|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1095-1407 |
3.50e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 78.05 E-value: 3.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1095 SESEMNDVKTKLLQLEDVVRAL-----------EKADSRESYRAELQRLSEENSVLK-----SDLGKIQLELGTSESRNE 1158
Cdd:COG1196 177 AERKLEATEENLERLEDILGELerqleplerqaEKAERYRELKEELKELEAELLLLKlreleAELEELEAELEELEAELE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1159 VQRQEIEVLKRDKEQACFDLEELSTQTQKYKDEMSQLNCRILQLEGDssglhtqkeenhaaIQVLMKKLEEAECREKQQG 1238
Cdd:COG1196 257 ELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD--------------IARLEERRRELEERLEELE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1239 DQIKHLKIELERVNEECQRLRLSQAELTGSLEESQGQLHSVQLRLEAAQSQHDRIVQGLQEQMSQLV-PGARVAELQHLL 1317
Cdd:COG1196 323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLeALRAAAELAAQL 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1318 SLREEEAERLNAQQEEYKQQLKAREDQVEEAEARLHNVEWLLQEKVEELRKQFEKNTRSDLLLKELYVENAHLMKAVQLT 1397
Cdd:COG1196 403 EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482
|
330
....*....|
gi 1958766557 1398 EEKQRGAEKK 1407
Cdd:COG1196 483 LEELAEAAAR 492
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1117-1427 |
9.49e-14 |
|
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: 76.63 E-value: 9.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1117 EKADSRESYRAELQRLSEENSVLKSDLGKIQLELGTSESRNEVQRQEIEVLKRDKEQACFDLEELSTQTQKYKDEMSQLN 1196
Cdd:TIGR02168 667 KTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1197 CRILQLEGDSSGLHTQKEENHAaiqvlmkKLEEAECREKQQGDQIKHLKIELERVNEECQRLRLSQAELTGSLEESQGQL 1276
Cdd:TIGR02168 747 ERIAQLSKELTELEAEIEELEE-------RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1277 HSVQLRLEAAQSQHDRIVQ----------GLQEQMSQLVpgARVAELQHLLSLREEEAERLNAQQEEYKQQLKAREDQVE 1346
Cdd:TIGR02168 820 ANLRERLESLERRIAATERrledleeqieELSEDIESLA--AEIEELEELIEELESELEALLNERASLEEALALLRSELE 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1347 EAEARLHNVEWLLQEKVEELRKQFEKNTRSDLLLKELYVENAHLMKAV--------QLTEEKQRGAEKKNCVLEEKVRAL 1418
Cdd:TIGR02168 898 ELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLseeysltlEEAEALENKIEDDEEEARRRLKRL 977
|
....*....
gi 1958766557 1419 NKLISKMAP 1427
Cdd:TIGR02168 978 ENKIKELGP 986
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1098-1401 |
3.39e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.51 E-value: 3.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1098 EMNDVKTKLLQLEDVVRALEKAdsRESYRAELQRLSEENSVLKSDLGKIQLELGTSESRNEVQRQEIEVLKRDKEQACFD 1177
Cdd:COG1196 233 KLRELEAELEELEAELEELEAE--LEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1178 LEELSTQTQKYKDEmsqlncrILQLEGDSSGLHTQKEENHAAIQVLMKKLEEAECREKQQGDQIKHLKIELERVNEECQR 1257
Cdd:COG1196 311 RRELEERLEELEEE-------LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1258 LRLSQAELTGSLEESQGQLHSVQLRLEAAQSQHDRIVQGLQEqmsqlvpgaRVAELQHLLSLREEEAERLNAQQEEyKQQ 1337
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE---------LEEALAELEEEEEEEEEALEEAAEE-EAE 453
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958766557 1338 LKAREDQVEEAEARLHNVEWLLQEKVEELRKQFEKNTRSDLLLKELYVENAHLMKAVQLTEEKQ 1401
Cdd:COG1196 454 LEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLA 517
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1098-1375 |
7.61e-12 |
|
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: 70.47 E-value: 7.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1098 EMNDVKTKLLQLEDVVRALEkaDSRESYRAELQRLSEENSVLKSDLGKIQLELGTSESRNEVQRQEIEVLKRDKEQACFD 1177
Cdd:TIGR02168 233 RLEELREELEELQEELKEAE--EELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1178 LEELSTQTQkykdemsQLNCRILQLEGDSSGLHTQKEENHAAIQVLMKKLEEAECREKQQGDQIKHLKIELERVNEECQR 1257
Cdd:TIGR02168 311 LANLERQLE-------ELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLET 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1258 LRLSQAELTGSLEESQGQLHSVQLRLEAAQSQHDRIVQGLQEQMSQLVPgARVAELQHLLSLREEEAERLNAQQEEYKQQ 1337
Cdd:TIGR02168 384 LRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE-AELKELQAELEELEEELEELQEELERLEEA 462
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1958766557 1338 LKAREDQVEEAEARLHNVEWLLQEK------VEELRKQFEKNTR 1375
Cdd:TIGR02168 463 LEELREELEEAEQALDAAERELAQLqarldsLERLQENLEGFSE 506
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1096-1429 |
2.90e-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: 68.54 E-value: 2.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1096 ESEMNDVKTKLLQLEDVVRALEKAdsresyraeLQRLSeensvLKSDLGKIQLELgtsesRNEVQRQEIEVLKRDKEQAC 1175
Cdd:TIGR02168 178 ERKLERTRENLDRLEDILNELERQ---------LKSLE-----RQAEKAERYKEL-----KAELRELELALLVLRLEELR 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1176 FDLEELSTQTQKYKDEMSQLNCRILQLEGDSSGLHTQKEENHAAIQVLMKKLEE--AECREKQQgdQIKHLKIELERVNE 1253
Cdd:TIGR02168 239 EELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYAlaNEISRLEQ--QKQILRERLANLER 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1254 ECQRLRLSQAELTGSLEESQGQLHSVQLRLEAAQSQHDRIVQGLQEQMSQLvpgarvAELQHLLSLREEEAERLNAQQEE 1333
Cdd:TIGR02168 317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEL------EELESRLEELEEQLETLRSKVAQ 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1334 YKQQLKAREDQVEEAEARL----HNVEWLLQEKvEELRKQFEKNTRSDLLLkELYVENAHLMKAVQLTEEKQRGAEKKNC 1409
Cdd:TIGR02168 391 LELQIASLNNEIERLEARLerleDRRERLQQEI-EELLKKLEEAELKELQA-ELEELEEELEELQEELERLEEALEELRE 468
|
330 340
....*....|....*....|
gi 1958766557 1410 VLEEKVRALNKLISKMAPAS 1429
Cdd:TIGR02168 469 ELEEAEQALDAAERELAQLQ 488
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1096-1378 |
7.65e-10 |
|
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: 63.92 E-value: 7.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1096 ESEMNDVKTKLLQLEDVVRALEKADSRESyrAELQRLSEENSVLKSDLGKIQLELGTSESRNEVQRQEIEVLKRDKEQAC 1175
