|
Name |
Accession |
Description |
Interval |
E-value |
| TMF_TATA_bd |
pfam12325 |
TATA element modulatory factor 1 TATA binding; This is the C-terminal conserved coiled coil ... |
432-543 |
2.29e-30 |
|
TATA element modulatory factor 1 TATA binding; This is the C-terminal conserved coiled coil region of a family of TATA element modulatory factor 1 proteins conserved in eukaryotes. The proteins bind to the TATA element of some RNA polymerase II promoters and repress their activity. by competing with the binding of TATA binding protein. TMF1_TATA_bd is the most conserved part of the TMFs. TMFs are evolutionarily conserved golgins that bind Rab6, a ubiquitous ras-like GTP-binding Golgi protein, and contribute to Golgi organization in animal and plant cells. The Rab6-binding domain appears to be the same region as this C-terminal family.
Pssm-ID: 432481 [Multi-domain] Cd Length: 115 Bit Score: 114.56 E-value: 2.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 432 GAGNVPDVSLLEQLATTIRRLEAELQTTKQQVAQLIIQRDQARQEIVDAYVNNDANEDSKKQVEELRLQLQNLEKEHAST 511
Cdd:pfam12325 4 TSGAGPSVQLVERLSSTIRRLEGELASLKEELARLEAQRDEARQEIVKLMKENEELKELKKELEELEKELKELEQRYETT 83
|
90 100 110
....*....|....*....|....*....|..
gi 19112828 512 LVTLKQKSDKVFELELDIKDMRELYVSQIDIL 543
Cdd:pfam12325 84 LELLGEKSEEVEELKADVEDLKEMYREQVQQL 115
|
|
| TMF_DNA_bd |
pfam12329 |
TATA element modulatory factor 1 DNA binding; This is the middle region of a family of TATA ... |
39-105 |
5.69e-10 |
|
TATA element modulatory factor 1 DNA binding; This is the middle region of a family of TATA element modulatory factor 1 proteins conserved in eukaryotes that contains at its N-terminal section a number of leucine zippers that could potentially form coiled coil structures.. The whole proteins bind to the TATA element of some RNA polymerase II promoters and repress their activity. by competing with the binding of TATA binding protein. TMFs are evolutionarily conserved golgins that bind Rab6, a ubiquitous ras-like GTP-binding Golgi protein, and contribute to Golgi organization in animal and plant cells.
Pssm-ID: 372049 [Multi-domain] Cd Length: 74 Bit Score: 55.78 E-value: 5.69e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19112828 39 KSKDEIIAKLLTEGQALSKNELKLNNTIKQLKKSLSEAETKLKRLDEKQATPELQVSDSKEMEEQLE 105
Cdd:pfam12329 8 KEKDEQIAQLMEEGEKLSKKELKLNNTIKKLRAKNKELEKEIAELKKKLEKLEKELENLEERLKRAE 74
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
54-257 |
4.22e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.22 E-value: 4.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 54 ALSKNELK-LNNTIKQLKKSLSEAETKLKRLDEKQATPELQVSDSK----EMEEQL-ELQKSQFE--KRISILEKEKEDL 125
Cdd:TIGR02168 228 ALLVLRLEeLREELEELQEELKEAEEELEELTAELQELEEKLEELRlevsELEEEIeELQKELYAlaNEISRLEQQKQIL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 126 QRKMEELTVESMEVVRLTRQVETLSTQYSIQRSQWVREDEKKKKEIQDLKE-------LYEKSEHGAKNWERERETFQNQ 198
Cdd:TIGR02168 308 RERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAeleeleaELEELESRLEELEEQLETLRSK 387
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19112828 199 VSQMSKQLDSLEKLCERKDEEIRSSQAFNMTLREENDTLA-----AQNLDLQTQLDRLQRELDT 257
Cdd:TIGR02168 388 VAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLkkleeAELKELQAELEELEEELEE 451
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
50-255 |
7.94e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.38 E-value: 7.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 50 TEGQALSKNELK-LNNTIKQLKKSLSEAETKLKRLDEKQATPELQVSDSKEMEEQLELQKSQFEKRISILEKEKEDLQRK 128
Cdd:COG4942 19 ADAAAEAEAELEqLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 129 MEELTVESMEVVRLTRQVETLST----------QYSIQRSQWVRE-DEKKKKEIQDLKELYEKSEHGAKNWERERETFQN 197
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPlalllspedfLDAVRRLQYLKYlAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 19112828 198 QVSQMSKQLDSLEKLCERKDEEIRSSQAFNMTLREENDTLAAQNLDLQTQLDRLQREL 255
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
61-220 |
1.31e-05 |
|
