEAAAWKSKASADKREVVKLLDR----IS 372
Cdd:TIGR02169 178 ELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKR---EYEGYELLKEKEALERQKEAIERQLASleeeLE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 373 MLKSSLAGRDHEIRDLKTALSDAEEKIFP----EKAQVKADIAKLLEEKIHRDDQFKELEANVRYLEDERRKVNNEKIEE 448
Cdd:TIGR02169 255 KLTEEISELEKRLEEIEQLLEELNKKIKDlgeeEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKL 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 449 EEKLKSEIEVLTLEKVEKgrciETLSRKVSELESEISRLGSEIKARDDRTMEMEKEVEKQRRELEEVAEEKREVIRQLCF 528
Cdd:TIGR02169 335 LAEIEELEREIEEERKRR----DKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDR 410
|
250
....*....|...
gi 1063741969 529 SLDYSRDEYKRLR 541
Cdd:TIGR02169 411 LQEELQRLSEELA 423
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
258-526 |
1.28e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.14 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 258 EKLQNSEDQIYILKSQLARylpsgLDDEQSEGAASTQELDIEtLSEELRITSLRLREAEKQNGIMRKEVEKSKSDDAKLK 337
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSS-----LQSELRRIENRLDELSQE-LSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLS 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 338 SLQDMLESAQKEAAAWKSKASADKREVVKLLDRISMLKSSLAGR-----DHEIRDLKTALSDAEEKIfpekAQVKADIAK 412
Cdd:TIGR02169 748 SLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSripeiQAELSKLEEEVSRIEARL----REIEQKLNR 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 413 LLEEKIHRDDQFKELEANVRYLEDERrkvnnekieeeEKLKSEIEVLTLEKVEKGRCIETLSRKVSELESEISRLGSEik 492
Cdd:TIGR02169 824 LTLEKEYLEKEIQELQEQRIDLKEQI-----------KSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKE-- 890
|
250 260 270
....*....|....*....|....*....|....
gi 1063741969 493 aRDDRTMEMeKEVEKQRRELEEVAEEKREVIRQL 526
Cdd:TIGR02169 891 -RDELEAQL-RELERKIEELEAQIEKKRKRLSEL 922
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
197-520 |
2.05e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.76 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 197 FQSLSKRIMDLEI--------ELREAKERLRMQLEGNTESLlprVKSETKFVDFPAKLAACEQELKDVNEKLQN-SEDQI 267
Cdd:TIGR02169 213 YQALLKEKREYEGyellkekeALERQKEAIERQLASLEEEL---EKLTEEISELEKRLEEIEQLLEELNKKIKDlGEEEQ 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 268 YILKSQLARYlpsGLDDEQSEGAASTQELDIETLSEELRITSLRLREAEKQNGIMRKEVEKSKSDDAKL----KSLQDML 343
Cdd:TIGR02169 290 LRVKEKIGEL---EAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLteeyAELKEEL 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 344 ESAQKEAAAWKSKASADKREVVKLLDRISMLKSSLagrdHEIRDLKTALSDAEEKIFPEKAQVKADIAKLLEEKIHRDDQ 423
Cdd:TIGR02169 367 EDLRAELEEVDKEFAETRDELKDYREKLEKLKREI----NELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEE 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 424 FKELEANVRYLEDErrkvnnekieeeeklkseievltlekvekgrcIETLSRKVSELESEISRLGSEIKarddrtmEMEK 503
Cdd:TIGR02169 443 KEDKALEIKKQEWK--------------------------------LEQLAADLSKYEQELYDLKEEYD-------RVEK 483
|
330
....*....|....*..