Cdd:TIGR02168 725 SRQISALRKDLARLEAEVEQLEERIAQLS--KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR 802
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1176 FDLEELSTQTQKYKDEMSQLNCRILQLEGDSSG-------LHTQKEENHAAIQVLMKKLEEAECREKQQGDQIKHLKIEL 1248
Cdd:TIGR02168 803 EALDELRAELTLLNEEAANLRERLESLERRIAAterrledLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNER 882
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1249 ERVNEECQRLRLSQA--------------ELTGSLEESQGQLHSVQLRLEAAQSQHDRIVQGLQEQmsqlvpgarvaelq 1314
Cdd:TIGR02168 883 ASLEEALALLRSELEelseelreleskrsELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEE-------------- 948
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958766557 1315 hlLSLREEEAERLNAQQEEYKQQLKAREDQVEEAEARLHNVEWLLQEKVEEL--RKQFEKNTRSDL 1378
Cdd:TIGR02168 949 --YSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELkeRYDFLTAQKEDL 1012
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1124-1372 |
2.53e-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: 62.01 E-value: 2.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1124 SYRAELQRLSEENSVLKSDLGKIQLELGTSESR--------NEVQRQ------EIEVLKRDKEQACFDLEELSTQTQK-- 1187
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRldelsqelSDASRKigeiekEIEQLEQEEEKLKERLEELEEDLSSle 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1188 -----YKDEMSQLNCRILQLEgdssglhtqkeenhAAIQVLMKKLEEAECREKQQgdQIKHLKIELERVNEECQRLRlsq 1262
Cdd:TIGR02169 751 qeienVKSELKELEARIEELE--------------EDLHKLEEALNDLEARLSHS--RIPEIQAELSKLEEEVSRIE--- 811
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1263 aeltGSLEESQGQLHSVQLRLEAAQSQhdriVQGLQEQMsqlvpgarvAELQHLLSLREEEAERLNAQQEEYKQQLKARE 1342
Cdd:TIGR02169 812 ----ARLREIEQKLNRLTLEKEYLEKE----IQELQEQR---------IDLKEQIKSIEKEIENLNGKKEELEEELEELE 874
|
250 260 270
....*....|....*....|....*....|
gi 1958766557 1343 DQVEEAEARLHNvewlLQEKVEELRKQFEK 1372
Cdd:TIGR02169 875 AALRDLESRLGD----LKKERDELEAQLRE 900
|
|
| EF-hand_7 |
pfam13499 |
EF-hand domain pair; |
199-260 |
8.86e-09 |
|
EF-hand domain pair;
Pssm-ID: 463900 [Multi-domain] Cd Length: 67 Bit Score: 53.03 E-value: 8.86e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958766557 199 ENQVQGIWHELGVGSSGHLNEQELAVVCRSIGLHG-LEKQELEELFSKLDRDGDGRVSLAEFQ 260
Cdd:pfam13499 1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEpLSDEEVEELFKEFDLDKDGRISFEEFL 63
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1096-1424 |
2.19e-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: 58.93 E-value: 2.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1096 ESEMNDVKTKLLQLEDvvRALEKADSRESYRAELQRLSEENSVLKSDLGKIQLELGTSESRNEVQRQEIEVLKRDKEQAC 1175
Cdd:TIGR02169 687 KRELSSLQSELRRIEN--RLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELE 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1176 FDLEELSTQTQKYKDEMSQLNCRIL-----QLEGDSSGLHTQKEENHAAIQVLMKKLEEAECREKQQGDQIKHLKIEL-- 1248
Cdd:TIGR02169 765 ARIEELEEDLHKLEEALNDLEARLShsripEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRid 844
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1249 --ERVNEECQRLRLSQA---ELTGSLEESQGQLHSVQLRLEAAQSQHDRivqgLQEQMSQLVPGARVAELQhlLSLREEE 1323
Cdd:TIGR02169 845 lkEQIKSIEKEIENLNGkkeELEEELEELEAALRDLESRLGDLKKERDE----LEAQLRELERKIEELEAQ--IEKKRKR 918
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1324 AERLNAQQEEYKQQLKAREDQVEE------AEARLHNVEWLLQEKVEELRKQFEKNtrsdlllkelyvenahlMKAVQLT 1397
Cdd:TIGR02169 919 LSELKAKLEALEEELSEIEDPKGEdeeipeEELSLEDVQAELQRVEEEIRALEPVN-----------------MLAIQEY 981
|
330 340 350
....*....|....*....|....*....|
gi 1958766557 1398 EEKQR---GAEKKNCVLEEKVRALNKLISK 1424
Cdd:TIGR02169 982 EEVLKrldELKEKRAKLEEERKAILERIEE 1011
|
|
| EFh |
cd00051 |
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ... |
213-260 |
2.28e-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: 2.28e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1958766557 213 SSGHLNEQELAVVCRSIGLhGLEKQELEELFSKLDRDGDGRVSLAEFQ 260
Cdd:cd00051 13 GDGTISADELKAALKSLGE-GLSEEEIDEMIREVDKDGDGKIDFEEFL 59
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
340-913 |
3.94e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.14 E-value: 3.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 340 EILQSLDFNVDEKVNLLELTW-ALDNEL--LTVDGVIQQAALACYRQELNFHQGQVEQLVQERDKARQDLEKAEKRNLDF 416
Cdd:TIGR02168 270 EELRLEVSELEEEIEELQKELyALANEIsrLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEEL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 417 VREMDDCHSALEQLTEKKikhleQEYRGRLSLLRSEvemerelfWEQARRQRAVLEQDVGRLQAEETSLREKLTLALKEN 496
Cdd:TIGR02168 350 KEELESLEAELEELEAEL-----EELESRLEELEEQ--------LETLRSKVAQLELQIASLNNEIERLEARLERLEDRR 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 497 SRLQKEIIEVVEKLSDSEKLVLRLQSDLQFVLKDKLEPQSMELLAQEEQFTAILNDYELKCRDLQDRNDELQAELEGLRV 576
Cdd:TIGR02168 417 ERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLER 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 577 RLPRSRQSPSG--TPGTHRRWTPGRGPAdnlfVGESIpvslETEIKMQQMKENYQELRMQ--LETKVNYYEKEIEVMKRN 652
Cdd:TIGR02168 497 LQENLEGFSEGvkALLKNQSGLSGILGV----LSELI----SVDEGYEAAIEAALGGRLQavVVENLNAAKKAIAFLKQN 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 653 fekdkkEMEQAFQLEVSVLEGQKAD-LETLYAKSQEVILGLkeqLQDAARSPEPAPAGLAPCCAQALC--TLAQRLGVEM 729
Cdd:TIGR02168 569 ------ELGRVTFLPLDSIKGTEIQgNDREILKNIEGFLGV---AKDLVKFDPKLRKALSYLLGGVLVvdDLDNALELAK 639
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 730 HLRHQDQLlqirlsdtVT---DSVLPRVCSPKGSRKRTGhpntkQTTERRVSGREAEEELNQKLSWLEAQHAACCESLSL 806
Cdd:TIGR02168 640 KLRPGYRI--------VTldgDLVRPGGVITGGSAKTNS-----SILERRREIEELEEKIEELEEKIAELEKALAELRKE 706
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 807 QHQCE-----KDQLLQTHLQRVKDLAAQLDLEKGwREEREQEVLAHCRRQQLKLQAVMSEEQARICRSFTLEKEKLE--Q 879
Cdd:TIGR02168 707 LEELEeeleqLRKELEELSRQISALRKDLARLEA-EVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAeiE 785
|
570 580 590
....*....|....*....|....*....|....
