|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
254-512 |
3.16e-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: 69.32 E-value: 3.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 254 VTEISALQVHLDEFQKILWKEREMRTALEKEIERLESALSLWKWKYEELKESKPKNVKEfdilLGQHNDEMQELSGNIKE 333
Cdd:TIGR02168 231 VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKE----LYALANEISRLEQQKQI 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 334 ESKSQNSKDRVICELRAELERLQAentsewdKREILEREKQGLERENRRLKIQVKEMEELLDKKNRLSANSQSpdfkmsq 413
Cdd:TIGR02168 307 LRERLANLERQLEELEAQLEELES-------KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELES------- 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 414 iDLQEKNQELLNLQHAYYKLNRQyqaniaeLTHANNRVDQNEAEVKKLRLRVEELKQGLNQKEDELDDslNQIRKLQRSL 493
Cdd:TIGR02168 373 -RLEELEEQLETLRSKVAQLELQ-------IASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE--AELKELQAEL 442
|
250
....*....|....*....
gi 1034604707 494 DEEKERNENLETELRHLQN 512
Cdd:TIGR02168 443 EELEEELEELQEELERLEE 461
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
268-508 |
2.63e-11 |
|
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: 66.62 E-value: 2.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 268 QKILWKEREMRTaLEKEIERLESALSLWKWKYEELK---ESKPKNVKEFDILLGQHNDEMQELSGNIKEESKSQNSKDRV 344
Cdd:TIGR02168 670 SSILERRREIEE-LEEKIEELEEKIAELEKALAELRkelEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 345 ICELRAELERLQAENTSEWDKREILEREKQGLERENRRLKIQVKEMEELLDKKNRLSANSQSpdfkmsqiDLQEKNQELL 424
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA--------ELTLLNEEAA 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 425 NLQHAYYKLNRQYQANIAELTHANNRVDQNEAEVKKLRLRVEELKQGLNQKEDELDDSLNQIRKLQRSLDEEKERNENLE 504
Cdd:TIGR02168 821 NLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELS 900
|
....
gi 1034604707 505 TELR 508
Cdd:TIGR02168 901 EELR 904
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
253-511 |
3.10e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.11 E-value: 3.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 253 EVTEISALQVHLDEFQKILWKEREMRTALEKEIERLESALSLWKWKYEELKESkpknVKEFDILLGQHNDEMQELSGNIK 332
Cdd:COG1196 223 KELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLE----LEELELELEEAQAEEYELLAELA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 333 EESKSQNSKDRVICELRAELERLQAENTSEWDKREILEREKQGLERENRRLKIQVKEMEELLDKKNRLSANSQSpDFKMS 412
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA-ELAEA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 413 QIDLQEKNQELLNLQHAYYKLNRQYQANIAELTHANNRVDQNEAEVKKLRLRVEELKQGLNQKEDELDDSLNQIRKLQRS 492
Cdd:COG1196 378 EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457
|
250
....*....|....*....
gi 1034604707 493 LDEEKERNENLETELRHLQ 511
Cdd:COG1196 458 EEALLELLAELLEEAALLE 476
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
242-510 |
1.40e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 64.32 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 242 RLKAINLPLENEVTEISALQVHLDEFQKILWKEREMRTALEKEIERLESALSLWKWKYEELKESkpknvkefdiLLGQHN 321
Cdd:TIGR02169 724 EIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEAR----------LSHSRI 793
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 322 DEMQELSGNIKEESKSQnskDRVICELRAELERLQAEntsewdkREILEREKQGLERENRRLKIQVKEMEELLDKKNRLS 401
Cdd:TIGR02169 794 PEIQAELSKLEEEVSRI---EARLREIEQKLNRLTLE-------KEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKK 863
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 402 ANSQSpdfkmsqiDLQEKNQELLNLQHAYYKLNRQYQANIAELTHANNRVDQNEAEVKKLRLRVEELKQGLNQKEDELDD 481
Cdd:TIGR02169 864 EELEE--------ELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSE 935
|
250 260 270
....*....|....*....|....*....|....*
gi 1034604707 482 SLNQIRKLQR------SLDEEKERNENLETELRHL 510
Cdd:TIGR02169 936 IEDPKGEDEEipeeelSLEDVQAELQRVEEEIRAL 970
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
250-478 |
1.93e-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: 63.54 E-value: 1.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 250 LENEVTEISALQVHLDEFQkilwkerEMRTALEKEIERLESALSLWKWKYEELKESKPKNVKEFDILLGQHNDEMQELS- 328
Cdd:TIGR02168 290 LYALANEISRLEQQKQILR-------ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEe 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 329 -GNIKEESKSQN-SKDRVICELRAELERLQAENTSEWDKREILEREKQGLERENRRLKIQVKEMEELLdkknrlsansQS 406
Cdd:TIGR02168 363 lEAELEELESRLeELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL----------EE 432
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034604707 407 PDFKMSQIDLQEKNQELLNLQHAYYKLNRQYQANIAELTHANNRVDQNEAEVKKLRLRVEELKQGLNQKEDE 478
Cdd:TIGR02168 433 AELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGF 504
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
250-512 |
3.07e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 59.69 E-value: 3.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 250 LENEVTEISALQVHLDEFQKILWKEREMRTALEKEIERLESALSLWKWKYEELKESKPKNVKEFDIL---LGQHNDEMQE 326
Cdd:TIGR02168 707 LEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAeeeLAEAEAEIEE 786
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 327 LSGNIKEESKSQNSKDRVICELRAELERLQAENTSEWDKREILEREKQGLERENRRLKIQVKEMEELLDKKNRLSANSQS 406
Cdd:TIGR02168 787 LEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEE 866
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 407 PDFKMsQIDLQEKNQELLNLQHAYYKLNRQYQANIAELTHANNRVDQNEAEVKKLRLRVEELK---QGLNQKEDELDDSL 483
Cdd:TIGR02168 867 LIEEL-ESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLElrlEGLEVRIDNLQERL 945
|
250 260
....*....|....*....|....*....