gi 1063741969 504 EVEKQRRELEEVAEEKR 520
Cdd:TIGR02169 484 ELSKLQRELAEAEAQAR 500
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
196-540 |
3.47e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 3.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 196 DFQSLSKRIMDLEIELREAKERLR--MQLEGNTESLLPRVKSEtkfvdfpakLAACEQELKDVNEKLQNSEDQIYILKSQ 273
Cdd:PRK03918 159 DYENAYKNLGEVIKEIKRRIERLEkfIKRTENIEELIKEKEKE---------LEEVLREINEISSELPELREELEKLEKE 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 274 LARYlpsglddeqSEGAASTQELDIETLSEELRITSL--RLREAEKQNGIMRKEVEKSKSDDAKLKSLQDMLESAQKEaa 351
Cdd:PRK03918 230 VKEL---------EELKEEIEELEKELESLEGSKRKLeeKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKL-- 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 352 awkskasadKREVVKLLDRISMLKSSLAGRDHEIRDLKTALSDAEEKifpekaqvKADIAKLLEEKIHRDDQFKELEANV 431
Cdd:PRK03918 299 ---------SEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEK--------EERLEELKKKLKELEKRLEELEERH 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 432 RYLEDERRKVNNEKIEEEEKLKSEIEVLT--LEKVEKGRciETLSRKVSELESEISRLGSEIKARDDRTMEMEKEVEK-- 507
Cdd:PRK03918 362 ELYEEAKAKKEELERLKKRLTGLTPEKLEkeLEELEKAK--EEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcp 439
|
330 340 350
....*....|....*....|....*....|....
gi 1063741969 508 -QRRELEEvaEEKREVIRQLCFSLDYSRDEYKRL 540
Cdd:PRK03918 440 vCGRELTE--EHRKELLEEYTAELKRIEKELKEI 471
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
200-526 |
7.64e-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: 45.88 E-value: 7.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 200 LSKRIMDLEIELREAKerlRMqLEGNTESLlprvksETKFVDFPAKLAACEQELKDVNEKLQNSEDQIYILKSQL-ARYL 278
Cdd:pfam15921 322 LESTVSQLRSELREAK---RM-YEDKIEEL------EKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLhKREK 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 279 PSGLDDEQSE---GAASTQELDIETLSEELRITSLRLREAEKQNGIMRKEVEKSKsdDAKLKSLQDMLESAQKeAAAWKS 355
Cdd:pfam15921 392 ELSLEKEQNKrlwDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQM--ERQMAAIQGKNESLEK-VSSLTA 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 356 KASADKREVVKLLDRISMLKSSLAGRDHEIRDLKTALSDAEEKIfpekAQVKADIAKLleeKIHRDDQFKELEanvrYLE 435
Cdd:pfam15921 469 QLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAI----EATNAEITKL---RSRVDLKLQELQ----HLK 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 436 DERRKVNNEKIEEEeklkseieVLTLEKVEKGRCIETLSRKVSELESEISRLGSEIKARDDRTMEMEKEVEKQRRELEE- 514
Cdd:pfam15921 538 NEGDHLRNVQTECE--------ALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEf 609
|
330
....*....|....
gi 1063741969 515 --VAEEKREVIRQL 526
Cdd:pfam15921 610 kiLKDKKDAKIREL 623
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
282-521 |
2.37e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.16 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 282 LDDEQSEGAASTQELDIETLSEELRITSLRLREAEKQNGIMRKEVEKsksDDAKLKSLQDMLESAQKEAAAWKSKASADK 361
Cdd:COG1196 232 LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEE---LELELEEAQAEEYELLAELARLEQDIARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 362 REVVKLLDRISMLKSSLAGRDHEIRDLKTALSDAEEKIFPEKAQVKADIAKLLEEKIHRDDQFKELEANVRYLEDERRKV 441
Cdd:COG1196 309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 442 NNEKIEEEEKLKSEIEVLTLEKVEKGRCIETLSRKVSELESEISRLGSEIKARDDRTMEMEKEVEKQRRE---LEEVAEE 518
Cdd:COG1196 389 LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEealLELLAEL 468
|
...