gi 1958766557 880 TYREQVEGLVQEADVLRALLKNGTTVVSDQQERI 913
Cdd:TIGR02168 786 ELEAQIEQLKEELKALREALDELRAELTLLNEEA 819
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1101-1426 |
5.91e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 57.66 E-value: 5.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1101 DVKTKLLQLEDVVRALEKADS-RESYRAELQRLSEENSVLKSDLGKIQLELGTSESRNEVQRQEIEVLKRDKEQ---ACF 1176
Cdd:PRK04863 356 DLEELEERLEEQNEVVEEADEqQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALERAKQLcglPDL 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1177 DLEELSTQTQKYKDEMSQLNCRILQLE---GDSSGLHTQKEENHAAIQVLMKKLEEAECREKQQgdqikhlkielervnE 1253
Cdd:PRK04863 436 TADNAEDWLEEFQAKEQEATEELLSLEqklSVAQAAHSQFEQAYQLVRKIAGEVSRSEAWDVAR---------------E 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1254 ECQRLRlSQAELTGSLEESQGQLHSVQLRLEAAQSQhDRIVQGLQEQMSQLVPGArvAELQHLLSLREEEAERLNAQQEE 1333
Cdd:PRK04863 501 LLRRLR-EQRHLAEQLQQLRMRLSELEQRLRQQQRA-ERLLAEFCKRLGKNLDDE--DELEQLQEELEARLESLSESVSE 576
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1334 YKQQLKAREDQVEEAEARLHNV-----EWL-LQEKVEELRKQFEkntrsdlllkELYVENAHLMKAVQLTEEKQRGAEKK 1407
Cdd:PRK04863 577 ARERRMALRQQLEQLQARIQRLaarapAWLaAQDALARLREQSG----------EEFEDSQDVTEYMQQLLERERELTVE 646
|
330
....*....|....*....
gi 1958766557 1408 NCVLEEKVRALNKLISKMA 1426
Cdd:PRK04863 647 RDELAARKQALDEEIERLS 665
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
375-583 |
1.90e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.10 E-value: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 375 QAALACYRQELNFHQGQVEQLVQERDKARQDLEKAEKRNLDFVREMDDCHSALEQLTEKKIKHLEQEYRGRLSLLRSEVE 454
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 455 MERelfweqARRQRAVLEQDVGRLQAEETSLREKLTLALKENSRLQKEIIEVVEKLSDSEKLVLRLQSDLQFVLKDKLep 534
Cdd:COG1196 318 LEE------LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL-- 389
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1958766557 535 qsmELLAQEEQFTAILNDYELKCRDLQDRNDELQAELEGLRVRLPRSRQ 583
Cdd:COG1196 390 ---EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE 435
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
382-578 |
3.90e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.94 E-value: 3.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 382 RQELNFHQGQVEQLVQERDKARQDLEKAEKRNLDFVREMDDCHSALEQLTEK---KIKHLEQEYRGRLSLLRSEVEMERE 458
Cdd:COG1196 301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEleeAEAELAEAEEALLEAEAELAEAEEE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 459 lfWEQARRQRAVLEQDVGRLQAEETSLREKLTLALKENSRLQKEIIEVVEKLSDSEKLVLRLQSDLQFVLKDKLepqsmE 538
Cdd:COG1196 381 --LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA-----E 453
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1958766557 539 LLAQEEQFTAILNDYELKCRDLQDRNDELQAELEGLRVRL 578
Cdd:COG1196 454 LEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL 493
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1174-1426 |
8.89e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.84 E-value: 8.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1174 ACFDLEELSTQTQKYKDEMSQLNCRILQLEGdssglhtQKEENHAAIQVLMKKLEEAECREKQQGDQIKHLKIELERVNE 1253
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEK-------ELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1254 ECQRLRLSQAELTGSLEESQGQLhSVQLRLEAAQSQHDRIVQGL-QEQMSQLVpgARVAELQHLLSLREEEAERLNAQQE 1332
Cdd:COG4942 84 ELAELEKEIAELRAELEAQKEEL-AELLRALYRLGRQPPLALLLsPEDFLDAV--RRLQYLKYLAPARREQAEELRADLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1333 EYKQQLKAREDQVEEAEArlhnvewLLQEKVEELRKQFEKNTRSDLLLKELyvenahlmkAVQLTEEKQRGAEkkncvLE 1412
Cdd:COG4942 161 ELAALRAELEAERAELEA-------LLAELEEERAALEALKAERQKLLARL---------EKELAELAAELAE-----LQ 219
|
250
....*....|....
gi 1958766557 1413 EKVRALNKLISKMA 1426
Cdd:COG4942 220 QEAEELEALIARLE 233
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1161-1371 |
9.01e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.77 E-value: 9.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1161 RQEIEVLKRDKEQacfdLEELSTQTQKYKDEMSQLNcrilQLEGDSSGLHTQKEEnhAAIQVLMKKLEEAECREKQQGDQ 1240
Cdd:COG4913 241 HEALEDAREQIEL----LEPIRELAERYAAARERLA----ELEYLRAALRLWFAQ--RRLELLEAELEELRAELARLEAE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1241 IKHLKIELERVNEECQRLRLSQAELTGsleesqGQLHSVQLRLEAAQSQHDRIVQGLQEQMsqlvpgARVAELQHLLSLR 1320
Cdd:COG4913 311 LERLEARLDALREELDELEAQIRGNGG------DRLEQLEREIERLERELEERERRRARLE------ALLAALGLPLPAS 378
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1958766557 1321 EEEAERLNAQQEEYKQQLKAREDQVEEAEARLHNVEWLLQEKVEELRKQFE 1371
Cdd:COG4913 379 AEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
373-583 |
9.86e-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: 53.52 E-value: 9.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 373 IQQAALACYRQELNFHQGQVEQLVQERDKARQ-------DLEKAEKRNLDFVREMDDCHSALEQLTEKKIKHLEQEYRGR 445
Cdd:TIGR02168 695 ELEKALAELRKELEELEEELEQLRKELEELSRqisalrkDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAE 774
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 446 LSLLRSEVEMER-ELFWEQARRQRAVLEQDVGRLQAEETSLREK---------------------LTLALKENSRLQKEI 503
Cdd:TIGR02168 775 EELAEAEAEIEElEAQIEQLKEELKALREALDELRAELTLLNEEaanlrerleslerriaaterrLEDLEEQIEELSEDI 854
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 504 IEVVEKLSDSEKLVLRLQSDLQFVL--KDKLEPQSMELLAQEEQFTAILNDYELKCRDLQDRNDELQAELEGLRVRLPRS 581
Cdd:TIGR02168 855 ESLAAEIEELEELIEELESELEALLneRASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGL 934
|
..
