|
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 2462511474 5 KLSKPELLTLFSILEGELEARDLVIEALKAQH-RDTFIEERYGKYNISDPLMALQRDFETLKEKNDGEKQP--VCTNPLS 81
Cdd:pfam09727 1 DLSKDDLLKLLSILEGELQARDIVIAVLKAEKvKQLLLEARYGFKYPSDPLLALQRDSELLRDQSQDEDVYeaMYEKPLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 82 ILKVVMKQCKNMQERMLSQLAAAESRHRKVILDLEEERQRHAQDTAEGDDVTYMLEKERERLTQQLEFEKSQVKKFEKEQ 161
Cdd:pfam09727 81 ELEKLVEKQRETQRRMLEQLAAAEKRHRRVIRELEEEKRKHARDTAQGDDFTYLLEKERERLKQELEQEKAQQKRLEKEL 160
|
170 180
....*....|....*....|....*..
gi 2462511474 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 2462511474 94 QERMLSQLAAAESRhrkvildLEEERQRHAQDTAEGDDVT---YMLEKERERLTQQLEFEKSQVKKFEKEQKKLSSQLEE 170
Cdd:COG1196 255 LEELEAELAELEAE-------LEELRLELEELELELEEAQaeeYELLAELARLEQDIARLEERRRELEERLEELEEELAE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 171 ERSRHKQLSSMLVLECKKATNKAAEEGQKAGELSlKLEKEKSRVSKLEEELAAERKRGLQTEAQVEKQLSEFDIEREQLR 250
Cdd:COG1196 328 LEEELEELEEELEELEEELEEAEEELEEAEAELA-EAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE 406
|
170 180
....*....|....*....|....*....
gi 2462511474 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 2462511474 100 QLAAAESRHRKVILDLEEERQRHAQDTAEGDDVTYMLEKERERLTQQLEFEKSQVKKFEKEQKKLSSQLEEERSRHKQLS 179
Cdd:TIGR02168 744 QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLR 823
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 180 SmlvlECKKATNKAAEEGQKAGELSLKLEKEKSRVSKLEEELAAERkrglQTEAQVEKQLSEFDIEREQLRAKLNREENR 259
Cdd:TIGR02168 824 E----RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELE----ELIEELESELEALLNERASLEEALALLRSE 895
|
170 180
....*....|....*....|....
gi 2462511474 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 2462511474 94 QERMLSQLAAAESRHRKVILDLEEERQRHAQdtaegddvtymLEKERERLTQQLEFEKSQVKKFE--KEQKKLSSQLEEE 171
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEELEE-----------LEAELEELREELEKLEKLLQLLPlyQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 172 RSRHKQLSsmlvleckkatnkaaEEGQKAGELSLKLEKEKSRVSKLEEELAAERKrglQTEAQVEKQLSEFDIEREQLRA 251
Cdd:COG4717 145 PERLEELE---------------ERLEELRELEEELEELEAELAELQEELEELLE---QLSLATEEELQDLAEELEELQQ 206
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2462511474 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 2462511474 98 LSQLAAAESRHRKVILDLEEERQRHAQDTAEGDDVTYMLEKERERLTQQLEFEKSQVKKFEKEQKKLSSQLEEERSRHKQ 177
Cdd:COG1196 283 LEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 178 LSSMLVLECKKATNKAAEEGQKAGELS------LKLEKEKSRVSKLEEELAAERKRGLQTEAQVEKQLSEFDIEREQLRA 251
Cdd:COG1196 363 AEEALLEAEAELAEAEEELEELAEELLealraaAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE 442
|
170 180 190
....*....|....*....|....*....|.
gi 2462511474 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 2462511474 91 KNMQERMLSQLAAAE-SRHRKVILDLEEERQRHAQDTAEGDDVTymLEKERERLTQQLEFEKSQVKKFEKEQKKLSSQL- 168
Cdd:PTZ00121 1576 KNMALRKAEEAKKAEeARIEEVMKLYEEEKKMKAEEAKKAEEAK--IKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELk 1653
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 169 ---EEERSRHKQLSSMLVLECKKA--TNKAAEEGQKAGELSLKLEKEKSRVSKLEEELAAERKRGlqteAQVEKQLSEFD 243
Cdd:PTZ00121 1654 kaeEENKIKAAEEAKKAEEDKKKAeeAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKA----EELKKAEEENK 1729
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2462511474 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 2462511474 96 RMLSQLAAAESRhrkvILDLEEERQRHAQDTAEgddvtymLEKERERLTQQLEFEKSQVKKFEKEQKKLSSQLEEERSRH 175
Cdd:COG1579 7 RALLDLQELDSE----LDRLEHRLKELPAELAE-------LEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 176 KQLSSMLvleckkATNKAAEEgQKAgeLSLKLEKEKSRVSKLEEEL--AAERKRGLQTE-AQVEKQLSEfdiEREQLRAK 252
Cdd:COG1579 76 KKYEEQL------GNVRNNKE-YEA--LQKEIESLKRRISDLEDEIleLMERIEELEEElAELEAELAE---LEAELEEK 143
|
170 180
....*....|....*....|....*...
gi 2462511474 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 2462511474 95 ERMLSQLAAAESRHRKVILDLEEERQRHAQDTAEGddvtymLEKERERLTQQLEFEKSQVKKFEKEQKKLSSQLEEERSR 174
Cdd:COG1196 223 KELEAELLLLKLRELEAELEELEAELEELEAELEE------LEAELAELEAELEELRLELEELELELEEAQAEEYELLAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 175 HKQLSSMLVLECKKATNKAAEEGQKAGELSL---KLEKEKSRVSKLEEELA---AERKRGLQTEAQVEKQLSEFDIEREQ 248
Cdd:COG1196 297 LARLEQDIARLEERRRELEERLEELEEELAEleeELEELEEELEELEEELEeaeEELEEAEAELAEAEEALLEAEAELAE 376
|
170 180 190
....*....|....*....|....*....|....
gi 2462511474 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 2462511474 109 RKVILDLEEERQRHAQDTAEGDDVTYMLEKERERLTQQLEfeksQVKKFEKEQKKLSSQLEEERSRHKQlssmlvlECKK 188
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELE----QLRKELEELSRQISALRKDLARLEA-------EVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 189 ATNKAAEEGQKAGELSLKLEKEKSRVSKLEEELAAERKRGLQTEAQVEKQLSEFDIEREQLRAkLNREENRTK----TLK 264
Cdd:TIGR02168 745 LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDE-LRAELTLLNeeaaNLR 823
|
170
....*....|....*.
