|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
254-512 |
9.11e-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: 67.77 E-value: 9.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 254 VTEISALQVHLDEFQKILWKEREMRTALEKEIERLESALSLWKWKYEELKESKPKNVKEfdilLGQHNDEMQELSGNIKE 333
Cdd:TIGR02168 231 VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKE----LYALANEISRLEQQKQI 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 334 ESKSQNSKDRVICELRAELERLQAentsewdKREILEREKQGLERENRRLKIQVKEMEELLDKKNRLSANSQSpdfkmsq 413
Cdd:TIGR02168 307 LRERLANLERQLEELEAQLEELES-------KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELES------- 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 414 iDLQEKNQELLNLQHAYYKLNRQyqaniaeLTHANNRVDQNEAEVKKLRLRVEELKQGLNQKEDELDDslNQIRKLQRSL 493
Cdd:TIGR02168 373 -RLEELEEQLETLRSKVAQLELQ-------IASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE--AELKELQAEL 442
|
250
....*....|....*....
gi 1677501347 494 DEEKERNENLETELRHLQN 512
Cdd:TIGR02168 443 EELEEELEELQEELERLEE 461
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
253-511 |
5.24e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.34 E-value: 5.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 253 EVTEISALQVHLDEFQKILWKEREMRTALEKEIERLESALSLWKWKYEELKESkpknVKEFDILLGQHNDEMQELSGNIK 332
Cdd:COG1196 223 KELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLE----LEELELELEEAQAEEYELLAELA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 333 EESKSQNSKDRVICELRAELERLQAENTSEWDKREILEREKQGLERENRRLKIQVKEMEELLDKKNRLSANSQSpDFKMS 412
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA-ELAEA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 413 QIDLQEKNQELLNLQHAYYKLNRQYQANIAELTHANNRVDQNEAEVKKLRLRVEELKQGLNQKEDELDDSLNQIRKLQRS 492
Cdd:COG1196 378 EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457
|
250
....*....|....*....
gi 1677501347 493 LDEEKERNENLETELRHLQ 511
Cdd:COG1196 458 EEALLELLAELLEEAALLE 476
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
268-508 |
6.83e-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: 65.08 E-value: 6.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 268 QKILWKEREMRTaLEKEIERLESALSLWKWKYEELK---ESKPKNVKEFDILLGQHNDEMQELSGNIKEESKSQNSKDRV 344
Cdd:TIGR02168 670 SSILERRREIEE-LEEKIEELEEKIAELEKALAELRkelEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 345 ICELRAELERLQAENTSEWDKREILEREKQGLERENRRLKIQVKEMEELLDKKNRLSANSQSpdfkmsqiDLQEKNQELL 424
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA--------ELTLLNEEAA 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 425 NLQHAYYKLNRQYQANIAELTHANNRVDQNEAEVKKLRLRVEELKQGLNQKEDELDDSLNQIRKLQRSLDEEKERNENLE 504
Cdd:TIGR02168 821 NLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELS 900
|
....
gi 1677501347 505 TELR 508
Cdd:TIGR02168 901 EELR 904
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
242-510 |
4.01e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 62.78 E-value: 4.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 242 RLKAINLPLENEVTEISALQVHLDEFQKILWKEREMRTALEKEIERLESALSLWKWKYEELKESkpknvkefdiLLGQHN 321
Cdd:TIGR02169 724 EIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEAR----------LSHSRI 793
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 322 DEMQELSGNIKEESKSQnskDRVICELRAELERLQAEntsewdkREILEREKQGLERENRRLKIQVKEMEELLDKKNRLS 401
Cdd:TIGR02169 794 PEIQAELSKLEEEVSRI---EARLREIEQKLNRLTLE-------KEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKK 863
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 402 ANSQSpdfkmsqiDLQEKNQELLNLQHAYYKLNRQYQANIAELTHANNRVDQNEAEVKKLRLRVEELKQGLNQKEDELDD 481
Cdd:TIGR02169 864 EELEE--------ELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSE 935
|
250 260 270
....*....|....*....|....*....|....*
gi 1677501347 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 |
4.90e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.38 E-value: 4.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 250 LENEVTEISALQVHLDEFQkilwkerEMRTALEKEIERLESALSLWKWKYEELKESKPKNVKEFDILLGQHNDEMQELS- 328
Cdd:TIGR02168 290 LYALANEISRLEQQKQILR-------ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEe 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 329 -GNIKEESKSQN-SKDRVICELRAELERLQAENTSEWDKREILEREKQGLERENRRLKIQVKEMEELLdkknrlsansQS 406
Cdd:TIGR02168 363 lEAELEELESRLeELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL----------EE 432
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1677501347 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 |
7.16e-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: 58.53 E-value: 7.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 250 LENEVTEISALQVHLDEFQKILWKEREMRTALEKEIERLESALSLWKWKYEELKESKPKNVKEFDIL---LGQHNDEMQE 326
Cdd:TIGR02168 707 LEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAeeeLAEAEAEIEE 786
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 327 LSGNIKEESKSQNSKDRVICELRAELERLQAENTSEWDKREILEREKQGLERENRRLKIQVKEMEELLDKKNRLSANSQS 406
Cdd:TIGR02168 787 LEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEE 866
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 407 PDFKMsQIDLQEKNQELLNLQHAYYKLNRQYQANIAELTHANNRVDQNEAEVKKLRLRVEELK---QGLNQKEDELDDSL 483
Cdd:TIGR02168 867 LIEEL-ESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLElrlEGLEVRIDNLQERL 945
|
250 260
....*....|....*....|....*....
