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Conserved domains on  [gi|19112828|ref|NP_596036|]
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TATA element modulatory factor-like protein [Schizosaccharomyces pombe]

Protein Classification

Graphical summary

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List of domain hits

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 super family cl37069
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]


The actual alignment was detected with superfamily member TIGR02168:

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
 
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
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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