gi 2462511474 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 2462511474 50 ISDPLMALQRDFETLKEKNDGEKQPVctnplSILKVVMKQCKNMQERMLSQLAAAESRHRKV---ILDLEEERQRHAQDT 126
Cdd:TIGR02169 679 LRERLEGLKRELSSLQSELRRIENRL-----DELSQELSDASRKIGEIEKEIEQLEQEEEKLkerLEELEEDLSSLEQEI 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 127 AEGDDVTYMLEKERERLTQQLEFEKSQVKKFE--------KEQKKLSSQLEEERSR-HKQLSSMLVLECKKATNKAAEEG 197
Cdd:TIGR02169 754 ENVKSELKELEARIEELEEDLHKLEEALNDLEarlshsriPEIQAELSKLEEEVSRiEARLREIEQKLNRLTLEKEYLEK 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 198 QKAGELSLKLE---KEKSRVSKLE------EELAAERKRGLQTEAQVEKQLSEFDIEREQLRAKLNREENRTKTLKEEME 268
Cdd:TIGR02169 834 EIQELQEQRIDlkeQIKSIEKEIEnlngkkEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIE 913
|
250
....*....|.
gi 2462511474 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 2462511474 103 AAESRHRKVILDLEEERQ----RHAQDTAEGDDVtymleKERERLTQQLEFEKSQVKKFEKEQKKLS-------SQLEEE 171
Cdd:PTZ00121 1518 AEEAKKADEAKKAEEAKKadeaKKAEEKKKADEL-----KKAEELKKAEEKKKAEEAKKAEEDKNMAlrkaeeaKKAEEA 1592
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 172 RSRHKQLSSMLVLECKKATNKAAEEGQKAGELSLKLEKEKSRVSKLEEELAAERKRGlqteAQVEKQLSEFDIEREQLRA 251
Cdd:PTZ00121 1593 RIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKA----EELKKAEEENKIKAAEEAK 1668
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2462511474 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 2462511474 80 LSILKVVMKQCKNMQERMLSQLAAAESRHR-------KVILDLEEERQRHAQDTAEGDDVT---YMLEKERERLTQQLEF 149
Cdd:TIGR02168 227 LALLVLRLEELREELEELQEELKEAEEELEeltaelqELEEKLEELRLEVSELEEEIEELQkelYALANEISRLEQQKQI 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 150 EKSQVKKFEKEQKKLSSQLEEERSRhkqlssmlvLECKKAtnKAAEEGQKAGELSLKLEKEKSRVSKLEEELAAerkrgl 229
Cdd:TIGR02168 307 LRERLANLERQLEELEAQLEELESK---------LDELAE--ELAELEEKLEELKEELESLEAELEELEAELEE------ 369
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462511474 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 2462511474 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 2462511474 94 QERMLSQLAAAESRHRKVILDLEEERQRHAQDTAEGDDVTYMLEKERERLTQQLEFEKSQVKKFEKEQKKLSSQLEEERS 173
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 174 ----------RHKQLSSMLVLECKKATNKAAEEGQKAGELS-------LKLEKEKSRVSKLEEELAAERKRGLQTEAQVE 236
Cdd:COG4942 105 elaellralyRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAparreqaEELRADLAELAALRAELEAERAELEALLAELE 184
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2462511474 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 2462511474 87 MKQCKNMQERMLSQLAAAESRHRKVILDLEEERQRHAQDTAEGDDVTYML---EKERERLTQQLEFEKSQVKKFEKEQKK 163
Cdd:pfam05483 396 MTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLqarEKEIHDLEIQLTAIKTSEEHYLKEVED 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 164 LSSQLEEERSRHKQLSS---MLVLECKKATnkaaeegQKAGELSLKLEKEKSRV---SKLEEELAAERKRGLQTEAQVEK 237
Cdd:pfam05483 476 LKTELEKEKLKNIELTAhcdKLLLENKELT-------QEASDMTLELKKHQEDIincKKQEERMLKQIENLEEKEMNLRD 548
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2462511474 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 2462511474 56 ALQRDFETLKEKNDGEKQpvctnplsILKVVMKQCKNMQErmlsQLAAAESRHRKVILDLEE-ERQRHAQDTAEGDDVTY 134
Cdd:TIGR02169 720 EIEKEIEQLEQEEEKLKE--------RLEELEEDLSSLEQ----EIENVKSELKELEARIEElEEDLHKLEEALNDLEAR 787
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 135 MLEKERERLTQQLEFEKSQVKKFEK---------EQKKLSSQLEEERSRHKQlSSMLVLECKKATNKAAEEGQKA--GEL 203
Cdd:TIGR02169 788 LSHSRIPEIQAELSKLEEEVSRIEArlreieqklNRLTLEKEYLEKEIQELQ-EQRIDLKEQIKSIEKEIENLNGkkEEL 866
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462511474 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 2462511474 94 QERMLSQLAAAESRHRKVILDLEE-ERQRHAQDTAEGDDVTYMLEKERERLTQQLEFEKSQVKKFEKEQKKLSSQLEEER 172
Cdd:COG4913 250 QIELLEPIRELAERYAAARERLAElEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 173 SRHKQLSSMLVLECKKatnKAAEEGQKAGELSLKLEKEKSRVSKLEEELAAERKRGLQTEAQVEKQLSEFDIEREQLRAK 252
Cdd:COG4913 330 AQIRGNGGDRLEQLER---EIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEA 406
|
170 180
....*....|....*....|....*....
gi 2462511474 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 2462511474 22 LEARDLVIEALKAQhRDTFIEERYG--KYnisDPLMALQRDFET---LKEKNDGEKQPV-CTNPLSILKVVMKQCKNMQE 95
Cdd:TIGR02169 186 IERLDLIIDEKRQQ-LERLRREREKaeRY---QALLKEKREYEGyelLKEKEALERQKEaIERQLASLEEELEKLTEEIS 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 96 RMLSQLAAAESRHRKV---ILDLEEERQRHAQDTAEGddvtymLEKERERLTQQLEFEKSQVKKFEKEQKKLSSQLEEER 172
Cdd:TIGR02169 262 ELEKRLEEIEQLLEELnkkIKDLGEEEQLRVKEKIGE------LEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLL 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 173 SRHKQLSsmlvlecKKATNKAAEEGQKAGELSLKLEKEKSRVSKLEEElAAERKRGLQTEAQVEKQLSEFDIEREQLRAK 252
Cdd:TIGR02169 336 AEIEELE-------REIEEERKRRDKLTEEYAELKEELEDLRAELEEV-DKEFAETRDELKDYREKLEKLKREINELKRE 407
|
250 260
....*....|....*....|....*....