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: 48.25 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 61 KLNNTIKQLKKSLSEAETKLKRLDEKQATPELQVSDSKEMEEQLELQKSQFEKRISILEKEKEDLQRKMEEltvESMEVV 140
Cdd:pfam01576 437 KLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEE---EEEAKR 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 141 RLTRQVETLSTQYSiqrsqwvredeKKKKEIQDLKELYEKSEHGAKNWERERETFQNQVSQMSKQLDSLEKLCERKDEEI 220
Cdd:pfam01576 514 NVERQLSTLQAQLS-----------DMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQEL 582
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
442-546 |
6.21e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 6.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 442 LEQLATTIRRLEAELQTTKQQVAQLIIQRDQARQEIVDAYvnNDANEDSKKQVEELRLQLQNLEKEHASTLVTLKQKSDK 521
Cdd:COG4913 290 LELLEAELEELRAELARLEAELERLEARLDALREELDELE--AQIRGNGGDRLEQLEREIERLERELEERERRRARLEAL 367
|
90 100
....*....|....*....|....*
gi 19112828 522 VFELELDIKDMRELYVSQIDILAGR 546
Cdd:COG4913 368 LAALGLPLPASAEEFAALRAEAAAL 392
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
61-218 |
1.28e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 61 KLNNTIKQLKKSLSEAETKLKRLDEkqatpelqvsdSKEMEEQLELQKSQFEKRISILEKEKEDLQRKMEELTVESMEVV 140
Cdd:PRK03918 211 EISSELPELREELEKLEKEVKELEE-----------LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELE 279
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19112828 141 RLTRQVETLstqysiqrsqwvredEKKKKEIQDLKELYEKSEHGAKNWERERETFQNQVSQMSKQLDSLEKLCERKDE 218
Cdd:PRK03918 280 EKVKELKEL---------------KEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEE 342
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
42-143 |
3.74e-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: 39.75 E-value: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 42 DEIIAKLLTEGQALSKNELKLNNTIKQLKKSLSEAETKLKRLDEKQATPELQVSDSKEMEEQLELQKSQFEKRISILEKE 121
Cdd:COG4942 142 KYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQE 221
|
90 100
....*....|....*....|..
gi 19112828 122 KEDLQRKMEELTVESMEVVRLT 143
Cdd:COG4942 222 AEELEALIARLEAEAAAAAERT 243
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| TMF_TATA_bd |
pfam12325 |
TATA element modulatory factor 1 TATA binding; This is the C-terminal conserved coiled coil ... |
432-543 |
2.29e-30 |
|
TATA element modulatory factor 1 TATA binding; This is the C-terminal conserved coiled coil region of a family of TATA element modulatory factor 1 proteins conserved in eukaryotes. The proteins bind to the TATA element of some RNA polymerase II promoters and repress their activity. by competing with the binding of TATA binding protein. TMF1_TATA_bd is the most conserved part of the TMFs. TMFs are evolutionarily conserved golgins that bind Rab6, a ubiquitous ras-like GTP-binding Golgi protein, and contribute to Golgi organization in animal and plant cells. The Rab6-binding domain appears to be the same region as this C-terminal family.
Pssm-ID: 432481 [Multi-domain] Cd Length: 115 Bit Score: 114.56 E-value: 2.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 432 GAGNVPDVSLLEQLATTIRRLEAELQTTKQQVAQLIIQRDQARQEIVDAYVNNDANEDSKKQVEELRLQLQNLEKEHAST 511
Cdd:pfam12325 4 TSGAGPSVQLVERLSSTIRRLEGELASLKEELARLEAQRDEARQEIVKLMKENEELKELKKELEELEKELKELEQRYETT 83
|
90 100 110
....*....|....*....|....*....|..
gi 19112828 512 LVTLKQKSDKVFELELDIKDMRELYVSQIDIL 543
Cdd:pfam12325 84 LELLGEKSEEVEELKADVEDLKEMYREQVQQL 115
|
|
| TMF_DNA_bd |
pfam12329 |
TATA element modulatory factor 1 DNA binding; This is the middle region of a family of TATA ... |
39-105 |
5.69e-10 |
|
TATA element modulatory factor 1 DNA binding; This is the middle region of a family of TATA element modulatory factor 1 proteins conserved in eukaryotes that contains at its N-terminal section a number of leucine zippers that could potentially form coiled coil structures.. The whole proteins bind to the TATA element of some RNA polymerase II promoters and repress their activity. by competing with the binding of TATA binding protein. TMFs are evolutionarily conserved golgins that bind Rab6, a ubiquitous ras-like GTP-binding Golgi protein, and contribute to Golgi organization in animal and plant cells.