gi 1034604707 484 NQirKLQRSLDEEKERNENLETELRHLQN 512
Cdd:TIGR02168 946 SE--EYSLTLEEAEALENKIEDDEEEARR 972
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
281-511 |
2.08e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.25 E-value: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 281 LEKEIERLES----ALslwkwKYEELKESKpknvKEFDILLGQHndEMQELSGNIKEESKSQNSKDRVICELRAELERLQ 356
Cdd:COG1196 198 LERQLEPLERqaekAE-----RYRELKEEL----KELEAELLLL--KLRELEAELEELEAELEELEAELEELEAELAELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 357 AENTSEwdkREILEREKQGLERENRRLKIQVKEMEELLDKKNRLSANSQSpdfkmSQIDLQEKNQELLNLQHAYYKLNRQ 436
Cdd:COG1196 267 AELEEL---RLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE-----LEERLEELEEELAELEEELEELEEE 338
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034604707 437 YQANIAELTHANNRVDQNEAEVKKLRLRVEELKQGLNQKEDELDDSLNQIRKLQRSLDEEKERNENLETELRHLQ 511
Cdd:COG1196 339 LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL 413
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
242-510 |
8.56e-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: 55.07 E-value: 8.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 242 RLKAINLPLENEVTEISALQVHLDEFQKILWKEREMRTALEKEIERLESALSLWKWKYEELKEskpkNVKEFDILLGQHN 321
Cdd:TIGR02169 682 RLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEE----DLSSLEQEIENVK 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 322 DEMQELSGNIKEesksqnsKDRVICELRAELERLQAE-NTSEWDKreiLEREKQGLERENRRLKIQVKEMEELLDKK--N 398
Cdd:TIGR02169 758 SELKELEARIEE-------LEEDLHKLEEALNDLEARlSHSRIPE---IQAELSKLEEEVSRIEARLREIEQKLNRLtlE 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 399 RLSANSQSPDFKMSQIDLQEKNQELLNLQHAyykLNRQYQANIAELTHANNRVDQNEAEVKKLRLRVEELKQGLNQKEDE 478
Cdd:TIGR02169 828 KEYLEKEIQELQEQRIDLKEQIKSIEKEIEN---LNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERK 904
|
250 260 270
....*....|....*....|....*....|..
gi 1034604707 479 LDDSLNQIRKLQRSLDEEKERNENLETELRHL 510
Cdd:TIGR02169 905 IEELEAQIEKKRKRLSELKAKLEALEEELSEI 936
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
347-499 |
2.02e-07 |
|
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: 52.23 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 347 ELRAELERLQAENTSEWDKREILEREKQGLERENRRLKIQVKEMEELLDKKNrlsansqspdfkmSQIDLQEKNQELLNL 426
Cdd:COG1579 28 ELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE-------------EQLGNVRNNKEYEAL 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034604707 427 QHAYYKLNRQYQANIAELTHANNRVDQNEAEVKKLRLRVEELKQGLNQKEDELDDSLNQIRKLQRSLDEEKER 499
Cdd:COG1579 95 QKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREE 167
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
265-511 |
1.15e-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: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 265 DEFQKILWKEREMRTALEKEIERLESALSLWKWKYEELKESKPKNVKEFDILLGQHNDEMQELSGNIKEESKSQNSKDRV 344
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 345 ICELRAELERLQAENTsewDKREILEREKQGLERENRRLK-------IQVKemEELLDKKNRLSANSQSPDFKMSQidLQ 417
Cdd:TIGR02169 246 LASLEEELEKLTEEIS---ELEKRLEEIEQLLEELNKKIKdlgeeeqLRVK--EKIGELEAEIASLERSIAEKERE--LE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 418 EKNQELLNLQHAYYKLNRQYQANIAELTHANNRVDQNEAEVKKLRLRVEELKQGLNQKEDELDDSLNQIRKLQRSLDEEK 497
Cdd:TIGR02169 319 DAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLK 398
|
250
....*....|....
gi 1034604707 498 ERNENLETELRHLQ 511
Cdd:TIGR02169 399 REINELKRELDRLQ 412
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
364-512 |
1.31e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.45 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 364 DKREILEREKQGLERENRRLKIQVKEMEELLDK-KNRLSANSQSPDFKMSQIDLQeknqellnlqhayyklnrQYQANIA 442
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDAlQERREALQRLAEYSWDEIDVA------------------SAEREIA 671
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 443 ELTHANNRVDQNEAEVKKLRLRVEELKQGLNQKEDELDDSLNQIRKLQRSLDEEKERNENLETELRHLQN 512
Cdd:COG4913 672 ELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAED 741
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
319-507 |
3.33e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.44 E-value: 3.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 319 QHNDEMQELSGNIKEESKSQNSKDrvicELRAELERLQAENTSEWDKREILEREKQGLERENRRLKIQVKEMEELLDKKN 398
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELD----ALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 399 RLSANSQSPDFKMSQIDLQEKNQELLNLQHAYYKLNRQYQANIAELTHANNRVDQNEAEVKKLRlrvEEL---KQGLNQK 475
Cdd:COG3883 93 RALYRSGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKL---AELealKAELEAA 169
|
170 180 190
....*....|....*....|....*....|..
gi 1034604707 476 EDELDDSLNQIRKLQRSLDEEKERNENLETEL 507
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAEL 201
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
353-512 |
4.39e-06 |
|
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: 49.79 E-value: 4.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 353 ERLQAENTSEWDKREILEREKQGLERENRRLKIQVKEMEELLDKKNRLSANSQSPDFKMSQIDLQEKNQEllnlQHAYYK 432
Cdd:pfam01576 920 EQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVKSKFKSSIAALEAKIAQLEEQLEQESRE----RQAANK 995
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 433 LNRQYQANIAELT----HANNRVDQNEAEVKKLRLRVEELKQGLNQKEDELDDSLNQIRKLQRSLDEEKERNENLETELR 508
Cdd:pfam01576 996 LVRRTEKKLKEVLlqveDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRELDDATESNESMNREVS 1075
|
....