gi 2462511474 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 2462511474 21 ELEARDLVIEALKAqhRDTFIEERYGKYNISDPL-MALQRDFETLK-EKNDGEKQPVCTNPLSILKVVMKQCKNMQ---- 94
Cdd:pfam17380 311 EVERRRKLEEAEKA--RQAEMDRQAAIYAEQERMaMERERELERIRqEERKRELERIRQEEIAMEISRMRELERLQmerq 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 95 ---ERMLSQLAAA-------ESRHRKVILDLEEERQRHAQDTAEGDDVTYMLEKERER---------LTQQLEFEKSQVK 155
Cdd:pfam17380 389 qknERVRQELEAArkvkileEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERARemervrleeQERQQQVERLRQQ 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 156 KFEKEQKKLSSQLEEERSRHKQLSSMLVLECKKATNKAA--EEGQKAGELSLKLEKEKSRVSKLEEELAAERKRGLQTEA 233
Cdd:pfam17380 469 EEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAmiEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEM 548
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2462511474 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 2462511474 137 EKERERLTQQLEFEKSQVKKFEKEQKKLSSQLEEERSRHKQLSSmlvleckkatnKAAEEGQKAGELSLKLEKEKSRVSK 216
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRK-----------ELEELSRQISALRKDLARLEAEVEQ 744
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462511474 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 2462511474 52 DPLMALQRDfETLKEKNDGEKQPVCTNPLSILKVVMKQCKNMQERML--SQLAAAESRHRKV--ILDLEEERQRHAQDTA 127
Cdd:PTZ00121 1575 DKNMALRKA-EEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIkaEELKKAEEEKKKVeqLKKKEAEEKKKAEELK 1653
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 128 EGDDVTYMLEKERERLTQQLEFEKSQVKKFEKEQKKLSSQL---EEERSRHKQLSSMLVLECKKA--TNKAAEEGQ-KAG 201
Cdd:PTZ00121 1654 KAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALkkeAEEAKKAEELKKKEAEEKKKAeeLKKAEEENKiKAE 1733
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462511474 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 2462511474 1 MNLEKLSKPELLTLFSILEGELEARDLVIEALKAQHRdtfIEERYGKYNISDPLMALQRDFETLKEKNDGEKQPVCTNPL 80
Cdd:pfam02463 659 AEKSEVKASLSELTKELLEIQELQEKAESELAKEEIL---RRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKIN 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 81 SILKVvmKQCKNMQERMLSQLAAAESR-------HRKVILDLEEERQRHAQ-DTAEGDDVTYMLEKERER--LTQQLEFE 150
Cdd:pfam02463 736 EELKL--LKQKIDEEEEEEEKSRLKKEekeeeksELSLKEKELAEEREKTEkLKVEEEKEEKLKAQEEELraLEEELKEE 813
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 151 KSQVKKFEKEQKKLSSQLEEERSRHKQLSSMLvlecKKATNKAAEEGQKAGELSLKLEKEKSRVSKLEEELAAERKRGLQ 230
Cdd:pfam02463 814 AELLEEEQLLIEQEEKIKEEELEELALELKEE----QKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELE 889
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2462511474 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 2462511474 91 KNMQERMLSQLAAAESRHRKVILDLEEERQR---HAQDTAEGDDVTYMLEKERERLTQQLEFEKSQVKKFEKEQKKLSSQ 167
Cdd:pfam17380 359 KRELERIRQEEIAMEISRMRELERLQMERQQkneRVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVR 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 168 -LEEERSRHKQLSSMLVLECKKATNKAAEEGQKAGELSLKLEKEKSRVSKLEEElaaeRKRGLQTEAQVEKQlsefdier 246
Cdd:pfam17380 439 rLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQ----RRKILEKELEERKQ-------- 506
|
170 180 190
....*....|....*....|....*....|..
gi 2462511474 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 2462511474 136 LEKERERLTQ---QLEFEKSQVKKFEKEQKKLSSQLEEERSRHKQLSSMlVLECKKATNKAaEEGQKAGELSLKLEKEKS 212
Cdd:PRK03918 233 LEELKEEIEElekELESLEGSKRKLEEKIRELEERIEELKKEIEELEEK-VKELKELKEKA-EEYIKLSEFYEEYLDELR 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 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 2462511474 95 ERMLSQLAAAESRHRKVILDLEEERQRHAQDTAEGDDVTYMLEKERERLTQQLEFEKSQVKKFEKEQKKLSSQLEEERSR 174
Cdd:PRK02224 271 EREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLRED 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 175 HKQLSSmlvlECKKATNKAAEEGQKAGELSLKLEKEKSRVSKLEEELAAERKRGLQTEAQVEKqLSEFdieREQLRAKLN 254
Cdd:PRK02224 351 ADDLEE----RAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGN-AEDF---LEELREERD 422
|
170 180
....*....|....*....|....*
gi 2462511474 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 2462511474 104 AESRHRKVILDLEEERQRHAQDTAEGDDVTYMLEKERERLTQQLEfeksQVKKFEKEQKKLSSQLEEERSRHKQLSSMLV 183
Cdd:PRK03918 163 AYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLR----EINEISSELPELREELEKLEKEVKELEELKE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 184 LECKKATNKAAEEGQKAG-------------ELSLKLEKEKSRVSKLEE---------ELAAERKRGLQTEAQVEKQLSE 241
Cdd:PRK03918 239 EIEELEKELESLEGSKRKleekireleerieELKKEIEELEEKVKELKElkekaeeyiKLSEFYEEYLDELREIEKRLSR 318
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2462511474 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 2462511474 130 DDVTYMLEKERERLTQQlefeKSQVKKFekeqKKLSSQLEEersRHKQLssmLVLECKKATNKAAEEGQKAGELSLKLEK 209
Cdd:COG1196 192 EDILGELERQLEPLERQ----AEKAERY----RELKEELKE---LEAEL---LLLKLRELEAELEELEAELEELEAELEE 257
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462511474 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 2462511474 95 ERMLSQLAAAESRHRKVILDLEE--------ERQRHA----QDTAEGDDVTYMLEKERERLTQQLEfeksQVKKFEKEQK 162
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEAleaeldalQERREAlqrlAEYSWDEIDVASAEREIAELEAELE----RLDASSDDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 163 KLSSQLEEERSRHKQLSSmlvlECKKATNKAAEEGQKAGELSLKLEKEKSRVSKLEE-------ELAAERKRGLQTEAQV 235
Cdd:COG4913 689 ALEEQLEELEAELEELEE----ELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDlarlelrALLEERFAAALGDAVE 764
|
170 180
....*....|....*....|....