gi 1677501347 484 NQirKLQRSLDEEKERNENLETELRHLQN 512
Cdd:TIGR02168 946 SE--EYSLTLEEAEALENKIEDDEEEARR 972
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
281-511 |
4.23e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.10 E-value: 4.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 281 LEKEIERLES----ALslwkwKYEELKESKpknvKEFDILLGQHndEMQELSGNIKEESKSQNSKDRVICELRAELERLQ 356
Cdd:COG1196 198 LERQLEPLERqaekAE-----RYRELKEEL----KELEAELLLL--KLRELEAELEELEAELEELEAELEELEAELAELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 357 AENTSEwdkREILEREKQGLERENRRLKIQVKEMEELLDKKNRLSANSQSpdfkmSQIDLQEKNQELLNLQHAYYKLNRQ 436
Cdd:COG1196 267 AELEEL---RLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE-----LEERLEELEEELAELEEELEELEEE 338
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1677501347 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 |
2.33e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.53 E-value: 2.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 242 RLKAINLPLENEVTEISALQVHLDEFQKILWKEREMRTALEKEIERLESALSLWKWKYEELKEskpkNVKEFDILLGQHN 321
Cdd:TIGR02169 682 RLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEE----DLSSLEQEIENVK 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 322 DEMQELSGNIKEesksqnsKDRVICELRAELERLQAE-NTSEWDKreiLEREKQGLERENRRLKIQVKEMEELLDKK--N 398
Cdd:TIGR02169 758 SELKELEARIEE-------LEEDLHKLEEALNDLEARlSHSRIPE---IQAELSKLEEEVSRIEARLREIEQKLNRLtlE 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 399 RLSANSQSPDFKMSQIDLQEKNQELLNLQHAyykLNRQYQANIAELTHANNRVDQNEAEVKKLRLRVEELKQGLNQKEDE 478
Cdd:TIGR02169 828 KEYLEKEIQELQEQRIDLKEQIKSIEKEIEN---LNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERK 904
|
250 260 270
....*....|....*....|....*....|..
gi 1677501347 479 LDDSLNQIRKLQRSLDEEKERNENLETELRHL 510
Cdd:TIGR02169 905 IEELEAQIEKKRKRLSELKAKLEALEEELSEI 936
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
364-511 |
3.51e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.00 E-value: 3.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 364 DKREILEREKQGLERENRRLKIQVKEMEELLDK-KNRLSANSQSPDFKMSQIDLQEKNQELLNLQHAyyklnrqyqanIA 442
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDAlQERREALQRLAEYSWDEIDVASAEREIAELEAE-----------LE 678
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1677501347 443 ELTHANNRVDQNEAEVKKLRLRVEELKQ---GLNQKEDELDDSLNQIRKLQRSLDEEKERNENLETELRHLQ 511
Cdd:COG4913 679 RLDASSDDLAALEEQLEELEAELEELEEeldELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL 750
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
347-499 |
3.64e-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: 51.08 E-value: 3.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 347 ELRAELERLQAENTSEWDKREILEREKQGLERENRRLKIQVKEMEELLDKKNrlsansqspdfkmSQIDLQEKNQELLNL 426
Cdd:COG1579 28 ELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE-------------EQLGNVRNNKEYEAL 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1677501347 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 |
2.82e-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: 50.07 E-value: 2.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 265 DEFQKILWKEREMRTALEKEIERLESALSLWKWKYEELKESKPKNVKEFDILLGQHNDEMQELSGNIKEESKSQNSKDRV 344
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 345 ICELRAELERLQAENTsewDKREILEREKQGLERENRRLK-------IQVKemEELLDKKNRLSANSQSPDFKMSQidLQ 417
Cdd:TIGR02169 246 LASLEEELEKLTEEIS---ELEKRLEEIEQLLEELNKKIKdlgeeeqLRVK--EKIGELEAEIASLERSIAEKERE--LE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 418 EKNQELLNLQHAYYKLNRQYQANIAELTHANNRVDQNEAEVKKLRLRVEELKQGLNQKEDELDDSLNQIRKLQRSLDEEK 497
Cdd:TIGR02169 319 DAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLK 398
|
250
....*....|....