gi 1063741969 519 KRE 521
Cdd:COG1196 469 LEE 471
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
241-526 |
2.81e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.90 E-value: 2.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 241 DFPAKLAACEQELKDVNEKLQNSEDQIYILKSQLARylpsgLDDEQsEGAASTQELDIETLSEELRITSLRLREAEKQNG 320
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEENIERLDLIIDEKRQQLER-----LRRER-EKAERYQALLKEKREYEGYELLKEKEALERQKE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 321 IMRKEVEKSKSDDAKLKSLQDML--ESAQKEAAAWKSKASADKR---EVVKLLDRISMLKSSLAGRDHEIRDLKTALSDA 395
Cdd:TIGR02169 241 AIERQLASLEEELEKLTEEISELekRLEEIEQLLEELNKKIKDLgeeEQLRVKEKIGELEAEIASLERSIAEKERELEDA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 396 EEKIfpekAQVKADIAKLLEEKIHRDDQFKELEANVRYLEDE---RRKVNNEKIEEEEKLKSEIEVLTLEKVEKGRCIET 472
Cdd:TIGR02169 321 EERL----AKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEyaeLKEELEDLRAELEEVDKEFAETRDELKDYREKLEK 396
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063741969 473 LSRKVSELESEISRLGSE---------------------IKARDDRTMEMEKEVEKQRRELEEVAEEKREVIRQL 526
Cdd:TIGR02169 397 LKREINELKRELDRLQEElqrlseeladlnaaiagieakINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQEL 471
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
327-526 |
4.18e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.83 E-value: 4.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 327 EKSKSDDAKLKSLQDMLESAQKEAAAWKSKASADKREVVKLLDRISMLKSSLAGRDHEIRDLKTALSDAEEKIF---PEK 403
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAelrAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 404 AQVKADIAKLL-----------EEKIHRDDQFKELEANVRYLederRKVNNEKIEEEEKLKSEIEVLTLEKVEKGRCIET 472
Cdd:COG4942 100 EAQKEELAELLralyrlgrqppLALLLSPEDFLDAVRRLQYL----KYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1063741969 473 LSRKVSELESEISRLGSEIKARDDRTMEMEKEVEKQRRELEEVAEEKREVIRQL 526
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
197-439 |
9.56e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.23 E-value: 9.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 197 FQSLSKRIMDLEIELREAK-ERLRMQLEGNTESLlprVKSETKFVDFPAKLAACEQELKDVNEKLQNSEDQI-------Y 268
Cdd:COG1196 215 YRELKEELKELEAELLLLKlRELEAELEELEAEL---EELEAELEELEAELAELEAELEELRLELEELELELeeaqaeeY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 269 ILKSQLARyLPSGLDDEQSEGAASTQELD------------IETLSEELRITSLRLREAEKQNGIMRKEVEKSKSDDAKL 336
Cdd:COG1196 292 ELLAELAR-LEQDIARLEERRRELEERLEeleeelaeleeeLEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 337 KSLQDMLESAQKEAAAWKSKASADKREVVKLLDRISMLKSSLAGRDHEIRDLKTALSDAEEKIFPEKAQVKADIAKLLEE 416
Cdd:COG1196 371 EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450
|
250 260
....*....|....*....|...