gi 2462511474 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 2462511474 96 RMLSQLAAAESRHRKVILDLEEERQRHAQDTAEgddVTYMLEKERERLTQQLEFEKSQVK----KFEKEQKKLSSQL--- 168
Cdd:PTZ00121 1552 KKAEELKKAEEKKKAEEAKKAEEDKNMALRKAE---EAKKAEEARIEEVMKLYEEEKKMKaeeaKKAEEAKIKAEELkka 1628
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 169 EEERSRHKQLSSMLVLECKKA--TNKAAEEGQ-KAGELSLKLEKEKSRVSKLEEELAAERKRGLQTEAQVEKQLsefdiE 245
Cdd:PTZ00121 1629 EEEKKKVEQLKKKEAEEKKKAeeLKKAEEENKiKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAK-----K 1703
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462511474 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 2462511474 91 KNMQERML---SQLAAAESRHRKVILD---LEEERQRHAQDTAEGDDVTYMLEKER----ERL---TQQLEFEKSQVK-- 155
Cdd:pfam01576 99 KKMQQHIQdleEQLDEEEAARQKLQLEkvtTEAKIKKLEEDILLLEDQNSKLSKERklleERIsefTSNLAEEEEKAKsl 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 156 -KFEKEQKKLSSQLEEERSRHKQLSSMLVLECKKATNKAAEEGQKAGELSLKLEKEKSRVSKLEEELAAERKRGLQTEAQ 234
Cdd:pfam01576 179 sKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQ 258
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2462511474 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 2462511474 91 KNMQERMLSQLAAAESRHRKVILDLEEERQRHAQDTAEGDDVTYMLEKERERLTQQLEFEKSQVKKFEKEqkklssqlEE 170
Cdd:PTZ00121 1559 KAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA--------EE 1630
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 171 ERSRHKQLSSMLVLECKKA--TNKAAEEGQ-KAGELSLKLEKEKSRVSKLEEELAAERKRGLQTE---------AQVEKQ 238
Cdd:PTZ00121 1631 EKKKVEQLKKKEAEEKKKAeeLKKAEEENKiKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKkeaeeakkaEELKKK 1710
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2462511474 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 2462511474 113 LDLEEERQRHAQDTAEGDDVTYMLEKERERLTQQLEFEKSQVKKFEKEQKKLSSQLEEERSRHKQLSSMLvlecKKATNK 192
Cdd:COG4372 13 LSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL----EELNEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 193 AAEEGQKAGELSLKLEKEKSRVSKLEEELAAerkrgLQTE-AQVEKQLSEFDIEREQLRAKLNREENRTKTLKEEMESLK 271
Cdd:COG4372 89 LQAAQAELAQAQEELESLQEEAEELQEELEE-----LQKErQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQ 163
|
170 180
....*....|....*....|.
gi 2462511474 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 2462511474 65 KEKNDGEKQPVCTNPLSILKVVMKQCKNMQERMLSQLAAAESRHRKVILDLEEER------QRHAQDTAEGDDVTYMLE- 137
Cdd:PTZ00121 1247 EERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKkkadeaKKKAEEAKKADEAKKKAEe 1326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 138 --KERERLTQQLEFEK--SQVKKFEKEQKKLSSQLEEERSRHKQLSSMLVLECKKATNKAAEEGQKAGELSLKLEKEKSR 213
Cdd:PTZ00121 1327 akKKADAAKKKAEEAKkaAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKK 1406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 214 VSKLEEELAAERK-RGLQTEAQVEKQLSEFDIEREQLR----AKLNREENR-TKTLKEEMESLKKiVKDLEASHQHSSPN 287
Cdd:PTZ00121 1407 ADELKKAAAAKKKaDEAKKKAEEKKKADEAKKKAEEAKkadeAKKKAEEAKkAEEAKKKAEEAKK-ADEAKKKAEEAKKA 1485
|
250
....*....|....*.
gi 2462511474 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 2462511474 136 LEKERERLTQQLEFEKSQVKKFEKEQKKLSSQLEEERSRHKQLSSMLVlECKKATNKAAEEGQKAGELSLKLEKEKSRVS 215
Cdd:COG4372 43 LQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQ-AAQAELAQAQEELESLQEEAEELQEELEELQ 121
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462511474 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 2462511474 20 GELEARdlvIEALKAQHrdtfiEERYGKYNISDPLMALQRDFETLKEKNDgekqpvctnplSILKVVMKQCKNMQERmls 99
Cdd:PRK02224 478 EELEAE---LEDLEEEV-----EEVEERLERAEDLVEAEDRIERLEERRE-----------DLEELIAERRETIEEK--- 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 100 QLAAAESRHRKVILDLEEERQRHAQDTAEGDdvtymLEKERERltqqlefeksqVKKFEKEQkklsSQLEEERSRHKQLS 179
Cdd:PRK02224 536 RERAEELRERAAELEAEAEEKREAAAEAEEE-----AEEAREE-----------VAELNSKL----AELKERIESLERIR 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 180 SMLVLeckkatnkAAEEGQKAGELSLKLE-------------KEKS-RVSKLEEELAAERKRGLQTE--------AQVEK 237
Cdd:PRK02224 596 TLLAA--------IADAEDEIERLREKREalaelnderrerlAEKReRKRELEAEFDEARIEEAREDkeraeeylEQVEE 667
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2462511474 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 2462511474 136 LEKERERLTQQLEFEKSQVKK----FEKEQKKLSSQ---LEEERSRHKQLSSMLVLECKKATNKAAEEGQKAGELSLKLE 208
Cdd:pfam07888 46 LLQAQEAANRQREKEKERYKRdreqWERQRRELESRvaeLKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 209 KEKSRVSKLEEELAAERKRGLQTEAQVEK----------QLSEFDIEREQLRAKLNREENRTKTLKEEMESLK------- 271
Cdd:pfam07888 126 AHEARIRELEEDIKTLTQRVLERETELERmkerakkagaQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRnslaqrd 205
|
170 180 190
....*....|....*....|....*....|..
