|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1040-1341 |
5.49e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 77.28 E-value: 5.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1040 SESEMNDVKTKLLQLEDVVRAL-----------EKADSRESYRAELQRLSEENSVLK-----SDLGKIQLELGTSESRNE 1103
Cdd:COG1196 177 AERKLEATEENLERLEDILGELerqleplerqaEKAERYRELKEELKELEAELLLLKlreleAELEELEAELEELEAELE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1104 VQRQEIEVLKRDKEQACFDLEELSTQTQKYKDEMSQLNCRILQLEGDSSGLHTQKEENHAAIQVLMKKLEEAECREKQQG 1183
Cdd:COG1196 257 ELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELE 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1184 DQIKHLKIELERVNEECQRLRLSQAELTGSLEESQGQLHSVQLRLEAAQSQHDRIVQGLQEQMSQL-VPGARVAELQHLL 1262
Cdd:COG1196 337 EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLeELEEAEEALLERL 416
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958766565 1263 SLREEEAERLNAQQEEYKQQLKAREDQVEEAEARLHNvewLLQEKVEELRKQFEKNTRSDLLLKELYVENAHLMKAVQL 1341
Cdd:COG1196 417 ERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE---LEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR 492
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1062-1372 |
1.70e-13 |
|
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: 75.86 E-value: 1.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1062 EKADSRESYRAELQRLSEENSVLKSDLGKIQLELGTSESRNEVQRQEIEVLKRDKEQACFDLEELSTQTQKYKDEMSQLN 1141
Cdd:TIGR02168 667 KTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1142 CRILQLEGDSSGLHTQKEENHAaiqvlmkKLEEAECREKQQGDQIKHLKIELERVNEECQRLRLSQAELTGSLEESQGQL 1221
Cdd:TIGR02168 747 ERIAQLSKELTELEAEIEELEE-------RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1222 HSVQLRLEAAQSQHDRIVQ----------GLQEQMSQLVpgARVAELQHLLSLREEEAERLNAQQEEYKQQLKAREDQVE 1291
Cdd:TIGR02168 820 ANLRERLESLERRIAATERrledleeqieELSEDIESLA--AEIEELEELIEELESELEALLNERASLEEALALLRSELE 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1292 EAEARLHNVEWLLQEKVEELRKQFEKNTRSDLLLKELYVENAHLMKAV--------QLTEEKQRGAEKKNCVLEEKVRAL 1363
Cdd:TIGR02168 898 ELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLseeysltlEEAEALENKIEDDEEEARRRLKRL 977
|
....*....
gi 1958766565 1364 NKLISKMAP 1372
Cdd:TIGR02168 978 ENKIKELGP 986
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1043-1349 |
4.89e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.74 E-value: 4.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1043 EMNDVKTKLLQLEDVVRALEKAdsRESYRAELQRLSEENSVLKSDLGKIQLELGTSESRNEVQRQEIEVLKRDKEQACFD 1122
Cdd:COG1196 233 KLRELEAELEELEAELEELEAE--LEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1123 LEELSTQTQKYKDEmsqlncrILQLEGDSSGLHTQKEENHAAIQVLMKKLEEAECREKQQGDQIKHLKIELERVNEECQR 1202
Cdd:COG1196 311 RRELEERLEELEEE-------LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1203 LRLSQAELTGSLEESQGQLHSVQLRLEAAQSQHDRIVQGLQEqmsqlvpgaRVAELQHLLSLREEEAERLNAQQEEyKQQ 1282
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE---------LEEALAELEEEEEEEEEALEEAAEE-EAE 453
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958766565 1283 LKAREDQVEEAEARLHNVEWLLQEKVEELRKQFEKNTRSDLLLKELYVENAHLMKAVQLTEEKQRGA 1349
Cdd:COG1196 454 LEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLR 520
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1043-1320 |
1.21e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 69.70 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1043 EMNDVKTKLLQLEDVVRALEkaDSRESYRAELQRLSEENSVLKSDLGKIQLELGTSESRNEVQRQEIEVLKRDKEQACFD 1122
Cdd:TIGR02168 233 RLEELREELEELQEELKEAE--EELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1123 LEELSTQTQkykdemsQLNCRILQLEGDSSGLHTQKEENHAAIQVLMKKLEEAECREKQQGDQIKHLKIELERVNEECQR 1202
Cdd:TIGR02168 311 LANLERQLE-------ELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLET 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1203 LRLSQAELTGSLEESQGQLHSVQLRLEAAQSQHDRIVQGLQEQMSQLVPgARVAELQHLLSLREEEAERLNAQQEEYKQQ 1282
Cdd:TIGR02168 384 LRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE-AELKELQAELEELEEELEELQEELERLEEA 462
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1958766565 1283 LKAREDQVEEAEARLHNVEWLLQEK------VEELRKQFEKNTR 1320
Cdd:TIGR02168 463 LEELREELEEAEQALDAAERELAQLqarldsLERLQENLEGFSE 506
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1041-1374 |
5.11e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.77 E-value: 5.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1041 ESEMNDVKTKLLQLEDVVRALEKAdsresyraeLQRLSeensvLKSDLGKIQLELgtsesRNEVQRQEIEVLKRDKEQAC 1120
Cdd:TIGR02168 178 ERKLERTRENLDRLEDILNELERQ---------LKSLE-----RQAEKAERYKEL-----KAELRELELALLVLRLEELR 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1121 FDLEELSTQTQKYKDEMSQLNCRILQLEGDSSGLHTQKEENHAAIQVLMKKLEE--AECREKQQgdQIKHLKIELERVNE 1198
Cdd:TIGR02168 239 EELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYAlaNEISRLEQ--QKQILRERLANLER 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1199 ECQRLRLSQAELTGSLEESQGQLHSVQLRLEAAQSQHDRIVQGLQEQMSQLvpgarvAELQHLLSLREEEAERLNAQQEE 1278
Cdd:TIGR02168 317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEL------EELESRLEELEEQLETLRSKVAQ 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1279 YKQQLKAREDQVEEAEARL----HNVEWLLQEKVEELRKQFEKntRSDLLLKELYVENAHLMKAVQLTEEKQRGAEKKNC 1354
Cdd:TIGR02168 391 LELQIASLNNEIERLEARLerleDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLEEALEELRE 468
|
330 340
....*....|....*....|
gi 1958766565 1355 VLEEKVRALNKLISKMAPAS 1374
Cdd:TIGR02168 469 ELEEAEQALDAAERELAQLQ 488
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1101-1367 |
7.01e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.27 E-value: 7.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1101 RNEVQRQeIEVLKRDKEQAcfdleelstqtQKYKDemsqlncriLQLEGDssglHTQKEENHAAIQVLMKKLEEAECREK 1180
Cdd:COG1196 195 LGELERQ-LEPLERQAEKA-----------ERYRE---------LKEELK----ELEAELLLLKLRELEAELEELEAELE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1181 QQGDQIKHLKIELERVNEECQRLRLSQAELTGSLEESQGQLHSVQLRLEAAQSQHDRIV---QGLQEQMSQLvpGARVAE 1257
Cdd:COG1196 250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEerrRELEERLEEL--EEELAE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1258 LQHLLSLREEEAERLNAQQEEYKQQLKAREDQVEEAEARLHNVEWLLQEKVEELRKQFEKNTRSDLLLKELYVENAHLMK 1337
Cdd:COG1196 328 LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE 407
|
250 260 270
....*....|....*....|....*....|
gi 1958766565 1338 AVQLTEEKQRGAEKKNCVLEEKVRALNKLI 1367
Cdd:COG1196 408 AEEALLERLERLEEELEELEEALAELEEEE 437
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1041-1323 |
1.23e-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: 63.15 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1041 ESEMNDVKTKLLQLEDVVRALEKADSRESyrAELQRLSEENSVLKSDLGKIQLELGTSESRNEVQRQEIEVLKRDKEQAC 1120
Cdd:TIGR02168 725 SRQISALRKDLARLEAEVEQLEERIAQLS--KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR 802
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1121 FDLEELSTQTQKYKDEMSQLNCRILQLEGDSSG-------LHTQKEENHAAIQVLMKKLEEAECREKQQGDQIKHLKIEL 1193
Cdd:TIGR02168 803 EALDELRAELTLLNEEAANLRERLESLERRIAAterrledLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNER 882
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1194 ERVNEECQRLRLSQA--------------ELTGSLEESQGQLHSVQLRLEAAQSQHDRIVQGLQEQmsqlvpgarvaelq 1259
Cdd:TIGR02168 883 ASLEEALALLRSELEelseelreleskrsELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEE-------------- 948
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958766565 1260 hlLSLREEEAERLNAQQEEYKQQLKAREDQVEEAEARLHNVEWLLQEKVEEL--RKQFEKNTRSDL 1323
Cdd:TIGR02168 949 --YSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELkeRYDFLTAQKEDL 1012
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1059-1317 |
4.22e-09 |
|
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: 61.24 E-value: 4.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1059 RALEKADSRESYRAELQRLSEENSVLKSDLGKIQLELGTSESRNEVQRQEIEVLKRDKEQACFDLEELSTQTQK------ 1132
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSleqeie 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1133 -YKDEMSQLNCRILQLEgdssglhtqkeenhAAIQVLMKKLEEAECREKQQgdQIKHLKIELERVNEECQRLRlsqaelt 1211
Cdd:TIGR02169 755 nVKSELKELEARIEELE--------------EDLHKLEEALNDLEARLSHS--RIPEIQAELSKLEEEVSRIE------- 811
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1212 GSLEESQGQLHSVQLRLEAAQSQhdriVQGLQEQMsqlvpgarvAELQHLLSLREEEAERLNAQQEEYKQQLKAREDQVE 1291
Cdd:TIGR02169 812 ARLREIEQKLNRLTLEKEYLEKE----IQELQEQR---------IDLKEQIKSIEKEIENLNGKKEELEEELEELEAALR 878
|
250 260
....*....|....*....|....*.
gi 1958766565 1292 EAEARLHNvewlLQEKVEELRKQFEK 1317
Cdd:TIGR02169 879 DLESRLGD----LKKERDELEAQLRE 900
|
|
| EF-hand_7 |
pfam13499 |
EF-hand domain pair; |
199-260 |
9.86e-09 |
|
EF-hand domain pair;
Pssm-ID: 463900 [Multi-domain] Cd Length: 67 Bit Score: 53.03 E-value: 9.86e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958766565 199 ENQVQGIWHELGVGSSGHLNEQELAVVCRSIGLHG-LEKQELEELFSKLDRDGDGRVSLAEFQ 260
Cdd:pfam13499 1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEpLSDEEVEELFKEFDLDKDGRISFEEFL 63
|
|
| EFh |
cd00051 |
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ... |
213-260 |
2.30e-08 |
|
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.