gi 1677501347 498 ERNENLETELRHLQ 511
Cdd:TIGR02169 399 REINELKRELDRLQ 412
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
353-512 |
9.60e-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: 48.63 E-value: 9.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 353 ERLQAENTSEWDKREILEREKQGLERENRRLKIQVKEMEELLDKKNRLSANSQSPDFKMSQIDLQEKNQELLNLQHAYYK 432
Cdd:pfam01576 920 EQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRR 999
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 433 LNRQYQANIAELTHANNRVDQNEAEVKKLRLRVEELKQGLNQKEDELDDSLNQIRKLQRSLDEEKERNENLETELRHLQN 512
Cdd:pfam01576 1000 TEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRELDDATESNESMNREVSTLKS 1079
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
319-507 |
1.18e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.52 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 319 QHNDEMQELSGNIKEESKSQNSKDrvicELRAELERLQAENTSEWDKREILEREKQGLERENRRLKIQVKEMEELLDKKN 398
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELD----ALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 399 RLSANSQSPDFKMSQIDLQEKNQELLNLQHAYYKLNRQYQANIAELTHANNRVDQNEAEVKKLRlrvEEL---KQGLNQK 475
Cdd:COG3883 93 RALYRSGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKL---AELealKAELEAA 169
|
170 180 190
....*....|....*....|....*....|..
gi 1677501347 476 EDELDDSLNQIRKLQRSLDEEKERNENLETEL 507
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAEL 201
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
274-493 |
1.44e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.01 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 274 EREMRTALEKEIERLESALSLWKWKYEELKESKPKNVKEFDILLGQHNDEMQELSGNIKEESKSQNSKDRVICELRAELE 353
Cdd:COG1196 307 LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 354 RLQAENTSEWDKREILEREKQGLERENRRLKIQVKEMEELLDKKNRLSANSQSpdfkmSQIDLQEKNQELLNLQHAYYKL 433
Cdd:COG1196 387 ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE-----EEEALEEAAEEEAELEEEEEAL 461
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 434 NRQYQANIAELTHANNRVDQNEAEVKKLRLRVEELKQGLNQKEDELDDSLNQIRKLQRSL 493
Cdd:COG1196 462 LELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRG 521
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
349-511 |
7.87e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.31 E-value: 7.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 349 RAELERLQaentsewDKREILEREKQGLERE----NRRLKIQvkemEELLDKKNRLSANsqspdfkmsQIDLQEKNQELL 424
Cdd:COG1196 185 EENLERLE-------DILGELERQLEPLERQaekaERYRELK----EELKELEAELLLL---------KLRELEAELEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 425 NLQHAyyKLNRQYQANIAELTHANNRVDQNEAEVKKLRLRVEELKQGLNQKEDELDDSLNQIRKLQRSLDEEKERNENLE 504
Cdd:COG1196 245 EAELE--ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELE 322
|
....*..
gi 1677501347 505 TELRHLQ 511
Cdd:COG1196 323 EELAELE 329
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
255-512 |
1.26e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 44.63 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 255 TEISALQVHLDEFQKILWKEREMRTALEKEIERLESALSLWKWKYEELKESKPKNVKEFDILLGQHNDEMQELSGN---I 331
Cdd:TIGR04523 412 EQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKqkeL 491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 332 KEESKSQNSKDRVICELRAELERLQAENTSEWDKREILEREKQGLERENRRLKIQVKEMEELLDKKNRlsansqspdfkm 411
Cdd:TIGR04523 492 KSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENL------------ 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 412 sQIDLQEKNQELLNLQHAYYKLnrqyqanIAELTHANNRVDQNEAEVKKLRLRVEELKQGLNQKEDELDDSLNQIRKLQR 491
Cdd:TIGR04523 560 -EKEIDEKNKEIEELKQTQKSL-------KKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSS 631
|
250 260
....*....|....*....|.