gi 1034604707 509 HLQN 512
Cdd:pfam01576 1076 TLKS 1079
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
274-493 |
9.84e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.39 E-value: 9.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 274 EREMRTALEKEIERLESALSLWKWKYEELKESKPKNVKEFDILLGQHND---EMQELSGNIKEESKSQNSKDRVICELRA 350
Cdd:COG1196 307 LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEaeaELAEAEEALLEAEAELAEAEEELEELAE 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 351 ELERLQAENTSEWDKREILEREKQGLERENRRLKIQVKEMEELLDKKNRLSANSQSpdfkmsqiDLQEKNQELLNLQHAY 430
Cdd:COG1196 387 ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE--------ALEEAAEEEAELEEEE 458
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034604707 431 YKLNRQYQANIAELTHANNRVDQNEAEVKKLRLRVEELKQGLNQKEDELDDSLNQIRKLQRSL 493
Cdd:COG1196 459 EALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRG 521
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
255-512 |
2.53e-05 |
|
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: 46.94 E-value: 2.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 255 TEISALQVHLDEFQKILWKEREMRTALEKEIERLESALSLWKWKYEELKESKPKNVKEFDILLGQHNDEMQELSGNIKE- 333
Cdd:TIGR04523 412 EQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKEl 491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 334 ESKSQ--NSKDRVICELRAELERLQAENTSEWDKREILEREKQGLERENRRLKIQVKEMEELLDKKNRlsansqspdfkm 411
Cdd:TIGR04523 492 KSKEKelKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENL------------ 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 412 sQIDLQEKNQELLNLQHAYYKLnrqyqanIAELTHANNRVDQNEAEVKKLRLRVEELKQGLNQKEDELDDSLNQIRKLQR 491
Cdd:TIGR04523 560 -EKEIDEKNKEIEELKQTQKSL-------KKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSS 631
|
250 260
....*....|....*....|.
gi 1034604707 492 SLDEEKERNENLETELRHLQN 512
Cdd:TIGR04523 632 IIKNIKSKKNKLKQEVKQIKE 652
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
349-511 |
4.38e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.47 E-value: 4.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 349 RAELERLQaentsewDKREILEREKQGLERE----NRRLKIQvkemEELLDKKNRLSANsqspdfkmsQIDLQEKNQELL 424
Cdd:COG1196 185 EENLERLE-------DILGELERQLEPLERQaekaERYRELK----EELKELEAELLLL---------KLRELEAELEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 425 NLQHAyyKLNRQYQANIAELTHANNRVDQNEAEVKKLRLRVEELKQGLNQKEDELDDSLNQIRKLQRSLDEEKERNENLE 504
Cdd:COG1196 245 EAELE--ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELE 322
|
....*..
gi 1034604707 505 TELRHLQ 511
Cdd:COG1196 323 EELAELE 329
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
255-512 |
5.43e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 5.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 255 TEISALQVHLDEFQKIlwkEREMRTALEKeIERLESALSLWKwKYEELKESKpknvkefdillgQHNDEMQELSgNIKEE 334
Cdd:COG4913 225 EAADALVEHFDDLERA---HEALEDAREQ-IELLEPIRELAE-RYAAARERL------------AELEYLRAAL-RLWFA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 335 SKSQNSKDRVICELRAELERLQAEntsewdkREILEREKQGLERENRRLKIQVKEMEelLDKKNRLSAnsqspdfkmsqi 414
Cdd:COG4913 287 QRRLELLEAELEELRAELARLEAE-------LERLEARLDALREELDELEAQIRGNG--GDRLEQLER------------ 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 415 DLQEKNQELLNLQHAYyklnRQYQANIAELTHAnnrVDQNEAEVKKLRLRVEELKQGLNQK----EDELDDSLNQIRKLQ 490
Cdd:COG4913 346 EIERLERELEERERRR----ARLEALLAALGLP---LPASAEEFAALRAEAAALLEALEEElealEEALAEAEAALRDLR 418
|
250 260
....*....|....*....|..
gi 1034604707 491 RSLDEekernenLETELRHLQN 512
Cdd:COG4913 419 RELRE-------LEAEIASLER 433
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
319-508 |
7.92e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.14 E-value: 7.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 319 QHNDEMQELSGNIKEESKSQNSKDRVICELRAELERLQAENTSEWDKREILEREKQGLERENRRLKIQVKEMEELLDKKN 398
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 399 RLSANSQSPDFKMSQIDL------QEKNQELLNLQHAYYKLNRQYQANIAELTHANNRVDQNEAEVKKLRLRVEELKQGL 472
Cdd:COG4942 104 EELAELLRALYRLGRQPPlalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1034604707 473 NQKEDELDDSLN------------------QIRKLQRSLDEEKERNENLETELR 508
Cdd:COG4942 184 EEERAALEALKAerqkllarlekelaelaaELAELQQEAEELEALIARLEAEAA 237
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
322-511 |
8.35e-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: 45.44 E-value: 8.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 322 DEMQELSGNIKEESKSQNSKDRVICELRAELERLQAENTSEWDKREILEREKQGLERENRRLKIQVKEMEELLDKKNRLS 401
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEI 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 402 ANSQSpDFKMSQIDLQEKNQELLNLQHAYYKLNRQYqaNIAELTHANNRVDQNEAEVKKLRLRVEELKQGLNQK------ 475
Cdd:TIGR02169 754 ENVKS-ELKELEARIEELEEDLHKLEEALNDLEARL--SHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLtlekey 830
|
170 180 190
....*....|....*....|....*....|....*..
gi 1034604707 476 -EDELDDSLNQIRKLQRSLDEEKERNENLETELRHLQ 511
Cdd:TIGR02169 831 lEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELE 867
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
347-512 |
9.34e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.43 E-value: 9.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 347 ELRAELERLQaentsewdkREILEREKQGLERENRRLKIQVKEMEELLDKKNRLSANSQSP-DFKMSQI-----DLQEKN 420
Cdd:TIGR02168 217 ELKAELRELE---------LALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKlEELRLEVseleeEIEELQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 421 QELLNLQHAYYKLNRQYQANIAELTHANNRVDQNEAEVKKLRLRVEELKQGLNQKEDELDDSLNQIRKLQRSLDEEKERN 500
Cdd:TIGR02168 288 KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEL 367
|
170
....*....|..
