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Conserved domains on  [gi|1034560209|ref|XP_016857295|]
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CTTNBP2 N-terminal-like protein isoform X1 [Homo sapiens]

Protein Classification

CortBP2 and SMC_prok_B domain-containing protein( domain architecture ID 12101109)

protein containing domains CortBP2, SMC_prok_B, and PHA03247

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CortBP2 pfam09727
Cortactin-binding protein-2; This entry is the first approximately 250 residues of ...
 5-188 2.70e-79

Cortactin-binding protein-2; This entry is the first approximately 250 residues of cortactin-binding protein 2. In addition to being a positional candidate for autism this protein is expressed at highest levels in the brain in humans. The human protein has six associated ankyrin repeat domains pfam00023 towards the C-terminus which act as protein-protein interaction domains.


:

Pssm-ID: 462860 [Multi-domain]  Cd Length: 187  Bit Score: 249.44  E-value: 2.70e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209   5 KLSKPELLTLFSILEGELEARDLVIEALKAQH-RDTFIEERYGKYNISDPLMALQRDFETLKEKNDGEKQP--VCTNPLS 81
Cdd:pfam09727   1 DLSKDDLLKLLSILEGELQARDIVIAVLKAEKvKQLLLEARYGFKYPSDPLLALQRDSELLRDQSQDEDVYeaMYEKPLA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  82 ILKVVMKQCKNMQERMLSQLAAAESRHRKVILDLEEERQRHAQDTAEGDDVTYMLEKERERLTQQLEFEKSQVKKFEKEQ 161
Cdd:pfam09727  81 ELEKLVEKQRETQRRMLEQLAAAEKRHRRVIRELEEEKRKHARDTAQGDDFTYLLEKERERLKQELEQEKAQQKRLEKEL 160

                         170       180
                  ....*....|....*....|....*..
gi 1034560209 162 KKLSSQLEEERSRHKQLSSMLVLECKK 188
Cdd:pfam09727 161 KKLLEKLEEELSKQKQIALLLVKERKR 187
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 100-283 1.45e-09

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 61.23  E-value: 1.45e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  100 QLAAAESRHRKVILDLEEERQRHAQDTAEGDDVTYMLEKERERLTQQLEFEKSQVKKFEKEQKKLSSQLEEERSRHKQLS 179
Cdd:TIGR02168  744 QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLR 823

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  180 SmlvlECKKATNKAAEEGQKAGELSLKLEKEKSRVSKLEEELAAERkrglQTEAQVEKQLSEFDIEREQLRAKLNREENR 259
Cdd:TIGR02168  824 E----RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELE----ELIEELESELEALLNERASLEEALALLRSE 895

                          170       180
                   ....*....|....*....|....
gi 1034560209  260 TKTLKEEMESLKKIVKDLEASHQH 283
Cdd:TIGR02168  896 LEELSEELRELESKRSELRRELEE 919
 
Name Accession Description Interval E-value
CortBP2 pfam09727
Cortactin-binding protein-2; This entry is the first approximately 250 residues of ...
 5-188 2.70e-79

Cortactin-binding protein-2; This entry is the first approximately 250 residues of cortactin-binding protein 2. In addition to being a positional candidate for autism this protein is expressed at highest levels in the brain in humans. The human protein has six associated ankyrin repeat domains pfam00023 towards the C-terminus which act as protein-protein interaction domains.


Pssm-ID: 462860 [Multi-domain]  Cd Length: 187  Bit Score: 249.44  E-value: 2.70e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209   5 KLSKPELLTLFSILEGELEARDLVIEALKAQH-RDTFIEERYGKYNISDPLMALQRDFETLKEKNDGEKQP--VCTNPLS 81
Cdd:pfam09727   1 DLSKDDLLKLLSILEGELQARDIVIAVLKAEKvKQLLLEARYGFKYPSDPLLALQRDSELLRDQSQDEDVYeaMYEKPLA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  82 ILKVVMKQCKNMQERMLSQLAAAESRHRKVILDLEEERQRHAQDTAEGDDVTYMLEKERERLTQQLEFEKSQVKKFEKEQ 161
Cdd:pfam09727  81 ELEKLVEKQRETQRRMLEQLAAAEKRHRRVIRELEEEKRKHARDTAQGDDFTYLLEKERERLKQELEQEKAQQKRLEKEL 160

                         170       180
                  ....*....|....*....|....*..
gi 1034560209 162 KKLSSQLEEERSRHKQLSSMLVLECKK 188
Cdd:pfam09727 161 KKLLEKLEEELSKQKQIALLLVKERKR 187
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 94-279 7.74e-11

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 65.34  E-value: 7.74e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  94 QERMLSQLAAAESRhrkvildLEEERQRHAQDTAEGDDVT---YMLEKERERLTQQLEFEKSQVKKFEKEQKKLSSQLEE 170
Cdd:COG1196   255 LEELEAELAELEAE-------LEELRLELEELELELEEAQaeeYELLAELARLEQDIARLEERRRELEERLEELEEELAE 327

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209 171 ERSRHKQLSSMLVLECKKATNKAAEEGQKAGELSlKLEKEKSRVSKLEEELAAERKRGLQTEAQVEKQLSEFDIEREQLR 250
Cdd:COG1196   328 LEEELEELEEELEELEEELEEAEEELEEAEAELA-EAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE 406

                         170       180
                  ....*....|....*....|....*....
gi 1034560209 251 AKLNREENRTKTLKEEMESLKKIVKDLEA 279
Cdd:COG1196   407 EAEEALLERLERLEEELEELEEALAELEE 435
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 100-283 1.45e-09

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 61.23  E-value: 1.45e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  100 QLAAAESRHRKVILDLEEERQRHAQDTAEGDDVTYMLEKERERLTQQLEFEKSQVKKFEKEQKKLSSQLEEERSRHKQLS 179
Cdd:TIGR02168  744 QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLR 823

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  180 SmlvlECKKATNKAAEEGQKAGELSLKLEKEKSRVSKLEEELAAERkrglQTEAQVEKQLSEFDIEREQLRAKLNREENR 259
Cdd:TIGR02168  824 E----RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELE----ELIEELESELEALLNERASLEEALALLRSE 895

                          170       180
                   ....*....|....*....|....
gi 1034560209  260 TKTLKEEMESLKKIVKDLEASHQH 283
Cdd:TIGR02168  896 LEELSEELRELESKRSELRRELEE 919
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
94-292 2.26e-09

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 60.55  E-value: 2.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  94 QERMLSQLAAAESRHRKVILDLEEERQRHAQdtaegddvtymLEKERERLTQQLEFEKSQVKKFE--KEQKKLSSQLEEE 171
Cdd:COG4717    76 LEEELKEAEEKEEEYAELQEELEELEEELEE-----------LEAELEELREELEKLEKLLQLLPlyQELEALEAELAEL 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209 172 RSRHKQLSsmlvleckkatnkaaEEGQKAGELSLKLEKEKSRVSKLEEELAAERKrglQTEAQVEKQLSEFDIEREQLRA 251
Cdd:COG4717   145 PERLEELE---------------ERLEELRELEEELEELEAELAELQEELEELLE---QLSLATEEELQDLAEELEELQQ 206

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1034560209 252 KLNREENRTKTLKEEMESLKKIVKDLEASHQHSSPNEQLKK 292
Cdd:COG4717   207 RLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKE 247
PTZ00121 PTZ00121
MAEBL; Provisional
 91-294 8.47e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 59.00  E-value: 8.47e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209   91 KNMQERMLSQLAAAE-SRHRKVILDLEEERQRHAQDTAEGDDVTymLEKERERLTQQLEFEKSQVKKFEKEQKKLSSQL- 168
Cdd:PTZ00121  1576 KNMALRKAEEAKKAEeARIEEVMKLYEEEKKMKAEEAKKAEEAK--IKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELk 1653

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  169 ---EEERSRHKQLSSMLVLECKKA--TNKAAEEGQKAGELSLKLEKEKSRVSKLEEELAAERKRGlqteAQVEKQLSEFD 243
Cdd:PTZ00121  1654 kaeEENKIKAAEEAKKAEEDKKKAeeAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKA----EELKKAEEENK 1729

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034560209  244 IEREQLRAKLNREENRTKTLKEEMESLKKIVKDLEASHQHSSPNEQLKKPV 294
Cdd:PTZ00121  1730 IKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAV 1780
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 50-279 5.71e-08

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 56.23  E-value: 5.71e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209   50 ISDPLMALQRDFETLKEKNDGEKQPVctnplSILKVVMKQCKNMQERMLSQLAAAESRHRKV---ILDLEEERQRHAQDT 126
Cdd:TIGR02169  679 LRERLEGLKRELSSLQSELRRIENRL-----DELSQELSDASRKIGEIEKEIEQLEQEEEKLkerLEELEEDLSSLEQEI 753

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  127 AEGDDVTYMLEKERERLTQQLEFEKSQVKKFE--------KEQKKLSSQLEEERSR-HKQLSSMLVLECKKATNKAAEEG 197
Cdd:TIGR02169  754 ENVKSELKELEARIEELEEDLHKLEEALNDLEarlshsriPEIQAELSKLEEEVSRiEARLREIEQKLNRLTLEKEYLEK 833

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  198 QKAGELSLKLE---KEKSRVSKLE------EELAAERKRGLQTEAQVEKQLSEFDIEREQLRAKLNREENRTKTLKEEME 268
Cdd:TIGR02169  834 EIQELQEQRIDlkeQIKSIEKEIEnlngkkEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIE 913

                          250
                   ....*....|.
gi 1034560209  269 SLKKIVKDLEA 279
Cdd:TIGR02169  914 KKRKRLSELKA 924
PTZ00121 PTZ00121
MAEBL; Provisional
 52-273 4.00e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.14  E-value: 4.00e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209   52 DPLMALQRDfETLKEKNDGEKQPVCTNPLSILKVVMKQCKNMQERML--SQLAAAESRHRKV--ILDLEEERQRHAQDTA 127
Cdd:PTZ00121  1575 DKNMALRKA-EEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIkaEELKKAEEEKKKVeqLKKKEAEEKKKAEELK 1653

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  128 EGDDVTYMLEKERERLTQQLEFEKSQVKKFEKEQKKLSSQL---EEERSRHKQLSSMLVLECKKA--TNKAAEEGQ-KAG 201
Cdd:PTZ00121  1654 KAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALkkeAEEAKKAEELKKKEAEEKKKAeeLKKAEEENKiKAE 1733

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034560209  202 ELSLKLEKEKSRVSKLEEElAAERKRGLQTEAQVEKQLSEFDIEREQLRaklnREENRTKTLKEEMESLKKI 273
Cdd:PTZ00121  1734 EAKKEAEEDKKKAEEAKKD-EEEKKKIAHLKKEEEKKAEEIRKEKEAVI----EEELDEEDEKRRMEVDKKI 1800
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 136-292 5.34e-05

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 46.04  E-value: 5.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209 136 LEKERERLTQQLEFEKSQVKK----FEKEQKKLSSQ---LEEERSRHKQLSSMLVLECKKATNKAAEEGQKAGELSLKLE 208
Cdd:pfam07888  46 LLQAQEAANRQREKEKERYKRdreqWERQRRELESRvaeLKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRA 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209 209 KEKSRVSKLEEELAAERKRGLQTEAQVEK----------QLSEFDIEREQLRAKLNREENRTKTLKEEMESLK------- 271
Cdd:pfam07888 126 AHEARIRELEEDIKTLTQRVLERETELERmkerakkagaQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRnslaqrd 205

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1034560209 272 -----------KIVKDLEASHQHSSPNEQLKK 292
Cdd:pfam07888 206 tqvlqlqdtitTLTQKLTTAHRKEAENEALLE 237
bHLH_TS_OLIG1 cd18942
basic helix-loop-helix (bHLH) domain found in oligodendrocyte transcription factor 1 (Oligo1) ...
 245-296 4.22e-03

basic helix-loop-helix (bHLH) domain found in oligodendrocyte transcription factor 1 (Oligo1) and similar proteins; Oligo1, also termed Class B basic helix-loop-helix protein 6 (bHLHb6), or Class E basic helix-loop-helix protein 21 (bHLHe21), is a bHLH transcription factor that promotes formation and maturation of oligodendrocytes, especially within the brain.