gi 1677501347 492 SLDEEKERNENLETELRHLQN 512
Cdd:TIGR04523 632 IIKNIKSKKNKLKQEVKQIKE 652
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
255-512 |
1.34e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 255 TEISALQVHLDEFQKIlwkEREMRTALEKeIERLESALSLWKwKYEELKESKpknvkefdillgQHNDEMQELSgNIKEE 334
Cdd:COG4913 225 EAADALVEHFDDLERA---HEALEDAREQ-IELLEPIRELAE-RYAAARERL------------AELEYLRAAL-RLWFA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 335 SKSQNSKDRVICELRAELERLQAEntsewdkREILEREKQGLERENRRLKIQVKEMEelLDKKNRLSAnsqspdfkmsqi 414
Cdd:COG4913 287 QRRLELLEAELEELRAELARLEAE-------LERLEARLDALREELDELEAQIRGNG--GDRLEQLER------------ 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 415 DLQEKNQELLNLQHAYyklnRQYQANIAELTHAnnrVDQNEAEVKKLRLRVEELKQGLNQK----EDELDDSLNQIRKLQ 490
Cdd:COG4913 346 EIERLERELEERERRR----ARLEALLAALGLP---LPASAEEFAALRAEAAALLEALEEElealEEALAEAEAALRDLR 418
|
250 260
....*....|....*....|..
gi 1677501347 491 RSLDEekernenLETELRHLQN 512
Cdd:COG4913 419 RELRE-------LEAEIASLER 433
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
322-511 |
1.62e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.67 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 322 DEMQELSGNIKEESKSQNSKDRVICELRAELERLQAENTSEWDKREILEREKQGLERENRRLKIQVKEMEELLDKKNRLS 401
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEI 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 402 ANSQSpDFKMSQIDLQEKNQELLNLQHAYYKLNRQYqaNIAELTHANNRVDQNEAEVKKLRLRVEELKQGLNQK------ 475
Cdd:TIGR02169 754 ENVKS-ELKELEARIEELEEDLHKLEEALNDLEARL--SHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLtlekey 830
|
170 180 190
....*....|....*....|....*....|....*..
gi 1677501347 476 -EDELDDSLNQIRKLQRSLDEEKERNENLETELRHLQ 511
Cdd:TIGR02169 831 lEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELE 867
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
319-508 |
1.63e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 319 QHNDEMQELSGNIKEESKSQNSKDRVICELRAELERLQAENTSEWDKREILEREKQGLERENRRLKIQVKEMEELLDKKN 398
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 399 RLSANSQSPDFKMSQIDL------QEKNQELLNLQHAYYKLNRQYQANIAELTHANNRVDQNEAEVKKLRLRVEELKQGL 472
Cdd:COG4942 104 EELAELLRALYRLGRQPPlalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1677501347 473 NQKEDELDDSLN------------------QIRKLQRSLDEEKERNENLETELR 508
Cdd:COG4942 184 EEERAALEALKAerqkllarlekelaelaaELAELQQEAEELEALIARLEAEAA 237
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
310-511 |
2.59e-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: 2.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 310 VKEFDILLGQHNDEMQELSGNIKEesksqnsKDRVICELRAELERLQAEntsewdkREILEREKQGLER-ENRRLKIQVK 388
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIER-------LDLIIDEKRQQLERLRRE-------REKAERYQALLKEkREYEGYELLK 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 389 EMEELLDKKNRLSANSQSPDFKMSQID--LQEKNQELlnlqHAYYKLNRQYQANIAELThaNNRVDQNEAEVKKLRLRVE 466
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTeeISELEKRL----EEIEQLLEELNKKIKDLG--EEEQLRVKEKIGELEAEIA 304
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1677501347 467 ELKQGLNQKEDELDDSLNQIRKLQRSLDEEKERNENLETELRHLQ 511
Cdd:TIGR02169 305 SLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEER 349
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
407-492 |
2.98e-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: 2.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 407 PDFKMSQIDLQEKNQELLNLQHAYYKLNRQYQANIAELTHANNRVDQNEAEVKKLRLRVEELKQGLNQKEDELDDslnQI 486
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE---RA 92
|
....*.