gi 1958766557 582 RQ 583
Cdd:TIGR02168 935 EV 936
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1101-1352 |
1.23e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.12 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1101 DVKTKLLQLEDVVRALEKAD----------SRESYRAELQRLSEENSVLKSDLGKIQLELGTSESRnevqRQEIEVLKRD 1170
Cdd:PRK02224 184 DQRGSLDQLKAQIEEKEEKDlherlnglesELAELDEEIERYEEQREQARETRDEADEVLEEHEER----REELETLEAE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1171 KEQACFDLEELSTQTQKYKDEMSQLNCRILQLEGDSSGLHTQKEENHAAIQVLMKKLEEAECREKQQGDQIKHLKIELER 1250
Cdd:PRK02224 260 IEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQA 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1251 VNEECQRLRLSQAELTGSLEESQGQLHSVQLRLEAAQSQHDR---IVQGLQEQMSQL---VPGARVA--ELQHLLSLREE 1322
Cdd:PRK02224 340 HNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDrreEIEELEEEIEELrerFGDAPVDlgNAEDFLEELRE 419
|
250 260 270
....*....|....*....|....*....|
gi 1958766557 1323 EAERLNAQQEEYKQQLKAREDQVEEAEARL 1352
Cdd:PRK02224 420 ERDELREREAELEATLRTARERVEEAEALL 449
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1154-1406 |
1.84e-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: 52.76 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1154 ESRNEVQRQEIEVLKRDKEQACFDLEELSTQTQKYKDEMSQ-LNCRILQLEgdssglhtqKEEnhAAIQVLMKKLEEAEc 1232
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKaERYQALLKE---------KRE--YEGYELLKEKEALE- 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1233 REKQQGD--------QIKHLKIELERVNEECQRLRLSQAELTGSL----EESQGQLHSVQLRLEAAQSQHDRIVQGLQEQ 1300
Cdd:TIGR02169 237 RQKEAIErqlasleeELEKLTEEISELEKRLEEIEQLLEELNKKIkdlgEEEQLRVKEKIGELEAEIASLERSIAEKERE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1301 MSQLvpGARVAELQHLLSLREEEAERLNAQQEEYKQQLKAREDQVEEAEARLHNVEWLLQEKVEELRKQFEK----NTRS 1376
Cdd:TIGR02169 317 LEDA--EERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDElkdyREKL 394
|
250 260 270
....*....|....*....|....*....|
gi 1958766557 1377 DLLLKELyveNAHLMKAVQLTEEKQRGAEK 1406
Cdd:TIGR02169 395 EKLKREI---NELKRELDRLQEELQRLSEE 421
|
|
| FRQ1 |
COG5126 |
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
213-259 |
2.55e-06 |
|
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 48.25 E-value: 2.55e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1958766557 213 SSGHLNEQELAvvcRSIGLHGLEKQELEELFSKLDRDGDGRVSLAEF 259
Cdd:COG5126 82 GDGKISADEFR---RLLTALGVSEEEADELFARLDTDGDGKISFEEF 125
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1095-1424 |
3.18e-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: 51.94 E-value: 3.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1095 SESEMNDVKTKLLQLEDVVRALEKadSRESYRAELQRLSEENSVLKSDLGKIqlelgtsESRNEVQRQEIEVLKRDKEQA 1174
Cdd:TIGR04523 354 SESENSEKQRELEEKQNEIEKLKK--ENQSYKQEIKNLESQINDLESKIQNQ-------EKLNQQKDEQIKKLQQEKELL 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1175 CFDLEELSTQTQKYKDEMSQLNCRILQLEGDSSGLHTQKEENHAAIQVLMKKLEEAECREKQQGDQIKHLKIELERVNEE 1254
Cdd:TIGR04523 425 EKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEE 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1255 CQRLRLSQAELT---GSLEESQGQLHSVQLRLEAAQSQHDRIVQGLQEQMSQLVPGARVAELQHLLSLREEEAERLNAQQ 1331
Cdd:TIGR04523 505 KKELEEKVKDLTkkiSSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQ 584
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1332 EEYKQQLKAREDQVEEAEARLHNVEWLLQEKVEELRKQFEKNTRSDLLLKEL------YVENAHLMK-AVQLTEEKQRGA 1404
Cdd:TIGR04523 585 EEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIkskknkLKQEVKQIKeTIKEIRNKWPEI 664
|
330 340
....*....|....*....|
gi 1958766557 1405 EKKNCVLEEKVRALNKLISK 1424
Cdd:TIGR04523 665 IKKIKESKTKIDDIIELMKD 684
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1117-1429 |
4.65e-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: 51.49 E-value: 4.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1117 EKADSRESYRAELQRLSEENSVLKSDLGKIQLELGTSESRNEVQRQEIEVLkrDKEQACFDLEELSTQT-----QKYKDE 1191
Cdd:COG3096 372 EAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQAVQAL--EKARALCGLPDLTPENaedylAAFRAK 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1192 MSQLNCRILQLE---GDSSGLHTQKEENHAAIQVLMKKLE--EAECREKQQGDQIKHLKIELERVneecQRLRLSQAELT 1266
Cdd:COG3096 450 EQQATEEVLELEqklSVADAARRQFEKAYELVCKIAGEVErsQAWQTARELLRRYRSQQALAQRL----QQLRAQLAELE 525
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1267 gsleesqgqlhsvqlRLEAAQSQHDRIVQGLQEQMSQLVPGArvAELQHLLSLREEEAERLNAQQEEYKQQLKAREDQVE 1346
Cdd:COG3096 526 ---------------QRLRQQQNAERLLEEFCQRIGQQLDAA--EELEELLAELEAQLEELEEQAAEAVEQRSELRQQLE 588
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1347 EAEARLHNVE-----WL-LQEKVEELRKQfekntrSDLLLKELyvenAHLMKAVQLTEEKQRGAEKKNCVLEEKVRALNK 1420
Cdd:COG3096 589 QLRARIKELAarapaWLaAQDALERLREQ------SGEALADS----QEVTAAMQQLLEREREATVERDELAARKQALES 658
|
....*....
gi 1958766557 1421 LISKMAPAS 1429
Cdd:COG3096 659 QIERLSQPG 667
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1221-1418 |
5.37e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.92 E-value: 5.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1221 QVLMKKLE-EAECREKQQGDQIKHLKIELERVNEECQRLRLSQAELTGSLEESQgQLHSVQLRLEAAQSQHDRIVQGLQE 1299
Cdd:COG4717 45 AMLLERLEkEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELE-ELEEELEELEAELEELREELEKLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1300 QMSQLVPGARVAELQHLLSLREEEAERLNAQQEEYKQ---QLKAREDQVEEAEARLHN--------VEWLLQEKVEELRK 1368
Cdd:COG4717 124 LLQLLPLYQELEALEAELAELPERLEELEERLEELREleeELEELEAELAELQEELEElleqlslaTEEELQDLAEELEE 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1369 QFEKNTRSDLLLKELYVENAHLMKAVQLTEEKQRGAEKKNCVLEEKVRAL 1418
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLL 253
|
|
| EF-hand_8 |
pfam13833 |
EF-hand domain pair; |
213-259 |
5.86e-06 |
|
EF-hand domain pair;
Pssm-ID: 404678 [Multi-domain] Cd Length: 54 Bit Score: 45.00 E-value: 5.86e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1958766557 213 SSGHLNEQELAVVCRSIGLHGLEKQELEELFSKLDRDGDGRVSLAEF 259
Cdd:pfam13833 1 EKGVITREELKRALALLGLKDLSEDEVDILFREFDTDGDGYISFDEF 47
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
384-691 |
6.06e-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: 51.22 E-value: 6.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 384 ELNFHQGQVEQLVQERDKARQDLEKAEKRNLDFVREMDDCHSALEQLTEKKIKHLEQEYRG-----------RLSLLRSE 452
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRvkekigeleaeIASLERSI 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 453 VEMERELfwEQARRQRAVLEQDVGRLQAEETSLREKLTlalkensRLQKEIIEVVEKLSDSEKLVLRLQSDLQFVLKD-- 530
Cdd:TIGR02169 311 AEKEREL--EDAEERLAKLEAEIDKLLAEIEELEREIE-------EERKRRDKLTEEYAELKEELEDLRAELEEVDKEfa 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 531 KLEPQSMELLAQEEQFTAILNDYELKCRDLQDRNDELQAELEGLRVRLPRSRQSpsgtpgthrrwtpgrgpadnlfVGES 610
Cdd:TIGR02169 382 ETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAK----------------------INEL 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 611 IPVSLETEIKMQQMKENYQELRMQLETkvnyYEKEIEVMKRNFEKDKKEMEQAfQLEVSVLEGQKADLET--LYAKSQEV 688
Cdd:TIGR02169 440 EEEKEDKALEIKKQEWKLEQLAADLSK----YEQELYDLKEEYDRVEKELSKL-QRELAEAEAQARASEErvRGGRAVEE 514
|
...