Pssm-ID: 372049 [Multi-domain] Cd Length: 74 Bit Score: 55.78 E-value: 5.69e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19112828 39 KSKDEIIAKLLTEGQALSKNELKLNNTIKQLKKSLSEAETKLKRLDEKQATPELQVSDSKEMEEQLE 105
Cdd:pfam12329 8 KEKDEQIAQLMEEGEKLSKKELKLNNTIKKLRAKNKELEKEIAELKKKLEKLEKELENLEERLKRAE 74
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
54-257 |
4.22e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.22 E-value: 4.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 54 ALSKNELK-LNNTIKQLKKSLSEAETKLKRLDEKQATPELQVSDSK----EMEEQL-ELQKSQFE--KRISILEKEKEDL 125
Cdd:TIGR02168 228 ALLVLRLEeLREELEELQEELKEAEEELEELTAELQELEEKLEELRlevsELEEEIeELQKELYAlaNEISRLEQQKQIL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 126 QRKMEELTVESMEVVRLTRQVETLSTQYSIQRSQWVREDEKKKKEIQDLKE-------LYEKSEHGAKNWERERETFQNQ 198
Cdd:TIGR02168 308 RERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAeleeleaELEELESRLEELEEQLETLRSK 387
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19112828 199 VSQMSKQLDSLEKLCERKDEEIRSSQAFNMTLREENDTLA-----AQNLDLQTQLDRLQRELDT 257
Cdd:TIGR02168 388 VAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLkkleeAELKELQAELEELEEELEE 451
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
50-255 |
7.94e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.38 E-value: 7.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 50 TEGQALSKNELK-LNNTIKQLKKSLSEAETKLKRLDEKQATPELQVSDSKEMEEQLELQKSQFEKRISILEKEKEDLQRK 128
Cdd:COG4942 19 ADAAAEAEAELEqLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 129 MEELTVESMEVVRLTRQVETLST----------QYSIQRSQWVRE-DEKKKKEIQDLKELYEKSEHGAKNWERERETFQN 197
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPlalllspedfLDAVRRLQYLKYlAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 19112828 198 QVSQMSKQLDSLEKLCERKDEEIRSSQAFNMTLREENDTLAAQNLDLQTQLDRLQREL 255
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
42-256 |
1.40e-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: 54.69 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 42 DEIIAKLLTE----GQALSKNELKLNNTIKQLKKSLSEAETKLKRLDEKQATPELQVSDSKEMEEQLELQKSQFEKRISI 117
Cdd:TIGR02169 169 DRKKEKALEEleevEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLAS 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 118 LEKEKEDLQRKMEELTVESMEVVRLTRQV--------------------ETLSTQYSIQRSQWVREDEKKK--KEIQDLK 175
Cdd:TIGR02169 249 LEEELEKLTEEISELEKRLEEIEQLLEELnkkikdlgeeeqlrvkekigELEAEIASLERSIAEKERELEDaeERLAKLE 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 176 ELYEKSEHGAKNWERERETFQNQVSQMSKQLDSLEKLCERKDEEIRSSQAFNMTLREENDTLAAQNLDLQTQLDRLQREL 255
Cdd:TIGR02169 329 AEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKREL 408
|
.
gi 19112828 256 D 256
Cdd:TIGR02169 409 D 409
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
45-269 |
3.89e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.02 E-value: 3.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 45 IAKLLTEGQALSKNELKLNNTIKQLKKSLSEAETKLKRLDEKQATPELQVSDSKEMEEQLELQKSQFEKRISILEKEKED 124
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 125 LQRKMEELTVESMEVVRLTRQVETLSTQYSIQRSQWVREDEKKKKEIQDLKELYEKSEHGAKNWERERETFQNQVSQMSK 204
Cdd:COG1196 349 AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE 428
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19112828 205 QLDSLEKLCERKDEEIRSSQAFNMTLREENDTLAAQNLDLQTQLDRLQRELDTNIRSNVKSKPKK 269
Cdd:COG1196 429 ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL 493
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
43-255 |
7.66e-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: 52.38 E-value: 7.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 43 EIIAKLLTEGQALSKNELKLNNTIKQLKKSLSEAETKLKRLDEKQATPELQVSDSKEMEEQLE-------LQKSQFEKRI 115
Cdd:TIGR02169 280 KIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEreieeerKRRDKLTEEY 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 116 SILEKEKEDLQRKMEELTVESMEVVRLTRQVEtlstqysiqrsqwvREDEKKKKEIQDLKELYEKSEHGAKNWERERETF 195
Cdd:TIGR02169 360 AELKEELEDLRAELEEVDKEFAETRDELKDYR--------------EKLEKLKREINELKRELDRLQEELQRLSEELADL 425
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 196 QNQVSQMSKQLDSLEKLCERKDEEIRSSQAFNMTLREENDTLAAQNLDLQTQLDRLQREL 255
Cdd:TIGR02169 426 NAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKEL 485
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
62-526 |