gi 2462511474 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 2462511474 131 DVTYMLEKERERLTQQ----------LEFEKSQVKKFEKEQKKLSSQLEEERSRHKQLSSMLVLECKKATNKAAEEGQKA 200
Cdd:PRK03918 307 DELREIEKRLSRLEEEingieerikeLEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTP 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 201 GELSLKLEKEKSRVSKLEEELA--AERKRGLQTE-AQVEKQLSEF---------------DIEREQL----RAKLNREEN 258
Cdd:PRK03918 387 EKLEKELEELEKAKEEIEEEISkiTARIGELKKEiKELKKAIEELkkakgkcpvcgreltEEHRKELleeyTAELKRIEK 466
|
170 180
....*....|....*....|
gi 2462511474 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 2462511474 3 LEKLSKpELLTLFSILEGELEARDL--VIEALKAqhrdtfIEERYGKYNISDpLMALQRDFETLKEKNDGEKqpvctnpl 80
Cdd:PRK03918 475 ERKLRK-ELRELEKVLKKESELIKLkeLAEQLKE------LEEKLKKYNLEE-LEKKAEEYEKLKEKLIKLK-------- 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 81 silkvvmKQCKNMQERmLSQLAAAESRHRKVILDLEEerqrhaqdtaegddvtymLEKERERLTQQLEfeksqvKKFEKE 160
Cdd:PRK03918 539 -------GEIKSLKKE-LEKLEELKKKLAELEKKLDE------------------LEEELAELLKELE------ELGFES 586
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 161 QKKLSSQLEEERSRHKQLssmlvLECKKATnKAAEEGQKagelslKLEKEKSRVSKLEEELAAERKRGLQTEAQVEKQLS 240
Cdd:PRK03918 587 VEELEERLKELEPFYNEY-----LELKDAE-KELEREEK------ELKKLEEELDKAFEELAETEKRLEELRKELEELEK 654
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2462511474 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 2462511474 88 KQCKNMQERMLSQLAAAESRHRKVILDLEEERQRHAQDTAEGDDVTYMLEKERERLTQQLEFEKSQVKKFEKEQKKLSSQ 167
Cdd:pfam02463 214 QLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAK 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 168 LEEERSRHKQLssmLVLECKKATNKAAEEGQKAGELSLKLEKEKSRVSKLEEELAAERKRGLQTEAQVEKQlsefdieRE 247
Cdd:pfam02463 294 EEEELKSELLK---LERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEEL-------EK 363
|
170 180 190
....*....|....*....|....*....|....*
gi 2462511474 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 2462511474 98 LSQLAAAESRHRKVILDLEEERQRHA----QDTAEgddvtyMLEKERErLTQQLefeKSQVKKFEKEQKKLSSQLEEERS 173
Cdd:COG3096 943 YLQAKEQQRRLKQQIFALSEVVQRRPhfsyEDAVG------LLGENSD-LNEKL---RARLEQAEEARREAREQLRQAQA 1012
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 174 RHKQLSSMLV-----LECKKATNKAAEEGQKAGELSLKLEKE---KSRVSKLEEELAAERKRglqtEAQVEKQLSEFDIE 245
Cdd:COG3096 1013 QYSQYNQVLAslkssRDAKQQTLQELEQELEELGVQADAEAEeraRIRRDELHEELSQNRSR----RSQLEKQLTRCEAE 1088
|
170 180
....*....|....*....|....*..
gi 2462511474 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 2462511474 136 LEKERERLTQQLEFEKSQVKKFEKEQKKLSSQLEEERSRHKQLSSMLvlecKKATNKAAEEGQKAGELSLKLEKEKSRVS 215
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRI----RALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 216 KLEEELaAERKRGLQTEAQVE---------------------KQLSEFDIER-EQLRAKLNREENRTKTLKEEMESLKKI 273
Cdd:COG4942 101 AQKEEL-AELLRALYRLGRQPplalllspedfldavrrlqylKYLAPARREQaEELRADLAELAALRAELEAERAELEAL 179
|
....*....
gi 2462511474 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 2462511474 114 DLEEERQRHAQDTAEGDDVTYmleKERERLTQQLEFEKSQVKKFEKEQKKLSSQLEEERSRHKQLSSMLVLECKKATNKA 193
Cdd:COG1196 626 TLVAARLEAALRRAVTLAGRL---REVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAE 702
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462511474 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 2462511474 83 LKVVMKQCKNMQERMLSQLAAAESRHRKVILDLEEERQRHAQDTAEGDDVTymLEKERERLTQQLEFEKSQVKKFEKEQK 162
Cdd:COG1579 36 LEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR--NNKEYEALQKEIESLKRRISDLEDEIL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 163 KLSSQLEEERSRhkqlssmlvleckkatnkaaeegqkagelslkLEKEKSRVSKLEEELAAERKRGLQTEAQVEKQLSEF 242
Cdd:COG1579 114 ELMERIEELEEE--------------------------------LAELEAELAELEAELEEKKAELDEELAELEAELEEL 161
|
170
....*....|....
gi 2462511474 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 2462511474 12 LTLFSILEGELEARDLVIealkaqhrdtFIEERYGKYNISDPLMALQRdfETLKEKNdgEKQPVCTNPLSILKVVMKQCK 91
Cdd:pfam05483 244 LLLIQITEKENKMKDLTF----------LLEESRDKANQLEEKTKLQD--ENLKELI--EKKDHLTKELEDIKMSLQRSM 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 92 NMQERMLSQLAAAEsrhrKVILDLEEERQRHAQDT-----------AEGDDVTYMLEKERERLTQQLEFEKSQVKKFEKE 160
Cdd:pfam05483 310 STQKALEEDLQIAT----KTICQLTEEKEAQMEELnkakaahsfvvTEFEATTCSLEELLRTEQQRLEKNEDQLKIITME 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 161 QKKLSSQLEEersrhkqlssmlVLECKKATNKAAEEGQKAGELSLKLEKEKSRVSKLEEELAAERKRGLQTEAQVEKQLS 240
Cdd:pfam05483 386 LQKKSSELEE------------MTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIH 453
|
250 260 270
....*....|....*....|....*....|....*...
gi 2462511474 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 2462511474 149 FEKSQVKKFEKEQKKLSSQLEEERSRHKQLSSMLVLECKkatnkaaeegQKAGELSLKLEKEksrVSKLEEELAAERKRG 228
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAK----------EEIHKLRNEFEKE---LRERRNELQKLEKRL 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2462511474 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 2462511474 21 ELEARDLVIEALKAQHRDtfIEERYGKYnISDPLMALQRDFETLKEKNDGEKQPVCTNPLSILKVVMKQCKNMQERMLSQ 100
Cdd:pfam12128 355 ELENLEERLKALTGKHQD--VTAKYNRR-RSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAG 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 101 LAAAESRHRKVILDLEEERQRHAQDTAEGDDVTYM------LEKERERLTQ------QLEFEKSQVKK-FEKEQKKL--- 164
Cdd:pfam12128 432 KLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLenfderIERAREEQEAanaeveRLQSELRQARKrRDQASEALrqa 511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 165 SSQLEEERSRHKQLSSMLV----------------------------LECKKATNKAAEEGQKAGELSL----------- 205
Cdd:pfam12128 512 SRRLEERQSALDELELQLFpqagtllhflrkeapdweqsigkvispeLLHRTDLDPEVWDGSVGGELNLygvkldlkrid 591
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 206 -----KLEKE-KSRVSKLEEELAAERKRGLQTE---AQVEKQLSEFDIEREQLRAKLNREENRTKTLKEEMESLKKIVKD 276
Cdd:pfam12128 592 vpewaASEEElRERLDKAEEALQSAREKQAAAEeqlVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNK 671
|
330
....*....|....*.