Pssm-ID: 381512  Cd Length: 75  Bit Score: 36.52  E-value: 4.22e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1034560209 245 EREQLRAKLN-REENRTKTLKEEMESLKKIVKDLEASHQHSSPNEQLKKPVTV 296
Cdd:cd18942     2 EQQQLRRKINsRERKRMQDLNLAMDALREVILPYSAAHCQSSPGRKLSKIATL 54
 
Name Accession Description Interval E-value
CortBP2 pfam09727
Cortactin-binding protein-2; This entry is the first approximately 250 residues of ...
 5-188 2.70e-79

Cortactin-binding protein-2; This entry is the first approximately 250 residues of cortactin-binding protein 2. In addition to being a positional candidate for autism this protein is expressed at highest levels in the brain in humans. The human protein has six associated ankyrin repeat domains pfam00023 towards the C-terminus which act as protein-protein interaction domains.


Pssm-ID: 462860 [Multi-domain]  Cd Length: 187  Bit Score: 249.44  E-value: 2.70e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209   5 KLSKPELLTLFSILEGELEARDLVIEALKAQH-RDTFIEERYGKYNISDPLMALQRDFETLKEKNDGEKQP--VCTNPLS 81
Cdd:pfam09727   1 DLSKDDLLKLLSILEGELQARDIVIAVLKAEKvKQLLLEARYGFKYPSDPLLALQRDSELLRDQSQDEDVYeaMYEKPLA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  82 ILKVVMKQCKNMQERMLSQLAAAESRHRKVILDLEEERQRHAQDTAEGDDVTYMLEKERERLTQQLEFEKSQVKKFEKEQ 161
Cdd:pfam09727  81 ELEKLVEKQRETQRRMLEQLAAAEKRHRRVIRELEEEKRKHARDTAQGDDFTYLLEKERERLKQELEQEKAQQKRLEKEL 160

                         170       180
                  ....*....|....*....|....*..
gi 1034560209 162 KKLSSQLEEERSRHKQLSSMLVLECKK 188
Cdd:pfam09727 161 KKLLEKLEEELSKQKQIALLLVKERKR 187
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 94-279 7.74e-11

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 65.34  E-value: 7.74e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  94 QERMLSQLAAAESRhrkvildLEEERQRHAQDTAEGDDVT---YMLEKERERLTQQLEFEKSQVKKFEKEQKKLSSQLEE 170
Cdd:COG1196   255 LEELEAELAELEAE-------LEELRLELEELELELEEAQaeeYELLAELARLEQDIARLEERRRELEERLEELEEELAE 327

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209 171 ERSRHKQLSSMLVLECKKATNKAAEEGQKAGELSlKLEKEKSRVSKLEEELAAERKRGLQTEAQVEKQLSEFDIEREQLR 250
Cdd:COG1196   328 LEEELEELEEELEELEEELEEAEEELEEAEAELA-EAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE 406

                         170       180
                  ....*....|....*....|....*....
gi 1034560209 251 AKLNREENRTKTLKEEMESLKKIVKDLEA 279
Cdd:COG1196   407 EAEEALLERLERLEEELEELEEALAELEE 435
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 100-283 1.45e-09

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 61.23  E-value: 1.45e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  100 QLAAAESRHRKVILDLEEERQRHAQDTAEGDDVTYMLEKERERLTQQLEFEKSQVKKFEKEQKKLSSQLEEERSRHKQLS 179
Cdd:TIGR02168  744 QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLR 823

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  180 SmlvlECKKATNKAAEEGQKAGELSLKLEKEKSRVSKLEEELAAERkrglQTEAQVEKQLSEFDIEREQLRAKLNREENR 259
Cdd:TIGR02168  824 E----RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELE----ELIEELESELEALLNERASLEEALALLRSE 895

                          170       180
                   ....*....|....*....|....
gi 1034560209  260 TKTLKEEMESLKKIVKDLEASHQH 283
Cdd:TIGR02168  896 LEELSEELRELESKRSELRRELEE 919
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
94-292 2.26e-09

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 60.55  E-value: 2.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  94 QERMLSQLAAAESRHRKVILDLEEERQRHAQdtaegddvtymLEKERERLTQQLEFEKSQVKKFE--KEQKKLSSQLEEE 171
Cdd:COG4717    76 LEEELKEAEEKEEEYAELQEELEELEEELEE-----------LEAELEELREELEKLEKLLQLLPlyQELEALEAELAEL 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209 172 RSRHKQLSsmlvleckkatnkaaEEGQKAGELSLKLEKEKSRVSKLEEELAAERKrglQTEAQVEKQLSEFDIEREQLRA 251
Cdd:COG4717   145 PERLEELE---------------ERLEELRELEEELEELEAELAELQEELEELLE---QLSLATEEELQDLAEELEELQQ 206

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1034560209 252 KLNREENRTKTLKEEMESLKKIVKDLEASHQHSSPNEQLKK 292
Cdd:COG4717   207 RLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKE 247
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 98-282 2.60e-09

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 60.34  E-value: 2.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  98 LSQLAAAESRHRKVILDLEEERQRHAQDTAEGDDVTYMLEKERERLTQQLEFEKSQVKKFEKEQKKLSSQLEEERSRHKQ 177
Cdd:COG1196   283 LEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209 178 LSSMLVLECKKATNKAAEEGQKAGELS------LKLEKEKSRVSKLEEELAAERKRGLQTEAQVEKQLSEFDIEREQLRA 251
Cdd:COG1196   363 AEEALLEAEAELAEAEEELEELAEELLealraaAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE 442

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1034560209 252 KLNREENRTKTLKEEMESLKKIVKDLEASHQ 282
Cdd:COG1196   443 ALEEAAEEEAELEEEEEALLELLAELLEEAA 473
PTZ00121 PTZ00121
MAEBL; Provisional
 91-294 8.47e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 59.00  E-value: 8.47e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209   91 KNMQERMLSQLAAAE-SRHRKVILDLEEERQRHAQDTAEGDDVTymLEKERERLTQQLEFEKSQVKKFEKEQKKLSSQL- 168
Cdd:PTZ00121  1576 KNMALRKAEEAKKAEeARIEEVMKLYEEEKKMKAEEAKKAEEAK--IKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELk 1653

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  169 ---EEERSRHKQLSSMLVLECKKA--TNKAAEEGQKAGELSLKLEKEKSRVSKLEEELAAERKRGlqteAQVEKQLSEFD 243
Cdd:PTZ00121  1654 kaeEENKIKAAEEAKKAEEDKKKAeeAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKA----EELKKAEEENK 1729

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034560209  244 IEREQLRAKLNREENRTKTLKEEMESLKKIVKDLEASHQHSSPNEQLKKPV 294
Cdd:PTZ00121  1730 IKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAV 1780
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 96-280 1.99e-08

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: 55.32  E-value: 1.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  96 RMLSQLAAAESRhrkvILDLEEERQRHAQDTAEgddvtymLEKERERLTQQLEFEKSQVKKFEKEQKKLSSQLEEERSRH 175
Cdd:COG1579     7 RALLDLQELDSE----LDRLEHRLKELPAELAE-------LEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARI 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209 176 KQLSSMLvleckkATNKAAEEgQKAgeLSLKLEKEKSRVSKLEEEL--AAERKRGLQTE-AQVEKQLSEfdiEREQLRAK 252
Cdd:COG1579    76 KKYEEQL------GNVRNNKE-YEA--LQKEIESLKRRISDLEDEIleLMERIEELEEElAELEAELAE---LEAELEEK 143

                         170       180
                  ....*....|....*....|....*...
gi 1034560209 253 LNREENRTKTLKEEMESLKKIVKDLEAS 280
Cdd:COG1579   144 KAELDEELAELEAELEELEAEREELAAK 171
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 95-282 2.35e-08

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 57.25  E-value: 2.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  95 ERMLSQLAAAESRHRKVILDLEEERQRHAQDTAEGddvtymLEKERERLTQQLEFEKSQVKKFEKEQKKLSSQLEEERSR 174
Cdd:COG1196   223 KELEAELLLLKLRELEAELEELEAELEELEAELEE------LEAELAELEAELEELRLELEELELELEEAQAEEYELLAE 296

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209 175 HKQLSSMLVLECKKATNKAAEEGQKAGELSL---KLEKEKSRVSKLEEELA---AERKRGLQTEAQVEKQLSEFDIEREQ 248
Cdd:COG1196   297 LARLEQDIARLEERRRELEERLEELEEELAEleeELEELEEELEELEEELEeaeEELEEAEAELAEAEEALLEAEAELAE 376

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1034560209 249 LRAKLNREENRTKTLKEEMESLKKIVKDLEASHQ 282
Cdd:COG1196   377 AEEELEELAEELLEALRAAAELAAQLEELEEAEE 410
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 109-280 2.56e-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: 57.37  E-value: 2.56e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  109 RKVILDLEEERQRHAQDTAEGDDVTYMLEKERERLTQQLEfeksQVKKFEKEQKKLSSQLEEERSRHKQlssmlvlECKK 188
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELE----QLRKELEELSRQISALRKDLARLEA-------EVEQ 744

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  189 ATNKAAEEGQKAGELSLKLEKEKSRVSKLEEELAAERKRGLQTEAQVEKQLSEFDIEREQLRAkLNREENRTK----TLK 264
Cdd:TIGR02168  745 LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDE-LRAELTLLNeeaaNLR 823

                          170
                   ....*....|....*.
gi 1034560209  265 EEMESLKKIVKDLEAS 280
Cdd:TIGR02168  824 ERLESLERRIAATERR 839
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 50-279 5.71e-08