gi 1063741969 417 KIHRDDQFKELEANVRYLEDERR 439
Cdd:COG1196 451 EAELEEEEEALLELLAELLEEAA 473
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
334-541 |
1.07e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.67 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 334 AKLKSLQDMLESAQKEAAAWKSKASADKREVVKLLDRISMLKSSLAGRDHEIRDLKTALSDAEEKIfpekAQVKADIAKL 413
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL----AELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 414 LEEKIHRDDQFKELeANVRYLEDERRKVNNEKIEEEEKLKSEIEVLtLEKVEKGR--CIETLSRKVSELEseisRLGSEI 491
Cdd:COG4942 96 RAELEAQKEELAEL-LRALYRLGRQPPLALLLSPEDFLDAVRRLQY-LKYLAPARreQAEELRADLAELA----ALRAEL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1063741969 492 KARDDRTMEMEKEVEKQRRELEEVAEEKREVIRQLCFSLDYSRDEYKRLR 541
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQ 219
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
195-521 |
1.13e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.93 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 195 SDFQSLSKRIMDLEIELREAKERLRMQLEGNTESLLPRVKSETKFVDfpaKLAACEQELKDVNEKLQNSEDQIYILKSQL 274
Cdd:TIGR04523 221 SELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKK---QLSEKQKELEQNNKKIKELEKQLNQLKSEI 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 275 arylpSGLDDEQSEGAASTQELDIETLSEELRITSLRLREAEKqngimrkeveksksddaKLKSLQDMLESAQKEAAAWK 354
Cdd:TIGR04523 298 -----SDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNK-----------------IISQLNEQISQLKKELTNSE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 355 SKASADKREVVKLLDRISMLKSSLAGRDHEIRDLKTALSDAEEKIfpekaQVKADIAKLLEEKIHRDDQFKE-LEANVRY 433
Cdd:TIGR04523 356 SENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKI-----QNQEKLNQQKDEQIKKLQQEKElLEKEIER 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 434 LEDERRKVNNEkieeeeklkseIEVLTLEKVEKGRCIETLSRKVSELESEISRLGSEIKARDDRTMEMEKEVEKQRRELE 513
Cdd:TIGR04523 431 LKETIIKNNSE-----------IKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELK 499
|
....*...
gi 1063741969 514 EVAEEKRE 521
Cdd:TIGR04523 500 KLNEEKKE 507
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
244-442 |
1.39e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 244 AKLAACEQELKDVNEKLQNSEDQIYILKSQLARYlpsgldDEQSEGAASTQELDietlSEELRITSLRLREAEKQNgimr 323
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDAL------QERREALQRLAEYS----WDEIDVASAEREIAELEA---- 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 324 kEVEKSKSDDAKLKSLQDMLESAQKEAAAWkskasadKREVVKLLDRISMLKSSLAGRDHEIRDLKTALSDAEEKifpEK 403
Cdd:COG4913 676 -ELERLDASSDDLAALEEQLEELEAELEEL-------EEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDL---AR 744
|
170 180 190
....*....|....*....|....*....|....*....
gi 1063741969 404 AQVKADIAKLLEEkIHRDDQFKELEANvryLEDERRKVN 442
Cdd:COG4913 745 LELRALLEERFAA-ALGDAVERELREN---LEERIDALR 779
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
198-514 |
1.46e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.59 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 198 QSLSKRIMDLEIELREAKERLRmQLEGNTESLLPRVKSETK-FVDFPAKLAACEQELKDVNEKLQNSEDQIYILKSQLAR 276
Cdd:TIGR02169 677 QRLRERLEGLKRELSSLQSELR-RIENRLDELSQELSDASRkIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIEN 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 277 YlpsglDDEQSEGAASTQELDIETLSEELRITSLRLREAEKQNGIMRKEVEKSKSDDAKLKSLQDMLESAQKeaaawksk 356
Cdd:TIGR02169 756 V-----KSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLN-------- 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 357 asadkrevvKLLDRISMLKSSLAGRDHEIRDLKTALSDAEEKIfpekAQVKADIAKLLEEKIHRDDQFKELEANVRYLED 436
Cdd:TIGR02169 823 ---------RLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEI----ENLNGKKEELEEELEELEAALRDLESRLGDLKK 889
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063741969 437 ERRKVNNEKIEEEEKLKSEIEVLTLEKVEKGRCIETLSRKVSELeSEISRLGSEIKARDDRTMEMEKeVEKQRRELEE 514
Cdd:TIGR02169 890 ERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEEL-SEIEDPKGEDEEIPEEELSLED-VQAELQRVEE 965
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
250-523 |
2.07e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.16 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 250 EQELKDVNEKLQNSEDQIYILKSQLARYLP--SGLDDEQSEGAASTQELDIETLSEELRITSL-RLREAEKQNgimRKEV 326
Cdd:TIGR04523 397 ESKIQNQEKLNQQKDEQIKKLQQEKELLEKeiERLKETIIKNNSEIKDLTNQDSVKELIIKNLdNTRESLETQ---LKVL 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 327 EKS-KSDDAKLKSLQDMLESAQKEAAAWKSKASADKREVVKLLDRISMLKSSLAGRDHEIRDLKTALSDAEEKIFPEKAQ 405
Cdd:TIGR04523 474 SRSiNKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFE 553
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 406 VKADiaKLLEEKIHRDDQFKELEANVRYLEDERRKVNNEKIEEEEKLKSeievLTLEKVEKGRCIETLSRKVSELESEIS 485
Cdd:TIGR04523 554 LKKE--NLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKD----LIKEIEEKEKKISSLEKELEKAKKENE 627
|
250 260 270
....*....|....*....|....*....|....*...