gi 1677501347 487 RKLQRS 492
Cdd:COG3883 93 RALYRS 98
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
278-513 |
3.81e-04 |
|
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: 42.96 E-value: 3.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 278 RTALEKEIERLESALSLWKWKYEELKE-------SKPKNVKEFDILLGQHNDEMQ---ELSGNIKEESKSQNSKDRVICE 347
Cdd:pfam07888 75 RRELESRVAELKEELRQSREKHEELEEkykelsaSSEELSEEKDALLAQRAAHEArirELEEDIKTLTQRVLERETELER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 348 LRAELERLQAENTSEWDKREILEREKQGLERENRRLKIQVKEMEELLDKKNRLSANSQSPDFKMSQ---------IDLQE 418
Cdd:pfam07888 155 MKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQklttahrkeAENEA 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 419 KNQELLNLQHAYYKLNRQYQANIAELTHANNRVDQNEAEVKKLRLRVEELKQGLNQKEDELDDSLNQIRK----LQRSLD 494
Cdd:pfam07888 235 LLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQeretLQQSAE 314
|
250
....*....|....*....
gi 1677501347 495 EEKERNENLETELRHLQNW 513
Cdd:pfam07888 315 ADKDRIEKLSAELQRLEER 333
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
376-511 |
4.69e-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: 4.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 376 LERENRRLKIQVKEMEELLDKKNRLSANSQSpdfkMSQIDLQEKNQELLNLQHAYYKLNRQYQAniaelthANNRVDQNE 455
Cdd:TIGR02168 198 LERQLKSLERQAEKAERYKELKAELRELELA----LLVLRLEELREELEELQEELKEAEEELEE-------LTAELQELE 266
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1677501347 456 AEVKKLRLRVEELKQGLNQKEDELDDSLNQIRKLQRSLDEEKERNENLETELRHLQ 511
Cdd:TIGR02168 267 EKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELE 322
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
436-512 |
6.56e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 6.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 436 QYQANIAELTHANNRVDQNEAEVKKLRLRVEELKQGLNQKEDELDDSLNQIRKLQRSLDE----EKERNENLETELRHLQ 511
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEaeaeIEERREELGERARALY 96
|
.
gi 1677501347 512 N 512
Cdd:COG3883 97 R 97
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
250-507 |
7.09e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 7.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 250 LENEVTEISALQVHLDEFQKILWKEREMRTALEKEIERLESALSLWKWKYEELKESKPKnVKEFDILLGQHNDEMQELSG 329
Cdd:PRK03918 233 LEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEK-AEEYIKLSEFYEEYLDELRE 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 330 NIKEESKSQnskdrvicELRAELERLQAENTSEWDKREILEREKQGLERENRRLKIQVKEMEELLDKKNRLSANSQspdf 409
Cdd:PRK03918 312 IEKRLSRLE--------EEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKK---- 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 410 KMSQIDLQEKNQELLNLQHAYYKLNRQYQANIAELTHANNRVDQNEAEVKKLR------------LRVEELKQGLNQKED 477
Cdd:PRK03918 380 RLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKkakgkcpvcgreLTEEHRKELLEEYTA 459
|
250 260 270
....*....|....*....|....*....|
gi 1677501347 478 ELDDSLNQIRKLQRSLDEEKERNENLETEL 507
Cdd:PRK03918 460 ELKRIEKELKEIEEKERKLRKELRELEKVL 489
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
415-499 |
7.24e-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: 42.06 E-value: 7.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 415 DLQEKNQELLNLQHAYYKLNRQYQANIAELTHANNRVDQNEAEVKKLRLRVEELKQGLNQKEDELDDSLNQIRKLQRSLD 494
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
....*
gi 1677501347 495 EEKER 499
Cdd:COG4942 101 AQKEE 105
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
330-507 |
7.80e-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: 42.27 E-value: 7.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 330 NIKEESKSQNSKDRVICELRAELERLQAENTSEWDKREILEREKqgLERENRRLKIQVKEMEELLDKKNRLSANSQspDF 409
Cdd:pfam02463 177 KLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLE--LEEEYLLYLDYLKLNEERIDLLQELLRDEQ--EE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 410 KMSQIDLQEKNQELLNLQHAYYKLNRQYQANIAELthannrVDQNEAEVKKLRLRVEELKQGLNQKEDELDDSLNQIRKL 489
Cdd:pfam02463 253 IESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEE------LKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKA 326
|
170
....*....|....*...