3.68e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.06 E-value: 3.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 62 LNNTIKQLKKSLSEAETKLKRLDEKQATPELQVSDSKEMEEQLELQKSQFEKRISILEKEKEDLQRKMEELTVESMEVVR 141
Cdd:TIGR02168 293 LANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELES 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 142 LTRQVETLSTQYSIQRSQWVREDEKKKKEIQDLKELYEKSEHGAKNWERERETFQ-----NQVSQMSKQLDSLEKLCERK 216
Cdd:TIGR02168 373 RLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLkkleeAELKELQAELEELEEELEEL 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 217 DEEIRSSQAFNMTLREENDTLAAQNLDLQTQLDRLQRELDT--NIRSNVKSKPKKIVTtggIPENNDYTVGKVDTL---- 290
Cdd:TIGR02168 453 QEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSleRLQENLEGFSEGVKA---LLKNQSGLSGILGVLseli 529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 291 KVTKEDEdpttptNAIPIPSSmSKRDEALENDKDNYFDDLHPLNISTSPQPSPLSFSEIPQSDTRNALENFLDNLPSPSE 370
Cdd:TIGR02168 530 SVDEGYE------AAIEAALG-GRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLG 602
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 371 ERSRISRSASEARKLGINAQSRYAsissAVLSPPSEASRKFSLYESEAISPTSG---TPSNLEKGAGNVPDVSLLEQ--- 444
Cdd:TIGR02168 603 VAKDLVKFDPKLRKALSYLLGGVL----VVDDLDNALELAKKLRPGYRIVTLDGdlvRPGGVITGGSAKTNSSILERrre 678
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 445 ---LATTIRRLEAELQTTKQQVAQLIIQRDQARQEIVDAyvnNDANEDSKKQVEELRLQLQNLEKEHASTLVTLKQKSDK 521
Cdd:TIGR02168 679 ieeLEEKIEELEEKIAELEKALAELRKELEELEEELEQL---RKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
....*
gi 19112828 522 VFELE 526
Cdd:TIGR02168 756 LTELE 760
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
61-257 |
6.81e-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: 49.30 E-value: 6.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 61 KLNNTIKQLKKSLSEAETKL-------KRLDEKQATPELQVSDSKEMEEQLELQKSQFEKRISILEKEKEDLQRKMEELT 133
Cdd:TIGR02169 699 RIENRLDELSQELSDASRKIgeiekeiEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLE 778
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 134 VE--------SMEVVR-LTRQVETLSTQYSIQRSQwVREDEKKKKEIQDLKELYEKSehgAKNWERERETFQNQVSQMSK 204
Cdd:TIGR02169 779 EAlndlearlSHSRIPeIQAELSKLEEEVSRIEAR-LREIEQKLNRLTLEKEYLEKE---IQELQEQRIDLKEQIKSIEK 854
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 19112828 205 QLDSLEKLCERKDEEIRSSQAFNMTLREENDTLAAQNLDLQTQLDRLQRELDT 257
Cdd:TIGR02169 855 EIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE 907
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
35-261 |
1.10e-05 |
|
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: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 35 RGNAKSKDEIIAKLLTEGQALSKNELKLNNTIKQLKKSLSEAEtklKRLDEKQATPELQVSDSKEMEEQLELQK---SQF 111
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELE---LELEEAQAEEYELLAELARLEQDIARLEerrREL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 112 EKRISILEKEKEDLQRKMEELTVE----SMEVVRLTRQVETLSTQYSIQRSQWVREDEKKKKEIQDLKELYEKsehgAKN 187
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEEleelEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE----LLE 390
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19112828 188 WERERETFQNQVSQMSKQLDSLEKLCERKDEEIRSSQAFNMTLREENDTLAAQNLDLQTQLDRLQRELDTNIRS 261
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEL 464
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
61-220 |
1.31e-05 |
|
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: 48.25 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 61 KLNNTIKQLKKSLSEAETKLKRLDEKQATPELQVSDSKEMEEQLELQKSQFEKRISILEKEKEDLQRKMEEltvESMEVV 140
Cdd:pfam01576 437 KLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEE---EEEAKR 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 141 RLTRQVETLSTQYSiqrsqwvredeKKKKEIQDLKELYEKSEHGAKNWERERETFQNQVSQMSKQLDSLEKLCERKDEEI 220
Cdd:pfam01576 514 NVERQLSTLQAQLS-----------DMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQEL 582
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
67-260 |
4.44e-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: 4.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 67 KQLKKSLS--EAETKLKRLDEKQATPELQVSDSKEMEEQLELQKSQFEKRISILEKEKEDLQRKMEELTVESMEVVRLTR 144
Cdd:COG1196 216 RELKEELKelEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 145 QVETLSTQ---YSIQRSQWVREDEKKKKEIQDLKELYEKSEHGAKNWERERETFQNQVSQMSKQLDSLEKLCERKDEEIR 221
Cdd:COG1196 296 ELARLEQDiarLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
170 180 190
....*....|....*....|....*....|....*....