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 56.23  E-value: 5.71e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209   50 ISDPLMALQRDFETLKEKNDGEKQPVctnplSILKVVMKQCKNMQERMLSQLAAAESRHRKV---ILDLEEERQRHAQDT 126
Cdd:TIGR02169  679 LRERLEGLKRELSSLQSELRRIENRL-----DELSQELSDASRKIGEIEKEIEQLEQEEEKLkerLEELEEDLSSLEQEI 753

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  127 AEGDDVTYMLEKERERLTQQLEFEKSQVKKFE--------KEQKKLSSQLEEERSR-HKQLSSMLVLECKKATNKAAEEG 197
Cdd:TIGR02169  754 ENVKSELKELEARIEELEEDLHKLEEALNDLEarlshsriPEIQAELSKLEEEVSRiEARLREIEQKLNRLTLEKEYLEK 833

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  198 QKAGELSLKLE---KEKSRVSKLE------EELAAERKRGLQTEAQVEKQLSEFDIEREQLRAKLNREENRTKTLKEEME 268
Cdd:TIGR02169  834 EIQELQEQRIDlkeQIKSIEKEIEnlngkkEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIE 913

                          250
                   ....*....|.
gi 1034560209  269 SLKKIVKDLEA 279
Cdd:TIGR02169  914 KKRKRLSELKA 924
PTZ00121 PTZ00121
MAEBL; Provisional
 103-303 1.27e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 55.15  E-value: 1.27e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  103 AAESRHRKVILDLEEERQ----RHAQDTAEGDDVtymleKERERLTQQLEFEKSQVKKFEKEQKKLS-------SQLEEE 171
Cdd:PTZ00121  1518 AEEAKKADEAKKAEEAKKadeaKKAEEKKKADEL-----KKAEELKKAEEKKKAEEAKKAEEDKNMAlrkaeeaKKAEEA 1592

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  172 RSRHKQLSSMLVLECKKATNKAAEEGQKAGELSLKLEKEKSRVSKLEEELAAERKRGlqteAQVEKQLSEFDIEREQLRA 251
Cdd:PTZ00121  1593 RIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKA----EELKKAEEENKIKAAEEAK 1668

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1034560209  252 KLNREENRTKTLKEEMESLKKIVKDLEASHQHSSPNEQLKKPVTVSKGTATE 303
Cdd:PTZ00121  1669 KAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEE 1720
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 80-294 1.38e-07

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 55.06  E-value: 1.38e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209   80 LSILKVVMKQCKNMQERMLSQLAAAESRHR-------KVILDLEEERQRHAQDTAEGDDVT---YMLEKERERLTQQLEF 149
Cdd:TIGR02168  227 LALLVLRLEELREELEELQEELKEAEEELEeltaelqELEEKLEELRLEVSELEEEIEELQkelYALANEISRLEQQKQI 306

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  150 EKSQVKKFEKEQKKLSSQLEEERSRhkqlssmlvLECKKAtnKAAEEGQKAGELSLKLEKEKSRVSKLEEELAAerkrgl 229
Cdd:TIGR02168  307 LRERLANLERQLEELEAQLEELESK---------LDELAE--ELAELEEKLEELKEELESLEAELEELEAELEE------ 369

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034560209  230 qteaqVEKQLSEFDIEREQLRAKLNREENRTKTLKEEMESLKKIVKDLEASHQ--HSSPNEQLKKPV 294
Cdd:TIGR02168  370 -----LESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRErlQQEIEELLKKLE 431
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
202-280 1.72e-07

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 54.48  E-value: 1.72e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034560209 202 ELSLKLEKEKSRVSKLEEELAAERKRgLQTEAQVEKQLSEFDIEREQLRAKLNREENRTKTLKEEMESLKKIVKdLEAS 280
Cdd:COG2433   431 ELEAELEEKDERIERLERELSEARSE-ERREIRKDREISRLDREIERLERELEEERERIEELKRKLERLKELWK-LEHS 507
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 94-279 2.66e-07

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 53.23  E-value: 2.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  94 QERMLSQLAAAESRHRKVILDLEEERQRHAQDTAEGDDVTYMLEKERERLTQQLEFEKSQVKKFEKEQKKLSSQLEEERS 173
Cdd:COG4942    25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209 174 ----------RHKQLSSMLVLECKKATNKAAEEGQKAGELS-------LKLEKEKSRVSKLEEELAAERKRGLQTEAQVE 236
Cdd:COG4942   105 elaellralyRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAparreqaEELRADLAELAALRAELEAERAELEALLAELE 184

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1034560209 237 KQLSEFDIEREQLRAKLNREENRTKTLKEEMESLKKIVKDLEA 279
Cdd:COG4942   185 EERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 87-278 6.93e-07

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 52.42  E-value: 6.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  87 MKQCKNMQERMLSQLAAAESRHRKVILDLEEERQRHAQDTAEGDDVTYML---EKERERLTQQLEFEKSQVKKFEKEQKK 163
Cdd:pfam05483 396 MTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLqarEKEIHDLEIQLTAIKTSEEHYLKEVED 475

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209 164 LSSQLEEERSRHKQLSS---MLVLECKKATnkaaeegQKAGELSLKLEKEKSRV---SKLEEELAAERKRGLQTEAQVEK 237
Cdd:pfam05483 476 LKTELEKEKLKNIELTAhcdKLLLENKELT-------QEASDMTLELKKHQEDIincKKQEERMLKQIENLEEKEMNLRD 548

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1034560209 238 QLS----EFDIEREQLRAKLNREENRTKTLKEEMESLKKIVKDLE 278
Cdd:pfam05483 549 ELEsvreEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILE 593
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 56-279 7.40e-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: 52.76  E-value: 7.40e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209   56 ALQRDFETLKEKNDGEKQpvctnplsILKVVMKQCKNMQErmlsQLAAAESRHRKVILDLEE-ERQRHAQDTAEGDDVTY 134
Cdd:TIGR02169  720 EIEKEIEQLEQEEEKLKE--------RLEELEEDLSSLEQ----EIENVKSELKELEARIEElEEDLHKLEEALNDLEAR 787

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  135 MLEKERERLTQQLEFEKSQVKKFEK---------EQKKLSSQLEEERSRHKQlSSMLVLECKKATNKAAEEGQKA--GEL 203
Cdd:TIGR02169  788 LSHSRIPEIQAELSKLEEEVSRIEArlreieqklNRLTLEKEYLEKEIQELQ-EQRIDLKEQIKSIEKEIENLNGkkEEL 866

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034560209  204 SLKLEKEKSRVSKLEEE---LAAERKRglqteaqVEKQLSEFDIEREQLRAKLNREENRTKTLKEEMESLKKIVKDLEA 279
Cdd:TIGR02169  867 EEELEELEAALRDLESRlgdLKKERDE-------LEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIED 938
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
94-281 1.08e-06

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 51.84  E-value: 1.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209   94 QERMLSQLAAAESRHRKVILDLEE-ERQRHAQDTAEGDDVTYMLEKERERLTQQLEFEKSQVKKFEKEQKKLSSQLEEER 172
Cdd:COG4913    250 QIELLEPIRELAERYAAARERLAElEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELE 329

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  173 SRHKQLSSMLVLECKKatnKAAEEGQKAGELSLKLEKEKSRVSKLEEELAAERKRGLQTEAQVEKQLSEFDIEREQLRAK 252
Cdd:COG4913    330 AQIRGNGGDRLEQLER---EIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEA 406

                          170       180
                   ....*....|....*....|....*....
gi 1034560209  253 LNREENRTKTLKEEMESLKKIVKDLEASH 281
Cdd:COG4913    407 LAEAEAALRDLRRELRELEAEIASLERRK 435
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 22-281 1.60e-06

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 51.61  E-value: 1.60e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209   22 LEARDLVIEALKAQhRDTFIEERYG--KYnisDPLMALQRDFET---LKEKNDGEKQPV-CTNPLSILKVVMKQCKNMQE 95
Cdd:TIGR02169  186 IERLDLIIDEKRQQ-LERLRREREKaeRY---QALLKEKREYEGyelLKEKEALERQKEaIERQLASLEEELEKLTEEIS 261

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209   96 RMLSQLAAAESRHRKV---ILDLEEERQRHAQDTAEGddvtymLEKERERLTQQLEFEKSQVKKFEKEQKKLSSQLEEER 172
Cdd:TIGR02169  262 ELEKRLEEIEQLLEELnkkIKDLGEEEQLRVKEKIGE------LEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLL 335

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  173 SRHKQLSsmlvlecKKATNKAAEEGQKAGELSLKLEKEKSRVSKLEEElAAERKRGLQTEAQVEKQLSEFDIEREQLRAK 252
Cdd:TIGR02169  336 AEIEELE-------REIEEERKRRDKLTEEYAELKEELEDLRAELEEV-DKEFAETRDELKDYREKLEKLKREINELKRE 407

                          250       260
                   ....*....|....*....|....*....
gi 1034560209  253 LNREENRTKTLKEEMESLKKIVKDLEASH 281
Cdd:TIGR02169  408 LDRLQEELQRLSEELADLNAAIAGIEAKI 436
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 21-276 2.31e-06

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 50.89  E-value: 2.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  21 ELEARDLVIEALKAqhRDTFIEERYGKYNISDPL-MALQRDFETLK-EKNDGEKQPVCTNPLSILKVVMKQCKNMQ---- 94
Cdd:pfam17380 311 EVERRRKLEEAEKA--RQAEMDRQAAIYAEQERMaMERERELERIRqEERKRELERIRQEEIAMEISRMRELERLQmerq 388

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  95 ---ERMLSQLAAA-------ESRHRKVILDLEEERQRHAQDTAEGDDVTYMLEKERER---------LTQQLEFEKSQVK 155
Cdd:pfam17380 389 qknERVRQELEAArkvkileEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERARemervrleeQERQQQVERLRQQ 468

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209 156 KFEKEQKKLSSQLEEERSRHKQLSSMLVLECKKATNKAA--EEGQKAGELSLKLEKEKSRVSKLEEELAAERKRGLQTEA 233
Cdd:pfam17380 469 EEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAmiEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEM 548

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1034560209 234 QVEKQLsefdieREQLRaKLNREENRTKTLKEEMESLKKIVKD 276
Cdd:pfam17380 549 EERRRI------QEQMR-KATEERSRLEAMEREREMMRQIVES 584
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 137-282 3.09e-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: 50.44  E-value: 3.09e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  137 EKERERLTQQLEFEKSQVKKFEKEQKKLSSQLEEERSRHKQLSSmlvleckkatnKAAEEGQKAGELSLKLEKEKSRVSK 216
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRK-----------ELEELSRQISALRKDLARLEAEVEQ 744