gi 1958766557 689 ILG 691
Cdd:TIGR02169 515 VLK 517
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1108-1351 |
6.44e-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: 50.15 E-value: 6.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1108 QLEDVVRALEKAdsresyRAELQRLSEENSVLKSDLGKIQLELGTSESRNEVQRQEIEVLKRDKEQACFDLEELSTQTQK 1187
Cdd:COG4942 28 ELEQLQQEIAEL------EKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1188 YKDEMSQLNcRILQLEGDSSG----LHTQKEENHAAIQVLMKKLEEAecrEKQQGDQIKHLKIELERVNEEcqrLRLSQA 1263
Cdd:COG4942 102 QKEELAELL-RALYRLGRQPPlallLSPEDFLDAVRRLQYLKYLAPA---RREQAEELRADLAELAALRAE---LEAERA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1264 ELTGSLEESQGQlhsvQLRLEAAQSQHDRIVQGLQEQMSQLvpgarvaelqhllslrEEEAERLNAQQEEYKQQLKARED 1343
Cdd:COG4942 175 ELEALLAELEEE----RAALEALKAERQKLLARLEKELAEL----------------AAELAELQQEAEELEALIARLEA 234
|
....*...
gi 1958766557 1344 QVEEAEAR 1351
Cdd:COG4942 235 EAAAAAER 242
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1115-1365 |
7.47e-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: 50.15 E-value: 7.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1115 ALEKADSRESYRAELQRLSEENSVLKSDLGKIQLELGTSESRNEVQRQEIEVLKRdkeqacfdleelstQTQKYKDEMSQ 1194
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALAR--------------RIRALEQELAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1195 LNCRILQLEGDSSGLHTQKEENHAAIQVLMKKLeeaecrekQQGDQIKHLKI--------ELERVNEECQRLRLSQAELT 1266
Cdd:COG4942 81 LEAELAELEKEIAELRAELEAQKEELAELLRAL--------YRLGRQPPLALllspedflDAVRRLQYLKYLAPARREQA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1267 GSLEESQGQLHSVQLRLEAAQSQHDRIVQGLQEQMsqlvpgarvAELQHLLSLREEEAERLNAQQEEYKQQLKAREDQVE 1346
Cdd:COG4942 153 EELRADLAELAALRAELEAERAELEALLAELEEER---------AALEALKAERQKLLARLEKELAELAAELAELQQEAE 223
|
250
....*....|....*....
gi 1958766557 1347 EAEARLHNVEWLLQEKVEE 1365
Cdd:COG4942 224 ELEALIARLEAEAAAAAER 242
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1123-1392 |
1.94e-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: 49.33 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1123 ESYRAELQRLSEENSVLKSdlgkIQLELGTSESRNEvqrqEIEVLKRDKEQACFDLEELSTQTQKYKDEMSQLNCRILQL 1202
Cdd:pfam05483 363 ELLRTEQQRLEKNEDQLKI----ITMELQKKSSELE----EMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEEL 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1203 EGDSSGLHTQKEENHAAIQVLMKKLEEAECREKQQGDQIKHLKIELER-------VNEECQRLRLSQAELTGSLEESQGQ 1275
Cdd:pfam05483 435 KGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKeklknieLTAHCDKLLLENKELTQEASDMTLE 514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1276 LHSVQLRLEAAQSQHDRI---VQGLQEQMSQLvpgarvaeLQHLLSLREEeaerLNAQQEEYKQQLKAREDQVEEAEARL 1352
Cdd:pfam05483 515 LKKHQEDIINCKKQEERMlkqIENLEEKEMNL--------RDELESVREE----FIQKGDEVKCKLDKSEENARSIEYEV 582
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1958766557 1353 HNVE---WLLQEKVEELRKQFEKNTRSdllLKELYVENAHLMK 1392
Cdd:pfam05483 583 LKKEkqmKILENKCNNLKKQIENKNKN---IEELHQENKALKK 622
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1059-1304 |
2.13e-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: 49.30 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1059 VQETPLQLRGETARMRPSLPYSELpNPQEAKVMSVMSESEMNDVKTKLLQLEDVVralekadsrESYRAELQRLSEENSV 1138
Cdd:TIGR02169 292 VKEKIGELEAEIASLERSIAEKER-ELEDAEERLAKLEAEIDKLLAEIEELEREI---------EEERKRRDKLTEEYAE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1139 LKSDLGKIQLELGTSESRNEVQRQEIEVLKRDKEQACFDLEELSTQTQKYKDEMSQLNCRILQLEGDSSGLHTQKEENHA 1218
Cdd:TIGR02169 362 LKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1219 AIQVLMKKLEEAECREKQQGDQIKHLKIELERVNEECQRL--RLSQAELTGS-LEESQGQLHSVQLRLEAAQSQHDRIVQ 1295
Cdd:TIGR02169 442 EKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVekELSKLQRELAeAEAQARASEERVRGGRAVEEVLKASIQ 521
|
....*....
gi 1958766557 1296 GLQEQMSQL 1304
Cdd:TIGR02169 522 GVHGTVAQL 530
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
375-503 |
2.59e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 2.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 375 QAALACYRQELNFHQGQVEQLVQERDKARQDLEKAEKRNLDF-VREMDDCHSALEQLTEKK--IKHLEQEYRGRLSLLRS 451
Cdd:COG4913 294 EAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELeeRERRRARLEALLAALGL 373
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1958766557 452 EVEMERELFWE---QARRQRAVLEQDVGRLQAEETSLREKLTLALKENSRLQKEI 503
Cdd:COG4913 374 PLPASAEEFAAlraEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEI 428
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1117-1383 |
3.62e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 3.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1117 EKADSRESYRAELQRLSEENSVLKSDLGKIQLELG------TSESRNEVQRQEIEVLKRDKEQ-ACFDLEELSTQTQKYK 1189
Cdd:PRK03918 449 HRKELLEEYTAELKRIEKELKEIEEKERKLRKELRelekvlKKESELIKLKELAEQLKELEEKlKKYNLEELEKKAEEYE 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1190 demsQLNCRILQLEGDSSGLHT---QKEENHAAIQVLMKKLEEAECREKQQGDQIKHLKIE-LERVNEECQRLRLSQAEL 1265
Cdd:PRK03918 529 ----KLKEKLIKLKGEIKSLKKeleKLEELKKKLAELEKKLDELEEELAELLKELEELGFEsVEELEERLKELEPFYNEY 604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1266 TgSLEESQGQLHSVQLRLEAAQSQHDRIVQGLQEQMSQLVP-GARVAELQHLLSlrEEEAERLNAQQEEYKQQLKAREDQ 1344
Cdd:PRK03918 605 L-ELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEElRKELEELEKKYS--EEEYEELREEYLELSRELAGLRAE 681
|
250 260 270
....*....|....*....|....*....|....*....