gi 19112828 222 SSQAFNMTLREENDTLAAQNLDLQTQLDRLQRELDTNIR 260
Cdd:COG1196 376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
9-217 |
7.32e-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: 45.82 E-value: 7.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 9 FLKKAMSNVETSIDKVldgnqieEMSRGNAKSKDEIIAKLLTEgqaLSKNELKLNNTIKQLKKSLSEAETKLKRLDEKQA 88
Cdd:TIGR02168 306 ILRERLANLERQLEEL-------EAQLEELESKLDELAEELAE---LEEKLEELKEELESLEAELEELEAELEELESRLE 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 89 TPELQVSDSKEMEEQLELQKSQFEKRISILEKEKEDLQRKMEELTVESMEVVRLTRQVETLSTQYSIQRSQwvREDEKKK 168
Cdd:TIGR02168 376 ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELE--EELEELQ 453
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 19112828 169 KEIQDLKELYEKSEHGAKNWERERETFQNQVSQMSKQLDSLEKLCERKD 217
Cdd:TIGR02168 454 EELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLE 502
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
28-243 |
7.64e-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: 45.82 E-value: 7.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 28 NQIEEMSRGNAKSKDEIIAkLLTEGQALSKNELKLNNTIKQLKKSLSEAETKLKRLDEKQATPEL-------QVSDSKEM 100
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAE-AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRErleslerRIAATERR 839
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 101 EEQLELQKSQFEKRISILEKEKEDLQRKMEELTVE----SMEVVRLTRQVETLSTQYSIQRSQwVREDEKKKKEI-QDLK 175
Cdd:TIGR02168 840 LEDLEEQIEELSEDIESLAAEIEELEELIEELESElealLNERASLEEALALLRSELEELSEE-LRELESKRSELrRELE 918
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19112828 176 ELYEKSEHGAKNWERERETFQNQVSQMSKQ----LDSLEKLCERKDEEIRSSQAFNMTLREENDTLAAQNLD 243
Cdd:TIGR02168 919 ELREKLAQLELRLEGLEVRIDNLQERLSEEysltLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLA 990
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
62-258 |
1.27e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.01 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 62 LNNTIKQLKKSLSEAETKLKRLDEKQatpelQVSDSKEMEEQLELQKSQFEKRISILEKEKEDLQRKMEEL--------- 132
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEFRQKN-----GLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALraqlgsgpd 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 133 ----TVESMEVVRLTRQVETLSTQYSIQRSQWVREDEK---KKKEIQDLKELYEKSEhgaknwERERETFQNQVSQMSKQ 205
Cdd:COG3206 255 alpeLLQSPVIQQLRAQLAELEAELAELSARYTPNHPDviaLRAQIAALRAQLQQEA------QRILASLEAELEALQAR 328
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 19112828 206 LDSLEKLCERKDEEIRSSQAfnmtlreendtlaaqnldLQTQLDRLQRELDTN 258
Cdd:COG3206 329 EASLQAQLAQLEARLAELPE------------------LEAELRRLEREVEVA 363
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
64-255 |
1.58e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 44.43 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 64 NTIKQLKKSLSEAETKLKRLDEKQATPELQVSDSKEMEEQLELQKSQFEKRISILEKEKEDLQRKMEE----LTVESMEV 139
Cdd:pfam10174 289 NKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEkesfLNKKTKQL 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 140 VRLTRQVETLSTQYSIQRSQWVREDEK---KKKEIQDLKELYEKSEHGAKNWERERETFQNQVSQMSKQLDSLE------ 210
Cdd:pfam10174 369 QDLTEEKSTLAGEIRDLKDMLDVKERKinvLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEealsek 448
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 19112828 211 -KLCER-KDEEIRSSQAFnmtlREENDTLAAQNLDLQTQLDRLQREL 255
Cdd:pfam10174 449 eRIIERlKEQREREDRER----LEELESLKKENKDLKEKVSALQPEL 491
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
28-225 |
1.83e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 28 NQIEEMSRGNAKsKDEIIAKLLTEGQALSKNELKLNNTIKQLKKSLSEAETKLKRLDEKQATPE---------LQVSDSK 98
Cdd:COG4717 53 KEADELFKPQGR-KPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELReelekleklLQLLPLY 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 99 EMEEQLELQKSQFEKRISILEKEKEDLQRKMEELTVESMEVVRLTRQVETLSTQYSIQrsqwvredekKKKEIQDLKELY 178
Cdd:COG4717 132 QELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLA----------TEEELQDLAEEL 201
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 19112828 179 EKSEHGAKNWERERETFQNQVSQMSKQLDSLEKLCERKDEEIRSSQA 225
Cdd:COG4717 202 EELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEA 248
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