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034560209  217 LEEELAaerkrglqteaQVEKQLSEFDIEREQLRAKLNREENRTKTLKEEMESLKKIVKDLEASHQ 282
Cdd:TIGR02168  745 LEERIA-----------QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELK 799
PTZ00121 PTZ00121
MAEBL; Provisional
 52-273 4.00e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.14  E-value: 4.00e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209   52 DPLMALQRDfETLKEKNDGEKQPVCTNPLSILKVVMKQCKNMQERML--SQLAAAESRHRKV--ILDLEEERQRHAQDTA 127
Cdd:PTZ00121  1575 DKNMALRKA-EEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIkaEELKKAEEEKKKVeqLKKKEAEEKKKAEELK 1653

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  128 EGDDVTYMLEKERERLTQQLEFEKSQVKKFEKEQKKLSSQL---EEERSRHKQLSSMLVLECKKA--TNKAAEEGQ-KAG 201
Cdd:PTZ00121  1654 KAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALkkeAEEAKKAEELKKKEAEEKKKAeeLKKAEEENKiKAE 1733

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034560209  202 ELSLKLEKEKSRVSKLEEElAAERKRGLQTEAQVEKQLSEFDIEREQLRaklnREENRTKTLKEEMESLKKI 273
Cdd:PTZ00121  1734 EAKKEAEEDKKKAEEAKKD-EEEKKKIAHLKKEEEKKAEEIRKEKEAVI----EEELDEEDEKRRMEVDKKI 1800
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 1-285 4.91e-06

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 49.97  E-value: 4.91e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209    1 MNLEKLSKPELLTLFSILEGELEARDLVIEALKAQHRdtfIEERYGKYNISDPLMALQRDFETLKEKNDGEKQPVCTNPL 80
Cdd:pfam02463  659 AEKSEVKASLSELTKELLEIQELQEKAESELAKEEIL---RRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKIN 735

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209   81 SILKVvmKQCKNMQERMLSQLAAAESR-------HRKVILDLEEERQRHAQ-DTAEGDDVTYMLEKERER--LTQQLEFE 150
Cdd:pfam02463  736 EELKL--LKQKIDEEEEEEEKSRLKKEekeeeksELSLKEKELAEEREKTEkLKVEEEKEEKLKAQEEELraLEEELKEE 813

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  151 KSQVKKFEKEQKKLSSQLEEERSRHKQLSSMLvlecKKATNKAAEEGQKAGELSLKLEKEKSRVSKLEEELAAERKRGLQ 230
Cdd:pfam02463  814 AELLEEEQLLIEQEEKIKEEELEELALELKEE----QKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELE 889

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1034560209  231 TEAQVEKQLsefDIEREQLRAKLNREENRTKTLKEEMESLKKIVKDLEASHQHSS 285
Cdd:pfam02463  890 SKEEKEKEE---KKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELL 941
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 91-278 5.03e-06

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 49.74  E-value: 5.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  91 KNMQERMLSQLAAAESRHRKVILDLEEERQR---HAQDTAEGDDVTYMLEKERERLTQQLEFEKSQVKKFEKEQKKLSSQ 167
Cdd:pfam17380 359 KRELERIRQEEIAMEISRMRELERLQMERQQkneRVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVR 438

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209 168 -LEEERSRHKQLSSMLVLECKKATNKAAEEGQKAGELSLKLEKEKSRVSKLEEElaaeRKRGLQTEAQVEKQlsefdier 246
Cdd:pfam17380 439 rLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQ----RRKILEKELEERKQ-------- 506

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1034560209 247 eqlraKLNREENRTKTLKEEMESLKKIVKDLE 278
Cdd:pfam17380 507 -----AMIEEERKRKLLEKEMEERQKAIYEEE 533
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
136-292 5.26e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 49.68  E-value: 5.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209 136 LEKERERLTQ---QLEFEKSQVKKFEKEQKKLSSQLEEERSRHKQLSSMlVLECKKATNKAaEEGQKAGELSLKLEKEKS 212
Cdd:PRK03918  233 LEELKEEIEElekELESLEGSKRKLEEKIRELEERIEELKKEIEELEEK-VKELKELKEKA-EEYIKLSEFYEEYLDELR 310

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209 213 RVSKLEEELAAERKrglqteaQVEKQLSefdiEREQLRAKLNREENRTKTLKEEMESLKKIVKDLEASHQHSSPNEQLKK 292
Cdd:PRK03918  311 EIEKRLSRLEEEIN-------GIEERIK----ELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKK 379
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
95-279 7.86e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 49.27  E-value: 7.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  95 ERMLSQLAAAESRHRKVILDLEEERQRHAQDTAEGDDVTYMLEKERERLTQQLEFEKSQVKKFEKEQKKLSSQLEEERSR 174
Cdd:PRK02224  271 EREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLRED 350

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209 175 HKQLSSmlvlECKKATNKAAEEGQKAGELSLKLEKEKSRVSKLEEELAAERKRGLQTEAQVEKqLSEFdieREQLRAKLN 254
Cdd:PRK02224  351 ADDLEE----RAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGN-AEDF---LEELREERD 422

                         170       180
                  ....*....|....*....|....*
gi 1034560209 255 REENRTKTLKEEMESLKKIVKDLEA 279
Cdd:PRK02224  423 ELREREAELEATLRTARERVEEAEA 447
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
104-282 7.94e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 49.29  E-value: 7.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209 104 AESRHRKVILDLEEERQRHAQDTAEGDDVTYMLEKERERLTQQLEfeksQVKKFEKEQKKLSSQLEEERSRHKQLSSMLV 183
Cdd:PRK03918  163 AYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLR----EINEISSELPELREELEKLEKEVKELEELKE 238

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209 184 LECKKATNKAAEEGQKAG-------------ELSLKLEKEKSRVSKLEE---------ELAAERKRGLQTEAQVEKQLSE 241
Cdd:PRK03918  239 EIEELEKELESLEGSKRKleekireleerieELKKEIEELEEKVKELKElkekaeeyiKLSEFYEEYLDELREIEKRLSR 318

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1034560209 242 FDIEREQLRA---KLNREENRTKTLKEEMESLKKIVKDLEASHQ 282
Cdd:PRK03918  319 LEEEINGIEErikELEEKEERLEELKKKLKELEKRLEELEERHE 362
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 130-282 9.15e-06

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.16  E-value: 9.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209 130 DDVTYMLEKERERLTQQlefeKSQVKKFekeqKKLSSQLEEersRHKQLssmLVLECKKATNKAAEEGQKAGELSLKLEK 209
Cdd:COG1196   192 EDILGELERQLEPLERQ----AEKAERY----RELKEELKE---LEAEL---LLLKLRELEAELEELEAELEELEAELEE 257

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034560209 210 EKSRVSKLEEELAAERKRGLQTEAQVE---KQLSEFDIEREQLRAKLNREENRTKTLKEEMESLKKIVKDLEASHQ 282
Cdd:COG1196   258 LEAELAELEAELEELRLELEELELELEeaqAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELE 333
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
95-259 1.10e-05

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 48.76  E-value: 1.10e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209   95 ERMLSQLAAAESRHRKVILDLEE--------ERQRHA----QDTAEGDDVTYMLEKERERLTQQLEfeksQVKKFEKEQK 162
Cdd:COG4913    613 AALEAELAELEEELAEAEERLEAleaeldalQERREAlqrlAEYSWDEIDVASAEREIAELEAELE----RLDASSDDLA 688

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  163 KLSSQLEEERSRHKQLSSmlvlECKKATNKAAEEGQKAGELSLKLEKEKSRVSKLEE-------ELAAERKRGLQTEAQV 235
Cdd:COG4913    689 ALEEQLEELEAELEELEE----ELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDlarlelrALLEERFAAALGDAVE 764

                          170       180
                   ....*....|....*....|....
gi 1034560209  236 EKQLSEFDIEREQLRAKLNREENR 259
Cdd:COG4913    765 RELRENLEERIDALRARLNRAEEE 788
PTZ00121 PTZ00121
MAEBL; Provisional
 96-303 1.28e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.60  E-value: 1.28e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209   96 RMLSQLAAAESRHRKVILDLEEERQRHAQDTAEgddVTYMLEKERERLTQQLEFEKSQVK----KFEKEQKKLSSQL--- 168
Cdd:PTZ00121  1552 KKAEELKKAEEKKKAEEAKKAEEDKNMALRKAE---EAKKAEEARIEEVMKLYEEEKKMKaeeaKKAEEAKIKAEELkka 1628

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  169 EEERSRHKQLSSMLVLECKKA--TNKAAEEGQ-KAGELSLKLEKEKSRVSKLEEELAAERKRGLQTEAQVEKQLsefdiE 245
Cdd:PTZ00121  1629 EEEKKKVEQLKKKEAEEKKKAeeLKKAEEENKiKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAK-----K 1703

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034560209  246 REQLRAKLNREENRTKTLKEEMESLKKIVkdleashqhsspnEQLKKPVTVSKGTATE 303
Cdd:PTZ00121  1704 AEELKKKEAEEKKKAEELKKAEEENKIKA-------------EEAKKEAEEDKKKAEE 1748
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 91-276 1.91e-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: 47.86  E-value: 1.91e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209   91 KNMQERML---SQLAAAESRHRKVILD---LEEERQRHAQDTAEGDDVTYMLEKER----ERL---TQQLEFEKSQVK-- 155
Cdd:pfam01576   99 KKMQQHIQdleEQLDEEEAARQKLQLEkvtTEAKIKKLEEDILLLEDQNSKLSKERklleERIsefTSNLAEEEEKAKsl 178

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  156 -KFEKEQKKLSSQLEEERSRHKQLSSMLVLECKKATNKAAEEGQKAGELSLKLEKEKSRVSKLEEELAAERKRGLQTEAQ 234
Cdd:pfam01576  179 sKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQ 258

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1034560209  235 ----------VEKQLSEFDIEREQLRAKLNREENRTKTLKEEMESLKKIVKD 276
Cdd:pfam01576  259 knnalkkireLEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELED 310
PTZ00121 PTZ00121
MAEBL; Provisional
 91-292 2.15e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.83  E-value: 2.15e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209   91 KNMQERMLSQLAAAESRHRKVILDLEEERQRHAQDTAEGDDVTYMLEKERERLTQQLEFEKSQVKKFEKEqkklssqlEE 170
Cdd:PTZ00121  1559 KAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA--------EE 1630

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  171 ERSRHKQLSSMLVLECKKA--TNKAAEEGQ-KAGELSLKLEKEKSRVSKLEEELAAERKRGLQTE---------AQVEKQ 238
Cdd:PTZ00121  1631 EKKKVEQLKKKEAEEKKKAeeLKKAEEENKiKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKkeaeeakkaEELKKK 1710

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1034560209  239 LSEFDIEREQLRAKLNREENRTKTLKEEMESLKKIVKDLEASHQHSSPNEQLKK 292
Cdd:PTZ00121  1711 EAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKK 1764
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
113-292 2.47e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.82  E-value: 2.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209 113 LDLEEERQRHAQDTAEGDDVTYMLEKERERLTQQLEFEKSQVKKFEKEQKKLSSQLEEERSRHKQLSSMLvlecKKATNK 192
Cdd:COG4372    13 LSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL----EELNEQ 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209 193 AAEEGQKAGELSLKLEKEKSRVSKLEEELAAerkrgLQTE-AQVEKQLSEFDIEREQLRAKLNREENRTKTLKEEMESLK 271
Cdd:COG4372    89 LQAAQAELAQAQEELESLQEEAEELQEELEE-----LQKErQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQ 163