gi 2462511474 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 2462511474 116 EEERQRHAQDTAEGDDVTYMLEKERERLT-------QQLEFEKSQVKKFEKEQKkLSSQLEEERSR------HKQLSSML 182
Cdd:pfam15709 358 EEQRRLQQEQLERAEKMREELELEQQRRFeeirlrkQRLEEERQRQEEEERKQR-LQLQAAQERARqqqeefRRKLQELQ 436
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462511474 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 2462511474 62 ETLKEKNDGEKQ-PVCTNPLSILKVVMKQCKNMQER----------MLSQLAAAESRHRKV--ILDLEEERQRHAQDTA- 127
Cdd:PRK03918 304 EYLDELREIEKRlSRLEEEINGIEERIKELEEKEERleelkkklkeLEKRLEELEERHELYeeAKAKKEELERLKKRLTg 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 128 -EGDDVTYML---EKERERLTQQLE---FEKSQVKKFEKEQKKLSSQLEEERSR-----------HKQlssMLVLECKKA 189
Cdd:PRK03918 384 lTPEKLEKELeelEKAKEEIEEEISkitARIGELKKEIKELKKAIEELKKAKGKcpvcgrelteeHRK---ELLEEYTAE 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 190 TNKAAEEGQKAGELSLKLEKEKSRVSKL---EEELAAERKRGLQTEAqVEKQLSEFDIER--------EQLRAKLNREEN 258
Cdd:PRK03918 461 LKRIEKELKEIEEKERKLRKELRELEKVlkkESELIKLKELAEQLKE-LEEKLKKYNLEElekkaeeyEKLKEKLIKLKG 539
|
250 260
....*....|....*....|.
gi 2462511474 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 2462511474 104 AESRHRKVILDLEEERQRHAQDTaegddvtymlEKERERLTQQLEFEksqVKKfekEQKKLSSQLEEE-RSRHKQLSSml 182
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEEA----------KKEAEAIKKEALLE---AKE---EIHKLRNEFEKElRERRNELQK-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 183 vLECKkatNKAAEEgqkagelslKLEKEKSRVSKLEEELAAERKRGLQTEAQVEKQLSEFDIEREQLRAKLNR------E 256
Cdd:PRK12704 87 -LEKR---LLQKEE---------NLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERisgltaE 153
|
170
....*....|...
gi 2462511474 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 2462511474 84 KVVMKQCKNMQERMLSQLAAAEsrHRKVILDLEEERQRHAQDTAEGDDVTY--MLEKERERLTQQLEF--EKSQVKKFEK 159
Cdd:pfam13868 31 KKRIKAEEKEEERRLDEMMEEE--RERALEEEEEKEEERKEERKRYRQELEeqIEEREQKRQEEYEEKlqEREQMDEIVE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 160 EQKKLSSQLEEERSRHKQLSSMLVLECKKATNKA--------AEEGQKAGE-LSLKLEKEKSRVSKLEEELAAERKRGLQ 230
Cdd:pfam13868 109 RIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWkelekeeeREEDERILEyLKEKAEREEEREAEREEIEEEKEREIAR 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2462511474 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 2462511474 95 ERMLSQLAAAESRHRKVILDLEEERQRHAQDTAEG-DDVTYMLEKERERLTQQLEFEKSQVKKFEKEQKKLSSQLEEERS 173
Cdd:COG5185 376 SEELDSFKDTIESTKESLDEIPQNQRGYAQEILATlEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMR 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 174 RHKQLSSMLVLECKKATNKaaEEGQKAGELSLKLEKEKSRVSKLEEELAAERKRG-------LQTEAQVEKQLSEFDIER 246
Cdd:COG5185 456 EADEESQSRLEEAYDEINR--SVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLerqlegvRSKLDQVAESLKDFMRAR 533
|
170 180
....*....|....*....|
gi 2462511474 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 2462511474 137 EKERERLTQQLEFEKSQVKKFEKEQKKLSS---QLEEErsrhkqlssmlvLECKKATNKAAEEGQKAGELSLKLEKE-KS 212
Cdd:pfam05667 334 EEELEELQEQLEDLESSIQELEKEIKKLESsikQVEEE------------LEELKEQNEELEKQYKVKKKTLDLLPDaEE 401
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462511474 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 2462511474 95 ERMLSQLAAAES-----RHRKVILDLEEERQRHAQDTAEgddvtymLEKERERLTQQLEFEKSQVKKFEKeQKKLSSQLE 169
Cdd:COG3206 185 PELRKELEEAEAaleefRQKNGLVDLSEEAKLLLQQLSE-------LESQLAEARAELAEAEARLAALRA-QLGSGPDAL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 170 EERSRHKQLSSmLVLECKKATNKAAEEGQKAGELSLKLEKEKSRVSKLEEELAAERKRGLqteAQVEKQLSEFDIEREQL 249
Cdd:COG3206 257 PELLQSPVIQQ-LRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRIL---ASLEAELEALQAREASL 332
|
170 180 190
....*....|....*....|....*....|...
gi 2462511474 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 2462511474 101 LAAAESRHRKVILDLEEERQRHAQDTAEGDDVTYMLEKERERLTQQLEFEKSQVKKFEKEQKKLSSQLEEERSRHKQLSS 180
Cdd:COG1196 607 DLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAE 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 181 MLvlecKKATNKAAEEGQKAGELSLKLEKEKSRVSKLEEELAAERKRGLQTEAQVEKQLSEFDIEREQLRAKLNREENRT 260
Cdd:COG1196 687 RL----AEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL 762
|
170
....*....|....*....
gi 2462511474 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 2462511474 96 RMLSQLAAAESRHRKVILDLEEERQRHAQDTAEGDDVTyMLEKERERLTQQLEFEKSQVKKFEKEQKKLSSQLEEERSRH 175
Cdd:COG4913 651 QRLAEYSWDEIDVASAEREIAELEAELERLDASSDDLA-ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEEL 729
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462511474 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 2462511474 95 ERMLSQLAAAESRHRKVILDLEEERQRHAQDTAEGDDVTYMLEKERErltqQLEFEKSQVKKFEKEQKKLSSQLEEERSR 174
Cdd:pfam02463 226 LLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLK----ENKEEEKEKKLQEEELKLLAKEEEELKSE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 175 HKQLSSMLVLECKKAtnKAAEEGQKAGELSLKLEKEK-SRVSKLEEELAAERKRGLQTEAQVEKQLSEFDIEREQLRAKL 253
Cdd:pfam02463 302 LLKLERRKVDDEEKL--KESEKEKKKAEKELKKEKEEiEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKK 379
|
170 180
....*....|....*....|....*.