Pssm-ID: 238008 [Multi-domain] Cd Length: 63 Bit Score: 51.78 E-value: 2.30e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1958766565 213 SSGHLNEQELAVVCRSIGLhGLEKQELEELFSKLDRDGDGRVSLAEFQ 260
Cdd:cd00051 13 GDGTISADELKAALKSLGE-GLSEEEIDEMIREVDKDGDGKIDFEEFL 59
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1041-1369 |
3.71e-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: 58.16 E-value: 3.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1041 ESEMNDVKTKLLQLEDvvRALEKADSRESYRAELQRLSEENSVLKSDLGKIQLELGTSESRNEVQRQEIEVLKRDKEQAC 1120
Cdd:TIGR02169 687 KRELSSLQSELRRIEN--RLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELE 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1121 FDLEELSTQTQKYKDEMSQLNCRIL-----QLEGDSSGLHTQKEENHAAIQVLMKKLEEAECREKQQGDQIKHLKIEL-- 1193
Cdd:TIGR02169 765 ARIEELEEDLHKLEEALNDLEARLShsripEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRid 844
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1194 --ERVNEECQRLRLSQA---ELTGSLEESQGQLHSVQLRLEAAQSQHDRivqgLQEQMSQLVPGARVAELQhlLSLREEE 1268
Cdd:TIGR02169 845 lkEQIKSIEKEIENLNGkkeELEEELEELEAALRDLESRLGDLKKERDE----LEAQLRELERKIEELEAQ--IEKKRKR 918
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1269 AERLNAQQEEYKQQLKAREDQVEE------AEARLHNVEWLLQEKVEELRKQFEKNtrsdlllkelyvenahlMKAVQLT 1342
Cdd:TIGR02169 919 LSELKAKLEALEEELSEIEDPKGEdeeipeEELSLEDVQAELQRVEEEIRALEPVN-----------------MLAIQEY 981
|
330 340 350
....*....|....*....|....*....|
gi 1958766565 1343 EEKQR---GAEKKNCVLEEKVRALNKLISK 1369
Cdd:TIGR02169 982 EEVLKrldELKEKRAKLEEERKAILERIEE 1011
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1046-1371 |
8.53e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 57.27 E-value: 8.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1046 DVKTKLLQLEDVVRALEKADS-RESYRAELQRLSEENSVLKSDLGKIQLELGTSESRNEVQRQEIEVLKRDKEQ---ACF 1121
Cdd:PRK04863 356 DLEELEERLEEQNEVVEEADEqQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALERAKQLcglPDL 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1122 DLEELSTQTQKYKDEMSQLNCRILQLE---GDSSGLHTQKEENHAAIQVLMKKLEEAECREKQQgdqikhlkielervnE 1198
Cdd:PRK04863 436 TADNAEDWLEEFQAKEQEATEELLSLEqklSVAQAAHSQFEQAYQLVRKIAGEVSRSEAWDVAR---------------E 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1199 ECQRLRlSQAELTGSLEESQGQLHSVQLRLEAAQSQhDRIVQGLQEQMSQLVPGArvAELQHLLSLREEEAERLNAQQEE 1278
Cdd:PRK04863 501 LLRRLR-EQRHLAEQLQQLRMRLSELEQRLRQQQRA-ERLLAEFCKRLGKNLDDE--DELEQLQEELEARLESLSESVSE 576
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1279 YKQQLKAREDQVEEAEARLHNV-----EWL-LQEKVEELRKQFEkntrsdlllkELYVENAHLMKAVQLTEEKQRGAEKK 1352
Cdd:PRK04863 577 ARERRMALRQQLEQLQARIQRLaarapAWLaAQDALARLREQSG----------EEFEDSQDVTEYMQQLLERERELTVE 646
|
330
....*....|....*....
gi 1958766565 1353 NCVLEEKVRALNKLISKMA 1371
Cdd:PRK04863 647 RDELAARKQALDEEIERLS 665
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
320-528 |
2.79e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.33 E-value: 2.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 320 QAALACYRQELNFHQGQVEQLVQERDKARQDLEKAEKRNLDFVREMDDCHSALEQLTEKKIKHLEQEYRGRLSLLRSEVE 399
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 400 MERelfweqARRQRAVLEQDVGRLQAEETSLREKLTLALKENSRLQKEIIEVVEKLSDSEKLVLRLQSDLQFVLKDKLep 479
Cdd:COG1196 318 LEE------LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL-- 389
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1958766565 480 qsmELLAQEEQFTAILNDYELKCRDLQDRNDELQAELEGLRVRLPRSRQ 528
Cdd:COG1196 390 ---EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE 435
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
291-858 |
4.67e-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: 54.68 E-value: 4.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 291 DFNVDEKVNLLELTW-ALDNEL--LTVDGVIQQAALACYRQELNFHQGQVEQLVQERDKARQDLEKAEKRNLDFVREMDD 367
Cdd:TIGR02168 276 VSELEEEIEELQKELyALANEIsrLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELES 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 368 CHSALEQLTEKKikhleQEYRGRLSLLRSEvemerelfWEQARRQRAVLEQDVGRLQAEETSLREKLTLALKENSRLQKE 447
Cdd:TIGR02168 356 LEAELEELEAEL-----EELESRLEELEEQ--------LETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQE 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 448 IIEVVEKLSDSEKLVLRLQSDLQFVLKDKLEPQSMELLAQEEQFTAILNDYELKCRDLQDRNDELQAELEGLRVRLPRSR 527
Cdd:TIGR02168 423 IEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLE 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 528 QSPSG--TPGTHRRWTPGRGPAdnlfVGESIpvslETEIKMQQMKENYQELRMQ--LETKVNYYEKEIEVMKRNfekdkk 603
Cdd:TIGR02168 503 GFSEGvkALLKNQSGLSGILGV----LSELI----SVDEGYEAAIEAALGGRLQavVVENLNAAKKAIAFLKQN------ 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 604 EMEQAFQLEVSVLEGQKAD-LETLYAKSQEVILGLkeqLQDAARSPEPAPAGLAPCCAQALC--TLAQRLGVEMHLRHQD 680
Cdd:TIGR02168 569 ELGRVTFLPLDSIKGTEIQgNDREILKNIEGFLGV---AKDLVKFDPKLRKALSYLLGGVLVvdDLDNALELAKKLRPGY 645
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 681 QLlqirlsdtVT---DSVLPRVCSPKGSRKRTGhpntkQTTERRVSGREAEEELNQKLSWLEAQHAACCESLSLQHQCE- 756
Cdd:TIGR02168 646 RI--------VTldgDLVRPGGVITGGSAKTNS-----SILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEe 712
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 757 ----KDQLLQTHLQRVKDLAAQLDLEKGwREEREQEVLAHCRRQQLKLQAVMSEEQARICRSFTLEKEKLE--QTYREQV 830
Cdd:TIGR02168 713 eleqLRKELEELSRQISALRKDLARLEA-EVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAeiEELEAQI 791
|
570 580
....*....|....*....|....*...
gi 1958766565 831 EGLVQEADVLRALLKNGTTVVSDQQERI 858
Cdd:TIGR02168 792 EQLKEELKALREALDELRAELTLLNEEA 819
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
327-523 |
5.45e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.56 E-value: 5.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 327 RQELNFHQGQVEQLVQERDKARQDLEKAEKRNLDFVREMDDCHSALEQLTEK---KIKHLEQEYRGRLSLLRSEVEMERE 403
Cdd:COG1196 301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEleeAEAELAEAEEALLEAEAELAEAEEE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 404 lfWEQARRQRAVLEQDVGRLQAEETSLREKLTLALKENSRLQKEIIEVVEKLSDSEKLVLRLQSDLQFVLKDKLepqsmE 483
Cdd:COG1196 381 --LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA-----E 453
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1958766565 484 LLAQEEQFTAILNDYELKCRDLQDRNDELQAELEGLRVRL 523
Cdd:COG1196 454 LEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL 493
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1106-1316 |
1.30e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.00 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1106 RQEIEVLKRDKEQacfdLEELSTQTQKYKDEMSQLNcrilQLEGDSSGLHTQKEEnhAAIQVLMKKLEEAECREKQQGDQ 1185
Cdd:COG4913 241 HEALEDAREQIEL----LEPIRELAERYAAARERLA----ELEYLRAALRLWFAQ--RRLELLEAELEELRAELARLEAE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1186 IKHLKIELERVNEECQRLRLSQAELTGsleesqGQLHSVQLRLEAAQSQHDRIVQGLQEQMsqlvpgARVAELQHLLSLR 1265
Cdd:COG4913 311 LERLEARLDALREELDELEAQIRGNGG------DRLEQLEREIERLERELEERERRRARLE------ALLAALGLPLPAS 378
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1958766565 1266 EEEAERLNAQQEEYKQQLKAREDQVEEAEARLHNVEWLLQEKVEELRKQFE 1316
Cdd:COG4913 379 AEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
318-528 |
1.41e-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: 53.14 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 318 IQQAALACYRQELNFHQGQVEQLVQERDKARQ-------DLEKAEKRNLDFVREMDDCHSALEQLTEKKIKHLEQEYRGR 390
Cdd:TIGR02168 695 ELEKALAELRKELEELEEELEQLRKELEELSRqisalrkDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAE 774
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 391 LSLLRSEVEMER-ELFWEQARRQRAVLEQDVGRLQAEETSLREK---------------------LTLALKENSRLQKEI 448
Cdd:TIGR02168 775 EELAEAEAEIEElEAQIEQLKEELKALREALDELRAELTLLNEEaanlrerleslerriaaterrLEDLEEQIEELSEDI 854
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 449 IEVVEKLSDSEKLVLRLQSDLQFVL--KDKLEPQSMELLAQEEQFTAILNDYELKCRDLQDRNDELQAELEGLRVRLPRS 526
Cdd:TIGR02168 855 ESLAAEIEELEELIEELESELEALLneRASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGL 934
|
..
gi 1958766565 527 RQ 528
Cdd:TIGR02168 935 EV 936
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1119-1371 |
1.42e-06 |
|
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: 52.07 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1119 ACFDLEELSTQTQKYKDEMSQLNCRILQLEgdssglhTQKEENHAAIQVLMKKLEEAECREKQQGDQIKHLKIELERVNE 1198
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELE-------KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1199 ECQRLRLSQAELTGSLEESQGQLhSVQLRLEAAQSQHDRIVQGL-QEQMSQLVpgARVAELQHLLSLREEEAERLNAQQE 1277
Cdd:COG4942 84 ELAELEKEIAELRAELEAQKEEL-AELLRALYRLGRQPPLALLLsPEDFLDAV--RRLQYLKYLAPARREQAEELRADLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1278 EYKQQLKAREDQVEEAEArlhnvewLLQEKVEELRKQFEKNTRSDLLLKELyvenahlmkAVQLTEEKQRGAEkkncvLE 1357
Cdd:COG4942 161 ELAALRAELEAERAELEA-------LLAELEEERAALEALKAERQKLLARL---------EKELAELAAELAE-----LQ 219
|
250
....*....|....