gi 1034604707 501 ENLETELRHLQN 512
Cdd:TIGR02168 368 EELESRLEELEE 379
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
310-511 |
1.11e-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: 45.06 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 310 VKEFDILLGQHNDEMQELSGNIKEesksqnsKDRVICELRAELERLQAEntsewdkREILEREKQGLER-ENRRLKIQVK 388
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIER-------LDLIIDEKRQQLERLRRE-------REKAERYQALLKEkREYEGYELLK 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 389 EMEELLDKKNRLSANSQSPDFKMSQID--LQEKNQELlnlqHAYYKLNRQYQANIAELThaNNRVDQNEAEVKKLRLRVE 466
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTeeISELEKRL----EEIEQLLEELNKKIKDLG--EEEQLRVKEKIGELEAEIA 304
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1034604707 467 ELKQGLNQKEDELDDSLNQIRKLQRSLDEEKERNENLETELRHLQ 511
Cdd:TIGR02169 305 SLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEER 349
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
407-492 |
1.20e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 407 PDFKMSQIDLQEKNQELLNLQHAYYKLNRQYQANIAELTHANNRVDQNEAEVKKLRLRVEELKQGLNQKEDELDDslnQI 486
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE---RA 92
|
....*.
gi 1034604707 487 RKLQRS 492
Cdd:COG3883 93 RALYRS 98
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
330-507 |
2.15e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 44.19 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 330 NIKEESKSQNSKDRVICELRAELERLQAENTSEWDKREILEREKqgLERENRRLKIQVKEMEELLDKKNRLSANSQspDF 409
Cdd:pfam02463 177 KLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLE--LEEEYLLYLDYLKLNEERIDLLQELLRDEQ--EE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 410 KMSQIDLQEKNQELLNLQHAYYKLNRQYQANIAELthannrVDQNEAEVKKLRLRVEELKQGLNQKEDELDDSLNQIRKL 489
Cdd:pfam02463 253 IESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEE------LKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKA 326
|
170
....*....|....*...
gi 1034604707 490 QRSLDEEKERNENLETEL 507
Cdd:pfam02463 327 EKELKKEKEEIEELEKEL 344
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
436-512 |
2.62e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 436 QYQANIAELTHANNRVDQNEAEVKKLRLRVEELKQGLNQKEDELDDSLNQIRKLQRSLDE----EKERNENLETELRHLQ 511
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEaeaeIEERREELGERARALY 96
|
.
gi 1034604707 512 N 512
Cdd:COG3883 97 R 97
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
376-511 |
2.75e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.89 E-value: 2.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 376 LERENRRLKIQVKEMEELLDKKNRLSANSQSpdfkMSQIDLQEKNQELLNLQHAYYKLNRQYQAniaelthANNRVDQNE 455
Cdd:TIGR02168 198 LERQLKSLERQAEKAERYKELKAELRELELA----LLVLRLEELREELEELQEELKEAEEELEE-------LTAELQELE 266
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034604707 456 AEVKKLRLRVEELKQGLNQKEDELDDSLNQIRKLQRSLDEEKERNENLETELRHLQ 511
Cdd:TIGR02168 267 EKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELE 322
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
250-507 |
3.02e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 3.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 250 LENEVTEISALQVHLDEFQKILWKEREMRTALEKEIERLESALSLWKWKYEELKESKPKnVKEFDILLGQHNDEMQELSG 329
Cdd:PRK03918 233 LEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEK-AEEYIKLSEFYEEYLDELRE 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 330 NIKEESKSQnskdrvicELRAELERLQAENTSEWDKREILEREKQGLERENRRLKIQVKEMEELLDKKNRLSANSQspdf 409
Cdd:PRK03918 312 IEKRLSRLE--------EEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKK---- 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 410 KMSQIDLQEKNQELLNLQHAYYKLNRQYQANIAELTHANNRVDQNEAEVKKLR------------LRVEELKQGLNQKED 477
Cdd:PRK03918 380 RLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKkakgkcpvcgreLTEEHRKELLEEYTA 459
|
250 260 270
....*....|....*....|....*....|
gi 1034604707 478 ELDDSLNQIRKLQRSLDEEKERNENLETEL 507
Cdd:PRK03918 460 ELKRIEKELKEIEEKERKLRKELRELEKVL 489
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
83-509 |
3.83e-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: 43.57 E-value: 3.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 83 ARAAQMEKTMRWWSDCTANWREKWSKVRAernsAREEGRQLRIKLEMAMKELSTLKKK----QSLPPQKEALEAKVTQDL 158
Cdd:pfam15921 486 AKKMTLESSERTVSDLTASLQEKERAIEA----TNAEITKLRSRVDLKLQELQHLKNEgdhlRNVQTECEALKLQMAEKD 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 159 KLPGFVEESCEHTDQF----------------QLSSQMHESIREYLVKRQFSTKEDTNNKEQGVVIDSLKLSEemkpnld 222
Cdd:pfam15921 562 KVIEILRQQIENMTQLvgqhgrtagamqvekaQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEK------- 634
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 223 gVDLFNnggSGNGETKTGLRLKAINLPLENEVTEISALQVHLDEFQKILW-----KEREMRTALEKEIERLESALSLWKW 297
Cdd:pfam15921 635 -VKLVN---AGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKrnfrnKSEEMETTTNKLKMQLKSAQSELEQ 710
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 298 KYEELKESKPKNVKEFDILLGQHND------EMQELSGNIK--EESKSQNSKDRVIceLRAELERLQAENTSEWDKREIL 369
Cdd:pfam15921 711 TRNTLKSMEGSDGHAMKVAMGMQKQitakrgQIDALQSKIQflEEAMTNANKEKHF--LKEEKNKLSQELSTVATEKNKM 788
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 370 EREKQGLERENRRLKIQVKEMEELLDKKNRLSANSQSPDFKMSQIDLQEKNQELLN---LQHAYYKLN-----RQYQANI 441
Cdd:pfam15921 789 AGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLKLQHTLDvkeLQGPGYTSNssmkpRLLQPAS 868
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 442 AELTHANNRVDQNEAE----------------VKKLRLRVEELKQGLNQKEdelDDSLNQIRKLQRSLD----EEKERNE 501
Cdd:pfam15921 869 FTRTHSNVPSSQSTASflshhsrktnalkedpTRDLKQLLQELRSVINEEP---TVQLSKAEDKGRAPSlgalDDRVRDC 945
|
....*...