gi 1677501347 490 QRSLDEEKERNENLETEL 507
Cdd:pfam02463 327 EKELKKEKEEIEELEKEL 344
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
256-474 |
1.18e-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: 41.58 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 256 EISALQVHLDEFQKILWKEREMRTALEKEIERLESALSLWKWKYEELKESKPKNvkefdillgqhNDEMQELSGNIKEES 335
Cdd:TIGR02168 797 ELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEEL-----------SEDIESLAAEIEELE 865
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 336 KSQNskdrvicELRAELERLQAENTSEWDKREILEREKQGLERENRRLKIQVKEMEELLDKKNRLSANsqspdfkmSQID 415
Cdd:TIGR02168 866 ELIE-------ELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQ--------LELR 930
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1677501347 416 LQEKNQELLNLQHayyKLNRQYQaniAELTHANNRVDQNEAEVKKLRLRVEELKQGLNQ 474
Cdd:TIGR02168 931 LEGLEVRIDNLQE---RLSEEYS---LTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
349-512 |
1.35e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.38 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 349 RAELERLQAENTSEWDKREILEREKQGLERENRRLKIQVKEMEELLDkknRLSAnsqspdfkmsqiDLQEKNQELLNLQH 428
Cdd:COG2433 384 ELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVE---ELEA------------ELEEKDERIERLER 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 429 AYYKLNRQYQANIAElthannrvdqnEAEVKKLRlrveelkqglnqkedelddslNQIRKLQRSLDEEKERNENLETELR 508
Cdd:COG2433 449 ELSEARSEERREIRK-----------DREISRLD---------------------REIERLERELEEERERIEELKRKLE 496
|
....
gi 1677501347 509 HLQN 512
Cdd:COG2433 497 RLKE 500
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
348-509 |
1.43e-03 |
|
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: 40.87 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 348 LRAELERLQAENTSEWDKREILEREKQGLERENRRLKIQVKEMEELLDKKNRLSAnsqspdfkmsQIDLQEKNQELLNLQ 427
Cdd:pfam00529 56 YQAALDSAEAQLAKAQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAAQA----------AVKAAQAQLAQAQID 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 428 HAYYKLNRQYQANIAE-LTHANNRVDQNEAEVKklrlrveELKQGLNQKEDELDDSLNQIRKLQRS--LDEEKERNEnLE 504
Cdd:pfam00529 126 LARRRVLAPIGGISREsLVTAGALVAQAQANLL-------ATVAQLDQIYVQITQSAAENQAEVRSelSGAQLQIAE-AE 197
|
....*
gi 1677501347 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 |
1.62e-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: 40.90 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 276 EMRTALEKEIERLESALSLWKWKYEELKESKPKNVKEfdilLGQHNDEMQELSGNIKEESKSQNSKDRVICELRAELERL 355
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQ----LAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 356 QAEntsEWDKREILEREKQGLERENRRLKIQVK-EMEELLDKKNRLSANSQSPDFKMSQID-LQEKNQELLNLQHAYYKL 433
Cdd:COG4942 96 RAE---LEAQKEELAELLRALYRLGRQPPLALLlSPEDFLDAVRRLQYLKYLAPARREQAEeLRADLAELAALRAELEAE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1677501347 434 NRQYQANIAELTHANNRVDQNEAEVKKLRLRVEELKQGLNQKEDELDDSLNQIRKLQRSLDEEKERNEN 502
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
83-509 |
1.72e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 41.26 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 83 ARAAQMEKTMRWWSDCTANWREKWSKVRAernsAREEGRQLRIKLEMAMKELSTLKKK----QSLPPQKEALEAKVTQDL 158
Cdd:pfam15921 486 AKKMTLESSERTVSDLTASLQEKERAIEA----TNAEITKLRSRVDLKLQELQHLKNEgdhlRNVQTECEALKLQMAEKD 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 159 KLPGFVEESCEHTDQF----------------QLSSQMHESIREYLVKRQFSTKEDTNNKEQGVVIDSLKLSEemkpnld 222
Cdd:pfam15921 562 KVIEILRQQIENMTQLvgqhgrtagamqvekaQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEK------- 634
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 223 gVDLFNnggSGNGETKTGLRLKAINLPLENEVTEISALQVHLDEFQKILW-----KEREMRTALEKEIERLESALSLWKW 297
Cdd:pfam15921 635 -VKLVN---AGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKrnfrnKSEEMETTTNKLKMQLKSAQSELEQ 710
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 298 KYEELKESKPKNVKEFDILLGQHND------EMQELSGNIK--EESKSQNSKDRVIceLRAELERLQAENTSEWDKREIL 369
Cdd:pfam15921 711 TRNTLKSMEGSDGHAMKVAMGMQKQitakrgQIDALQSKIQflEEAMTNANKEKHF--LKEEKNKLSQELSTVATEKNKM 788
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 370 EREKQGLERENRRLKIQVKEMEELLDKKNRLSANSQSPDFKMSQIDLQEKNQELLN---LQHAYYKLN-----RQYQANI 441
Cdd:pfam15921 789 AGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLKLQHTLDvkeLQGPGYTSNssmkpRLLQPAS 868
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 442 AELTHANNRVDQNEAE----------------VKKLRLRVEELKQGLNQKEdelDDSLNQIRKLQRSLD----EEKERNE 501
Cdd:pfam15921 869 FTRTHSNVPSSQSTASflshhsrktnalkedpTRDLKQLLQELRSVINEEP---TVQLSKAEDKGRAPSlgalDDRVRDC 945
|
....*...