gi 1063741969 486 RLGSEIKARDDRTMEMEKEVEKQRRELEEVAEEKREVI 523
Cdd:TIGR04523 628 KLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEII 665
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
196-521 |
2.14e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.18 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 196 DFQSLSKRIMDLEIELREAKERLRMQ------LEGNTESLLPRVKS-ETKFVDFPAKLAACEQELKDVNEKLQNSEDQIY 268
Cdd:PRK02224 308 DAEAVEARREELEDRDEELRDRLEECrvaaqaHNEEAESLREDADDlEERAEELREEAAELESELEEAREAVEDRREEIE 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 269 ILKSQLArylpsglDDEQSEGAASTQELDIETLSEELRITSLRLREAEKQNGIMRKEVEKSKSDDAKLKSLQDMLESAQK 348
Cdd:PRK02224 388 ELEEEIE-------ELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPECGQP 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 349 EAAAWKSKASADKRE-VVKLLDRISMLKSSLAGRDHEIRDLKTALSdaEEKIFPEKAQVKADIAKLLEEK----IHRDDQ 423
Cdd:PRK02224 461 VEGSPHVETIEEDRErVEELEAELEDLEEEVEEVEERLERAEDLVE--AEDRIERLEERREDLEELIAERretiEEKRER 538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 424 FKELEANVRYLE---DERRKVNNEKIEEEEKLKSEIEVLTLEKVEKGRCIETLsRKVSELESEISRLGSEIKARDDRtME 500
Cdd:PRK02224 539 AEELRERAAELEaeaEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL-ERIRTLLAAIADAEDEIERLREK-RE 616
|
330 340
....*....|....*....|..