gi 1958766557 1345 VEEAEARLHNVEWLLQEKVEELRKQFEKNTRSDLLLKEL 1383
Cdd:PRK03918 682 LEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKAL 720
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
391-578 |
4.68e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 4.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 391 QVEQLVQERDKARQDLEKAEKRnldfvremddchsaLEQLTEKKikhleQEYRGRLSLLRSEVEM-ERELFWEQARRQRA 469
Cdd:COG4913 611 KLAALEAELAELEEELAEAEER--------------LEALEAEL-----DALQERREALQRLAEYsWDEIDVASAEREIA 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 470 VLEQ----------DVGRLQAEETSLREKLTLALKENSRLQKEIIEVVEKLSDSEKLVLRLQSDLQFVLKDKLEPQSMEL 539
Cdd:COG4913 672 ELEAelerldassdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALL 751
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1958766557 540 laqEEQFTAILND--YELKCRDLQDRNDELQAELEGLRVRL 578
Cdd:COG4913 752 ---EERFAAALGDavERELRENLEERIDALRARLNRAEEEL 789
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1096-1424 |
4.78e-05 |
|
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: 48.09 E-value: 4.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1096 ESEMNDVKTKLLQLEDVVRALEkadsresyrAELQRLSEE-----NSVLKSDLGKIQLELGTSESRNEVQRQEIEVLKRD 1170
Cdd:TIGR04523 273 QKELEQNNKKIKELEKQLNQLK---------SEISDLNNQkeqdwNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQ 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1171 KEQACFDLEELSTQTQKYKDEMSQLNCRILQLEGDSSGLHTQKEENHAAIQVLMKKLEEAECREKQQGDQIKHLKIELER 1250
Cdd:TIGR04523 344 ISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKEL 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1251 VNEECQRLR----------------------------LSQAELTGSLEESQGQLHSVQLRLEAAQSQHDRIVQ---GLQE 1299
Cdd:TIGR04523 424 LEKEIERLKetiiknnseikdltnqdsvkeliiknldNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKelkKLNE 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1300 QMSQLvpGARVAELQHLLSLREEEAERLNAQQEEYKQQLKAREDQVEEAEARL--HNVEWLLQEKVEELRKQFE------ 1371
Cdd:TIGR04523 504 EKKEL--EEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELkkENLEKEIDEKNKEIEELKQtqkslk 581
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1958766557 1372 -KNTRSDLLLKELYVENAHLMKAVQLTEEKQRGAEKKNCVLEEKVRALNKLISK 1424
Cdd:TIGR04523 582 kKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKN 635
|
|
| FRQ1 |
COG5126 |
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
203-263 |
5.01e-05 |
|
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 44.78 E-value: 5.01e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958766557 203 QGIWHELGVGSSGHLNEQELAVVCRSIGLHGLEkQELEELFSKLDRDGDGRVSLAEFQLGL 263
Cdd:COG5126 36 ATLFSEADTDGDGRISREEFVAGMESLFEATVE-PFARAAFDLLDTDGDGKISADEFRRLL 95
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
392-700 |
6.97e-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: 47.76 E-value: 6.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 392 VEQLVQERDKARQDLEKAEKRNLDFVREMDDCHSALEQLTEKKIKHLeqEYRGRLSLLRSEVEMERELFWEQARRQRAVL 471
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE--RYQALLKEKREYEGYELLKEKEALERQKEAI 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 472 EQDVGRLQAEETSLREKLtlalkenSRLQKEIIEVVEKLSDSEKLVLRLQSDLQFVLKDKLEpqsmELLAQEEQFTAILN 551
Cdd:TIGR02169 243 ERQLASLEEELEKLTEEI-------SELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIG----ELEAEIASLERSIA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 552 DYELKCRDLQDRNDELQAELEGLRVRLPRSRQSPSGTPGTHRRWTPGrgpadnlfVGESIPVSLETEIKMQQMKENYQEL 631
Cdd:TIGR02169 312 EKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEE--------YAELKEELEDLRAELEEVDKEFAET 383
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958766557 632 R---MQLETKVNYYEKEIEVMKRNF-----EKDKKEMEQAF-QLEVSVLEGQKADLETLYAKSQEVILGLKEQLQDAA 700
Cdd:TIGR02169 384 RdelKDYREKLEKLKREINELKRELdrlqeELQRLSEELADlNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLA 461
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1096-1372 |
7.84e-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: 47.37 E-value: 7.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1096 ESEMNDVKTKLLQLEDVVRALEKA-----------------DSRESYRAELQRLSEENSVLKSDLGKIQLELGTSESRNE 1158
Cdd:TIGR02169 757 KSELKELEARIEELEEDLHKLEEAlndlearlshsripeiqAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQ 836
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1159 VQRQEIEVLKRDKEQACFDLEELSTQTQKYKDEMSQLNCRILQLEGDSSGLHTQKEENHAAIQVLMKKLEEAECREKQQG 1238
Cdd:TIGR02169 837 ELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKR 916
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1239 DQIKHLKIELERVNEEcqrlrLSQAE-LTGSLEESQGQLhsvqLRLEAAQSQHDRIvqglQEQMSQLVPGARVAELQHll 1317
Cdd:TIGR02169 917 KRLSELKAKLEALEEE-----LSEIEdPKGEDEEIPEEE----LSLEDVQAELQRV----EEEIRALEPVNMLAIQEY-- 981
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1958766557 1318 slrEEEAERLNaqqeEYKQQLKAREdqvEEAEARLHNVEWLLQEKVEELRKQFEK 1372
Cdd:TIGR02169 982 ---EEVLKRLD----ELKEKRAKLE---EERKAILERIEEYEKKKREVFMEAFEA 1026
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1095-1372 |
1.00e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1095 SESEMNDVKTKLLQLEDVVRALEKAdsrESYRAELQRLSEENSVLKSDLGKIQLELGTSESRNEVQRQEIEVLKRDKEQA 1174
Cdd:PRK03918 143 SDESREKVVRQILGLDDYENAYKNL---GEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPEL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1175 CFDLEELSTQTQKY---KDEMSQLNCRILQLEGDSSGLHTQKEENHAAIQVLMKKLEEAEcrekqqgDQIKHLKiELERV 1251
Cdd:PRK03918 220 REELEKLEKEVKELeelKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELE-------EKVKELK-ELKEK 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1252 NEECQRLRlsqaeltGSLEESQGQLHSVQLRLEAAQSQhdriVQGLQEQMSQLVP-GARVAELQHLLSLREEEAERLNAQ 1330
Cdd:PRK03918 292 AEEYIKLS-------EFYEEYLDELREIEKRLSRLEEE----INGIEERIKELEEkEERLEELKKKLKELEKRLEELEER 360
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1958766557 1331 QEEYkQQLKAREDQVEEAEARLHNVEwllQEKVEELRKQFEK 1372
Cdd:PRK03918 361 HELY-EEAKAKKEELERLKKRLTGLT---PEKLEKELEELEK 398
|
|
| XopAW |
NF041410 |
XopAW family type III secretion system calcium-binding effector; |
240-301 |
1.08e-04 |
|
XopAW family type III secretion system calcium-binding effector;
Pssm-ID: 469301 [Multi-domain] Cd Length: 227 Bit Score: 45.44 E-value: 1.08e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958766557 240 EELFSKLDRDGDGRVSLAEFQLGLFGHEPPSLPASSSLIKPNGPWSHYQEESGCHTTTTSSL 301
Cdd:NF041410 139 SQLFSALDSDGDGSVSSDELAAALQPPPPPPLFSLSSQGSSSSTQPSDSSTASSSSNTTEAL 200
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1220-1429 |
1.15e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1220 IQVLMKKLEEAECREKQQGDQIKHLKIELERVNEECQRLRLSQAELTGSLEESQGQLHSVQLRLEAAQSQHDRIVQGLQE 1299