28-254 |
2.51e-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: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 28 NQIEEMSRGNAKSKDEIIAKLltegQALSKNELKLNNTIKQLKKSLSEAETKLKRLDEKQATPELQVSDSKEMEEQLELQ 107
Cdd:TIGR02169 801 SKLEEEVSRIEARLREIEQKL----NRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAA 876
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 108 KSQFEKRISILEKEKEDLQRKMEEltvesmevvrLTRQVETLSTQYsiqrsqwvredEKKKKEIQDLKELYEKSEHGAKN 187
Cdd:TIGR02169 877 LRDLESRLGDLKKERDELEAQLRE----------LERKIEELEAQI-----------EKKRKRLSELKAKLEALEEELSE 935
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19112828 188 WERERETFQnQVSQMSKQLDSLEKLCERKDEEIRSSQAFNMTLREENDTLAAQNLDLQTQLDRLQRE 254
Cdd:TIGR02169 936 IEDPKGEDE-EIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEE 1001
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
442-546 |
6.21e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 6.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 442 LEQLATTIRRLEAELQTTKQQVAQLIIQRDQARQEIVDAYvnNDANEDSKKQVEELRLQLQNLEKEHASTLVTLKQKSDK 521
Cdd:COG4913 290 LELLEAELEELRAELARLEAELERLEARLDALREELDELE--AQIRGNGGDRLEQLEREIERLERELEERERRRARLEAL 367
|
90 100
....*....|....*....|....*
gi 19112828 522 VFELELDIKDMRELYVSQIDILAGR 546
Cdd:COG4913 368 LAALGLPLPASAEEFAALRAEAAAL 392
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
44-510 |
6.39e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 6.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 44 IIAKLLTEGQALSK----NELKLNNTIKQLKKSLSEAETKLKRLDEKQAtpelQVSDSKEMEEQLELQKSQFEKRISILE 119
Cdd:COG4717 47 LLERLEKEADELFKpqgrKPELNLKELKELEEELKEAEEKEEEYAELQE----ELEELEEELEELEAELEELREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 120 KEKEdLQRKMEELTVESMEVVRLTRQVETLSTQYSiQRSQWVREDEKKKKEIQDLK-ELYEKsehgaknWERERETFQNQ 198
Cdd:COG4717 123 KLLQ-LLPLYQELEALEAELAELPERLEELEERLE-ELRELEEELEELEAELAELQeELEEL-------LEQLSLATEEE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 199 VSQMSKQLDSLEKLCERKDEEIRSSQAFNMTLREENDTLAAQNLDLQTQLDRLQRELDTNIRSNVKSkpkkIVTTGGIPE 278
Cdd:COG4717 194 LQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLA----LLGLGGSLL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 279 NNDYTVGKVDTLKVTKededpttptnAIPIPSSMSKRDEALENDKDNYFDDLHPLNISTSPQPSPLSFSEIPQSDTRNAL 358
Cdd:COG4717 270 SLILTIAGVLFLVLGL----------LALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEEL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 359 ENFLDNLPSPSEERSRISRSASEARKLGINAQsRYASISSAVLSPPSEASRKFSLYE-----SEAISPTSGTPSNLEKGA 433
Cdd:COG4717 340 LELLDRIEELQELLREAEELEEELQLEELEQE-IAALLAEAGVEDEEELRAALEQAEeyqelKEELEELEEQLEELLGEL 418
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19112828 434 GNVPDVSLLEQLATTIRRLEAELQTTKQQVAQLIIQRDQARQEIvDAYVNNDANEDSKKQVEELRLQLQNLEKEHAS 510
Cdd:COG4717 419 EELLEALDEEELEEELEELEEELEELEEELEELREELAELEAEL-EQLEEDGELAELLQELEELKAELRELAEEWAA 494
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
29-273 |
1.05e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.93 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 29 QIEEMSRGNAKSKDEIiaKLLTEGQALSKNELK-LNNTIKQLKKSLSEAETKLKRLDEKQATPELQVSDSKEMEEQLELQ 107
Cdd:TIGR04523 427 EIERLKETIIKNNSEI--KDLTNQDSVKELIIKnLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEE 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 108 KSQFEKRISILEKEKEDLQRKMEELTVESMEVVRLTRQVET--LSTQYSIQRSQWVREDEKKKKEIQDLKELYEKSEHGA 185
Cdd:TIGR04523 505 KKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDelNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQ 584
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 186 KNWERERETFQNQVSQMSKQLDSLEKLCERKDEEIRSSQAFNMTLREENDTLAAQNLDLQTQLDRLQRELDT--NIRSNV 263
Cdd:TIGR04523 585 EEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEirNKWPEI 664
|
250
....*....|
gi 19112828 264 KSKPKKIVTT 273
Cdd:TIGR04523 665 IKKIKESKTK 674
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
110-206 |
1.06e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.99 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 110 QFEKRISILEKEKEDLQRKMEELTVESMEvvRLTRQVETLSTQYSIQRSQWVREDEkKKKEIQDLKELYEKSEHGAKNWE 189
Cdd:COG0542 415 ELERRLEQLEIEKEALKKEQDEASFERLA--ELRDELAELEEELEALKARWEAEKE-LIEEIQELKEELEQRYGKIPELE 491
|
90
....*....|....*..