gi 1958766565 1358 EKVRALNKLISKMA 1371
Cdd:COG4942 220 QEAEELEALIARLE 233
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1046-1297 |
1.81e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.73 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1046 DVKTKLLQLEDVVRALEKAD----------SRESYRAELQRLSEENSVLKSDLGKIQLELGTSESRnevqRQEIEVLKRD 1115
Cdd:PRK02224 184 DQRGSLDQLKAQIEEKEEKDlherlnglesELAELDEEIERYEEQREQARETRDEADEVLEEHEER----REELETLEAE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1116 KEQACFDLEELSTQTQKYKDEMSQLNCRILQLEGDSSGLHTQKEENHAAIQVLMKKLEEAECREKQQGDQIKHLKIELER 1195
Cdd:PRK02224 260 IEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQA 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1196 VNEECQRLRLSQAELTGSLEESQGQLHSVQLRLEAAQSQHDR---IVQGLQEQMSQL---VPGARVA--ELQHLLSLREE 1267
Cdd:PRK02224 340 HNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDrreEIEELEEEIEELrerFGDAPVDlgNAEDFLEELRE 419
|
250 260 270
....*....|....*....|....*....|
gi 1958766565 1268 EAERLNAQQEEYKQQLKAREDQVEEAEARL 1297
Cdd:PRK02224 420 ERDELREREAELEATLRTARERVEEAEALL 449
|
|
| FRQ1 |
COG5126 |
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
213-259 |
2.62e-06 |
|
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 48.25 E-value: 2.62e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1958766565 213 SSGHLNEQELAvvcRSIGLHGLEKQELEELFSKLDRDGDGRVSLAEF 259
Cdd:COG5126 82 GDGKISADEFR---RLLTALGVSEEEADELFARLDTDGDGKISFEEF 125
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1099-1351 |
2.94e-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: 51.99 E-value: 2.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1099 ESRNEVQRQEIEVLKRDKEQACFDLEELSTQTQKYKDEMSQ-LNCRILQLEgdssglhtqKEEnhAAIQVLMKKLEEAEc 1177
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKaERYQALLKE---------KRE--YEGYELLKEKEALE- 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1178 REKQQGD--------QIKHLKIELERVNEECQRLRLSQAELTGSL----EESQGQLHSVQLRLEAAQSQHDRIVQGLQEQ 1245
Cdd:TIGR02169 237 RQKEAIErqlasleeELEKLTEEISELEKRLEEIEQLLEELNKKIkdlgEEEQLRVKEKIGELEAEIASLERSIAEKERE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1246 MSQLvpGARVAELQHLLSLREEEAERLNAQQEEYKQQLKAREDQVEEAEARLHNVEWLLQEKVEELRKQFEKNTRSDLLL 1325
Cdd:TIGR02169 317 LEDA--EERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKL 394
|
250 260
....*....|....*....|....*..
gi 1958766565 1326 KELYVE-NAHLMKAVQLTEEKQRGAEK 1351
Cdd:TIGR02169 395 EKLKREiNELKRELDRLQEELQRLSEE 421
|
|
| EF-hand_8 |
pfam13833 |
EF-hand domain pair; |
213-259 |
5.64e-06 |
|
EF-hand domain pair;
Pssm-ID: 404678 [Multi-domain] Cd Length: 54 Bit Score: 45.00 E-value: 5.64e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1958766565 213 SSGHLNEQELAVVCRSIGLHGLEKQELEELFSKLDRDGDGRVSLAEF 259
Cdd:pfam13833 1 EKGVITREELKRALALLGLKDLSEDEVDILFREFDTDGDGYISFDEF 47
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1040-1369 |
5.69e-06 |
|
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: 50.79 E-value: 5.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1040 SESEMNDVKTKLLQLEDVVRALEKadSRESYRAELQRLSEENSVLKSDLGKIqlelgtsESRNEVQRQEIEVLKRDKEQA 1119
Cdd:TIGR04523 354 SESENSEKQRELEEKQNEIEKLKK--ENQSYKQEIKNLESQINDLESKIQNQ-------EKLNQQKDEQIKKLQQEKELL 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1120 CFDLEELSTQTQKYKDEMSQLNCRILQLEGDSSGLHTQKEENHAAIQVLMKKLEEAECREKQQGDQIKHLKIELERVNEE 1199
Cdd:TIGR04523 425 EKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEE 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1200 CQRLRLSQAELT---GSLEESQGQLHSVQLRLEAAQSQHDRIVQGLQEQMSQLVPGARVAELQHLLSLREEEAERLNAQQ 1276
Cdd:TIGR04523 505 KKELEEKVKDLTkkiSSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQ 584
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1277 EEYKQQLKAREDQVEEAEARLHNVEWLLQEKVEELRKQFEKNTRSDLLLKEL------YVENAHLMK-AVQLTEEKQRGA 1349
Cdd:TIGR04523 585 EEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIkskknkLKQEVKQIKeTIKEIRNKWPEI 664
|
330 340
....*....|....*....|
gi 1958766565 1350 EKKNCVLEEKVRALNKLISK 1369
Cdd:TIGR04523 665 IKKIKESKTKIDDIIELMKD 684
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1062-1374 |
6.83e-06 |
|
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: 50.72 E-value: 6.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1062 EKADSRESYRAELQRLSEENSVLKSDLGKIQLELGTSESRNEVQRQEIEVLkrDKEQACFDLEELSTQT-----QKYKDE 1136
Cdd:COG3096 372 EAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQAVQAL--EKARALCGLPDLTPENaedylAAFRAK 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1137 MSQLNCRILQLE---GDSSGLHTQKEENHAAIQVLMKKLE--EAECREKQQGDQIKHLKIELERVneecQRLRLSQAELT 1211
Cdd:COG3096 450 EQQATEEVLELEqklSVADAARRQFEKAYELVCKIAGEVErsQAWQTARELLRRYRSQQALAQRL----QQLRAQLAELE 525
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1212 gsleesqgqlhsvqlRLEAAQSQHDRIVQGLQEQMSQLVPGArvAELQHLLSLREEEAERLNAQQEEYKQQLKAREDQVE 1291
Cdd:COG3096 526 ---------------QRLRQQQNAERLLEEFCQRIGQQLDAA--EELEELLAELEAQLEELEEQAAEAVEQRSELRQQLE 588
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1292 EAEARLHNVE-----WL-LQEKVEELRKQfekntrsdllLKELYVENAHLMKAVQLTEEKQRGAEKKNCVLEEKVRALNK 1365
Cdd:COG3096 589 QLRARIKELAarapaWLaAQDALERLREQ----------SGEALADSQEVTAAMQQLLEREREATVERDELAARKQALES 658
|
....*....
gi 1958766565 1366 LISKMAPAS 1374
Cdd:COG3096 659 QIERLSQPG 667
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1166-1363 |
8.86e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 8.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1166 QVLMKKLE-EAECREKQQGDQIKHLKIELERVNEECQRLRLSQAELTGSLEESQgQLHSVQLRLEAAQSQHDRIVQGLQE 1244
Cdd:COG4717 45 AMLLERLEkEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELE-ELEEELEELEAELEELREELEKLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1245 QMSQLVPGARVAELQHLLSLREEEAERLNAQQEEYKQ---QLKAREDQVEEAEARLHN--------VEWLLQEKVEELRK 1313
Cdd:COG4717 124 LLQLLPLYQELEALEAELAELPERLEELEERLEELREleeELEELEAELAELQEELEElleqlslaTEEELQDLAEELEE 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1314 QFEKNTRSDLLLKELYVENAHLMKAVQLTEEKQRGAEKKNCVLEEKVRAL 1363
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLL 253
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1053-1296 |
9.52e-06 |
|
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: 49.76 E-value: 9.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1053 QLEDVVRALEKAdsresyRAELQRLSEENSVLKSDLGKIQLELGTSESRNEVQRQEIEVLKRDKEQACFDLEELSTQTQK 1132
Cdd:COG4942 28 ELEQLQQEIAEL------EKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1133 YKDEMSQLNcRILQLEGDSSG----LHTQKEENHAAIQVLMKKLEEAecrEKQQGDQIKHLKIELERVNEEcqrLRLSQA 1208
Cdd:COG4942 102 QKEELAELL-RALYRLGRQPPlallLSPEDFLDAVRRLQYLKYLAPA---RREQAEELRADLAELAALRAE---LEAERA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1209 ELTGSLEESQGQlhsvQLRLEAAQSQHDRIVQGLQEQMSQLvpgarvaelqhllslrEEEAERLNAQQEEYKQQLKARED 1288
Cdd:COG4942 175 ELEALLAELEEE----RAALEALKAERQKLLARLEKELAEL----------------AAELAELQQEAEELEALIARLEA 234
|
....*...
gi 1958766565 1289 QVEEAEAR 1296
Cdd:COG4942 235 EAAAAAER 242
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
329-636 |
1.02e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.45 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 329 ELNFHQGQVEQLVQERDKARQDLEKAEKRNLDFVREMDDCHSALEQLTEKKIKHLEQEYRG-----------RLSLLRSE 397
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRvkekigeleaeIASLERSI 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 398 VEMERELfwEQARRQRAVLEQDVGRLQAEETSLREKLTlalkensRLQKEIIEVVEKLSDSEKLVLRLQSDLQFVLKD-- 475
Cdd:TIGR02169 311 AEKEREL--EDAEERLAKLEAEIDKLLAEIEELEREIE-------EERKRRDKLTEEYAELKEELEDLRAELEEVDKEfa 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 476 KLEPQSMELLAQEEQFTAILNDYELKCRDLQDRNDELQAELEGLRVRLPRSRQSpsgtpgthrrwtpgrgpadnlfVGES 555
Cdd:TIGR02169 382 ETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAK----------------------INEL 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 556 IPVSLETEIKMQQMKENYQELRMQLETkvnyYEKEIEVMKRNFEKDKKEMEQAfQLEVSVLEGQKADLET--LYAKSQEV 633
Cdd:TIGR02169 440 EEEKEDKALEIKKQEWKLEQLAADLSK----YEQELYDLKEEYDRVEKELSKL-QRELAEAEAQARASEErvRGGRAVEE 514
|
...
gi 1958766565 634 ILG 636
Cdd:TIGR02169 515 VLK 517
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1060-1310 |
1.09e-05 |
|
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: 49.38 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1060 ALEKADSRESYRAELQRLSEENSVLKSDLGKIQLELGTSESRNEVQRQEIEVLKRdkeqacfdleelstQTQKYKDEMSQ 1139
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALAR--------------RIRALEQELAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1140 LNCRILQLEGDSSGLHTQKEENHAAIQVLMKKLeeaecrekQQGDQIKHLKI--------ELERVNEECQRLRLSQAELT 1211
Cdd:COG4942 81 LEAELAELEKEIAELRAELEAQKEELAELLRAL--------YRLGRQPPLALllspedflDAVRRLQYLKYLAPARREQA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1212 GSLEESQGQLHSVQLRLEAAQSQHDRIVQGLQEQMsqlvpgarvAELQHLLSLREEEAERLNAQQEEYKQQLKAREDQVE 1291
Cdd:COG4942 153 EELRADLAELAALRAELEAERAELEALLAELEEER---------AALEALKAERQKLLARLEKELAELAAELAELQQEAE 223
|
250
....*....|....*....