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1300 QMSQLV----------PGARVAELQHLLSLREEEAERLNAQQEEyKQQLKAREDQVEEAEARLHNVEWLLQEKVEELRKQ 1369
Cdd:COG3883 98 SGGSVSyldvllgsesFSDFLDRLSALSKIADADADLLEELKAD-KAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1370 FEKNTRsdlLLKELYVENAHLMKAVQLTEEKQRGAEKKNCVLEEKVRALNKLISKMAPAS 1429
Cdd:COG3883 177 QAEQEA---LLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1110-1416 |
1.74e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1110 EDVVRALEKADSRESYRAELQRLSEE----NSVLKSDLGKIQLELGTSESRNEVQRQEIEvlKRDKEQACFDLEELSTQT 1185
Cdd:PTZ00121 1513 DEAKKAEEAKKADEAKKAEEAKKADEakkaEEKKKADELKKAEELKKAEEKKKAEEAKKA--EEDKNMALRKAEEAKKAE 1590
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1186 QKYKDEMSQLNCRILQLEGDSsgLHTQKEENHAAIQVlmKKLEEaecrEKQQGDQIKHLKIELERVNEECQRlrlsqael 1265
Cdd:PTZ00121 1591 EARIEEVMKLYEEEKKMKAEE--AKKAEEAKIKAEEL--KKAEE----EKKKVEQLKKKEAEEKKKAEELKK-------- 1654
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1266 tgslEESQGQLHSVQLRLEAAQSQHdrivqglqeqmsqlvpgaRVAELQHLLSLREEEAERLNAQQEEYK--QQLKARED 1343
Cdd:PTZ00121 1655 ----AEEENKIKAAEEAKKAEEDKK------------------KAEEAKKAEEDEKKAAEALKKEAEEAKkaEELKKKEA 1712
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958766557 1344 QVEEAEARLHNVEWLLQEKVEELRKQFEKNTRSdllLKELYVENAHLMKAVQLTEEKQRGAE----KKNCVLEEKVR 1416
Cdd:PTZ00121 1713 EEKKKAEELKKAEEENKIKAEEAKKEAEEDKKK---AEEAKKDEEEKKKIAHLKKEEEKKAEeirkEKEAVIEEELD 1786
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1128-1428 |
1.94e-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: 46.26 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1128 ELQRLSEENSVLKSDL-GKIQLELGTSESRNEvqrqEIEVLKRDKEQacfdLEELSTQTQKYKDEMSQLNCRILQLEGDS 1206
Cdd:pfam15921 427 EVQRLEALLKAMKSECqGQMERQMAAIQGKNE----SLEKVSSLTAQ----LESTKEMLRKVVEELTAKKMTLESSERTV 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1207 SGLHTQKEENHAAIQVLMKKLEEAECREKQQGDQIKHLKIE---LERVNEECQRLRLSQAELTGSLEESQGQLHSVQLRL 1283
Cdd:pfam15921 499 SDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEgdhLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLV 578
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1284 eaaqSQHDRIVQGLQEQMSQLvpgarvaelqhllslrEEEAERLNAQQEEYKQQLKAREDQVEEAEARLHNVEW----LL 1359
Cdd:pfam15921 579 ----GQHGRTAGAMQVEKAQL----------------EKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELekvkLV 638
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958766557 1360 QEKVEELRKQFEKNTRSDLLLKELYVENAHLMKAVQLTEEKQRGAEKKNcvlEEKVRALNKLISKMAPA 1428
Cdd:pfam15921 639 NAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKS---EEMETTTNKLKMQLKSA 704
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1123-1424 |
2.20e-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: 46.12 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1123 ESYRAELQRLSEENSVLKSDLGKIQLELGTSESRNEVQRQEIEVLKRDKEQACFDLEELSTQT---QKYKDEMSQLNCRI 1199
Cdd:pfam02463 166 RLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYldyLKLNEERIDLLQEL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1200 LQLEGDSSGLHTQKEENHAAIQVLMKKLEEAECREKQQGD-QIKHLKIELERVNEECQRLRLSQAELTGSLEESQGQLHS 1278
Cdd:pfam02463 246 LRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEeELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKK 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1279 VQLRLEAAQSQHDRIVQGLQE-QMSQLVPGARVAELQHLLSLREEEAERLNAQQEEYKQQLKAREDQVEEAEARLHNVEW 1357
Cdd:pfam02463 326 AEKELKKEKEEIEELEKELKElEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEK 405
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958766557 1358 LLQEKVEELRKQF-----EKNTRSDLLLKELYVENAHLMKA--VQLTEEKQRGAEKKNCVLEEKVRALNKLISK 1424
Cdd:pfam02463 406 EAQLLLELARQLEdllkeEKKEELEILEEEEESIELKQGKLteEKEELEKQELKLLKDELELKKSEDLLKETQL 479
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1183-1377 |
2.27e-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: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1183 TQTQKYKDEMSQLNCRILQLEGDSSGLHTQKEENHAAIQVLMKKLEEAECREKQQGDQIKHLKIELERVNEEC-QRLRLS 1261
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELgERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1262 Q---------AELTGSleESQGQLHSVQLRLEAAQSQHDRIVQGLQEQMSQLVpgARVAELQHLLSLREEEAERLNAQQE 1332
Cdd:COG3883 96 YrsggsvsylDVLLGS--ESFSDFLDRLSALSKIADADADLLEELKADKAELE--AKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1958766557 1333 EYKQQLKAREDQVEEAEARLHNVEWLLQEKVEELRKQFEKNTRSD 1377
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| FRQ1 |
COG5126 |
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
1-71 |
2.42e-04 |
|
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 42.86 E-value: 2.42e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958766557 1 MDNEEENHYVSRLRDVYSSCDTTGTGFLDQEELTQLCTKLGLEEQLPALLHILL---GDGRLarvNFEEFKEGF 71
Cdd:COG5126 59 MESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTALGVSEEEADELFARLdtdGDGKI---SFEEFVAAV 129
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1110-1333 |
4.47e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 4.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1110 EDVVRALEKADS----RESYRaELQRLSEENSVLKSDLGKIQLElgTSESRNEVQRQEIEVLKRDKEQACFDLEELSTQT 1185
Cdd:COG4913 242 EALEDAREQIELlepiRELAE-RYAAARERLAELEYLRAALRLW--FAQRRLELLEAELEELRAELARLEAELERLEARL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1186 QKYKDEMSQLNCRILQLEGDssglhtQKEENHAAIQVLMKKLEEAECREKQQGDQIKHLKIELERVNEECQRLRLSQAEL 1265
Cdd:COG4913 319 DALREELDELEAQIRGNGGD------RLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAAL 392
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958766557 1266 TGSLEESQGQLHSVQLRLEAAQSQHDRIVQGLQEQMSQL------VPgarvaelQHLLSLREEEAERLNAQQEE 1333
Cdd:COG4913 393 LEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLerrksnIP-------ARLLALRDALAEALGLDEAE 459
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1126-1387 |
4.69e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 4.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1126 RAELQRLSEENSVLKSDLGKIQLELGTSESRNEVQRQEIEVLKRDKEQACFDLEELSTQTQKYKDEMSQLNCRILQLEGD 1205
Cdd:COG4372 44 QEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1206 SSGLHTQKEENHAAIQVLMKKLEEAECREKQQGDQIKHLKIELERVNEECQRLRLSQA--ELTGSLEESQGQLHSVQLRL 1283
Cdd:COG4372 124 RQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAeqALDELLKEANRNAEKEEELA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1284 EAAQSQHDRIVQGLQEQMSQLVPGARVAELQHLLSLREEEAERLNAQQEEYKQQLKAREDQVEEAEARLHNVEWLLQEKV 1363
Cdd:COG4372 204 EAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAAL 283
|
250 260
....*....|....*....|....