                         170       180
                  ....*....|....*....|.
gi 1034560209 272 KIVKDLEASHQHSSPNEQLKK 292
Cdd:COG4372   164 EELAALEQELQALSEAEAEQA 184
PTZ00121 PTZ00121
MAEBL; Provisional
 65-303 2.53e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.83  E-value: 2.53e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209   65 KEKNDGEKQPVCTNPLSILKVVMKQCKNMQERMLSQLAAAESRHRKVILDLEEER------QRHAQDTAEGDDVTYMLE- 137
Cdd:PTZ00121  1247 EERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKkkadeaKKKAEEAKKADEAKKKAEe 1326

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  138 --KERERLTQQLEFEK--SQVKKFEKEQKKLSSQLEEERSRHKQLSSMLVLECKKATNKAAEEGQKAGELSLKLEKEKSR 213
Cdd:PTZ00121  1327 akKKADAAKKKAEEAKkaAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKK 1406

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  214 VSKLEEELAAERK-RGLQTEAQVEKQLSEFDIEREQLR----AKLNREENR-TKTLKEEMESLKKiVKDLEASHQHSSPN 287
Cdd:PTZ00121  1407 ADELKKAAAAKKKaDEAKKKAEEKKKADEAKKKAEEAKkadeAKKKAEEAKkAEEAKKKAEEAKK-ADEAKKKAEEAKKA 1485

                          250
                   ....*....|....*.
gi 1034560209  288 EQLKKPVTVSKGTATE 303
Cdd:PTZ00121  1486 DEAKKKAEEAKKKADE 1501
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
136-292 3.64e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.43  E-value: 3.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209 136 LEKERERLTQQLEFEKSQVKKFEKEQKKLSSQLEEERSRHKQLSSMLVlECKKATNKAAEEGQKAGELSLKLEKEKSRVS 215
Cdd:COG4372    43 LQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQ-AAQAELAQAQEELESLQEEAEELQEELEELQ 121

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034560209 216 KLEEELAAERKRGLQTEAQVEKQLSEFDIEREQLRAKLNREENRTKTLKEEMESLKKIVKDLEASHQHSSPNEQLKK 292
Cdd:COG4372   122 KERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEK 198
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
20-281 4.35e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 46.57  E-value: 4.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  20 GELEARdlvIEALKAQHrdtfiEERYGKYNISDPLMALQRDFETLKEKNDgekqpvctnplSILKVVMKQCKNMQERmls 99
Cdd:PRK02224  478 EELEAE---LEDLEEEV-----EEVEERLERAEDLVEAEDRIERLEERRE-----------DLEELIAERRETIEEK--- 535

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209 100 QLAAAESRHRKVILDLEEERQRHAQDTAEGDdvtymLEKERERltqqlefeksqVKKFEKEQkklsSQLEEERSRHKQLS 179
Cdd:PRK02224  536 RERAEELRERAAELEAEAEEKREAAAEAEEE-----AEEAREE-----------VAELNSKL----AELKERIESLERIR 595

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209 180 SMLVLeckkatnkAAEEGQKAGELSLKLE-------------KEKS-RVSKLEEELAAERKRGLQTE--------AQVEK 237
Cdd:PRK02224  596 TLLAA--------IADAEDEIERLREKREalaelnderrerlAEKReRKRELEAEFDEARIEEAREDkeraeeylEQVEE 667

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1034560209 238 QLSEFDIEREQLRAKLNREEN---RTKTLKEEMESLKKIVKDLEASH 281
Cdd:PRK02224  668 KLDELREERDDLQAEIGAVENeleELEELRERREALENRVEALEALY 714
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 136-292 5.34e-05

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 46.04  E-value: 5.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209 136 LEKERERLTQQLEFEKSQVKK----FEKEQKKLSSQ---LEEERSRHKQLSSMLVLECKKATNKAAEEGQKAGELSLKLE 208
Cdd:pfam07888  46 LLQAQEAANRQREKEKERYKRdreqWERQRRELESRvaeLKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRA 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209 209 KEKSRVSKLEEELAAERKRGLQTEAQVEK----------QLSEFDIEREQLRAKLNREENRTKTLKEEMESLK------- 271
Cdd:pfam07888 126 AHEARIRELEEDIKTLTQRVLERETELERmkerakkagaQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRnslaqrd 205

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1034560209 272 -----------KIVKDLEASHQHSSPNEQLKK 292
Cdd:pfam07888 206 tqvlqlqdtitTLTQKLTTAHRKEAENEALLE 237
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
131-278 5.63e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.21  E-value: 5.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209 131 DVTYMLEKERERLTQQ----------LEFEKSQVKKFEKEQKKLSSQLEEERSRHKQLSSMLVLECKKATNKAAEEGQKA 200
Cdd:PRK03918  307 DELREIEKRLSRLEEEingieerikeLEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTP 386

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209 201 GELSLKLEKEKSRVSKLEEELA--AERKRGLQTE-AQVEKQLSEF---------------DIEREQL----RAKLNREEN 258
Cdd:PRK03918  387 EKLEKELEELEKAKEEIEEEISkiTARIGELKKEiKELKKAIEELkkakgkcpvcgreltEEHRKELleeyTAELKRIEK 466

                         170       180
                  ....*....|....*....|
gi 1034560209 259 RTKTLKEEMESLKKIVKDLE 278
Cdd:PRK03918  467 ELKEIEEKERKLRKELRELE 486
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
3-280 1.32e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.05  E-value: 1.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209   3 LEKLSKpELLTLFSILEGELEARDL--VIEALKAqhrdtfIEERYGKYNISDpLMALQRDFETLKEKNDGEKqpvctnpl 80
Cdd:PRK03918  475 ERKLRK-ELRELEKVLKKESELIKLkeLAEQLKE------LEEKLKKYNLEE-LEKKAEEYEKLKEKLIKLK-------- 538

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  81 silkvvmKQCKNMQERmLSQLAAAESRHRKVILDLEEerqrhaqdtaegddvtymLEKERERLTQQLEfeksqvKKFEKE 160
Cdd:PRK03918  539 -------GEIKSLKKE-LEKLEELKKKLAELEKKLDE------------------LEEELAELLKELE------ELGFES 586

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209 161 QKKLSSQLEEERSRHKQLssmlvLECKKATnKAAEEGQKagelslKLEKEKSRVSKLEEELAAERKRGLQTEAQVEKQLS 240
Cdd:PRK03918  587 VEELEERLKELEPFYNEY-----LELKDAE-KELEREEK------ELKKLEEELDKAFEELAETEKRLEELRKELEELEK 654

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1034560209 241 EFDIER-EQLRAKLNREENRTKTLKEEMESLKKIVKDLEAS 280
Cdd:PRK03918  655 KYSEEEyEELREEYLELSRELAGLRAELEELEKRREEIKKT 695
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 88-282 1.37e-04

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 45.35  E-value: 1.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209   88 KQCKNMQERMLSQLAAAESRHRKVILDLEEERQRHAQDTAEGDDVTYMLEKERERLTQQLEFEKSQVKKFEKEQKKLSSQ 167
Cdd:pfam02463  214 QLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAK 293

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  168 LEEERSRHKQLssmLVLECKKATNKAAEEGQKAGELSLKLEKEKSRVSKLEEELAAERKRGLQTEAQVEKQlsefdieRE 247
Cdd:pfam02463  294 EEEELKSELLK---LERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEEL-------EK 363

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1034560209  248 QLRAKLNREENRTKTLKEEMESLKKIVKDLEASHQ 282
Cdd:pfam02463  364 LQEKLEQLEEELLAKKKLESERLSSAAKLKEEELE 398
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 98-272 1.66e-04

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 44.94  E-value: 1.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209   98 LSQLAAAESRHRKVILDLEEERQRHA----QDTAEgddvtyMLEKERErLTQQLefeKSQVKKFEKEQKKLSSQLEEERS 173
Cdd:COG3096    943 YLQAKEQQRRLKQQIFALSEVVQRRPhfsyEDAVG------LLGENSD-LNEKL---RARLEQAEEARREAREQLRQAQA 1012

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  174 RHKQLSSMLV-----LECKKATNKAAEEGQKAGELSLKLEKE---KSRVSKLEEELAAERKRglqtEAQVEKQLSEFDIE 245
Cdd:COG3096   1013 QYSQYNQVLAslkssRDAKQQTLQELEQELEELGVQADAEAEeraRIRRDELHEELSQNRSR----RSQLEKQLTRCEAE 1088

                          170       180
                   ....*....|....*....|....*..
gi 1034560209  246 REQLRAKLNREENRTKTLKEEMESLKK 272
Cdd:COG3096   1089 MDSLQKRLRKAERDYKQEREQVVQAKA 1115
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 136-282 1.74e-04

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 44.37  E-value: 1.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209 136 LEKERERLTQQLEFEKSQVKKFEKEQKKLSSQLEEERSRHKQLSSMLvlecKKATNKAAEEGQKAGELSLKLEKEKSRVS 215
Cdd:COG4942    25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRI----RALEQELAALEAELAELEKEIAELRAELE 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209 216 KLEEELaAERKRGLQTEAQVE---------------------KQLSEFDIER-EQLRAKLNREENRTKTLKEEMESLKKI 273
Cdd:COG4942   101 AQKEEL-AELLRALYRLGRQPplalllspedfldavrrlqylKYLAPARREQaEELRADLAELAALRAELEAERAELEAL 179


                  ....*....
gi 1034560209 274 VKDLEASHQ 282
Cdd:COG4942   180 LAELEEERA 188
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 114-270 1.87e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 1.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209 114 DLEEERQRHAQDTAEGDDVTYmleKERERLTQQLEFEKSQVKKFEKEQKKLSSQLEEERSRHKQLSSMLVLECKKATNKA 193
Cdd:COG1196   626 TLVAARLEAALRRAVTLAGRL---REVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAE 702

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034560209 194 AEEGQKAGELSLKLEKEKSRVSKLEEELAAERKRGLQTEAQVEKQLSEFDIEREQLRAKLNREENRTKTLKEEMESL 270
Cdd:COG1196   703 EEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 83-256 2.05e-04

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: 43.37  E-value: 2.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  83 LKVVMKQCKNMQERMLSQLAAAESRHRKVILDLEEERQRHAQDTAEGDDVTymLEKERERLTQQLEFEKSQVKKFEKEQK 162
Cdd:COG1579    36 LEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR--NNKEYEALQKEIESLKRRISDLEDEIL 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209 163 KLSSQLEEERSRhkqlssmlvleckkatnkaaeegqkagelslkLEKEKSRVSKLEEELAAERKRGLQTEAQVEKQLSEF 242
Cdd:COG1579   114 ELMERIEELEEE--------------------------------LAELEAELAELEAELEEKKAELDEELAELEAELEEL 161