gi 1958766565 1292 EAEARLHNVEWLLQEKVEE 1310
Cdd:COG4942 224 ELEALIARLEAEAAAAAER 242
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1004-1249 |
2.93e-05 |
|
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: 48.91 E-value: 2.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1004 VQETPLQLRGETARMRPSLPYSELpNPQEAKVMSVMSESEMNDVKTKLLQLEDVVralekadsrESYRAELQRLSEENSV 1083
Cdd:TIGR02169 292 VKEKIGELEAEIASLERSIAEKER-ELEDAEERLAKLEAEIDKLLAEIEELEREI---------EEERKRRDKLTEEYAE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1084 LKSDLGKIQLELGTSESRNEVQRQEIEVLKRDKEQACFDLEELSTQTQKYKDEMSQLNCRILQLEGDSSGLHTQKEENHA 1163
Cdd:TIGR02169 362 LKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1164 AIQVLMKKLEEAECREKQQGDQIKHLKIELERVNEECQRL--RLSQAELTGS-LEESQGQLHSVQLRLEAAQSQHDRIVQ 1240
Cdd:TIGR02169 442 EKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVekELSKLQRELAeAEAQARASEERVRGGRAVEEVLKASIQ 521
|
....*....
gi 1958766565 1241 GLQEQMSQL 1249
Cdd:TIGR02169 522 GVHGTVAQL 530
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
320-448 |
3.06e-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: 3.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 320 QAALACYRQELNFHQGQVEQLVQERDKARQDLEKAEKRNLDF-VREMDDCHSALEQLTEKK--IKHLEQEYRGRLSLLRS 396
Cdd:COG4913 294 EAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELeeRERRRARLEALLAALGL 373
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1958766565 397 EVEMERELFWE---QARRQRAVLEQDVGRLQAEETSLREKLTLALKENSRLQKEI 448
Cdd:COG4913 374 PLPASAEEFAAlraEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEI 428
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1068-1337 |
3.87e-05 |
|
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: 48.18 E-value: 3.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1068 ESYRAELQRLSEENSVLKSdlgkIQLELGTSESRNEvqrqEIEVLKRDKEQACFDLEELSTQTQKYKDEMSQLNCRILQL 1147
Cdd:pfam05483 363 ELLRTEQQRLEKNEDQLKI----ITMELQKKSSELE----EMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEEL 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1148 EGDSSGLHTQKEENHAAIQVLMKKLEEAECREKQQGDQIKHLKIELER-------VNEECQRLRLSQAELTGSLEESQGQ 1220
Cdd:pfam05483 435 KGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKeklknieLTAHCDKLLLENKELTQEASDMTLE 514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1221 LHSVQLRLEAAQSQHDRI---VQGLQEQMSQLvpgarvaeLQHLLSLREEeaerLNAQQEEYKQQLKAREDQVEEAEARL 1297
Cdd:pfam05483 515 LKKHQEDIINCKKQEERMlkqIENLEEKEMNL--------RDELESVREE----FIQKGDEVKCKLDKSEENARSIEYEV 582
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1958766565 1298 HNVE---WLLQEKVEELRKQFEKNTRSdllLKELYVENAHLMK 1337
Cdd:pfam05483 583 LKKEkqmKILENKCNNLKKQIENKNKN---IEELHQENKALKK 622
|
|
| FRQ1 |
COG5126 |
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
203-263 |
5.05e-05 |
|
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 44.40 E-value: 5.05e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958766565 203 QGIWHELGVGSSGHLNEQELAVVCRSIGLHGLEkQELEELFSKLDRDGDGRVSLAEFQLGL 263
Cdd:COG5126 36 ATLFSEADTDGDGRISREEFVAGMESLFEATVE-PFARAAFDLLDTDGDGKISADEFRRLL 95
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
336-523 |
5.96e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 5.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 336 QVEQLVQERDKARQDLEKAEKRnldfvremddchsaLEQLTEKKikhleQEYRGRLSLLRSEVEM-ERELFWEQARRQRA 414
Cdd:COG4913 611 KLAALEAELAELEEELAEAEER--------------LEALEAEL-----DALQERREALQRLAEYsWDEIDVASAEREIA 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 415 VLEQ----------DVGRLQAEETSLREKLTLALKENSRLQKEIIEVVEKLSDSEKLVLRLQSDLQFVLKDKLEPQSMEL 484
Cdd:COG4913 672 ELEAelerldassdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALL 751
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1958766565 485 laqEEQFTAILND--YELKCRDLQDRNDELQAELEGLRVRL 523
Cdd:COG4913 752 ---EERFAAALGDavERELRENLEERIDALRARLNRAEEEL 789
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1062-1328 |
6.54e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 6.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1062 EKADSRESYRAELQRLSEENSVLKSDLGKIQLELG------TSESRNEVQRQEIEVLKRDKEQ-ACFDLEELSTQTQKYK 1134
Cdd:PRK03918 449 HRKELLEEYTAELKRIEKELKEIEEKERKLRKELRelekvlKKESELIKLKELAEQLKELEEKlKKYNLEELEKKAEEYE 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1135 demsQLNCRILQLEGDSSGLHT---QKEENHAAIQVLMKKLEEAECREKQQGDQIKHLKIE-LERVNEECQRLRLSQAEL 1210
Cdd:PRK03918 529 ----KLKEKLIKLKGEIKSLKKeleKLEELKKKLAELEKKLDELEEELAELLKELEELGFEsVEELEERLKELEPFYNEY 604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1211 TgSLEESQGQLHSVQLRLEAAQSQHDRIVQGLQEQMSQLVP-GARVAELQHLLSlrEEEAERLNAQQEEYKQQLKAREDQ 1289
Cdd:PRK03918 605 L-ELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEElRKELEELEKKYS--EEEYEELREEYLELSRELAGLRAE 681
|
250 260 270
....*....|....*....|....*....|....*....
gi 1958766565 1290 VEEAEARLHNVEWLLQEKVEELRKQFEKNTRSDLLLKEL 1328
Cdd:PRK03918 682 LEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKAL 720
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1041-1369 |
1.04e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.94 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1041 ESEMNDVKTKLLQLEDVVRALEkadsresyrAELQRLSEE-----NSVLKSDLGKIQLELGTSESRNEVQRQEIEVLKRD 1115
Cdd:TIGR04523 273 QKELEQNNKKIKELEKQLNQLK---------SEISDLNNQkeqdwNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQ 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1116 KEQACFDLEELSTQTQKYKDEMSQLNCRILQLEGDSSGLHTQKEENHAAIQVLMKKLEEAECREKQQGDQIKHLKIELER 1195
Cdd:TIGR04523 344 ISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKEL 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1196 VNEECQRLR----------------------------LSQAELTGSLEESQGQLHSVQLRLEAAQSQHDRIVQ---GLQE 1244
Cdd:TIGR04523 424 LEKEIERLKetiiknnseikdltnqdsvkeliiknldNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKelkKLNE 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1245 QMSQLvpGARVAELQHLLSLREEEAERLNAQQEEYKQQLKAREDQVEEAEARL--HNVEWLLQEKVEELRKQFE------ 1316
Cdd:TIGR04523 504 EKKEL--EEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELkkENLEKEIDEKNKEIEELKQtqkslk 581
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1958766565 1317 -KNTRSDLLLKELYVENAHLMKAVQLTEEKQRGAEKKNCVLEEKVRALNKLISK 1369
Cdd:TIGR04523 582 kKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKN 635
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1041-1284 |
1.11e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.98 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1041 ESEMNDVKTKLLQLEDVVRALEKA-----------------DSRESYRAELQRLSEENSVLKSDLGKIQLELGTSESRNE 1103
Cdd:TIGR02169 757 KSELKELEARIEELEEDLHKLEEAlndlearlshsripeiqAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQ 836
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1104 VQRQEIEVLKRDKEQACFDLEELSTQTQKYKDEMSQLNCRILQLEGDSSGLHTQKEENHAAIQVLMKKLEEAECREKQQG 1183
Cdd:TIGR02169 837 ELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKR 916
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1184 DQIKHLKIELERVNEECQRLRLSQAEL------TGSLEESQGQLHSVQLRLEAAQSQHDRIVQGLQEQMsqlvpgARVAE 1257
Cdd:TIGR02169 917 KRLSELKAKLEALEEELSEIEDPKGEDeeipeeELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVL------KRLDE 990
|
250 260
....*....|....*....|....*..