gi 1034604707 502 NLETELRH 509
Cdd:pfam15921 946 IIESSLRS 953
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
256-496 |
4.67e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.12 E-value: 4.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 256 EISALQVHLDEFQKILWKEREMRTALEKEIERLESALSLWKWKYEELKESKPKNvkefdillgqhNDEMQELSGNIKEES 335
Cdd:TIGR02168 797 ELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEEL-----------SEDIESLAAEIEELE 865
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 336 KSQNskdrvicELRAELERLQAENTSEWDKREILEREKQGLERENRRLKIQVKEMEELLDKKN-RLSAnsqspdfkmSQI 414
Cdd:TIGR02168 866 ELIE-------ELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELReKLAQ---------LEL 929
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 415 DLQEKNQELLNLQHayyKLNRQYQANIAE-LTHANNRVDQN---EAEVKKLRLRVEEL-----------------KQGLN 473
Cdd:TIGR02168 930 RLEGLEVRIDNLQE---RLSEEYSLTLEEaEALENKIEDDEeeaRRRLKRLENKIKELgpvnlaaieeyeelkerYDFLT 1006
|
250 260
....*....|....*....|...
gi 1034604707 474 QKEDELDDSLNQIRKLQRSLDEE 496
Cdd:TIGR02168 1007 AQKEDLTEAKETLEEAIEEIDRE 1029
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
415-499 |
4.90e-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: 42.44 E-value: 4.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 415 DLQEKNQELLNLQHAYYKLNRQYQANIAELTHANNRVDQNEAEVKKLRLRVEELKQGLNQKEDELDDSLNQIRKLQRSLD 494
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
....*
gi 1034604707 495 EEKER 499
Cdd:COG4942 101 AQKEE 105
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
282-512 |
7.96e-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: 42.31 E-value: 7.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 282 EKEIERLESALSLWKWKYEELKESKPKNV-KEFDILLGQHNDEMQELSGNIKEESKSQNSKDRVICELRAELERLQAENT 360
Cdd:TIGR04523 280 NKKIKELEKQLNQLKSEISDLNNQKEQDWnKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENS 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 361 S-------EWDKREILEREKQGLERENRRLKIQVKEMEELLDKKNRLSansqspdfkmsqidlQEKNQELLNLQHAYYKL 433
Cdd:TIGR04523 360 EkqreleeKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLN---------------QQKDEQIKKLQQEKELL 424
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034604707 434 NRQYQANIAELTHANNRVDQNEAEVKKLRLRVEELKQGLNQKEDELDDSLNQIRKLQRSLDEEKERNENLETELRHLQN 512
Cdd:TIGR04523 425 EKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNE 503
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
240-508 |
7.97e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 7.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 240 GLRLKAINLPLENEVTEISALQVHLDEFQKILWKEREMRTALEKEIERLESALS-----------------------LWK 296
Cdd:PRK03918 376 RLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEelkkakgkcpvcgrelteehrkeLLE 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 297 WKYEELKESKpKNVKEFDILLGQHNDEMQELSGNIKEESKSQNSKDRV--ICELRAELERLQAENTSE-WDKREILEREK 373
Cdd:PRK03918 456 EYTAELKRIE-KELKEIEEKERKLRKELRELEKVLKKESELIKLKELAeqLKELEEKLKKYNLEELEKkAEEYEKLKEKL 534
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 374 QGLERENRRLKIQVKEMEELLDKKNRLSANSQSPDFKMSQI----------DLQEKNQELLNLQHAYYKLNrqyqaniaE 443
Cdd:PRK03918 535 IKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELlkeleelgfeSVEELEERLKELEPFYNEYL--------E 606
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034604707 444 LTHANNRVDQNEAEVKKLRLRVEELKQGLNQKEDELDDSLNQIRKLQRSLDEEK-ERNENLETELR 508
Cdd:PRK03918 607 LKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEyEELREEYLELS 672
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
348-509 |
8.34e-04 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 41.64 E-value: 8.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 348 LRAELERLQAENTSEWDKREILEREKQGLERENRRLKIQVKEMEELLDKKNRLSAnsqspdfkmsQIDLQEKNQELLNLQ 427
Cdd:pfam00529 56 YQAALDSAEAQLAKAQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAAQA----------AVKAAQAQLAQAQID 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 428 HAYYKLNRQYQANIAE-LTHANNRVDQNEAEVKklrlrveELKQGLNQKEDELDDSLNQIRKLQRS--LDEEKERNEnLE 504
Cdd:pfam00529 126 LARRRVLAPIGGISREsLVTAGALVAQAQANLL-------ATVAQLDQIYVQITQSAAENQAEVRSelSGAQLQIAE-AE 197
|
....*
gi 1034604707 505 TELRH 509
Cdd:pfam00529 198 AELKL 202
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
276-502 |
9.11e-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: 41.67 E-value: 9.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 276 EMRTALEKEIERLESALSLWKWKYEELKESKPKNVKEfdilLGQHNDEMQELSGNIKEESKSQNSKDRVICELRAELERL 355
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQ----LAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 356 QAEntsEWDKREILEREKQGLERENRRLKIQVK-EMEELLDKKNRLSANSQSPDFKMSQID-LQEKNQELLNLQHAYYKL 433
Cdd:COG4942 96 RAE---LEAQKEELAELLRALYRLGRQPPLALLlSPEDFLDAVRRLQYLKYLAPARREQAEeLRADLAELAALRAELEAE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034604707 434 NRQYQANIAELTHANNRVDQNEAEVKKLRLRVEELKQGLNQKEDELDDSLNQIRKLQRSLDEEKERNEN 502
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
349-512 |
1.02e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.77 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 349 RAELERLQAENTSEWDKREILEREKQGLERENRRLKIQVKEMEELLDkknRLSAnsqspdfkmsqiDLQEKNQELLNLQH 428
Cdd:COG2433 384 ELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVE---ELEA------------ELEEKDERIERLER 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 429 AYYKLNRQYQANIAElthannrvdqnEAEVKKLRlrveelkqglnqkedelddslNQIRKLQRSLDEEKERNENLETELR 508
Cdd:COG2433 449 ELSEARSEERREIRK-----------DREISRLD---------------------REIERLERELEEERERIEELKRKLE 496
|
....