gi 1677501347 502 NLETELRH 509
Cdd:pfam15921 946 IIESSLRS 953
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
240-508 |
2.44e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 240 GLRLKAINLPLENEVTEISALQVHLDEFQKILWKEREMRTALEKEIERLESALS-----------------------LWK 296
Cdd:PRK03918 376 RLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEelkkakgkcpvcgrelteehrkeLLE 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 297 WKYEELKESKpKNVKEFDILLGQHNDEMQELSGNIKEESKSQNSKDRV--ICELRAELERLQAENTSE-WDKREILEREK 373
Cdd:PRK03918 456 EYTAELKRIE-KELKEIEEKERKLRKELRELEKVLKKESELIKLKELAeqLKELEEKLKKYNLEELEKkAEEYEKLKEKL 534
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 374 QGLERENRRLKIQVKEMEELLDKKNRLSANSQSPDFKMSQI----------DLQEKNQELLNLQHAYYKLNrqyqaniaE 443
Cdd:PRK03918 535 IKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELlkeleelgfeSVEELEERLKELEPFYNEYL--------E 606
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1677501347 444 LTHANNRVDQNEAEVKKLRLRVEELKQGLNQKEDELDDSLNQIRKLQRSLDEEK-ERNENLETELR 508
Cdd:PRK03918 607 LKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEyEELREEYLELS 672
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
282-512 |
3.67e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.00 E-value: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 282 EKEIERLESALSLWKWKYEELKESKPKNV-KEFDILLGQHNDEMQELSGNIKEESKSQNSKDRVICELRAELERLQAENT 360
Cdd:TIGR04523 280 NKKIKELEKQLNQLKSEISDLNNQKEQDWnKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENS 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 361 S-------EWDKREILEREKQGLERENRRLKIQVKEMEELLDKKNRLSansqspdfkmsqidlQEKNQELLNLQHAYYKL 433
Cdd:TIGR04523 360 EkqreleeKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLN---------------QQKDEQIKKLQQEKELL 424
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1677501347 434 NRQYQANIAELTHANNRVDQNEAEVKKLRLRVEELKQGLNQKEDELDDSLNQIRKLQRSLDEEKERNENLETELRHLQN 512
Cdd:TIGR04523 425 EKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNE 503
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
414-510 |
5.40e-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: 38.75 E-value: 5.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 414 IDLQEKNQELLNLQHAYYKLNRQYQANIAELTHANNRVDQNEAEVKKLRLRVEELKQGLNQKEDELDDS---LNQIRK-- 488
Cdd:COG1579 10 LDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYeeqLGNVRNnk 89
|
90 100
....*....|....*....|....*.
gi 1677501347 489 ----LQRSLDEEKERNENLETELRHL 510
Cdd:COG1579 90 eyeaLQKEIESLKRRISDLEDEILEL 115
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
272-512 |
5.58e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.51 E-value: 5.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 272 WKEREMRTALEKEIERLESALSLWKWKYEELKEskpknvkefdilLGQHNDEMQELSGNIKEESKSQN---SKDRVICEL 348
Cdd:COG4913 606 FDNRAKLAALEAELAELEEELAEAEERLEALEA------------ELDALQERREALQRLAEYSWDEIdvaSAEREIAEL 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 349 RAELERLQAENtsewDKREILEREKQGLERENRRLKiqvKEMEELLDKKNRLSANsqspdfkmsQIDLQEKNQELLNLQH 428
Cdd:COG4913 674 EAELERLDASS----DDLAALEEQLEELEAELEELE---EELDELKGEIGRLEKE---------LEQAEEELDELQDRLE 737
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 429 AYYKLNRQYQANIAELTHANNRVDQNEAEVKK-LRLRVEELKQGLNQKEDELDDSLNQIRK----LQRSLDEEKERNENL 503
Cdd:COG4913 738 AAEDLARLELRALLEERFAAALGDAVERELREnLEERIDALRARLNRAEEELERAMRAFNRewpaETADLDADLESLPEY 817
|
....*....