gi 1958766565 1258 LQHLLSLREEEAERLNAQQEEYKQQLK 1284
Cdd:TIGR02169 991 LKEKRAKLEEERKAILERIEEYEKKKR 1017
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
337-645 |
1.13e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.98 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 337 VEQLVQERDKARQDLEKAEKRNLDFVREMDDCHSALEQLTEKKIKHLeqEYRGRLSLLRSEVEMERELFWEQARRQRAVL 416
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE--RYQALLKEKREYEGYELLKEKEALERQKEAI 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 417 EQDVGRLQAEETSLREKLtlalkenSRLQKEIIEVVEKLSDSEKLVLRLQSDLQFVLKDKLEpqsmELLAQEEQFTAILN 496
Cdd:TIGR02169 243 ERQLASLEEELEKLTEEI-------SELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIG----ELEAEIASLERSIA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 497 DYELKCRDLQDRNDELQAELEGLRVRLPRSRQSPSGTPGTHRRWTPGrgpadnlfVGESIPVSLETEIKMQQMKENYQEL 576
Cdd:TIGR02169 312 EKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEE--------YAELKEELEDLRAELEEVDKEFAET 383
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958766565 577 R---MQLETKVNYYEKEIEVMKRNF-----EKDKKEMEQAF-QLEVSVLEGQKADLETLYAKSQEVILGLKEQLQDAA 645
Cdd:TIGR02169 384 RdelKDYREKLEKLKREINELKRELdrlqeELQRLSEELADlNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLA 461
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1165-1374 |
1.31e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1165 IQVLMKKLEEAECREKQQGDQIKHLKIELERVNEECQRLRLSQAELTGSLEESQGQLHSVQLRLEAAQSQHDRIVQGLQE 1244
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1245 QMSQLV----------PGARVAELQHLLSLREEEAERLNAQQEEyKQQLKAREDQVEEAEARLHNVEWLLQEKVEELRKQ 1314
Cdd:COG3883 98 SGGSVSyldvllgsesFSDFLDRLSALSKIADADADLLEELKAD-KAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1315 FEKNTRsdlLLKELYVENAHLMKAVQLTEEKQRGAEKKNCVLEEKVRALNKLISKMAPAS 1374
Cdd:COG3883 177 QAEQEA---LLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1040-1317 |
2.16e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1040 SESEMNDVKTKLLQLEDVVRALEKAdsrESYRAELQRLSEENSVLKSDLGKIQLELGTSESRNEVQRQEIEVLKRDKEQA 1119
Cdd:PRK03918 143 SDESREKVVRQILGLDDYENAYKNL---GEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPEL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1120 CFDLEELSTQTQKY---KDEMSQLNCRILQLEGDSSGLHTQKEENHAAIQVLMKKLEEAEcrekqqgDQIKHLKiELERV 1196
Cdd:PRK03918 220 REELEKLEKEVKELeelKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELE-------EKVKELK-ELKEK 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1197 NEECQRLRlsqaeltGSLEESQGQLHSVQLRLEAAQSQhdriVQGLQEQMSQLVP-GARVAELQHLLSLREEEAERLNAQ 1275
Cdd:PRK03918 292 AEEYIKLS-------EFYEEYLDELREIEKRLSRLEEE----INGIEERIKELEEkEERLEELKKKLKELEKRLEELEER 360
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1958766565 1276 QEEYkQQLKAREDQVEEAEARLHNVEwllQEKVEELRKQFEK 1317
Cdd:PRK03918 361 HELY-EEAKAKKEELERLKKRLTGLT---PEKLEKELEELEK 398
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1073-1373 |
2.48e-04 |
|
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: 45.88 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1073 ELQRLSEENSVLKSDL-GKIQLELGTSESRNEvqrqEIEVLKRDKEQacfdLEELSTQTQKYKDEMSQLNCRILQLEGDS 1151
Cdd:pfam15921 427 EVQRLEALLKAMKSECqGQMERQMAAIQGKNE----SLEKVSSLTAQ----LESTKEMLRKVVEELTAKKMTLESSERTV 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1152 SGLHTQKEENHAAIQVLMKKLEEAECREKQQGDQIKHLKIE---LERVNEECQRLRLSQAELTGSLEESQGQLHSVQLRL 1228
Cdd:pfam15921 499 SDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEgdhLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLV 578
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1229 eaaqSQHDRIVQGLQEQMSQLvpgarvaelqhllslrEEEAERLNAQQEEYKQQLKAREDQVEEAEARLHNVEW----LL 1304
Cdd:pfam15921 579 ----GQHGRTAGAMQVEKAQL----------------EKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELekvkLV 638
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958766565 1305 QEKVEELRKQFEKNTRSDLLLKELYVENAHLMKAVQLTEEKQRGAEKKNcvlEEKVRALNKLISKMAPA 1373
Cdd:pfam15921 639 NAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKS---EEMETTTNKLKMQLKSA 704
|
|
| FRQ1 |
COG5126 |
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
1-71 |
2.48e-04 |
|
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 42.47 E-value: 2.48e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958766565 1 MDNEEENHYVSRLRDVYSSCDTTGTGFLDQEELTQLCTKLGLEEQLPALLHILL---GDGRLarvNFEEFKEGF 71
Cdd:COG5126 59 MESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTALGVSEEEADELFARLdtdGDGKI---SFEEFVAAV 129
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1128-1322 |
2.60e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1128 TQTQKYKDEMSQLNCRILQLEGDSSGLHTQKEENHAAIQVLMKKLEEAECREKQQGDQIKHLKIELERVNEEC-QRLRLS 1206
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELgERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1207 Q---------AELTGSleESQGQLHSVQLRLEAAQSQHDRIVQGLQEQMSQLVpgARVAELQHLLSLREEEAERLNAQQE 1277
Cdd:COG3883 96 YrsggsvsylDVLLGS--ESFSDFLDRLSALSKIADADADLLEELKADKAELE--AKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1958766565 1278 EYKQQLKAREDQVEEAEARLHNVEWLLQEKVEELRKQFEKNTRSD 1322
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1055-1361 |
3.32e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.52 E-value: 3.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1055 EDVVRALEKADSRESYRAELQRLSEE----NSVLKSDLGKIQLELGTSESRNEVQRQEIEvlKRDKEQACFDLEELSTQT 1130
Cdd:PTZ00121 1513 DEAKKAEEAKKADEAKKAEEAKKADEakkaEEKKKADELKKAEELKKAEEKKKAEEAKKA--EEDKNMALRKAEEAKKAE 1590
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1131 QKYKDEMSQLNCRILQLEGDSsgLHTQKEENHAAIQVlmKKLEEaecrEKQQGDQIKHLKIELERVNEECQRlrlsqael 1210
Cdd:PTZ00121 1591 EARIEEVMKLYEEEKKMKAEE--AKKAEEAKIKAEEL--KKAEE----EKKKVEQLKKKEAEEKKKAEELKK-------- 1654
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1211 tgslEESQGQLHSVQLRLEAAQSQHdrivqglqeqmsqlvpgaRVAELQHLLSLREEEAERLNAQQEEYK--QQLKARED 1288
Cdd:PTZ00121 1655 ----AEEENKIKAAEEAKKAEEDKK------------------KAEEAKKAEEDEKKAAEALKKEAEEAKkaEELKKKEA 1712
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958766565 1289 QVEEAEARLHNVEWLLQEKVEELRKQFEKNTRSdllLKELYVENAHLMKAVQLTEEKQRGAE----KKNCVLEEKVR 1361
Cdd:PTZ00121 1713 EEKKKAEELKKAEEENKIKAEEAKKEAEEDKKK---AEEAKKDEEEKKKIAHLKKEEEKKAEeirkEKEAVIEEELD 1786
|
|
| XopAW |
NF041410 |
XopAW family type III secretion system calcium-binding effector; |
240-276 |
3.50e-04 |
|
XopAW family type III secretion system calcium-binding effector;
Pssm-ID: 469301 [Multi-domain] Cd Length: 227 Bit Score: 43.52 E-value: 3.50e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1958766565 240 EELFSKLDRDGDGRVSLAEFQLGLFGHEPPSLPASSS 276
Cdd:NF041410 139 SQLFSALDSDGDGSVSSDELAAALQPPPPPPLFSLSS 175
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1068-1369 |
4.40e-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: 44.96 E-value: 4.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1068 ESYRAELQRLSEENSVLKSDLGKIQLELGTSESRNEVQRQEIEVLKRDKEQACFDLEELSTQT---QKYKDEMSQLNCRI 1144
Cdd:pfam02463 166 RLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYldyLKLNEERIDLLQEL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1145 LQLEGDSSGLHTQKEENHAAIQVLMKKLEEAECREKQQGD-QIKHLKIELERVNEECQRLRLSQAELTGSLEESQGQLHS 1223
Cdd:pfam02463 246 LRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEeELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKK 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1224 VQLRLEAAQSQHDRIVQGLQE-QMSQLVPGARVAELQHLLSLREEEAERLNAQQEEYKQQLKAREDQVEEAEARLHNVEW 1302
Cdd:pfam02463 326 AEKELKKEKEEIEELEKELKElEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEK 405
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958766565 1303 LLQEKVEELRKQF-----EKNTRSDLLLKELYVENAHLMKA--VQLTEEKQRGAEKKNCVLEEKVRALNKLISK 1369
Cdd:pfam02463 406 EAQLLLELARQLEdllkeEKKEELEILEEEEESIELKQGKLteEKEELEKQELKLLKDELELKKSEDLLKETQL 479
|
|
| EFh |
smart00054 |
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ... |
238-259 |
5.31e-04 |
|
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in pairs. Links between disease states and genes encoding EF-hands, particularly the S100 subclass, are emerging. Each motif consists of a 12 residue loop flanked on either side by a 12 residue alpha-helix. EF-hands undergo a conformational change unpon binding calcium ions.
Pssm-ID: 197492 [Multi-domain] Cd Length: 29 Bit Score: 38.51 E-value: 5.31e-04
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1055-1278 |
5.66e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 5.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1055 EDVVRALEKADS----RESYRaELQRLSEENSVLKSDLGKIQLElgTSESRNEVQRQEIEVLKRDKEQACFDLEELSTQT 1130
Cdd:COG4913 242 EALEDAREQIELlepiRELAE-RYAAARERLAELEYLRAALRLW--FAQRRLELLEAELEELRAELARLEAELERLEARL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1131 QKYKDEMSQLNCRILQLEGDssglhtQKEENHAAIQVLMKKLEEAECREKQQGDQIKHLKIELERVNEECQRLRLSQAEL 1210
Cdd:COG4913 319 DALREELDELEAQIRGNGGD------RLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAAL 392
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958766565 1211 TGSLEESQGQLHSVQLRLEAAQSQHDRIVQGLQEQMSQL------VPgarvaelQHLLSLREEEAERLNAQQEE 1278
Cdd:COG4913 393 LEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLerrksnIP-------ARLLALRDALAEALGLDEAE 459
|
|
| EF-hand_1 |
pfam00036 |
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ... |
238-263 |
6.24e-04 |
|
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering/transport proteins. The first group is the largest and includes the most well-known members of the family such as calmodulin, troponin C and S100B. These proteins typically undergo a calcium-dependent conformational change which opens a target binding site. The latter group is represented by calbindin D9k and do not undergo calcium dependent conformational changes.
Pssm-ID: 425435 [Multi-domain] Cd Length: 29 Bit Score: 38.15 E-value: 6.24e-04
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1106-1323 |
6.64e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 6.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1106 RQEIEVLKRDKEQACFDLEELSTQTQKYKDEMSQLNCRILQLEG---------DSSGLHTQkeenHAAIQVLMKKLEEAE 1176
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRlaeyswdeiDVASAERE----IAELEAELERLDASS 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1177 CREKQQGDQIKHLKIELERVNEECQRLRLSQAELTGSLEESQGQLHSVQLRLEAA-QSQHDRIVQGLQEQMSQLVPGARV 1255
Cdd:COG4913 685 DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAeDLARLELRALLEERFAAALGDAVE 764
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1256 AELQHLL--------SLREEEAERLNAQQEEYKQQLKARE-------DQVEEAEARLHNVEWL-LQEKVEELRKQFEKNT 1319
Cdd:COG4913 765 RELRENLeeridalrARLNRAEEELERAMRAFNREWPAETadldadlESLPEYLALLDRLEEDgLPEYEERFKELLNENS 844
|
....
gi 1958766565 1320 RSDL 1323
Cdd:COG4913 845 IEFV 848
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
409-592 |
7.54e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 7.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 409 ARRQRAVLEQDVGRLQAEETSLREKLTL--ALKENSRLQKEIIEVVEKLSDSEKLVLRLQSDLQfVLKDKLE------PQ 480
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEERLEAleAELDALQERREALQRLAEYSWDEIDVASAEREIA-ELEAELErldassDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 481 SMELLAQEEQFTAILNDYELKCRDLQDRNDELQAELEGLRVRLPRSRQSPSGTPGTHRRWTpgRGPADNLFVGESIPVSL 560
Cdd:COG4913 687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLEL--RALLEERFAAALGDAVE 764
|
170 180 190
....*....|....*....|....*....|..