gi 2462511474 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 2462511474 161 QKKLSSQLEEERSRHKQLS---SMLVLECKKATNKAAEEGQKAGELSLKLEKEKSRVSKLEEELAAERKRglqtEAQVEK 237
Cdd:TIGR02169 669 SRSEPAELQRLRERLEGLKrelSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKER----LEELEE 744
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2462511474 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 2462511474 132 VTYMLEKERERLTQQLEFEKSQVKKFEKEQKKLSSQLEEERSRHKQLSsmLVLECKKATNKAAEEGQKAGELSLKLEKEK 211
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVD--LSEEAKLLLQQLSELESQLAEARAELAEAE 239
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462511474 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 2462511474 88 KQCKNMQERMLSQLAAAESRHRKviLDLEEERQRHAQDTAEGDDVTYmlekerERLTQQLEFEKSQVKKFEKEQKKLSSQ 167
Cdd:pfam15921 370 QESGNLDDQLQKLLADLHKREKE--LSLEKEQNKRLWDRDTGNSITI------DHLRRELDDRNMEVQRLEALLKAMKSE 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 168 LEEERSRHkqlssMLVLECKKatnkaaEEGQKAGELSLKLEKEKSRVSKLEEELAA--------------------ERKR 227
Cdd:pfam15921 442 CQGQMERQ-----MAAIQGKN------ESLEKVSSLTAQLESTKEMLRKVVEELTAkkmtlessertvsdltaslqEKER 510
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2462511474 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 2462511474 135 MLEKERERLTQQLEFEKSQVKK--FEKEQKKLSSQLEEERSRHKQLSSMLVLECKKATNKAaeeGQKAGELSLKLEKEKS 212
Cdd:PRK06669 30 LSIKEKERLREEEEEQVEQLREeaNDEAKEIIEEAEEDAFEIVEAAEEEAKEELLKKTDEA---SSIIEKLQMQIEREQE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 213 RV-SKLEEELAAERKRGLQT--EAQVEKQLSEFDIEREQLRA---KLNRE-ENRTKTLKEEMESL-----KKIVKDLEAS 280
Cdd:PRK06669 107 EWeEELERLIEEAKAEGYEEgyEKGREEGLEEVRELIEQLNKiieKLIKKrEEILESSEEEIVELaldiaKKVIKEISEN 186
|
..
gi 2462511474 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 2462511474 94 QERMLSQLAAAESRHRKVILDLEEERQRHAQDTAEGDDVTY-----MLEKERERLTQQLEFEKSQVKKFEKEQKKLssql 168
Cdd:TIGR00618 177 QYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYherkqVLEKELKHLREALQQTQQSHAYLTQKREAQ---- 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 169 eEERSRHKQLSSMLVLECKKATN--KAAEEGQKAGELSLKLEKeksrvskleeeLAAERKRGLQTEAQVEKQLSEFDiER 246
Cdd:TIGR00618 253 -EEQLKKQQLLKQLRARIEELRAqeAVLEETQERINRARKAAP-----------LAAHIKAVTQIEQQAQRIHTELQ-SK 319
|
170 180 190
....*....|....*....|....*....|....*..
gi 2462511474 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 2462511474 95 ERMLSQLAAAESRHRKVILDLE----EERQRHAQDTAEGD-------DVTYMLEKErERLTQQLEFEK----SQVKKFEK 159
Cdd:pfam01576 60 EEMRARLAARKQELEEILHELEsrleEEEERSQQLQNEKKkmqqhiqDLEEQLDEE-EAARQKLQLEKvtteAKIKKLEE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 160 EqkklSSQLEEERSRHKQLSSMLVLECKKATNKAAEEGQKAGELSLKLEKEKSRVSKLEEELAAERKRGLQTE------- 232
Cdd:pfam01576 139 D----ILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEkakrkle 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 233 ---AQVEKQLSEFDIEREQLRAKLNREE------------------NRTKTLKEEMESLKKIVKDLEASHQHSSPNEQLK 291
Cdd:pfam01576 215 gesTDLQEQIAELQAQIAELRAQLAKKEeelqaalarleeetaqknNALKKIRELEAQISELQEDLESERAARNKAEKQR 294
|
.
gi 2462511474 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 2462511474 100 QLAAAESRHRKVILDLEEERQRHAQDTAEGDDVTYMLEKERERLTQQLEFEKSQVKKFEKEQKKLSSQLEEERSRHKQLS 179
Cdd:COG1196 631 RLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELA 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 180 SMLVLECKKATNKAAEEGQKAGELSLKLEKEkSRVSKLEEELAAERKRGLQTEAQVEKQLSEFDIEREQL-----RA--K 252
Cdd:COG1196 711 EAEEERLEEELEEEALEEQLEAEREELLEEL-LEEEELLEEEALEELPEPPDLEELERELERLEREIEALgpvnlLAieE 789
|
170 180 190
....*....|....*....|....*....|....
gi 2462511474 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 2462511474 101 LAAAESRHRKVILDLEEERQRHAQDTAEGDDVTYMLEKERERLTQQLEFEKSQVKKFEKEQKKLSSQLEEERSRHKQLSS 180
Cdd:COG4717 286 LALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQL 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 181 MLVLE-----CKKATNKAAEEGQKAGELSLKLEKEKSRVSKLEEELAAERK-RGLQTEAQVEKQLSEfdiEREQLRAKLN 254
Cdd:COG4717 366 EELEQeiaalLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGeLEELLEALDEEELEE---ELEELEEELE 442
|
170 180 190
....*....|....*....|....*....|
gi 2462511474 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 2462511474 163 KLSSQLEEERSRHKQLSSMLVLECKKATnKAAEEGQKAGELSLKLEKEKSRVSKLEEELAAERKRGLQTEAQVEKQLSEF 242
Cdd:pfam04871 1 AKKSELESEASSLKNENTELKAELQELS-KQYNSLEQKESQAKELEAEVKKLEEALKKLKAELSEEKQKEKEKQSELDDL 79
|
90 100
....*....|....*....|....*..