                         170
                  ....*....|....
gi 1034560209 243 DIEREQLRAKLNRE 256
Cdd:COG1579   162 EAEREELAAKIPPE 175
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 12-273 2.18e-04

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 44.33  E-value: 2.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  12 LTLFSILEGELEARDLVIealkaqhrdtFIEERYGKYNISDPLMALQRdfETLKEKNdgEKQPVCTNPLSILKVVMKQCK 91
Cdd:pfam05483 244 LLLIQITEKENKMKDLTF----------LLEESRDKANQLEEKTKLQD--ENLKELI--EKKDHLTKELEDIKMSLQRSM 309

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  92 NMQERMLSQLAAAEsrhrKVILDLEEERQRHAQDT-----------AEGDDVTYMLEKERERLTQQLEFEKSQVKKFEKE 160
Cdd:pfam05483 310 STQKALEEDLQIAT----KTICQLTEEKEAQMEELnkakaahsfvvTEFEATTCSLEELLRTEQQRLEKNEDQLKIITME 385

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209 161 QKKLSSQLEEersrhkqlssmlVLECKKATNKAAEEGQKAGELSLKLEKEKSRVSKLEEELAAERKRGLQTEAQVEKQLS 240
Cdd:pfam05483 386 LQKKSSELEE------------MTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIH 453

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1034560209 241 EFDIereQLRAKLNREENRTKTLKE-----EMESLKKI 273
Cdd:pfam05483 454 DLEI---QLTAIKTSEEHYLKEVEDlktelEKEKLKNI 488
PRK12704 PRK12704
phosphodiesterase; Provisional
 149-279 2.26e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 44.00  E-value: 2.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209 149 FEKSQVKKFEKEQKKLSSQLEEERSRHKQLSSMLVLECKkatnkaaeegQKAGELSLKLEKEksrVSKLEEELAAERKRG 228
Cdd:PRK12704   25 RKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAK----------EEIHKLRNEFEKE---LRERRNELQKLEKRL 91

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1034560209 229 LQTEAQVEKQLSEFDIEREQLRAKLNREENRTKTLKEEMESLKKIVKDLEA 279
Cdd:PRK12704   92 LQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQ 142
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 21-292 2.71e-04

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 44.44  E-value: 2.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209   21 ELEARDLVIEALKAQHRDtfIEERYGKYnISDPLMALQRDFETLKEKNDGEKQPVCTNPLSILKVVMKQCKNMQERMLSQ 100
Cdd:pfam12128  355 ELENLEERLKALTGKHQD--VTAKYNRR-RSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAG 431

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  101 LAAAESRHRKVILDLEEERQRHAQDTAEGDDVTYM------LEKERERLTQ------QLEFEKSQVKK-FEKEQKKL--- 164
Cdd:pfam12128  432 KLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLenfderIERAREEQEAanaeveRLQSELRQARKrRDQASEALrqa 511

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  165 SSQLEEERSRHKQLSSMLV----------------------------LECKKATNKAAEEGQKAGELSL----------- 205
Cdd:pfam12128  512 SRRLEERQSALDELELQLFpqagtllhflrkeapdweqsigkvispeLLHRTDLDPEVWDGSVGGELNLygvkldlkrid 591

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  206 -----KLEKE-KSRVSKLEEELAAERKRGLQTE---AQVEKQLSEFDIEREQLRAKLNREENRTKTLKEEMESLKKIVKD 276
Cdd:pfam12128  592 vpewaASEEElRERLDKAEEALQSAREKQAAAEeqlVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNK 671

                          330
                   ....*....|....*.
gi 1034560209  277 LEASHQHSSpNEQLKK 292
Cdd:pfam12128  672 ALAERKDSA-NERLNS 686
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 116-257 2.91e-04

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 43.79  E-value: 2.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209 116 EEERQRHAQDTAEGDDVTYMLEKERERLT-------QQLEFEKSQVKKFEKEQKkLSSQLEEERSR------HKQLSSML 182
Cdd:pfam15709 358 EEQRRLQQEQLERAEKMREELELEQQRRFeeirlrkQRLEEERQRQEEEERKQR-LQLQAAQERARqqqeefRRKLQELQ 436

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034560209 183 VLECKKATNKAAEEGQKAGELSLKLEKEKSRVSKLEEELAAERKRGLQTEAQVEKQLSEFDIEREQLRAKLNREE 257
Cdd:pfam15709 437 RKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQRQKQEAEEKARLEAEERRQKEEEAARLALEE 511
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
62-279 3.09e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.90  E-value: 3.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  62 ETLKEKNDGEKQ-PVCTNPLSILKVVMKQCKNMQER----------MLSQLAAAESRHRKV--ILDLEEERQRHAQDTA- 127
Cdd:PRK03918  304 EYLDELREIEKRlSRLEEEINGIEERIKELEEKEERleelkkklkeLEKRLEELEERHELYeeAKAKKEELERLKKRLTg 383

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209 128 -EGDDVTYML---EKERERLTQQLE---FEKSQVKKFEKEQKKLSSQLEEERSR-----------HKQlssMLVLECKKA 189
Cdd:PRK03918  384 lTPEKLEKELeelEKAKEEIEEEISkitARIGELKKEIKELKKAIEELKKAKGKcpvcgrelteeHRK---ELLEEYTAE 460

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209 190 TNKAAEEGQKAGELSLKLEKEKSRVSKL---EEELAAERKRGLQTEAqVEKQLSEFDIER--------EQLRAKLNREEN 258
Cdd:PRK03918  461 LKRIEKELKEIEEKERKLRKELRELEKVlkkESELIKLKELAEQLKE-LEEKLKKYNLEElekkaeeyEKLKEKLIKLKG 539

                         250       260
                  ....*....|....*....|.
gi 1034560209 259 RTKTLKEEMESLKKIVKDLEA 279
Cdd:PRK03918  540 EIKSLKKELEKLEELKKKLAE 560
PRK12704 PRK12704
phosphodiesterase; Provisional
 104-269 4.71e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 43.23  E-value: 4.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209 104 AESRHRKVILDLEEERQRHAQDTaegddvtymlEKERERLTQQLEFEksqVKKfekEQKKLSSQLEEE-RSRHKQLSSml 182
Cdd:PRK12704   25 RKKIAEAKIKEAEEEAKRILEEA----------KKEAEAIKKEALLE---AKE---EIHKLRNEFEKElRERRNELQK-- 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209 183 vLECKkatNKAAEEgqkagelslKLEKEKSRVSKLEEELAAERKRGLQTEAQVEKQLSEFDIEREQLRAKLNR------E 256
Cdd:PRK12704   87 -LEKR---LLQKEE---------NLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERisgltaE 153

                         170
                  ....*....|...
gi 1034560209 257 ENRtKTLKEEMES 269
Cdd:PRK12704  154 EAK-EILLEKVEE 165
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 84-273 7.92e-04

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 42.21  E-value: 7.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  84 KVVMKQCKNMQERMLSQLAAAEsrHRKVILDLEEERQRHAQDTAEGDDVTY--MLEKERERLTQQLEF--EKSQVKKFEK 159
Cdd:pfam13868  31 KKRIKAEEKEEERRLDEMMEEE--RERALEEEEEKEEERKEERKRYRQELEeqIEEREQKRQEEYEEKlqEREQMDEIVE 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209 160 EQKKLSSQLEEERSRHKQLSSMLVLECKKATNKA--------AEEGQKAGE-LSLKLEKEKSRVSKLEEELAAERKRGLQ 230
Cdd:pfam13868 109 RIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWkelekeeeREEDERILEyLKEKAEREEEREAEREEIEEEKEREIAR 188

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1034560209 231 TEAQVEKQLSEFDiEREQLRAKLNREENRTKT-LKEEMESLKKI 273
Cdd:pfam13868 189 LRAQQEKAQDEKA-ERDELRAKLYQEEQERKErQKEREEAEKKA 231
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 95-266 8.58e-04

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 42.25  E-value: 8.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  95 ERMLSQLAAAESRHRKVILDLEEERQRHAQDTAEG-DDVTYMLEKERERLTQQLEFEKSQVKKFEKEQKKLSSQLEEERS 173
Cdd:COG5185   376 SEELDSFKDTIESTKESLDEIPQNQRGYAQEILATlEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMR 455

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209 174 RHKQLSSMLVLECKKATNKaaEEGQKAGELSLKLEKEKSRVSKLEEELAAERKRG-------LQTEAQVEKQLSEFDIER 246
Cdd:COG5185   456 EADEESQSRLEEAYDEINR--SVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLerqlegvRSKLDQVAESLKDFMRAR 533

                         170       180
                  ....*....|....*....|
gi 1034560209 247 EQLRAKLNREENRTKTLKEE 266
Cdd:COG5185   534 GYAHILALENLIPASELIQA 553
CCDC22 pfam05667
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
 137-279 9.03e-04

Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.


Pssm-ID: 461708 [Multi-domain]  Cd Length: 600  Bit Score: 42.32  E-value: 9.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209 137 EKERERLTQQLEFEKSQVKKFEKEQKKLSS---QLEEErsrhkqlssmlvLECKKATNKAAEEGQKAGELSLKLEKE-KS 212
Cdd:pfam05667 334 EEELEELQEQLEDLESSIQELEKEIKKLESsikQVEEE------------LEELKEQNEELEKQYKVKKKTLDLLPDaEE 401

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034560209 213 RVSKLEEELAAERKRGLQTEAQVEKQLSEFDIEREQLRAKLNREENRTKTLKEEMESLKKIVKDLEA 279
Cdd:pfam05667 402 NIAKLQALVDASAQRLVELAGQWEKHRVPLIEEYRALKEAKSNKEDESQRKLEEIKELREKIKEVAE 468
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
95-282 9.65e-04

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 42.31  E-value: 9.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  95 ERMLSQLAAAES-----RHRKVILDLEEERQRHAQDTAEgddvtymLEKERERLTQQLEFEKSQVKKFEKeQKKLSSQLE 169
Cdd:COG3206   185 PELRKELEEAEAaleefRQKNGLVDLSEEAKLLLQQLSE-------LESQLAEARAELAEAEARLAALRA-QLGSGPDAL 256

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209 170 EERSRHKQLSSmLVLECKKATNKAAEEGQKAGELSLKLEKEKSRVSKLEEELAAERKRGLqteAQVEKQLSEFDIEREQL 249
Cdd:COG3206   257 PELLQSPVIQQ-LRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRIL---ASLEAELEALQAREASL 332

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1034560209 250 RAKLNREENRTKTLKEEMESLKKIVKDLEASHQ 282
Cdd:COG3206   333 QAQLAQLEARLAELPELEAELRRLEREVEVARE 365
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 101-279 1.04e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209 101 LAAAESRHRKVILDLEEERQRHAQDTAEGDDVTYMLEKERERLTQQLEFEKSQVKKFEKEQKKLSSQLEEERSRHKQLSS 180
Cdd:COG1196   607 DLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAE 686