gi 1958766565 561 eteikmQQMKENYQELRMQLETKVNYYEKEIE 592
Cdd:COG4913 765 ------RELRENLEERIDALRARLNRAEEELE 790
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1046-1371 |
7.62e-04 |
|
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: 43.95 E-value: 7.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1046 DVKTKLLQLEDVVRALEKADSRESYRAELQRLSEENSVLKSDLGKIQLELGTSESRNEVQR------------QEIEVLK 1113
Cdd:pfam15921 114 DLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQlrkmmlshegvlQEIRSIL 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1114 RDKEQAC----FDLEELSTQ------------TQKYKDEMSQLNCRILQLEGDssgLHTQKEENHAAIQVLMKkleeaec 1177
Cdd:pfam15921 194 VDFEEASgkkiYEHDSMSTMhfrslgsaiskiLRELDTEISYLKGRIFPVEDQ---LEALKSESQNKIELLLQ------- 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1178 rekQQGDQIKHL----KIELERVNEECQRLRlSQAEltgsleESQGQLHSVQLRLEAAQSQHDRIVQGLQEQMSQLVPGA 1253
Cdd:pfam15921 264 ---QHQDRIEQLisehEVEITGLTEKASSAR-SQAN------SIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSEL 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1254 RVA---------ELQHLLSLREEEAERLNAQQEEYKQQLKAREDQVEEAEARLHNVEWLLQEKVEELRKQFEKNTRS--- 1321
Cdd:pfam15921 334 REAkrmyedkieELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNsit 413
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958766565 1322 -DLLLKELYVENAH------LMKAvqLTEEKQRGAEKKNCVLEEKVRALNKLISKMA 1371
Cdd:pfam15921 414 iDHLRRELDDRNMEvqrleaLLKA--MKSECQGQMERQMAAIQGKNESLEKVSSLTA 468
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1099-1294 |
7.76e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 43.73 E-value: 7.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1099 ESRNEVQRQEIEVLKRDKEQACFDLEELSTQTQKYKDEMSQLNCRILQLEGDSSGLHTQKEENHAAIQVLMKKLEEAECR 1178
Cdd:pfam07888 51 EAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEAR 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1179 EKQQGDQIKHLKIELERVNEECQRLRLSQAELTGSLEESQGQLHSVQLRLEAAQSQHDRIVQGLQEQMSQLvpGARVAEL 1258
Cdd:pfam07888 131 IRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSL--AQRDTQV 208
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1958766565 1259 QHL------LSLREEEAERLNAQQEEYKQQLKAREDQVEEAE 1294
Cdd:pfam07888 209 LQLqdtittLTQKLTTAHRKEAENEALLEELRSLQERLNASE 250
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
327-490 |
7.76e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 7.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 327 RQELNFHQGQVEQLVQERDKARQDLEKAEKRNLDFVREMDDCHSALEQL-TEKKIKHLEQEYRGRLSLLRSEVEMERElf 405
Cdd:COG4717 80 LKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLpLYQELEALEAELAELPERLEELEERLEE-- 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 406 WEQARRQRAVLEQDVGRLQAEETSLREKLTLALKEN-SRLQKEIIEVVEKLSDSEKLVLRLQSDLQFVLKDKLEPQSMEL 484
Cdd:COG4717 158 LRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELE 237
|
....*.
gi 1958766565 485 LAQEEQ 490
Cdd:COG4717 238 AAALEE 243
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1107-1317 |
8.13e-04 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 43.69 E-value: 8.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1107 QEIEVLKRDKEQACFDLEELstQTQKYKDEMSQLNCRILQLEGDssglhTQKEENhaAIQVLMKKLEEAECREKQQGDQI 1186
Cdd:pfam06160 237 KEIQQLEEQLEENLALLENL--ELDEAEEALEEIEERIDQLYDL-----LEKEVD--AKKYVEKNLPEIEDYLEHAEEQN 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1187 KHLKIELERVNeecQRLRLSQAELtGSLEESQGQLHSVqlrleaaQSQHDRIVQGLQEQMsqlvpgARVAELQHLLSLRE 1266
Cdd:pfam06160 308 KELKEELERVQ---QSYTLNENEL-ERVRGLEKQLEEL-------EKRYDEIVERLEEKE------VAYSELQEELEEIL 370
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1958766565 1267 EEAERLNAQQEEYKQQLKAREDQVEEAEARLHNvewlLQEKVEELRKQFEK 1317
Cdd:pfam06160 371 EQLEEIEEEQEEFKESLQSLRKDELEAREKLDE----FKLELREIKRLVEK 417
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1071-1332 |
8.92e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 8.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1071 RAELQRLSEENSVLKSDLGKIQLELGTSESRNEVQRQEIEVLKRDKEQACFDLEELSTQTQKYKDEMSQLNCRILQLEGD 1150
Cdd:COG4372 44 QEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1151 SSGLHTQKEENHAAIQVLMKKLEEAECREKQQGDQIKHLKIELERVNEECQRLRLSQA--ELTGSLEESQGQLHSVQLRL 1228
Cdd:COG4372 124 RQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAeqALDELLKEANRNAEKEEELA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1229 EAAQSQHDRIVQGLQEQMSQLVPGARVAELQHLLSLREEEAERLNAQQEEYKQQLKAREDQVEEAEARLHNVEWLLQEKV 1308
Cdd:COG4372 204 EAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAAL 283
|
250 260
....*....|....*....|....
gi 1958766565 1309 EELRKQFEKNTRSDLLLKELYVEN 1332
Cdd:COG4372 284 ELEALEEAALELKLLALLLNLAAL 307
|
|
| EFh_parvalbumin_like |
cd16251 |
EF-hand, calcium binding motif, found in parvalbumin-like EF-hand family; The family includes ... |
195-260 |
1.24e-03 |
|
EF-hand, calcium binding motif, found in parvalbumin-like EF-hand family; The family includes alpha- and beta-parvalbumins, and a group of uncharacterized calglandulin-like proteins. Parvalbumins are small, acidic, cytosolic EF-hand-containing Ca2+-buffer and Ca2+ transporter/shuttle proteins belonging to EF-hand superfamily. They are expressed by vertebrates in fast-twitch muscle cells, specific neurons of the central and peripheral nervous system, sensory cells of the mammalian auditory organ (Corti's cell), and some other cells, and characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix) called AB, CD, and EF, but only CD and EF can chelate metal ions, such as Ca2+ and Mg2+. Thus, they may play an additional role in Mg2+ handling. Moreover, parvalbumins represent one of the major animal allergens. In metal-bound states, parvalbumins possess a rigid and stable tertiary structure and display strong allergenicity. In contrast, the metal-free parvalbumins are intrinsically disordered, and the loss of metal ions results in a conformational change that decreases their IgE binding capacity. Furthermore, parvalbumins have been widely used as a neuronal marker for a variety of functional brain systems. They also function as a Ca2+ shuttle transporting Ca2+ from troponin-C (TnC) to the sarcoplasmic reticulum (SR) Ca2+ pump during muscle relaxation. Thus they may facilitate myocardial relaxation and play important roles in cardiac diastolic dysfunction. Parvalbumins consists of alpha- and beta- sublineages, which can be distinguished on the basis of isoelectric point (pI > 5 for alpha; pI
Pssm-ID: 319994 [Multi-domain] Cd Length: 101 Bit Score: 39.82 E-value: 1.24e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958766565 195 FNTPENQVQGIWHELGVGSSGHLNEQELAVVCRSIGLHG--LEKQELEELFSKLDRDGDGRVSLAEFQ 260
Cdd:cd16251 29 KQKSEDQIKKVFQILDKDKSGFIEEEELKYILKGFSIAGrdLTDEETKALLAAGDTDGDGKIGVEEFA 96
|
|
| EFh_parvalbumin_alpha |
cd16254 |
EF-hand, calcium binding motif, found in alpha-parvalbumin; Alpha-parvalbumin is cytosolic Ca2 ... |
201-259 |
1.31e-03 |
|
EF-hand, calcium binding motif, found in alpha-parvalbumin; Alpha-parvalbumin is cytosolic Ca2+/Mg2+-binding protein expressed mainly in fast-twitch skeletal myofibrils, where it may act as a soluble relaxing factor facilitating the Ca2+-mediated relaxation phase. It is also expressed in rapidly firing neurons, particularly GABA-ergic neurons, and thus may confer protection against Ca2+ toxicity. The major role of alpha-parvalbumin is metal buffering and transport of Ca2+. It binds different metal cations, and exhibits very high affinity for Ca2+ and physiologically significant affinity for Mg2+. Alpha-parvalbumin is characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix) called AB, CD, and EF, but only CD and EF can chelate metal ions, such as Ca2+ and Mg2+. Both metal ion-binding sites in alpha-parvalbumin are high-affinity sites. Additionally, in contrast to beta-parvalbumin, alpha-parvalbumin is less acidic and has an additional residue in the C-terminal helix.
Pssm-ID: 319997 [Multi-domain] Cd Length: 101 Bit Score: 39.42 E-value: 1.31e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958766565 201 QVQGIWHELGVGSSGHLNEQELAVVCRSIGLHG--LEKQELEELFSKLDRDGDGRVSLAEF 259
Cdd:cd16254 35 DVKKVFHILDKDKSGFIEEDELKFVLKGFSPDGrdLSDKETKALLAAGDKDGDGKIGIDEF 95
|
|
| EF-hand_6 |
pfam13405 |
EF-hand domain; |
238-263 |
1.39e-03 |
|
EF-hand domain;
Pssm-ID: 463869 [Multi-domain] Cd Length: 30 Bit Score: 37.54 E-value: 1.39e-03
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1080-1363 |
1.51e-03 |
|
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: 43.19 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1080 ENSVLKSDLGKIQLELGTSESRNE--VQRQEIEVLKRDKEQACFDLEELSTQTQKYKDEMSQLNcRILQLEGDSSGLHTQ 1157
Cdd:pfam17380 267 ENEFLNQLLHIVQHQKAVSERQQQekFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMD-RQAAIYAEQERMAME 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1158 KEENHAAIQVLMKKLEEAECREKQqgdqikhLKIELERVnEECQRLRLsqaeltgsleESQGQLHSVQLRLEAAQSQHdr 1237
Cdd:pfam17380 346 RERELERIRQEERKRELERIRQEE-------IAMEISRM-RELERLQM----------ERQQKNERVRQELEAARKVK-- 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1238 ivqgLQEQmsqlvpgarvaELQHLLSLREEEAERLNAQQEEYKQ-QLKAREDQVEEAEARLHNVEWLLQEKVEELRKQFE 1316
Cdd:pfam17380 406 ----ILEE-----------ERQRKIQQQKVEMEQIRAEQEEARQrEVRRLEEERAREMERVRLEEQERQQQVERLRQQEE 470
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1958766565 1317 KNTRSDLLLKELYVENAHLMKAVQLTEEKQRGAEKKNCVLEEKVRAL 1363
Cdd:pfam17380 471 ERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKL 517
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
326-523 |
1.64e-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: 43.13 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 326 YRQELNFHQGQVEQLVQERDKARQDLEKAEKRNLDFVREMDDCHSALEQLtEKKIKHLE---QEYRGRLSLLRSEVE--- 399
Cdd:TIGR02169 707 LSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENV-KSELKELEariEELEEDLHKLEEALNdle 785
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 400 -MERELFWEQARRQRAVLEQDVGRLQAEETSLREKLTLALKENSRLQKEIIEVVEKLSDSEKLVLRLQSDLqfvlkDKLE 478
Cdd:TIGR02169 786 aRLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEI-----ENLN 860
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1958766565 479 PQSMELLAQEEQFTAILNDYELKCRDLQDRNDELQAELEGLRVRL 523
Cdd:TIGR02169 861 GKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKI 905
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
319-519 |
1.80e-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: 42.74 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 319 QQAALACYRQELNFHQGQVEQLVQERDKARQDLEKAEKRNLDFVREMDDCHSALEQLTEKKIKHLEQeyrgrLSLLRSEV 398
Cdd:TIGR02168 822 LRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEA-----LALLRSEL 896
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 399 EmerelfweQARRQRAVLEQDVGRLQAEETSLREKLTLALKENSRLQKEIIEVVEKLSDSEKLVLRLQSDLQFVLKDKLE 478
Cdd:TIGR02168 897 E--------ELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEE 968
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1958766565 479 PQSMELLAQEEQFTAI-------LNDYElkcrDLQDRNDELQAELEGL 519
Cdd:TIGR02168 969 EARRRLKRLENKIKELgpvnlaaIEEYE----ELKERYDFLTAQKEDL 1012
|
|
| XopAW |
NF041410 |
XopAW family type III secretion system calcium-binding effector; |
213-307 |
1.81e-03 |
|
XopAW family type III secretion system calcium-binding effector;
Pssm-ID: 469301 [Multi-domain] Cd Length: 227 Bit Score: 41.59 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 213 SSGHLNEQELAVVCRS---IGLHGLEKQELEELFSKLDRDGDGRVSLAEFQLGLFGHEppSLPASSSLIKPngpwshyqs 289
Cdd:NF041410 76 GDGSLSSDELAAAAPPpppPPDQAPSTELADDLLSALDTDGDGSISSDELSAGLTSAG--SSADSSQLFSA--------- 144
|
90
....*....|....*...