gi 19112828 190 RERETFQNQVSQMSKQL 206
Cdd:COG0542 492 KELAELEEELAELAPLL 508
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
61-218 |
1.28e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 61 KLNNTIKQLKKSLSEAETKLKRLDEkqatpelqvsdSKEMEEQLELQKSQFEKRISILEKEKEDLQRKMEELTVESMEVV 140
Cdd:PRK03918 211 EISSELPELREELEKLEKEVKELEE-----------LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELE 279
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19112828 141 RLTRQVETLstqysiqrsqwvredEKKKKEIQDLKELYEKSEHGAKNWERERETFQNQVSQMSKQLDSLEKLCERKDE 218
Cdd:PRK03918 280 EKVKELKEL---------------KEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEE 342
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
73-261 |
1.36e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.46 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 73 LSEAETKLKRLdEKQATpelQVSDSKEMEEQL-ELQKSQFEKRISILEKEKEDLQRKMEELTVESMEVVRLTRQVETLST 151
Cdd:COG1196 195 LGELERQLEPL-ERQAE---KAERYRELKEELkELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 152 QYSIQRSQWVREDEKKKKEIQDLKELYEKSEHGAKNWERERETFQNQVSQMSKQLDSLEKLCERKDEEIRSSQAFNMTLR 231
Cdd:COG1196 271 ELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE 350
|
170 180 190
....*....|....*....|....*....|
gi 19112828 232 EENDTLAAQNLDLQTQLDRLQRELDTNIRS 261
Cdd:COG1196 351 EELEEAEAELAEAEEALLEAEAELAEAEEE 380
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
10-257 |
1.45e-03 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 41.28 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 10 LKKAMSNVETSIDKVLDGNQIEEMSRGNAKSKDEIIAKLLTEGQALSKNELKLNNTikQLKKSLSEAETKLKRLDEKQAt 89
Cdd:pfam09731 228 LDNVEEKVEKAQSLAKLVDQYKELVASERIVFQQELVSIFPDIIPVLKEDNLLSND--DLNSLIAHAHREIDQLSKKLA- 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 90 pELQVSDSKEMEEQLELQKSQFEK------------RISILEKEKEDLQRKMEELTVESMEVVRLTRQVETLSTQYSIQR 157
Cdd:pfam09731 305 -ELKKREEKHIERALEKQKEELDKlaeelsarleevRAADEAQLRLEFEREREEIRESYEEKLRTELERQAEAHEEHLKD 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 158 SQWVREDEKKKKEIQDLKELYEKsehgaknwerERETFQNQVSQMSKQLDSLEKLCE-RKDEEI--RSSQAFNMTLREEN 234
Cdd:pfam09731 384 VLVEQEIELQREFLQDIKEKVEE----------ERAGRLLKLNELLANLKGLEKATSsHSEVEDenRKAQQLWLAVEALR 453
|
250 260
....*....|....*....|...
gi 19112828 235 DTLAAQNLDLQTQLdrLQRELDT 257
Cdd:pfam09731 454 STLEDGSADSRPRP--LVRELKA 474
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
66-254 |
1.68e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 66 IKQLKKSLSEAETKLKRLDEKQATPELQVSDSKEMEEQLELQKSQFEKRISI--LEKEKEDLQRKMEELTVESMEVVRLT 143
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVasAEREIAELEAELERLDASSDDLAALE 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 144 RQVEtlstqysiqrsQWVREDEKKKKEIQDLKELYEKSEHGAKNWERERETFQNQVSQMSK--QLDSLEKLCERKDEEIR 221
Cdd:COG4913 692 EQLE-----------ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDlaRLELRALLEERFAAALG 760
|
170 180 190
....*....|....*....|....*....|....*
gi 19112828 222 SSQAFNM--TLREENDTLAAQNLDLQTQLDRLQRE 254
Cdd:COG4913 761 DAVERELreNLEERIDALRARLNRAEEELERAMRA 795
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
45-176 |
1.83e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.29 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 45 IAKLLTEGQALSKNELKLNNTIKQLKKSLSEAETKLKRLDEKQATPELQ---VSDSKEMeEQLELQKSQFEKRISILEKE 121
Cdd:COG1579 33 LAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnVRNNKEY-EALQKEIESLKRRISDLEDE 111
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 19112828 122 KEDLQRKMEELTVesmEVVRLTRQVETLSTQYSIQRSQWVREDEKKKKEIQDLKE 176
Cdd:COG1579 112 ILELMERIEELEE---ELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
69-184 |
1.96e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.07 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 69 LKKSLSEAETKLKRLDEKqatpELQVSDSKEMEEQLelqkSQFEKRISILEKEKEDLQRKMEELTVE------------S 136
Cdd:PRK05771 186 LKELSDEVEEELKKLGFE----RLELEEEGTPSELI----REIKEELEEIEKERESLLEELKELAKKyleellalyeylE 257
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 19112828 137 MEVVRLTRQVETLSTQYSIQRSQWVREDEKKKkeiqdLKELYEKSEHG 184
Cdd:PRK05771 258 IELERAEALSKFLKTDKTFAIEGWVPEDRVKK-----LKELIDKATGG 300
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
66-222 |