gi 1677501347 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 |
5.60e-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: 38.98 E-value: 5.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 242 RLKAINLPLENEVTEISALQVHLDEFQKILWKEREMRTALEKEIERLESALSLWKWKYEELKESKPKNVKEFDILL---- 317
Cdd:COG4942 35 EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLraly 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 318 --GQHNDEMQELSG-NIKEESKSQNSKDRVICELRAELERLQAENTSEWDKREILEREKQGLERENRRLKIQVKEMEELL 394
Cdd:COG4942 115 rlGRQPPLALLLSPeDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALK 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 395 DKKNRLSANSQSpdfkmsqiDLQEKNQELLNLQHAYYKLNRQYQANIAELTHANNRVDQNEAEVKKLRLR 464
Cdd:COG4942 195 AERQKLLARLEK--------ELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKLP 256
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
250-472 |
6.70e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.15 E-value: 6.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 250 LENEVTEISALQVHLDEFQKILWKEREMRTALEKEIERLESALSLWKwkyEELKESKpKNVKEFDILLGQHNDEMQELSG 329
Cdd:COG1196 304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE---EELEEAE-AELAEAEEALLEAEAELAEAEE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 330 NIKEESKSQNSKDRVICELRAELERLQAENTSEWDKREILEREKQGLERENRRLKIQVKEMEELLDKKNRLSANSQSpDF 409
Cdd:COG1196 380 ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE-EE 458
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1677501347 410 KMSQIDLQEKNQELLNLQHAYYKLNRQYQANIAELTHANNRVDQNEAEVKKLRLRVEELKQGL 472
Cdd:COG1196 459 EALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRG 521
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
255-512 |
6.78e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 39.33 E-value: 6.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 255 TEISALQVHLDEFQKilwKEREMRTALEKEIERLESALSLWKWKYEELKESKPKNVKEFDILLGQHNDEMQELSGNIKEE 334
Cdd:pfam15921 292 SQANSIQSQLEIIQE---QARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQF 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 335 SKSQNSKDRVICELRAELERLQAENTSEWDKREILEREKQG-------LERENRRLKIQVKEMEELLdkKNRLSANSQSP 407
Cdd:pfam15921 369 SQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGnsitidhLRRELDDRNMEVQRLEALL--KAMKSECQGQM 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 408 DFKMSQIdlQEKNQELLNLQhayyKLNRQYQANIAELTHANNRVDQNEAEVKKLRLRVEELKQGLNQKEDELDDSLNQIR 487
Cdd:pfam15921 447 ERQMAAI--QGKNESLEKVS----SLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEIT 520
|
250 260
....*....|....*....|....*
gi 1677501347 488 KLQRSLDEEKERNENLETELRHLQN 512
Cdd:pfam15921 521 KLRSRVDLKLQELQHLKNEGDHLRN 545
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
374-504 |
6.86e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 39.04 E-value: 6.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 374 QGLERENRRLKIQVKEMEELLDKKNRLsansqspdfKMSQIDLQEKNQEllNLQHAYYKLNRQYQANIAELthannrvdQ 453
Cdd:PRK00409 523 ASLEELERELEQKAEEAEALLKEAEKL---------KEELEEKKEKLQE--EEDKLLEEAEKEAQQAIKEA--------K 583
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1677501347 454 NEAEVKKLRLRVEELKQGLNQKEDELDDSLNQIRK----LQRSLDEEKERNENLE 504
Cdd:PRK00409 584 KEADEIIKELRQLQKGGYASVKAHELIEARKRLNKanekKEKKKKKQKEKQEELK 638
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
455-511 |
7.84e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 38.99 E-value: 7.84e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1677501347 455 EAEVKKLRLRVEELKQGLNQKEDELDDSLNQIRKLQRSLDEEKERNENLETELRHLQ 511
Cdd:PRK12704 74 EKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKE 130
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
419-508 |
9.73e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 38.61 E-value: 9.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677501347 419 KNQELLNLQHAYYKLNRQYQAniaELTHANNRVDQNEaevKKLRLRVEELK---QGLNQKEDELDDSLNQIRKLQRSLDE 495
Cdd:PRK12704 55 KKEALLEAKEEIHKLRNEFEK---ELRERRNELQKLE---KRLLQKEENLDrklELLEKREEELEKKEKELEQKQQELEK 128
|
90
....*....|...
gi 1677501347 496 EKERNENLETELR 508
Cdd:PRK12704 129 KEEELEELIEEQL 141
|
|
| |