gi 1958766565 290 LDFNVDEKVNLLELTWAL 307
Cdd:NF041410 145 LDSDGDGSVSSDELAAAL 162
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1043-1245 |
1.86e-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: 42.74 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1043 EMNDVKTKLLQLEDVVRALEKadSRESYRAELQRLSEENSVLKSDLGKIQLELGT-------SESRNEVQRQEIEVLKRD 1115
Cdd:TIGR02168 310 RLANLERQLEELEAQLEELES--KLDELAEELAELEEKLEELKEELESLEAELEEleaeleeLESRLEELEEQLETLRSK 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1116 KEQACFDLEELSTQTQKYKDEMSQLNCRILQLEGDSSGLHTQKEEnhAAIQVLMKKLEEAECREKQQGDQIKHLKIELER 1195
Cdd:TIGR02168 388 VAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE--AELKELQAELEELEEELEELQEELERLEEALEE 465
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1196 VNEECQRLRLSQAELTGSLEESQGQLHSVQLRLEAAQSQHDRIVQGLQEQ 1245
Cdd:TIGR02168 466 LREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQ 515
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
327-478 |
2.06e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 327 RQELNFHQGQVEQLVQERDKARQDLEKAEKRNLDFVREMDDCHSALEQLtEKKIKhleqEYRGRLSLLRSEVE---MERE 403
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEV-EARIK----KYEEQLGNVRNNKEyeaLQKE 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958766565 404 LfwEQARRQRAVLEQDVGRLQAEETSLREKLTLALKENSRLQKEIIEVVEKLsdsEKLVLRLQSDLQFVLKDKLE 478
Cdd:COG1579 98 I--ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEL---DEELAELEAELEELEAEREE 167
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
319-522 |
2.22e-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: 42.75 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 319 QQAALACYRQELNFHQGQVEQLVQERDKARQDLEKAEKRNLDFVREMDDCHSALEQLTE--KKIKHLEQEYRGRLSLLRS 396
Cdd:TIGR02169 810 IEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEelEELEAALRDLESRLGDLKK 889
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 397 EV-EMERELFWEQARRQRAVLEQDVGRLQAEEtsLREKLTLALKENS---RLQKEIIEVVEKLSDSEKLVLRLQSDLQFV 472
Cdd:TIGR02169 890 ERdELEAQLRELERKIEELEAQIEKKRKRLSE--LKAKLEALEEELSeieDPKGEDEEIPEEELSLEDVQAELQRVEEEI 967
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1958766565 473 lkDKLEPQSMellAQEEQFTAILNDYElkcrDLQDRNDELQAELEGLRVR 522
Cdd:TIGR02169 968 --RALEPVNM---LAIQEYEEVLKRLD----ELKEKRAKLEEERKAILER 1008
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1041-1353 |
2.23e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1041 ESEMNDVKTKLLQLEDVVRALEKADSrESYRAELQRLSEENSVLKSDLGKIQLELGTSESRNEVQRQEIEVLKRDKEQAC 1120
Cdd:COG4717 162 EEELEELEAELAELQEELEELLEQLS-LATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1121 fDLEELSTQTQkykdeMSQLNCRILQLEGDSSGLHTQKEENHAAIQV-----------LMKKLEEAECREKQQGDQIKHL 1189
Cdd:COG4717 241 -LEERLKEARL-----LLLIAAALLALLGLGGSLLSLILTIAGVLFLvlgllallfllLAREKASLGKEAEELQALPALE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1190 KIELERVNEECQRLRLSQAELTGSLEESQGQLHSVQLRLEAAQSQHDRI-VQGLQEQMSQLVPGARVAELQHLLSL--RE 1266
Cdd:COG4717 315 ELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELqLEELEQEIAALLAEAGVEDEEELRAAleQA 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1267 EEAERLNAQQEEYKQQLKAREDQVEEAEARLHNVEWL-----LQEKVEELRKQFEKNTRSdllLKELYVENAHLMKAVQL 1341
Cdd:COG4717 395 EEYQELKEELEELEEQLEELLGELEELLEALDEEELEeeleeLEEELEELEEELEELREE---LAELEAELEQLEEDGEL 471
|
330
....*....|..
gi 1958766565 1342 TEEKQRGAEKKN 1353
Cdd:COG4717 472 AELLQELEELKA 483
|
|
| EF-hand_7 |
pfam13499 |
EF-hand domain pair; |
11-71 |
2.36e-03 |
|
EF-hand domain pair;
Pssm-ID: 463900 [Multi-domain] Cd Length: 67 Bit Score: 38.00 E-value: 2.36e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958766565 11 SRLRDVYSSCDTTGTGFLDQEELTQLCTKLGLEEQLP--ALLHILL-----GDGrlaRVNFEEFKEGF 71
Cdd:pfam13499 2 EKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEPLSdeEVEELFKefdldKDG---RISFEEFLELY 66
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1041-1371 |
2.39e-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: 42.52 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1041 ESEMNDVKTKLLQLEDVVRALEKA-DSRESYRAElqRLSEENSVLKSDLGKIQ--LELGTSESRNEVQRQEIEVlkrdKE 1117
Cdd:pfam12128 353 QSELENLEERLKALTGKHQDVTAKyNRRRSKIKE--QNNRDIAGIKDKLAKIReaRDRQLAVAEDDLQALESEL----RE 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1118 QACFDLEELSTQTQKYKDEMSQLNCRILQLEGdSSGLHTQKEENHAAIQVLMKKLEEAECREKQQGDQIKHLKIELERVN 1197
Cdd:pfam12128 427 QLEAGKLEFNEEEYRLKSRLGELKLRLNQATA-TPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQAS 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1198 EECQRLRLSQAELTGSLEESQGQL----HSVQ--LRLEAAQ-SQH-DRIVQGLQEQMSQLVP---GARVAELQHLLSLRE 1266
Cdd:pfam12128 506 EALRQASRRLEERQSALDELELQLfpqaGTLLhfLRKEAPDwEQSiGKVISPELLHRTDLDPevwDGSVGGELNLYGVKL 585
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1267 EeAERLNAQQ-EEYKQQLKAREDQVEEAEARLHNVEWLLQEKVEELRKQFEKNTRSDLLLKELYvENAHLmKAVQLTEEK 1345
Cdd:pfam12128 586 D-LKRIDVPEwAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTAL-KNARL-DLRRLFDEK 662
|
330 340
....*....|....*....|....*.
gi 1958766565 1346 QRGAEKKNCVLEEKVRALNKLISKMA 1371
Cdd:pfam12128 663 QSEKDKKNKALAERKDSANERLNSLE 688
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
336-531 |
2.57e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 336 QVEQLVQERDK---ARQDLEKAEKRnLDFVREMDDCHSALEQLTEKkIKHLEQEyRGRLSLLRSEVEM---ERELfwEQA 409
Cdd:COG4913 226 AADALVEHFDDlerAHEALEDAREQ-IELLEPIRELAERYAAARER-LAELEYL-RAALRLWFAQRRLellEAEL--EEL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 410 RRQRAVLEQDVGRLQAEETSLREK---LTLALKENS-----RLQKEIIEVVEKLSDSEKLVLRLQSDLQFV-LKDKLEPQ 480
Cdd:COG4913 301 RAELARLEAELERLEARLDALREEldeLEAQIRGNGgdrleQLEREIERLERELEERERRRARLEALLAALgLPLPASAE 380
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958766565 481 SMELLAQE-----EQFTAILNDYELKCRDLQDRNDELQAELEGLRVRLPRSRQSPS 531
Cdd:COG4913 381 EFAALRAEaaallEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKS 436
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1031-1362 |
3.00e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1031 QEAKVMSVMSESEMNDVKTKLLQLEDVVRALEKADSRESYRAELQRLSEENSVLK-----SDLGKIQLELGTSESRN-EV 1104
Cdd:PTZ00121 1101 EEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEiarkaEDARKAEEARKAEDAKKaEA 1180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1105 QRQEIEVLKRDKEQACFDLEELStQTQKYKDEMSQLNCRILQLEgdssglhtQKEENHAAIQVLMKKLEEAECREKQQGD 1184
Cdd:PTZ00121 1181 ARKAEEVRKAEELRKAEDARKAE-AARKAEEERKAEEARKAEDA--------KKAEAVKKAEEAKKDAEEAKKAEEERNN 1251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1185 QiKHLKIELERVNEECQRLRLSQAELTGSLEESQgQLHSVQLRLEAAQSQHDRIVQGLQEQMSQlvpGARVAELQHLLSL 1264
Cdd:PTZ00121 1252 E-EIRKFEEARMAHFARRQAAIKAEEARKADELK-KAEEKKKADEAKKAEEKKKADEAKKKAEE---AKKADEAKKKAEE 1326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1265 REEEAERLNAQQEEYKQ-------QLKAREDQVEEAEARLHNVEWLLQE---KVEELRKQFEKNTRSDLLLKELYvENAH 1334
Cdd:PTZ00121 1327 AKKKADAAKKKAEEAKKaaeaakaEAEAAADEAEAAEEKAEAAEKKKEEakkKADAAKKKAEEKKKADEAKKKAE-EDKK 1405
|
330 340
....*....|....*....|....*...
gi 1958766565 1335 LMKAVQLTEEKQRGAEKKNCVLEEKVRA 1362
Cdd:PTZ00121 1406 KADELKKAAAAKKKADEAKKKAEEKKKA 1433
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1123-1297 |
3.07e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 42.09 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1123 LEELSTQTQKYKDEMSQLNCRILQLEGDSSGLhTQKEENHAAIQVLMKKLEEAecREKQQGDQIKHLKIELERVNEECQR 1202
Cdd:PRK10246 218 VQSLTASLQVLTDEEKQLLTAQQQQQQSLNWL-TRLDELQQEASRRQQALQQA--LAAEEKAQPQLAALSLAQPARQLRP 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1203 LRLSQAELTGSLEESQGQLHSVQLRLEAAQSQHDRIVQGLQEQMSQLvpgarVAELQHLLS-LREEEAERL--------- 1272
Cdd:PRK10246 295 HWERIQEQSAALAHTRQQIEEVNTRLQSTMALRARIRHHAAKQSAEL-----QAQQQSLNTwLAEHDRFRQwnnelagwr 369
|
170 180
....*....|....*....|....*..