2.18e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 66 IKQLKKSLSEAETKLKRLDEKQATPELQVSDSKEMEEQLELQKSQFE-KRISILEKEKEDLQRKMEELtveSMEVVRLTR 144
Cdd:COG4913 290 LELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEER---ERRRARLEA 366
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19112828 145 QVETLstqysiqrsqwvreDEKKKKEIQDLKELYEKSEHGAKNWERERETFQNQVSQMSKQLDSLEKLCERKDEEIRS 222
Cdd:COG4913 367 LLAAL--------------GLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
55-180 |
2.75e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.58 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 55 LSKNELKLNNTIKQLKKSLSEAETKLKRLDEK-QATPELQvsdsKEMEEQLELQKSQFEKRISILEKEkedLQRKMEELT 133
Cdd:PRK00409 511 IGEDKEKLNELIASLEELERELEQKAEEAEALlKEAEKLK----EELEEKKEKLQEEEDKLLEEAEKE---AQQAIKEAK 583
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 19112828 134 VESMEVVRLTRQVETLstQYSIQRSQwvrEDEKKKKEIQDLKELYEK 180
Cdd:PRK00409 584 KEADEIIKELRQLQKG--GYASVKAH---ELIEARKRLNKANEKKEK 625
|
|
| DUF3450 |
pfam11932 |
Protein of unknown function (DUF3450); This family of proteins are functionally ... |
61-177 |
2.96e-03 |
|
Protein of unknown function (DUF3450); This family of proteins are functionally uncharacterized. This protein is found in bacteria and eukaryotes. Proteins in this family are about 260 amino acids in length.
Pssm-ID: 432198 [Multi-domain] Cd Length: 238 Bit Score: 39.52 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 61 KLNNTIKQLKKSLSEAETKLKRLDEKQATPELQVSDSKEMEEQLELQKSQFEKRISILEKEKEDLQRKMEELTVESMEVV 140
Cdd:pfam11932 17 QALDLAEKAVAAAAQSQKKIDKWDDEKQELLAEYRALKAELESLEVYNRQLERLVASQEQEIASLERQIEEIERTERELV 96
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 19112828 141 -RLTRQVETLstqysiqrSQWVRED-----EKKKKEIQDLKEL 177
Cdd:pfam11932 97 pLMLKMLDRL--------EQFVALDlpfllEERQARLARLREL 131
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
42-143 |
3.74e-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: 39.75 E-value: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 42 DEIIAKLLTEGQALSKNELKLNNTIKQLKKSLSEAETKLKRLDEKQATPELQVSDSKEMEEQLELQKSQFEKRISILEKE 121
Cdd:COG4942 142 KYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQE 221
|
90 100
....*....|....*....|..
gi 19112828 122 KEDLQRKMEELTVESMEVVRLT 143
Cdd:COG4942 222 AEELEALIARLEAEAAAAAERT 243
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
57-270 |
6.92e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.28 E-value: 6.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 57 KNELKLNNtIKQLKKSLSEAETKLKRLDEKQATPELQVSDSKEMEEqLELQKSQFEKRISILEKEKEDLQRKMEELTVES 136
Cdd:PRK03918 509 EEKLKKYN-LEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEE-LKKKLAELEKKLDELEEELAELLKELEELGFES 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 137 MEVVRLT-RQVETLSTQYsIQRSQWVREDEKKKKEIQDLKELYEKSEHGAKNWERERETFQNQVSQMSKQLDslEKLCER 215
Cdd:PRK03918 587 VEELEERlKELEPFYNEY-LELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYS--EEEYEE 663
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 19112828 216 KDEEIRSSQAFNMTLREENDTLAAQNLDLQTQLDRLQRELDTniRSNVKSKPKKI 270
Cdd:PRK03918 664 LREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEE--REKAKKELEKL 716
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
19-132 |
7.17e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 39.07 E-value: 7.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 19 TSIDKVLDGnQIEEMSRGNAKSKDEIIAKLLTEGQALSKNELKLNNTIKQLKKSLSEAETKLKRLDEKQATPELQVSDSK 98
Cdd:COG2433 376 LSIEEALEE-LIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEAR 454
|
90 100 110
....*....|....*....|....*....|....*...
gi 19112828 99 EmEEQLELQK----SQFEKRISILEKEKEDLQRKMEEL 132
Cdd:COG2433 455 S-EERREIRKdreiSRLDREIERLERELEEERERIEEL 491
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
53-153 |
8.75e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 38.84 E-value: 8.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112828 53 QALSKNELKLNNTIKQLKKSLSEAETKLKRLDEKQATPELQVSD-SKEMEEQLELQKSQFEKRISILEKEKEDLQRKMEE 131
Cdd:COG3206 266 QQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQeAQRILASLEAELEALQAREASLQAQLAQLEARLAE 345
|
90 100
....*....|....*....|..
gi 19112828 132 LTVESMEVVRLTRQVETLSTQY 153
Cdd:COG3206 346 LPELEAELRRLEREVEVARELY 367
|
|
|