gi 2462511474 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 2462511474 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 2462511474 72 KQPVCTNPLS------ILKVVMKQCKNMQERmLSQLAAAESRHRKVILDLEEErqrhaqdtaegddvtymLEKERERLTQ 145
Cdd:PRK03918 437 KCPVCGRELTeehrkeLLEEYTAELKRIEKE-LKEIEEKERKLRKELRELEKV-----------------LKKESELIKL 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 146 QLEFEksQVKKFEKEQKKLSSQLEEERSRHKQLSSMLVLECKKATNKAAEEGQKAGELSLKLEKEKSRVSKLEEELAA-- 223
Cdd:PRK03918 499 KELAE--QLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAEll 576
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462511474 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 2462511474 166 SQLEEERSRHKQLSSMLVLECKKATNKAAEEGQKAGELSlKLEKEKSRVSKLEEELAAERKRGLQTEAQVEKQLSefdiE 245
Cdd:PRK09039 53 SALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLS-AAEAERSRLQALLAELAGAGAAAEGRAGELAQELD----S 127
|
90 100 110
....*....|....*....|....*....|....
gi 2462511474 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 2462511474 57 LQRDFETLKEKNDGEKQPV--CTNPLSILKVVMKQCKNMQERMLSQLAAAESRHRKVILDLEEERQRHAQDTAEGDdvty 134
Cdd:TIGR04523 424 LEKEIERLKETIIKNNSEIkdLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELK---- 499
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 135 MLEKERERLTQQLEFEKSQVKKFEKEQKKLSSQLEEERSRHKQLSSMLVlecKKATNKAAEegqkagelslKLEKEKSRV 214
Cdd:TIGR04523 500 KLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELN---KDDFELKKE----------NLEKEIDEK 566
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462511474 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 2462511474 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 2462511474 18 LEGELEARDLVIEALKAQHRDTfiEERYGKynISDPLMALQRDFETLKEKNDGEKQpvctnplSILKVVMKQCKNMQERM 97
Cdd:COG4942 53 LLKQLAALERRIAALARRIRAL--EQELAA--LEAELAELEKEIAELRAELEAQKE-------ELAELLRALYRLGRQPP 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 98 LSQLAAAES-----RHRKVILDLEEERQRHAQDTAEgddvtymLEKERERLTQQLEFEKSQVKKFEKEQKKLSSQLEEER 172
Cdd:COG4942 122 LALLLSPEDfldavRRLQYLKYLAPARREQAEELRA-------DLAELAALRAELEAERAELEALLAELEEERAALEALK 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2462511474 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 2462511474 136 LEKERERLTQQLEFEKsqvKKFEKEQKKLSSQLEEER-------SRHKQLSSMLV-----LECKKATNKA-AEE--GQKA 200
Cdd:pfam00038 122 LEAKIESLKEELAFLK---KNHEEEVRELQAQVSDTQvnvemdaARKLDLTSALAeiraqYEEIAAKNREeAEEwyQSKL 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 201 GELSLKLEKEKSRVSKLEEELAAERKR--GLQTE--------AQVEKQLSE----FDIEREQLRAKLNREENRTKTLKEE 266
Cdd:pfam00038 199 EELQQAAARNGDALRSAKEEITELRRTiqSLEIElqslkkqkASLERQLAEteerYELQLADYQELISELEAELQETRQE 278
|
..
gi 2462511474 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 2462511474 192 KAAEEGQKAGELSLKLEKEKSRVSKLEEELAAERKRglqtEAQVEKQLSEFDIEREQLRAKLNREENRTKTLKEEMESLK 271
Cdd:COG1196 219 KEELKELEAELLLLKLRELEAELEELEAELEELEAE----LEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294
|
90
....*....|..
gi 2462511474 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 2462511474 83 LKVVMKQCKNMQERMLSQLAAAESRHRKVILDLEEERQRHAQDTAEGDDVTYMLEKERERLTQQLEFEKSQVK-KFEKEQ 161
Cdd:pfam12128 324 LEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKdKLAKIR 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 162 KKLSSQLEEERSRHKQLSSMLVLECKKATNKAAEEGQ----KAGELSLKL-------------EKEKSRVSKLEEELAAE 224
Cdd:pfam12128 404 EARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYrlksRLGELKLRLnqatatpelllqlENFDERIERAREEQEAA 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2462511474 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 2462511474 10 ELLTLFSILEGELEARDLVIEALKAQhRDTFIEERYgkyNISDPLMALQRDFETLKEK--NDGEKQPVCTNPLSILKVVM 87
Cdd:TIGR02168 765 ELEERLEEAEEELAEAEAEIEELEAQ-IEQLKEELK---ALREALDELRAELTLLNEEaaNLRERLESLERRIAATERRL 840
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 88 KQCKNMQERMLSQLAAAESRhrkvILDLEEERQRHAQDTAEGDDVTYMLEKERERLTQQLEFEKSQVKKFEKEQKKLSSQ 167
Cdd:TIGR02168 841 EDLEEQIEELSEDIESLAAE----IEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRE 916
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 168 LEEERsrhkqlssmlvleckkatnkaaeegQKAGELSLKLEKEKSRVSKLEEELAAERKRGLQ----TEAQVEKQLSEFD 243
Cdd:TIGR02168 917 LEELR-------------------------EKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEeaeaLENKIEDDEEEAR 971
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2462511474 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 2462511474 117 EERQRHAQDTAEGDDVTYMLEKERERLTQQLEFEKSQVKKFEKEQKKLSSQLE---EERSRHKQLSSMLVLECKKA--TN 191
Cdd:PTZ00121 1332 DAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKkkaEEKKKADEAKKKAEEDKKKAdeLK 1411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 192 KAAEEGQKAGELSLKLEkEKSRVSKLEEElAAERKRGLQTEAQVEKQLSEFDIEREQLRAKLNREENRTKTLKEEMESLK 271
Cdd:PTZ00121 1412 KAAAAKKKADEAKKKAE-EKKKADEAKKK-AEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAK 1489
|
170 180
....*....|....*....|.
gi 2462511474 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 2462511474 95 ERMLSQLAAAESRHRKVildLEEERQRHAQDTAEGDDVTYmlEKERERLtQQLEFEKSQVKKFEKEQKK--LSSQLEEER 172
Cdd:COG4913 228 DALVEHFDDLERAHEAL---EDAREQIELLEPIRELAERY--AAARERL-AELEYLRAALRLWFAQRRLelLEAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511474 173 SRHKQLssmlvlECKKATNKAAEEGQKAGELSLKLEKEKS---RVSKLEEELAA---ERKRGLQTEAQVEKQLSEFDIE- 245
Cdd:COG4913 302 AELARL------EAELERLEARLDALREELDELEAQIRGNggdRLEQLEREIERlerELEERERRRARLEALLAALGLPl 375
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2462511474 246 ----------REQLRAKLNREENRTKTLKEEMESLKKIVKDLEASHQ 282
Cdd:COG4913 376 pasaeefaalRAEAAALLEALEEELEALEEALAEAEAALRDLRRELR 422
|
|
| |