gi 1034604707 509 HLQN 512
Cdd:COG2433 497 RLKE 500
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
278-513 |
1.77e-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: 41.03 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 278 RTALEKEIERLESALSLWKWKYEELKE-------SKPKNVKEFDILLGQHNDEMQ---ELSGNIKEESKSQNSKDRVICE 347
Cdd:pfam07888 75 RRELESRVAELKEELRQSREKHEELEEkykelsaSSEELSEEKDALLAQRAAHEArirELEEDIKTLTQRVLERETELER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 348 LRAELERLQAENTSEWDKREILEREKQGLERENRRLKIQVKEMEELLDKKNRLSANSQSPDFKMSQ---------IDLQE 418
Cdd:pfam07888 155 MKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQklttahrkeAENEA 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 419 KNQELLNLQHAYYKLNRQYQANIAELTHANNRVDQNEAEVKKLRLRVEEL---------------------KQGLNQ--- 474
Cdd:pfam07888 235 LLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLtlqladaslalregrarwaqeRETLQQsae 314
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1034604707 475 KEDELDDSLNQ-IRKLQRSLDEEKERNENLETELRHLQNC 513
Cdd:pfam07888 315 ADKDRIEKLSAeLQRLEERLQEERMEREKLEVELGREKDC 354
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
272-512 |
2.90e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 272 WKEREMRTALEKEIERLESALSLWKWKYEELKEskpknvkefdilLGQHNDEMQELSGNIKEESKSQN---SKDRVICEL 348
Cdd:COG4913 606 FDNRAKLAALEAELAELEEELAEAEERLEALEA------------ELDALQERREALQRLAEYSWDEIdvaSAEREIAEL 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 349 RAELERLQAENtsewDKREILEREKQGLERENRRLKiqvKEMEELLDKKNRLSANsqspdfkmsQIDLQEKNQELLNLQH 428
Cdd:COG4913 674 EAELERLDASS----DDLAALEEQLEELEAELEELE---EELDELKGEIGRLEKE---------LEQAEEELDELQDRLE 737
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 429 AYYKLNRQYQANIAELTHANNRVDQNEAEVKK-LRLRVEELKQGLNQKEDELDDSLNQIRK----LQRSLDEEKERNENL 503
Cdd:COG4913 738 AAEDLARLELRALLEERFAAALGDAVERELREnLEERIDALRARLNRAEEELERAMRAFNRewpaETADLDADLESLPEY 817
|
....*....
gi 1034604707 504 ETELRHLQN 512
Cdd:COG4913 818 LALLDRLEE 826
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
242-464 |
3.04e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.13 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 242 RLKAINLPLENEVTEISALQVHLDEFQKILWKEREMRTALEKEIERLESALSLWKWKYEELKESKPKNVKEFDILL---- 317
Cdd:COG4942 35 EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLraly 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 318 --GQHNDEMQELSG-NIKEESKSQNSKDRVICELRAELERLQAENTSEWDKREILEREKQGLERENRRLKIQVKEMEELL 394
Cdd:COG4942 115 rlGRQPPLALLLSPeDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALK 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 395 DKKNRLSANSQSpdfkmsqiDLQEKNQELLNLQHAYYKLNRQYQANIAELTHANNRVDQNEAEVKKLRLR 464
Cdd:COG4942 195 AERQKLLARLEK--------ELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKLP 256
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
239-512 |
3.20e-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: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 239 TGLRLKAinlplENEVTEISALQVHLDEFQKilwKEREMRTALEKEIERLESALSLWKWKYEELKESKPKNVKEFDILLG 318
Cdd:pfam15921 281 TGLTEKA-----SSARSQANSIQSQLEIIQE---QARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLV 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 319 QHNDEMQELSGNIKEESKSQNSKDRVICELRAELERLQAENTSEWDKREILEREKQG-------LERENRRLKIQVKEME 391
Cdd:pfam15921 353 LANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGnsitidhLRRELDDRNMEVQRLE 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 392 ELLdkKNRLSANSQSPDFKMSQIdlQEKNQELLNLQhayyKLNRQYQANIAELTHANNRVDQNEAEVKKLRLRVEELKQG 471
Cdd:pfam15921 433 ALL--KAMKSECQGQMERQMAAI--QGKNESLEKVS----SLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTAS 504
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1034604707 472 LNQKEDELDDSLNQIRKLQRSLDEEKERNENLETELRHLQN 512
Cdd:pfam15921 505 LQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRN 545
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
414-510 |
3.25e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.14 E-value: 3.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 414 IDLQEKNQELLNLQHAYYKLNRQYQANIAELTHANNRVDQNEAEVKKLRLRVEELKQGLNQKEDELDDS---LNQIRK-- 488
Cdd:COG1579 10 LDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYeeqLGNVRNnk 89
|
90 100
....*....|....*....|....*.
gi 1034604707 489 ----LQRSLDEEKERNENLETELRHL 510
Cdd:COG1579 90 eyeaLQKEIESLKRRISDLEDEILEL 115
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
249-491 |
4.21e-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: 4.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 249 PLENEVTEISALQVHLDEFQKILWKEREMRTALEKEIERLESALSLWKWKYEELKESKPKNVKEFDILLgqhnDEMQELS 328
Cdd:TIGR00618 529 RMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQ----DLTEKLS 604
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 329 gnikeesksqNSKDRVICELRAELERLQAENtsewDKREILEREKQGLERENRRLKIQVKEMEELLDKKNRLSANSqspd 408
Cdd:TIGR00618 605 ----------EAEDMLACEQHALLRKLQPEQ----DLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALS---- 666
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 409 fkmSQIDLQEKNQELLNLQHAYYKLNRQYQANIAELTHANNRVDQNEAEVKKLRLRVEEL-------KQGLNQKEDELDD 481
Cdd:TIGR00618 667 ---IRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIenassslGSDLAAREDALNQ 743
|
250
....*....|
gi 1034604707 482 SLNQIRKLQR 491
Cdd:TIGR00618 744 SLKELMHQAR 753
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
250-472 |
4.30e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.92 E-value: 4.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 250 LENEVTEISALQVHLDEFQKILWKEREMRTALEKEIERLESALSLWKwkyEELKESKpKNVKEFDILLGQHNDEMQELSG 329
Cdd:COG1196 304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE---EELEEAE-AELAEAEEALLEAEAELAEAEE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 330 NIKEESKSQNSKDRVICELRAELERLQAENTSEWDKREILEREKQGLERENRRLKIQVKEMEELLDKKNRLSANSQSpDF 409
Cdd:COG1196 380 ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE-EE 458
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034604707 410 KMSQIDLQEKNQELLNLQHAYYKLNRQYQANIAELTHANNRVDQNEAEVKKLRLRVEELKQGL 472
Cdd:COG1196 459 EALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRG 521
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
260-510 |
4.59e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 39.49 E-value: 4.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 260 LQVHLDEFQK----ILWKEREMRTALEKEIERLESALSLWKWKYEELKEskpkNVKEFDILLGQHNDEMQELSGNIKEES 335
Cdd:pfam07888 32 LQNRLEECLQeraeLLQAQEAANRQREKEKERYKRDREQWERQRRELES----RVAELKEELRQSREKHEELEEKYKELS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 336 KSQNSKDRVICELRAELERLQAENTSEWDKREILEREKQGLERENRRLKIQVKEMEELLdkknrlsaNSQSPDFKMSQID 415
Cdd:pfam07888 108 ASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQR--------KEEEAERKQLQAK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 416 LQEKNQELLNLQhayyklnrqyqaniAELTHANNRVDQNEAEVKKLRLRVEELKQGLN---QKEDELDDSLNQIRKLQRS 492
Cdd:pfam07888 180 LQQTEEELRSLS--------------KEFQELRNSLAQRDTQVLQLQDTITTLTQKLTtahRKEAENEALLEELRSLQER 245
|
250
....*....|....*...