gi 1958766565 1273 --NAQQEEYKQQLKAREDQVEEAEARL 1297
Cdd:PRK10246 370 aqFSQQTSDREQLRQWQQQLTHAEQKL 396
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1100-1351 |
3.73e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.96 E-value: 3.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1100 SRNEVQRQEIEVLKRDKEQAcfDLEELSTQTQKYKDEMSQLNCRILQLEGDSSGLHTQKEENHAAIQVLMKKLEEAECRE 1179
Cdd:TIGR00606 236 SREIVKSYENELDPLKNRLK--EIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRT 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1180 -KQQGDQIKHLKIELERVNEECQRLRLSQAEL-----TGSLEESQGQLH---------SVQLRLEAAQSQHD-------- 1236
Cdd:TIGR00606 314 vREKERELVDCQRELEKLNKERRLLNQEKTELlveqgRLQLQADRHQEHirardsliqSLATRLELDGFERGpfserqik 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1237 ---RIVQGLQEQMSQLVpGARVAELQHLLSLREEEAERLNAQQEEYKQQLKAREDQVEEAEARLHNVEWLLQ-------- 1305
Cdd:TIGR00606 394 nfhTLVIERQEDEAKTA-AQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQqlegssdr 472
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1958766565 1306 --EKVEELRK------QFEKNTRSDLLLKE-LYVENAHLMKAVQLTEEKQRGAEK 1351
Cdd:TIGR00606 473 ilELDQELRKaerelsKAEKNSLTETLKKEvKSLQNEKADLDRKLRKLDQEMEQL 527
|
|
| EF-hand_5 |
pfam13202 |
EF hand; |
239-260 |
3.91e-03 |
|
EF hand;
Pssm-ID: 433035 [Multi-domain] Cd Length: 25 Bit Score: 36.14 E-value: 3.91e-03
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1203-1314 |
4.27e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 40.80 E-value: 4.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1203 LRLSQAELTGSLEESQGQLHSVQLRLEAAQSQhdrivQGLQEQMSQLVpgARVAELQHLLSLREEEAERLNA-QQEEY-- 1279
Cdd:COG1566 74 ARLDPTDLQAALAQAEAQLAAAEAQLARLEAE-----LGAEAEIAAAE--AQLAAAQAQLDLAQRELERYQAlYKKGAvs 146
|
90 100 110
....*....|....*....|....*....|....*
gi 1958766565 1280 KQQLKAREDQVEEAEARLHNvewlLQEKVEELRKQ 1314
Cdd:COG1566 147 QQELDEARAALDAAQAQLEA----AQAQLAQAQAG 177
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
327-440 |
4.61e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 4.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 327 RQELNFHQGQVEQLVQERDKARQDLEKAEKRNLDFVREMDDCHSALEQLTEKKIKHLEQEYRGRLsllrsevemERELFW 406
Cdd:COG4913 691 EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERF---------AAALGD 761
|
90 100 110
....*....|....*....|....*....|....
gi 1958766565 407 EQARRQRAVLEQDVGRLQAEETSLREKLTLALKE 440
Cdd:COG4913 762 AVERELRENLEERIDALRARLNRAEEELERAMRA 795
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1064-1370 |
4.98e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 41.43 E-value: 4.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1064 ADSRESYRAELQRLSEENSVLKSDLGKIQLEL-----GTSESRNEVQRQEIEVL----------KRDKEQ-ACFDLEELS 1127
Cdd:PLN02939 55 APKQRSSNSKLQSNTDENGQLENTSLRTVMELpqkstSSDDDHNRASMQRDEAIaaidneqqtnSKDGEQlSDFQLEDLV 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1128 TQTQKYKDEMSQLNCRILQLEGDSSGLHTQKEENHAAIQVLMKKLEEAECREKQQ----------GDQIKHLKIEL---- 1193
Cdd:PLN02939 135 GMIQNAEKNILLLNQARLQALEDLEKILTEKEALQGKINILEMRLSETDARIKLAaqekihveilEEQLEKLRNELlirg 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1194 -------ERVNEECQRLRLSQAELTGSLEESQGQLHSVQ------LRLEAAQSQHDRIVQGL-------QEQMSQLVP-- 1251
Cdd:PLN02939 215 ateglcvHSLSKELDVLKEENMLLKDDIQFLKAELIEVAeteervFKLEKERSLLDASLRELeskfivaQEDVSKLSPlq 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1252 ----GARVAELQHLLSLREEEAERLNAQQEEYkQQLKAREDQVEE--AEARLHN-----VEwLLQEKVEELRKQFEKNTR 1320
Cdd:PLN02939 295 ydcwWEKVENLQDLLDRATNQVEKAALVLDQN-QDLRDKVDKLEAslKEANVSKfssykVE-LLQQKLKLLEERLQASDH 372
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1321 SDLLLKELYVEnahlmkavqLTEEKQRGAEKknCVLEEKVRALNKLISKM 1370
Cdd:PLN02939 373 EIHSYIQLYQE---------SIKEFQDTLSK--LKEESKKRSLEHPADDM 411
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1205-1365 |
5.55e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.72 E-value: 5.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1205 LSQaELTG---SLEESQGQLH--SVQLRLEAAQSQhdrivqGLQEQMSQLVPGARVAE-----LQHLLSLREEEAERLNA 1274
Cdd:PRK09039 44 LSR-EISGkdsALDRLNSQIAelADLLSLERQGNQ------DLQDSVANLRASLSAAEaersrLQALLAELAGAGAAAEG 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1275 QQEEYKQQLKAREDQVEEAEARLHnvewLLQEKVEELRKQFekntrsdlllkelyvenAHLMKAVQLTEEKQRGAEKK-- 1352
Cdd:PRK09039 117 RAGELAQELDSEKQVSARALAQVE----LLNQQIAALRRQL-----------------AALEAALDASEKRDRESQAKia 175
|
170
....*....|....*....
gi 1958766565 1353 ------NCVLEEKVRALNK 1365
Cdd:PRK09039 176 dlgrrlNVALAQRVQELNR 194
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
344-523 |
7.34e-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: 7.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 344 RDKARQDLEKAEkRNL----DFVREMDdchSALEQLTE--------KKIKHLEQEYRGRLSLLRsevemerelfWEQARR 411
Cdd:COG1196 174 KEEAERKLEATE-ENLerleDILGELE---RQLEPLERqaekaeryRELKEELKELEAELLLLK----------LRELEA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 412 QRAVLEQDVGRLQAEETSLREKLTLALKENSRLQKEIIEVVEKLSDSEKLVLRLQSDLQfvlkdKLEPQSMELLAQEEQF 491
Cdd:COG1196 240 ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA-----RLEQDIARLEERRREL 314
|
170 180 190
....*....|....*....|....*....|..
gi 1958766565 492 TAILNDYELKCRDLQDRNDELQAELEGLRVRL 523
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEEL 346
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
330-633 |
8.65e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 40.83 E-value: 8.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 330 LNFHQGQVEQLVQERDKARQDLEkaEKRNLDFVREMDDCHSALEQLTEKKIKhleqEYRGRLSLLRSEVE-MEREL---- 404
Cdd:COG5022 776 VIQHGFRLRRLVDYELKWRLFIK--LQPLLSLLGSRKEYRSYLACIIKLQKT----IKREKKLRETEEVEfSLKAEvliq 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 405 -FWEQARRQR--------AVLEQDVGRLQAEETSLRE-----KLTLALKE-NSRLQKEIIEVVEKLSDSEKLVLRLQSDL 469
Cdd:COG5022 850 kFGRSLKAKKrfsllkkeTIYLQSAQRVELAERQLQElkidvKSISSLKLvNLELESEIIELKKSLSSDLIENLEFKTEL 929
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 470 QFVLKDKL------EPQSMELLAQE----------------EQFTAILNDYELKCRDLQDRNDELQ------AELEGLRV 521
Cdd:COG5022 930 IARLKKLLnnidleEGPSIEYVKLPelnklhevesklketsEEYEDLLKKSTILVREGNKANSELKnfkkelAELSKQYG 1009
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 522 RLPRSRQSPsgtpgTHRRWTPGRGPADnlfvgeSIPVSLETEIKMQQMKEnyQELRMQLETKVNYYEKEIEVMKRnfekd 601
Cdd:COG5022 1010 ALQESTKQL-----KELPVEVAELQSA------SKIISSESTELSILKPL--QKLKGLLLLENNQLQARYKALKL----- 1071
|
330 340 350
....*....|....*....|....*....|..
gi 1958766565 602 KKEMEQAFQLEVSVLEGQKADLETLYAKSQEV 633
Cdd:COG5022 1072 RRENSLLDDKQLYQLESTENLLKTINVKDLEV 1103
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1209-1369 |
9.46e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.31 E-value: 9.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1209 ELTGSLEESQGQLHSVQLRLEAAQSQHDRivqglqeqmsqlvpgARVAELQHLLSLREEEAERLNAQQEEYKQQLKARED 1288
Cdd:COG1196 217 ELKEELKELEAELLLLKLRELEAELEELE---------------AELEELEAELEELEAELAELEAELEELRLELEELEL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1289 QVEEAEARLHNVEWLLQEKVEELRKQFEKNTRSDLLLKELYVENAHLMKAVQLTEEKQRGAEKKNCVLEEKVRALNKLIS 1368
Cdd:COG1196 282 ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361
|
.
gi 1958766565 1369 K 1369
Cdd:COG1196 362 E 362
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1031-1362 |
9.91e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.51 E-value: 9.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1031 QEAKVMSVMSESEMNDVKTKLLQLEDVVRALEKADSRESYRAE-LQRLSEEnsVLKSDLGKIQLELGTSESrNEVQRQEI 1109
Cdd:PTZ00121 1339 EEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADaAKKKAEE--KKKADEAKKKAEEDKKKA-DELKKAAA 1415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1110 EVLKRDKEQACFDLEELSTQTQKYKDEMSQLNcrilqlEGDSSGLHTQKEENHAAIQVLMKKLEEAE--CREKQQGDQIK 1187
Cdd:PTZ00121 1416 AKKKADEAKKKAEEKKKADEAKKKAEEAKKAD------EAKKKAEEAKKAEEAKKKAEEAKKADEAKkkAEEAKKADEAK 1489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1188 HLKIELERVNEECQRlrlsQAELTGSLEESQgQLHSVQLRLEAAQSQHDRIVQGLQ--EQMSQLVPGARVAELQHLLSLR 1265
Cdd:PTZ00121 1490 KKAEEAKKKADEAKK----AAEAKKKADEAK-KAEEAKKADEAKKAEEAKKADEAKkaEEKKKADELKKAEELKKAEEKK 1564
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766565 1266 EEEAERlnaQQEEYKQQLKAREDQVEEAE-ARLHNVEWLLQE----KVEELRKQFEKNTRSDLLLKELYVENAHLMKAVQ 1340
Cdd:PTZ00121 1565 KAEEAK---KAEEDKNMALRKAEEAKKAEeARIEEVMKLYEEekkmKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKK 1641
|
330 340
....*....|....*....|..
gi 1958766565 1341 LTEEKQRGAEKKNCVLEEKVRA 1362
Cdd:PTZ00121 1642 EAEEKKKAEELKKAEEENKIKA 1663
|
|
| |