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209 181 MLvlecKKATNKAAEEGQKAGELSLKLEKEKSRVSKLEEELAAERKRGLQTEAQVEKQLSEFDIEREQLRAKLNREENRT 260
Cdd:COG1196   687 RL----AEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL 762

                         170
                  ....*....|....*....
gi 1034560209 261 KTLKEEMESLKKIVKDLEA 279
Cdd:COG1196   763 EELERELERLEREIEALGP 781
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
96-245 1.33e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.82  E-value: 1.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209   96 RMLSQLAAAESRHRKVILDLEEERQRHAQDTAEGDDVTyMLEKERERLTQQLEFEKSQVKKFEKEQKKLSSQLEEERSRH 175
Cdd:COG4913    651 QRLAEYSWDEIDVASAEREIAELEAELERLDASSDDLA-ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEEL 729

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034560209  176 KQLSSML---VLECKKATNKAAEEgQKAGELSLKLEKEKSRvsKLEEELAAERKRGLQTEAQVEKQLSEFDIE 245
Cdd:COG4913    730 DELQDRLeaaEDLARLELRALLEE-RFAAALGDAVERELRE--NLEERIDALRARLNRAEEELERAMRAFNRE 799
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 95-276 1.50e-03

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 41.88  E-value: 1.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209   95 ERMLSQLAAAESRHRKVILDLEEERQRHAQDTAEGDDVTYMLEKERErltqQLEFEKSQVKKFEKEQKKLSSQLEEERSR 174
Cdd:pfam02463  226 LLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLK----ENKEEEKEKKLQEEELKLLAKEEEELKSE 301

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  175 HKQLSSMLVLECKKAtnKAAEEGQKAGELSLKLEKEK-SRVSKLEEELAAERKRGLQTEAQVEKQLSEFDIEREQLRAKL 253
Cdd:pfam02463  302 LLKLERRKVDDEEKL--KESEKEKKKAEKELKKEKEEiEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKK 379

                          170       180
                   ....*....|....*....|....*.
gi 1034560209  254 NREENRTKT---LKEEMESLKKIVKD 276
Cdd:pfam02463  380 KLESERLSSaakLKEEELELKSEEEK 405
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 161-284 1.56e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.59  E-value: 1.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  161 QKKLSSQLEEERSRHKQLS---SMLVLECKKATNKAAEEGQKAGELSLKLEKEKSRVSKLEEELAAERKRglqtEAQVEK 237
Cdd:TIGR02169  669 SRSEPAELQRLRERLEGLKrelSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKER----LEELEE 744

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1034560209  238 QLSEFDIEREQLRAKLNREENRTKTLKEEMESLKKIVKDLEASHQHS 284
Cdd:TIGR02169  745 DLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHS 791
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
132-272 1.80e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.54  E-value: 1.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209 132 VTYMLEKERERLTQQLEFEKSQVKKFEKEQKKLSSQLEEERSRHKQLSsmLVLECKKATNKAAEEGQKAGELSLKLEKEK 211
Cdd:COG3206   162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVD--LSEEAKLLLQQLSELESQLAEARAELAEAE 239

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034560209 212 SRVSKLEEELAAERK-----RGLQTEAQVEKQLSEFDIEREQLRAKLNREENRTKTLKEEMESLKK 272
Cdd:COG3206   240 ARLAALRAQLGSGPDalpelLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRA 305
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 88-271 1.83e-03

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 41.64  E-value: 1.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209   88 KQCKNMQERMLSQLAAAESRHRKviLDLEEERQRHAQDTAEGDDVTYmlekerERLTQQLEFEKSQVKKFEKEQKKLSSQ 167
Cdd:pfam15921  370 QESGNLDDQLQKLLADLHKREKE--LSLEKEQNKRLWDRDTGNSITI------DHLRRELDDRNMEVQRLEALLKAMKSE 441

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  168 LEEERSRHkqlssMLVLECKKatnkaaEEGQKAGELSLKLEKEKSRVSKLEEELAA--------------------ERKR 227
Cdd:pfam15921  442 CQGQMERQ-----MAAIQGKN------ESLEKVSSLTAQLESTKEMLRKVVEELTAkkmtlessertvsdltaslqEKER 510

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1034560209  228 GLQ-TEAQVEKQLSEFDIEREQLRaKLNREENRTKTLKEEMESLK 271
Cdd:pfam15921  511 AIEaTNAEITKLRSRVDLKLQELQ-HLKNEGDHLRNVQTECEALK 554
fliH PRK06669
flagellar assembly protein H; Validated
 135-282 2.31e-03

flagellar assembly protein H; Validated


Pssm-ID: 235850 [Multi-domain]  Cd Length: 281  Bit Score: 40.38  E-value: 2.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209 135 MLEKERERLTQQLEFEKSQVKK--FEKEQKKLSSQLEEERSRHKQLSSMLVLECKKATNKAaeeGQKAGELSLKLEKEKS 212
Cdd:PRK06669   30 LSIKEKERLREEEEEQVEQLREeaNDEAKEIIEEAEEDAFEIVEAAEEEAKEELLKKTDEA---SSIIEKLQMQIEREQE 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209 213 RV-SKLEEELAAERKRGLQT--EAQVEKQLSEFDIEREQLRA---KLNRE-ENRTKTLKEEMESL-----KKIVKDLEAS 280
Cdd:PRK06669  107 EWeEELERLIEEAKAEGYEEgyEKGREEGLEEVRELIEQLNKiieKLIKKrEEILESSEEEIVELaldiaKKVIKEISEN 186


                  ..
gi 1034560209 281 HQ 282
Cdd:PRK06669  187 SK 188
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 94-283 3.02e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 40.72  E-value: 3.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209   94 QERMLSQLAAAESRHRKVILDLEEERQRHAQDTAEGDDVTY-----MLEKERERLTQQLEFEKSQVKKFEKEQKKLssql 168
Cdd:TIGR00618  177 QYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYherkqVLEKELKHLREALQQTQQSHAYLTQKREAQ---- 252

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  169 eEERSRHKQLSSMLVLECKKATN--KAAEEGQKAGELSLKLEKeksrvskleeeLAAERKRGLQTEAQVEKQLSEFDiER 246
Cdd:TIGR00618  253 -EEQLKKQQLLKQLRARIEELRAqeAVLEETQERINRARKAAP-----------LAAHIKAVTQIEQQAQRIHTELQ-SK 319

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1034560209  247 EQLRAKLNREENRTKTLKEEMESLKKIVKDLEASHQH 283
Cdd:TIGR00618  320 MRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIH 356
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 95-292 3.30e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 40.54  E-value: 3.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209   95 ERMLSQLAAAESRHRKVILDLE----EERQRHAQDTAEGD-------DVTYMLEKErERLTQQLEFEK----SQVKKFEK 159
Cdd:pfam01576   60 EEMRARLAARKQELEEILHELEsrleEEEERSQQLQNEKKkmqqhiqDLEEQLDEE-EAARQKLQLEKvtteAKIKKLEE 138

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  160 EqkklSSQLEEERSRHKQLSSMLVLECKKATNKAAEEGQKAGELSLKLEKEKSRVSKLEEELAAERKRGLQTE------- 232
Cdd:pfam01576  139 D----ILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEkakrkle 214

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  233 ---AQVEKQLSEFDIEREQLRAKLNREE------------------NRTKTLKEEMESLKKIVKDLEASHQHSSPNEQLK 291
Cdd:pfam01576  215 gesTDLQEQIAELQAQIAELRAQLAKKEeelqaalarleeetaqknNALKKIRELEAQISELQEDLESERAARNKAEKQR 294


                   .
gi 1034560209  292 K 292
Cdd:pfam01576  295 R 295
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 100-279 3.52e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 3.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209 100 QLAAAESRHRKVILDLEEERQRHAQDTAEGDDVTYMLEKERERLTQQLEFEKSQVKKFEKEQKKLSSQLEEERSRHKQLS 179
Cdd:COG1196   631 RLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELA 710

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209 180 SMLVLECKKATNKAAEEGQKAGELSLKLEKEkSRVSKLEEELAAERKRGLQTEAQVEKQLSEFDIEREQL-----RA--K 252
Cdd:COG1196   711 EAEEERLEEELEEEALEEQLEAEREELLEEL-LEEEELLEEEALEELPEPPDLEELERELERLEREIEALgpvnlLAieE 789

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1034560209 253 LNREENR-------TKTLKEEMESLKKIVKDLEA 279
Cdd:COG1196   790 YEELEERydflseqREDLEEARETLEEAIEEIDR 823
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
101-284 3.67e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 3.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209 101 LAAAESRHRKVILDLEEERQRHAQDTAEGDDVTYMLEKERERLTQQLEFEKSQVKKFEKEQKKLSSQLEEERSRHKQLSS 180
Cdd:COG4717   286 LALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQL 365

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209 181 MLVLE-----CKKATNKAAEEGQKAGELSLKLEKEKSRVSKLEEELAAERK-RGLQTEAQVEKQLSEfdiEREQLRAKLN 254
Cdd:COG4717   366 EELEQeiaalLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGeLEELLEALDEEELEE---ELEELEEELE 442

                         170       180       190
                  ....*....|....*....|....*....|
gi 1034560209 255 REENRTKTLKEEMESLKKIVKDLEASHQHS 284
Cdd:COG4717   443 ELEEELEELREELAELEAELEQLEEDGELA 472
Uso1_p115_C pfam04871
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ...
 163-269 4.19e-03

Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular transport factor, Transcytosis associate protein (TAP) and Vesicle docking protein, this myosin-shaped molecule consists of an N-terminal globular head region, a coiled-coil tail which mediates dimerization, and a short C-terminal acidic region. p115 tethers COP1 vesicles to the Golgi by binding the coiled coil proteins giantin (on the vesicles) and GM130 (on the Golgi), via its C-terminal acidic region. It is required for intercisternal transport in the golgi stack. This family consists of the acidic C-terminus, which binds to the golgins giantin and GM130. p115 is thought to juxtapose two membranes by binding giantin with one acidic region, and GM130 with another.


Pssm-ID: 461461 [Multi-domain]  Cd Length: 121  Bit Score: 37.76  E-value: 4.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209 163 KLSSQLEEERSRHKQLSSMLVLECKKATnKAAEEGQKAGELSLKLEKEKSRVSKLEEELAAERKRGLQTEAQVEKQLSEF 242
Cdd:pfam04871   1 AKKSELESEASSLKNENTELKAELQELS-KQYNSLEQKESQAKELEAEVKKLEEALKKLKAELSEEKQKEKEKQSELDDL 79

                          90       100
                  ....*....|....*....|....*..
gi 1034560209 243 DIEREQLRAKLNREENRTKTLKEEMES 269
Cdd:pfam04871  80 LLLLGDLEEKVEKYKARLKELGEEVLS 106
bHLH_TS_OLIG1 cd18942
basic helix-loop-helix (bHLH) domain found in oligodendrocyte transcription factor 1 (Oligo1) ...
 245-296 4.22e-03

basic helix-loop-helix (bHLH) domain found in oligodendrocyte transcription factor 1 (Oligo1) and similar proteins; Oligo1, also termed Class B basic helix-loop-helix protein 6 (bHLHb6), or Class E basic helix-loop-helix protein 21 (bHLHe21), is a bHLH transcription factor that promotes formation and maturation of oligodendrocytes, especially within the brain.