gi 1034604707 493 LDEEKERNENLETELRHL 510
Cdd:pfam07888 246 LNASERKVEGLGEELSSM 263
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
96-400 |
5.00e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 39.67 E-value: 5.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 96 SDCTANWREK---WSKVRAERNSAREEGRQLRIKLEMAMKELSTLK-KKQSLPPQKEALEAKVTQDLKLPGFVEESCEHt 171
Cdd:TIGR02169 712 SDASRKIGEIekeIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKsELKELEARIEELEEDLHKLEEALNDLEARLSH- 790
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 172 DQFQLSSQMHESIREYlVKRQFSTKEDTNNKEQGVVIDSLKLSEEMKPNLDGVDLFNNggsgngetktglRLKAINLPLE 251
Cdd:TIGR02169 791 SRIPEIQAELSKLEEE-VSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKE------------QIKSIEKEIE 857
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 252 NEVTEISALQVHLDEFQKILWKEREMRTALEKEIERLESALSLWKWKYEELK---ESKPKNVKEFDILLGQHNDEMQELS 328
Cdd:TIGR02169 858 NLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEaqiEKKRKRLSELKAKLEALEEELSEIE 937
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034604707 329 GNIKEEsKSQNSKDRVICELRAELERLQAE-------NTSEWDKREILEREKQGLERENRRLKIQVKEMEELLDKKNRL 400
Cdd:TIGR02169 938 DPKGED-EEIPEEELSLEDVQAELQRVEEEiralepvNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKK 1015
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
374-504 |
5.23e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 39.42 E-value: 5.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 374 QGLERENRRLKIQVKEMEELLDKKNRLsansqspdfKMSQIDLQEKNQEllNLQHAYYKLNRQYQANIAELthannrvdQ 453
Cdd:PRK00409 523 ASLEELERELEQKAEEAEALLKEAEKL---------KEELEEKKEKLQE--EEDKLLEEAEKEAQQAIKEA--------K 583
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1034604707 454 NEAEVKKLRLRVEELKQGLNQKEDELDDSLNQIRK----LQRSLDEEKERNENLE 504
Cdd:PRK00409 584 KEADEIIKELRQLQKGGYASVKAHELIEARKRLNKanekKEKKKKKQKEKQEELK 638
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
103-397 |
5.31e-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: 39.65 E-value: 5.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 103 REKWSKVRAERNSAREEGRQLRIKLEMAMKELSTLKKK-----QSLPPQKEALEAKVTQDLKLPGFVEESCEHTDQFQLS 177
Cdd:TIGR02168 238 REELEELQEELKEAEEELEELTAELQELEEKLEELRLEvseleEEIEELQKELYALANEISRLEQQKQILRERLANLERQ 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 178 SQMHESIREYLVKRQFSTKEDTNNKEqgvvidslKLSEEMKPNLDGVDLfnnggsgngetktglRLKAINLPLENEVTEI 257
Cdd:TIGR02168 318 LEELEAQLEELESKLDELAEELAELE--------EKLEELKEELESLEA---------------ELEELEAELEELESRL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 258 SALQVHLDEFQKILWKEREMRTALEKEIERLESALslwkwkyEELKESKPKNVKEfdilLGQHNDEMQELsgNIKEESKS 337
Cdd:TIGR02168 375 EELEEQLETLRSKVAQLELQIASLNNEIERLEARL-------ERLEDRRERLQQE----IEELLKKLEEA--ELKELQAE 441
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 338 QNSKDRVICELRAELERLQAENTSEWDKREILEREKQGLERENRRLKIQVKEMEELLDKK 397
Cdd:TIGR02168 442 LEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENL 501
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
365-499 |
5.55e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.37 E-value: 5.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 365 KREILEREKQGLERENRRLKIQVKEMEELLDKKNRLSAnsqspdfkmsQIDLQEKNQELLNLQHAYYKLNRQYQANIAEL 444
Cdd:COG4717 65 KPELNLKELKELEEELKEAEEKEEEYAELQEELEELEE----------ELEELEAELEELREELEKLEKLLQLLPLYQEL 134
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1034604707 445 THANNRVDQNEAEVKKLRLRVEELKQglnqKEDELDDSLNQIRKLQRSLDEEKER 499
Cdd:COG4717 135 EALEAELAELPERLEELEERLEELRE----LEEELEELEAELAELQEELEELLEQ 185
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
455-511 |
6.67e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 38.99 E-value: 6.67e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034604707 455 EAEVKKLRLRVEELKQGLNQKEDELDDSLNQIRKLQRSLDEEKERNENLETELRHLQ 511
Cdd:PRK12704 74 EKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKE 130
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
419-508 |
6.90e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 38.99 E-value: 6.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 419 KNQELLNLQHAYYKLNRQYQAniaELTHANNRVDQNEaevKKLRLRVEELK---QGLNQKEDELDDSLNQIRKLQRSLDE 495
Cdd:PRK12704 55 KKEALLEAKEEIHKLRNEFEK---ELRERRNELQKLE---KRLLQKEENLDrklELLEKREEELEKKEKELEQKQQELEK 128
|
90
....*....|...