gi 1063741969 501 MEKEVEKQRRE-LEEVAEEKRE 521
Cdd:PRK02224 617 ALAELNDERRErLAEKRERKRE 638
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
200-522 |
2.87e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 200 LSKRIMDLEIELREAKERLR-----MQLEGNTESLLPRVKSETKfVDFPAKLAACEQELKDVNEKLQNSEDQIYILKSQL 274
Cdd:PRK03918 343 LKKKLKELEKRLEELEERHElyeeaKAKKEELERLKKRLTGLTP-EKLEKELEELEKAKEEIEEEISKITARIGELKKEI 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 275 ARYLPS----------------GLDDEQSEGAASTQELDIETLSEELRITSLRLREAEKQNGIMRKEVEKsKSDDAKLKS 338
Cdd:PRK03918 422 KELKKAieelkkakgkcpvcgrELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKK-ESELIKLKE 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 339 LQDMLESAQK--------EAAAWKSKASADKREVVKL----------LDRISMLKSSLAGRDHEIRDLKTALSDAEEKI- 399
Cdd:PRK03918 501 LAEQLKELEEklkkynleELEKKAEEYEKLKEKLIKLkgeikslkkeLEKLEELKKKLAELEKKLDELEEELAELLKELe 580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 400 ---FPEKAQVKADIAKLleEKIHRD-----DQFKELEANVRYLEDERRKVN----NEKIEEEEKLKSEIEVLTLEKVEKG 467
Cdd:PRK03918 581 elgFESVEELEERLKEL--EPFYNEylelkDAEKELEREEKELKKLEEELDkafeELAETEKRLEELRKELEELEKKYSE 658
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1063741969 468 RCIETLSRKVSELESEISRLGSEIKARDDRTMEMEKEVEKQRRELEEVAEEKREV 522
Cdd:PRK03918 659 EEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKEL 713
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
195-430 |
3.27e-03 |
|
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: 40.43 E-value: 3.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 195 SDFQSLSKRIMDLEIELREAKERLRmQLEGNTESL-LPRVKSETKFVDFPAKLAACEQELKDVNEKLQNSEDQIYILKSQ 273
Cdd:TIGR02168 288 KELYALANEISRLEQQKQILRERLA-NLERQLEELeAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAE 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 274 LarylpsglddEQSEGAASTQELDIETLSEELRITSLRLREAEKQNGIMRKEVEKSKSDDAKLKSLQDMLESAQKEAAAW 353
Cdd:TIGR02168 367 L----------EELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELK 436
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063741969 354 KSKASAD--KREVVKLLDRISMLKSSLAGRDHEIRDLKTALSDAEEKIFPEKAQVKAdIAKLLEEKIHRDDQFKELEAN 430
Cdd:TIGR02168 437 ELQAELEelEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS-LERLQENLEGFSEGVKALLKN 514
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
385-526 |
3.55e-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: 3.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 385 IRDLK-TALSDAEEKIFPEKAQVKADIAKLLEEKIHRDDQFKELEANVRYLEDErrkvnnekieeeeklkseievltlek 463
Cdd:COG2433 382 LEELIeKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAE-------------------------- 435
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063741969 464 vekgrcIETLSRKVSELESEISRLGSEIKARDDRTME---MEKEVEKQRRELEEVAEEKREVIRQL 526
Cdd:COG2433 436 ------LEEKDERIERLERELSEARSEERREIRKDREisrLDREIERLERELEEERERIEELKRKL 495
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
208-540 |
5.13e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 39.95 E-value: 5.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 208 EIELREAKERLR--MQLEGNTESLLPRVKSETKFVD-FPAKLAACEQELKDVNEKLQNSEDQIYILKSQLARYLpsGLDD 284
Cdd:TIGR00618 458 KIHLQESAQSLKerEQQLQTKEQIHLQETRKKAVVLaRLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQ--RGEQ 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 285 EQSEGAASTQELDIETLSEELRITSLRLREAEKQN---GIMRKEVEKSKSDDAKLKSLQDMLESAQKEAAAWKSKASADK 361
Cdd:TIGR00618 536 TYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQsfsILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQH 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 362 REVVKLLDRISMLKSSLAGRD--HEIRDLKTALSDAEEKIFPEKAQVKADIAKLLEEKIHRDDQFKEleanvRYLEDERR 439
Cdd:TIGR00618 616 ALLRKLQPEQDLQDVRLHLQQcsQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLAL-----QKMQSEKE 690
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 440 KVNNEKIEEEEKLKSEIEVLTLekvekgrcIETLSRKVSELESEISRLGSEIKARDDRTMEMEKEVEKQRRELEEVAEEK 519
Cdd:TIGR00618 691 QLTYWKEMLAQCQTLLRELETH--------IEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEA 762
|
330 340
....*....|....*....|.