Pssm-ID: 381512  Cd Length: 75  Bit Score: 36.52  E-value: 4.22e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1034560209 245 EREQLRAKLN-REENRTKTLKEEMESLKKIVKDLEASHQHSSPNEQLKKPVTV 296
Cdd:cd18942     2 EQQQLRRKINsRERKRMQDLNLAMDALREVILPYSAAHCQSSPGRKLSKIATL 54
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
72-278 4.88e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.05  E-value: 4.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  72 KQPVCTNPLS------ILKVVMKQCKNMQERmLSQLAAAESRHRKVILDLEEErqrhaqdtaegddvtymLEKERERLTQ 145
Cdd:PRK03918  437 KCPVCGRELTeehrkeLLEEYTAELKRIEKE-LKEIEEKERKLRKELRELEKV-----------------LKKESELIKL 498

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209 146 QLEFEksQVKKFEKEQKKLSSQLEEERSRHKQLSSMLVLECKKATNKAAEEGQKAGELSLKLEKEKSRVSKLEEELAA-- 223
Cdd:PRK03918  499 KELAE--QLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAEll 576

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034560209 224 --ERKRGLQTEAQVEKQLSEFD-IEREQLRAK-----LNREENRTKTLKEEmesLKKIVKDLE 278
Cdd:PRK03918  577 keLEELGFESVEELEERLKELEpFYNEYLELKdaekeLEREEKELKKLEEE---LDKAFEELA 636
PRK09039 PRK09039
peptidoglycan -binding protein;
166-279 4.89e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 39.56  E-value: 4.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209 166 SQLEEERSRHKQLSSMLVLECKKATNKAAEEGQKAGELSlKLEKEKSRVSKLEEELAAERKRGLQTEAQVEKQLSefdiE 245
Cdd:PRK09039   53 SALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLS-AAEAERSRLQALLAELAGAGAAAEGRAGELAQELD----S 127

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1034560209 246 REQLRAklnREENRTKTLKEEMESLKKIVKDLEA 279
Cdd:PRK09039  128 EKQVSA---RALAQVELLNQQIAALRRQLAALEA 158
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 57-279 4.89e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 40.00  E-value: 4.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  57 LQRDFETLKEKNDGEKQPV--CTNPLSILKVVMKQCKNMQERMLSQLAAAESRHRKVILDLEEERQRHAQDTAEGDdvty 134
Cdd:TIGR04523 424 LEKEIERLKETIIKNNSEIkdLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELK---- 499

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209 135 MLEKERERLTQQLEFEKSQVKKFEKEQKKLSSQLEEERSRHKQLSSMLVlecKKATNKAAEegqkagelslKLEKEKSRV 214
Cdd:TIGR04523 500 KLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELN---KDDFELKKE----------NLEKEIDEK 566

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034560209 215 SKLEEELAAERKRGLQTEAQVEKQLSEFDIEREQLRAKLNREENRTKTLKEEMESLKKIVKDLEA 279
Cdd:TIGR04523 567 NKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSS 631
PRK05431 PRK05431
seryl-tRNA synthetase; Provisional
 153-223 5.27e-03

seryl-tRNA synthetase; Provisional


Pssm-ID: 235461 [Multi-domain]  Cd Length: 425  Bit Score: 39.67  E-value: 5.27e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034560209 153 QVKKFEKEQKKLSSQLEEERSRHKQLSsmlvleckKATNKAAEEGQKAGELSLKLEKEKSRVSKLEEELAA 223
Cdd:PRK05431   29 ELLELDEERRELQTELEELQAERNALS--------KEIGQAKRKGEDAEALIAEVKELKEEIKALEAELDE 91
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 18-227 5.50e-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: 39.36  E-value: 5.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  18 LEGELEARDLVIEALKAQHRDTfiEERYGKynISDPLMALQRDFETLKEKNDGEKQpvctnplSILKVVMKQCKNMQERM 97
Cdd:COG4942    53 LLKQLAALERRIAALARRIRAL--EQELAA--LEAELAELEKEIAELRAELEAQKE-------ELAELLRALYRLGRQPP 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  98 LSQLAAAES-----RHRKVILDLEEERQRHAQDTAEgddvtymLEKERERLTQQLEFEKSQVKKFEKEQKKLSSQLEEER 172
Cdd:COG4942   122 LALLLSPEDfldavRRLQYLKYLAPARREQAEELRA-------DLAELAALRAELEAERAELEALLAELEEERAALEALK 194

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1034560209 173 SRHKQLSSMLVLECKKATNKAAEEGQKAGELslklekeKSRVSKLEEELAAERKR 227
Cdd:COG4942   195 AERQKLLARLEKELAELAAELAELQQEAEEL-------EALIARLEAEAAAAAER 242
Filament pfam00038
Intermediate filament protein;
136-268 6.73e-03

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 39.13  E-value: 6.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209 136 LEKERERLTQQLEFEKsqvKKFEKEQKKLSSQLEEER-------SRHKQLSSMLV-----LECKKATNKA-AEE--GQKA 200
Cdd:pfam00038 122 LEAKIESLKEELAFLK---KNHEEEVRELQAQVSDTQvnvemdaARKLDLTSALAeiraqYEEIAAKNREeAEEwyQSKL 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209 201 GELSLKLEKEKSRVSKLEEELAAERKR--GLQTE--------AQVEKQLSE----FDIEREQLRAKLNREENRTKTLKEE 266
Cdd:pfam00038 199 EELQQAAARNGDALRSAKEEITELRRTiqSLEIElqslkkqkASLERQLAEteerYELQLADYQELISELEAELQETRQE 278


                  ..
gi 1034560209 267 ME 268
Cdd:pfam00038 279 MA 280
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 192-283 7.98e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.53  E-value: 7.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209 192 KAAEEGQKAGELSLKLEKEKSRVSKLEEELAAERKRglqtEAQVEKQLSEFDIEREQLRAKLNREENRTKTLKEEMESLK 271
Cdd:COG1196   219 KEELKELEAELLLLKLRELEAELEELEAELEELEAE----LEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294

                          90
                  ....*....|..
gi 1034560209 272 KIVKDLEASHQH 283
Cdd:COG1196   295 AELARLEQDIAR 306
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 83-271 8.13e-03

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 39.44  E-value: 8.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209   83 LKVVMKQCKNMQERMLSQLAAAESRHRKVILDLEEERQRHAQDTAEGDDVTYMLEKERERLTQQLEFEKSQVK-KFEKEQ 161
Cdd:pfam12128  324 LEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKdKLAKIR 403

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  162 KKLSSQLEEERSRHKQLSSMLVLECKKATNKAAEEGQ----KAGELSLKL-------------EKEKSRVSKLEEELAAE 224
Cdd:pfam12128  404 EARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYrlksRLGELKLRLnqatatpelllqlENFDERIERAREEQEAA 483

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1034560209  225 RKRglQTEAQVEkqLSEFDIEREQLRAKLNREENRTKTLKEEMESLK 271
Cdd:pfam12128  484 NAE--VERLQSE--LRQARKRRDQASEALRQASRRLEERQSALDELE 526
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 10-278 8.22e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 39.27  E-value: 8.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209   10 ELLTLFSILEGELEARDLVIEALKAQhRDTFIEERYgkyNISDPLMALQRDFETLKEK--NDGEKQPVCTNPLSILKVVM 87
Cdd:TIGR02168  765 ELEERLEEAEEELAEAEAEIEELEAQ-IEQLKEELK---ALREALDELRAELTLLNEEaaNLRERLESLERRIAATERRL 840

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209   88 KQCKNMQERMLSQLAAAESRhrkvILDLEEERQRHAQDTAEGDDVTYMLEKERERLTQQLEFEKSQVKKFEKEQKKLSSQ 167
Cdd:TIGR02168  841 EDLEEQIEELSEDIESLAAE----IEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRE 916

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  168 LEEERsrhkqlssmlvleckkatnkaaeegQKAGELSLKLEKEKSRVSKLEEELAAERKRGLQ----TEAQVEKQLSEFD 243
Cdd:TIGR02168  917 LEELR-------------------------EKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEeaeaLENKIEDDEEEAR 971

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1034560209  244 IEREQLRAKLNR--------------EENRTKTLKEEMESLKKIVKDLE 278
Cdd:TIGR02168  972 RRLKRLENKIKElgpvnlaaieeyeeLKERYDFLTAQKEDLTEAKETLE 1020
PTZ00121 PTZ00121
MAEBL; Provisional
 117-292 8.40e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.35  E-value: 8.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  117 EERQRHAQDTAEGDDVTYMLEKERERLTQQLEFEKSQVKKFEKEQKKLSSQLE---EERSRHKQLSSMLVLECKKA--TN 191
Cdd:PTZ00121  1332 DAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKkkaEEKKKADEAKKKAEEDKKKAdeLK 1411

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  192 KAAEEGQKAGELSLKLEkEKSRVSKLEEElAAERKRGLQTEAQVEKQLSEFDIEREQLRAKLNREENRTKTLKEEMESLK 271
Cdd:PTZ00121  1412 KAAAAKKKADEAKKKAE-EKKKADEAKKK-AEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAK 1489

                          170       180
                   ....*....|....*....|.
gi 1034560209  272 KIVKDLEASHQHSSPNEQLKK 292
Cdd:PTZ00121  1490 KKAEEAKKKADEAKKAAEAKK 1510
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
95-282 8.67e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.51  E-value: 8.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209   95 ERMLSQLAAAESRHRKVildLEEERQRHAQDTAEGDDVTYmlEKERERLtQQLEFEKSQVKKFEKEQKK--LSSQLEEER 172
Cdd:COG4913    228 DALVEHFDDLERAHEAL---EDAREQIELLEPIRELAERY--AAARERL-AELEYLRAALRLWFAQRRLelLEAELEELR 301

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560209  173 SRHKQLssmlvlECKKATNKAAEEGQKAGELSLKLEKEKS---RVSKLEEELAA---ERKRGLQTEAQVEKQLSEFDIE- 245
Cdd:COG4913    302 AELARL------EAELERLEARLDALREELDELEAQIRGNggdRLEQLEREIERlerELEERERRRARLEALLAALGLPl 375

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1034560209  246 ----------REQLRAKLNREENRTKTLKEEMESLKKIVKDLEASHQ 282
Cdd:COG4913    376 pasaeefaalRAEAAALLEALEEELEALEEALAEAEAALRDLRRELR 422
 
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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