gi 1034604707 496 EKERNENLETELR 508
Cdd:PRK12704 129 KEEELEELIEEQL 141
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
241-470 |
7.28e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.28 E-value: 7.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 241 LRLKAINLPLENEVTEISALQVHLDEFQKILWKEREMRTALE--KEIERLESALSLW-------KWK-YEELKESKPKNV 310
Cdd:PRK03918 459 AELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKElaEQLKELEEKLKKYnleelekKAEeYEKLKEKLIKLK 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 311 KEFDILLGQHNdEMQELSGNIKEESKSQNSKDRVICELRAELERLQAENTSEwDKREILERE------------KQGLER 378
Cdd:PRK03918 539 GEIKSLKKELE-KLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEE-LEERLKELEpfyneylelkdaEKELER 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 379 ENRRLKIQVKEMEELLDKKNRLSANSQSPDFKMSQIDLQEKNQELLNLQHAYYKLNRQYQANIAELTHANNRVDQNEAEV 458
Cdd:PRK03918 617 EEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTL 696
|
250
....*....|..
gi 1034604707 459 KKLRLRVEELKQ 470
Cdd:PRK03918 697 EKLKEELEEREK 708
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
323-509 |
7.34e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 39.28 E-value: 7.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 323 EMQELSGNIKEESKSQNSKDRVICELRAELERLQaentsewDKREILEREKQGLERENRRLKiqvKEMEELLDKKNRLSA 402
Cdd:TIGR02169 647 ELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLR-------ERLEGLKRELSSLQSELRRIE---NRLDELSQELSDASR 716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 403 nsqspdfkmsQIDLQEKNQELLNLQHAyyklnrqyqaniaelthannrvdQNEAEVKKLRLRVEELKQGLNQKEDELDDS 482
Cdd:TIGR02169 717 ----------KIGEIEKEIEQLEQEEE-----------------------KLKERLEELEEDLSSLEQEIENVKSELKEL 763
|
170 180
....*....|....*....|....*..
gi 1034604707 483 LNQIRKLQRSLDEEKERNENLETELRH 509
Cdd:TIGR02169 764 EARIEELEEDLHKLEEALNDLEARLSH 790
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
365-511 |
7.61e-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: 39.27 E-value: 7.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 365 KREI--LEREKQGLERENRRLKIQVKEMEELLDKKNRlsansqspDFKMSQIDLQEKNQELLNLQHAYYKLNRQYQANIA 442
Cdd:TIGR02168 676 RREIeeLEEKIEELEEKIAELEKALAELRKELEELEE--------ELEQLRKELEELSRQISALRKDLARLEAEVEQLEE 747
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034604707 443 ELTHANNRVDQNEAEVKKLRLRVEELKQGLNQKEDELDDSLNQIRKLQRSLDEEKERNENLETELRHLQ 511
Cdd:TIGR02168 748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLN 816
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
353-512 |
7.97e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 38.73 E-value: 7.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 353 ERLQAENTSEWDKREILEREKQGLERENRRLKIQVKEMEELLDKKNRLSANSQSpDFKMSQIDLQEKNQELLNLQHAYYK 432
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQARE-ELEQLEEELEQARSELEQLEEELEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 433 LNRQYQANIAELTHANNRVDQNEAEVKKLRLRVEELKQGLNQKEDELDDSLNQIRKLQRSLDEEKERNENLETELRHLQN 512
Cdd:COG4372 85 LNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQE 164
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
264-511 |
9.10e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 38.89 E-value: 9.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 264 LDEFQKILWKEREMRTALEKEIERLESALSlwkwkyeelkesKPKNVKEfdiLLGQHNDEMQELSGNIKEESKSQNSKDR 343
Cdd:PRK03918 157 LDDYENAYKNLGEVIKEIKRRIERLEKFIK------------RTENIEE---LIKEKEKELEEVLREINEISSELPELRE 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 344 VICELRAELERLqaENTSEwdKREILEREKQGLERENRRLKIQVKEMEELLDKKnrlsansqspdfKMSQIDLQEKNQEL 423
Cdd:PRK03918 222 ELEKLEKEVKEL--EELKE--EIEELEKELESLEGSKRKLEEKIRELEERIEEL------------KKEIEELEEKVKEL 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 424 LNLQ---HAYYKLNRQYqaniaelthanNRVDQNEAEVKKLRLRVEELKQGLNQKEDELDDSLNQIRKLQRSLDEEKERN 500
Cdd:PRK03918 286 KELKekaEEYIKLSEFY-----------EEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRL 354
|
250
....*....|.
gi 1034604707 501 ENLETELRHLQ 511
Cdd:PRK03918 355 EELEERHELYE 365
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
442-511 |
9.39e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 38.59 E-value: 9.39e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 442 AELTHANNRVDQNEAEVKKLRLRVEELKQGLNQKEDELDDSLNQIRKLQRSLDEEKERNENLETELRHLQ 511
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE 82
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
271-511 |
9.91e-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: 38.62 E-value: 9.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 271 LWKEREMRTALEKEIERLESALSLWKWKYEELKEskpkNVKEFDILLGQHNDEMQELSGNIKEESKSQNSKDRVICELRA 350
Cdd:pfam01576 196 LKKEEKGRQELEKAKRKLEGESTDLQEQIAELQA----QIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEA 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 351 ELERLQAENTSEWDKREILEREKQGLERENRRLKiqvKEMEELLDKKNrlsansqspdfkmSQIDLQEK-NQELLNLQHA 429
Cdd:pfam01576 272 QISELQEDLESERAARNKAEKQRRDLGEELEALK---TELEDTLDTTA-------------AQQELRSKrEQEVTELKKA 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604707 430 YYKLNRQYQANIAEL----THANNRVDQNEAEVKKLRLRVEELKQGLNQKEDELDdslNQIRKLQRSLDEEKERNENLET 505
Cdd:pfam01576 336 LEEETRSHEAQLQEMrqkhTQALEELTEQLEQAKRNKANLEKAKQALESENAELQ---AELRTLQQAKQDSEHKRKKLEG 412
|
....*.
gi 1034604707 506 ELRHLQ 511
Cdd:pfam01576 413 QLQELQ 418
|
|
| |