gi 1063741969 520 REVIRQLCFSLDYSRDEYKRL 540
Cdd:TIGR00618 763 HFNNNEEVTAALQTGAELSHL 783
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
198-526 |
6.14e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 39.57 E-value: 6.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 198 QSLSKRIMDLEIELREAKERLRMQLEGNTESLLPRVKSETKFVDFPAKLAACEQELKDVNEKLQNSED------------ 265
Cdd:TIGR00618 527 TRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVrlqdlteklsea 606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 266 ---------------QIYILKSQLARYLPSGLDDEQSEGAASTQELdIETLSEELRITSLRLREAEKQNGIMRK-EVEKS 329
Cdd:TIGR00618 607 edmlaceqhallrklQPEQDLQDVRLHLQQCSQELALKLTALHALQ-LTLTQERVREHALSIRVLPKELLASRQlALQKM 685
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 330 KSDDAKLKSLQDMLESAQKEAAAWKSKASADKREVVKLLDRISMLKSSLAGRDHEIRD-LKTALSDAEEKIfpeKAQVKA 408
Cdd:TIGR00618 686 QSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQsLKELMHQARTVL---KARTEA 762
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 409 DIAKLLEE--KIHRDDQFKELEANV----RYLEDERRKVNNEKIEEEEKLKSEIEVLTLEKVEKGRCIETLSRKVSELES 482
Cdd:TIGR00618 763 HFNNNEEVtaALQTGAELSHLAAEIqffnRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSA 842
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1063741969 483 EISRLGSEIKARDDRTMEMEKEVEKQRRELEEvaEEKREVIRQL 526
Cdd:TIGR00618 843 TLGEITHQLLKYEECSKQLAQLTQEQAKIIQL--SDKLNGINQI 884
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
208-511 |
6.39e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.53 E-value: 6.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 208 EIELREAK-ERLRMQLEGNTESLLPRVKSETKFVdfpAKLAACEQELKDVNEKLQNSEDQIYILKSQLARYLpsgLDDEQ 286
Cdd:COG1196 261 ELAELEAElEELRLELEELELELEEAQAEEYELL---AELARLEQDIARLEERRRELEERLEELEEELAELE---EELEE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 287 SEGAASTQELDIETLSEELRITSLRLREAEKQngiMRKEVEKSKSDDAKLKSLQDMLESAQKEAAAWKSKASADKREVVK 366
Cdd:COG1196 335 LEEELEELEEELEEAEEELEEAEAELAEAEEA---LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEA 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 367 LLDRISMLKSSLAGRDHEIRDLKTALSDAEEKIFPEKAQVKADIAKLLEEKIHRDDQFKELEANVRYLEDERRKVNNEKI 446
Cdd:COG1196 412 LLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAA 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 447 EEEEKLKSEIE-------VLTLEKVEKGR--------CIETLSRKVSELESEISRLGSEIKARDDRTMEMEKEVEKQRRE 511
Cdd:COG1196 492 RLLLLLEAEADyegflegVKAALLLAGLRglagavavLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKA 571
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
250-432 |
7.63e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 39.23 E-value: 7.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 250 EQELKDVNEKLQNSEDQIYILKSQlarylpSGLDDEQSEGAASTQELdiETLSEELRITSLRLREAEkqngimrkeveks 329
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFRQK------NGLVDLSEEAKLLLQQL--SELESQLAEARAELAEAE------------- 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741969 330 ksddAKLKSLQDMLESAQKEAAAWKSKasadkREVVKLLDRISMLKSSLA------GRDH-EIRDLKTALSDAEEKIFPE 402
Cdd:COG3206 240 ----ARLAALRAQLGSGPDALPELLQS-----PVIQQLRAQLAELEAELAelsaryTPNHpDVIALRAQIAALRAQLQQE 310
|
170 180 190
....*....|....*....|....*....|
gi 1063741969 403 KAQVKADIAKLLEEKIHRDDQFKELEANVR 432
Cdd:COG3206 311 AQRILASLEAELEALQAREASLQAQLAQLE 340
|
|
| |