gi 1958766557 1364 EELRKQFEKNTRSDLLLKELYVEN 1387
Cdd:COG4372 284 ELEALEEAALELKLLALLLNLAAL 307
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1162-1372 |
4.92e-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: 44.46 E-value: 4.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1162 QEIEVLKRDKEQACFDLEELstQTQKYKDEMSQLNCRILQLEGDssglhTQKEENhaAIQVLMKKLEEAECREKQQGDQI 1241
Cdd:pfam06160 237 KEIQQLEEQLEENLALLENL--ELDEAEEALEEIEERIDQLYDL-----LEKEVD--AKKYVEKNLPEIEDYLEHAEEQN 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1242 KHLKIELERVNeecQRLRLSQAELtGSLEESQGQLHSVqlrleaaQSQHDRIVQGLQEQMsqlvpgARVAELQHLLSLRE 1321
Cdd:pfam06160 308 KELKEELERVQ---QSYTLNENEL-ERVRGLEKQLEEL-------EKRYDEIVERLEEKE------VAYSELQEELEEIL 370
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1958766557 1322 EEAERLNAQQEEYKQQLKAREDQVEEAEARLHNvewlLQEKVEELRKQFEK 1372
Cdd:pfam06160 371 EQLEEIEEEQEEFKESLQSLRKDELEAREKLDE----FKLELREIKRLVEK 417
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
382-545 |
5.04e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 5.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 382 RQELNFHQGQVEQLVQERDKARQDLEKAEKRNLDFVREMDDCHSALEQL-TEKKIKHLEQEYRGRLSLLRSEVEMERElf 460
Cdd:COG4717 80 LKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLpLYQELEALEAELAELPERLEELEERLEE-- 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 461 WEQARRQRAVLEQDVGRLQAEETSLREKLTLALKEN-SRLQKEIIEVVEKLSDSEKLVLRLQSDLQFVLKDKLEPQSMEL 539
Cdd:COG4717 158 LRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELE 237
|
....*.
gi 1958766557 540 LAQEEQ 545
Cdd:COG4717 238 AAALEE 243
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1101-1426 |
5.05e-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: 44.72 E-value: 5.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1101 DVKTKLLQLEDVVRALEKADSRESYRAELQRLSEENSVLKSDLGKIQLELGTSESRNEVQR------------QEIEVLK 1168
Cdd:pfam15921 114 DLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQlrkmmlshegvlQEIRSIL 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1169 RDKEQAC----FDLEELSTQ------------TQKYKDEMSQLNCRILQLEGDssgLHTQKEENHAAIQVLMKkleeaec 1232
Cdd:pfam15921 194 VDFEEASgkkiYEHDSMSTMhfrslgsaiskiLRELDTEISYLKGRIFPVEDQ---LEALKSESQNKIELLLQ------- 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1233 rekQQGDQIKHL----KIELERVNEECQRLRlSQAEltgsleESQGQLHSVQLRLEAAQSQHDRIVQGLQEQMSQLVPGA 1308
Cdd:pfam15921 264 ---QHQDRIEQLisehEVEITGLTEKASSAR-SQAN------SIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSEL 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1309 RVA---------ELQHLLSLREEEAERLNAQQEEYKQQLKAREDQVEEAEARLHNVEWLLQEKVEELRKQFEKNTRS--- 1376
Cdd:pfam15921 334 REAkrmyedkieELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNsit 413
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958766557 1377 -DLLLKELYVENAH------LMKAvqLTEEKQRGAEKKNCVLEEKVRALNKLISKMA 1426
Cdd:pfam15921 414 iDHLRRELDDRNMEvqrleaLLKA--MKSECQGQMERQMAAIQGKNESLEKVSSLTA 468
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1161-1378 |
5.21e-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: 5.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1161 RQEIEVLKRDKEQACFDLEELSTQTQKYKDEMSQLNCRILQLEG---------DSSGLHTQkeenHAAIQVLMKKLEEAE 1231
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRlaeyswdeiDVASAERE----IAELEAELERLDASS 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1232 CREKQQGDQIKHLKIELERVNEECQRLRLSQAELTGSLEESQGQLHSVQLRLEAA-QSQHDRIVQGLQEQMSQLVPGARV 1310
Cdd:COG4913 685 DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAeDLARLELRALLEERFAAALGDAVE 764
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1311 AELQHLL--------SLREEEAERLNAQQEEYKQQLKARE-------DQVEEAEARLHNVEWL-LQEKVEELRKQFEKNT 1374
Cdd:COG4913 765 RELRENLeeridalrARLNRAEEELERAMRAFNREWPAETadldadlESLPEYLALLDRLEEDgLPEYEERFKELLNENS 844
|
....
gi 1958766557 1375 RSDL 1378
Cdd:COG4913 845 IEFV 848
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1154-1349 |
5.42e-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: 44.12 E-value: 5.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1154 ESRNEVQRQEIEVLKRDKEQACFDLEELSTQTQKYKDEMSQLNCRILQLEGDSSGLHTQKEENHAAIQVLMKKLEEAECR 1233
Cdd:pfam07888 51 EAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEAR 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1234 EKQQGDQIKHLKIELERVNEECQRLRLSQAELTGSLEESQGQLHSVQLRLEAAQSQHDRIVQGLQEQMSQLvpGARVAEL 1313
Cdd:pfam07888 131 IRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSL--AQRDTQV 208
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1958766557 1314 QHL------LSLREEEAERLNAQQEEYKQQLKAREDQVEEAE 1349
Cdd:pfam07888 209 LQLqdtittLTQKLTTAHRKEAENEALLEELRSLQERLNASE 250
|
|
| EFh |
smart00054 |
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ... |
238-259 |
5.52e-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: 5.52e-04
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
464-647 |
6.07e-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: 6.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 464 ARRQRAVLEQDVGRLQAEETSLREKLTL--ALKENSRLQKEIIEVVEKLSDSEKLVLRLQSDLQfVLKDKLE------PQ 535
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEERLEAleAELDALQERREALQRLAEYSWDEIDVASAEREIA-ELEAELErldassDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 536 SMELLAQEEQFTAILNDYELKCRDLQDRNDELQAELEGLRVRLPRSRQSPSGTPGTHRRWTpgRGPADNLFVGESIPVSL 615
Cdd:COG4913 687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLEL--RALLEERFAAALGDAVE 764
|
170 180 190
....*....|....*....|....*....|..
gi 1958766557 616 eteikmQQMKENYQELRMQLETKVNYYEKEIE 647
Cdd:COG4913 765 ------RELRENLEERIDALRARLNRAEEELE 790
|
|
| EF-hand_1 |
pfam00036 |
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ... |
238-263 |
6.49e-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: 6.49e-04
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1135-1418 |
7.82e-04 |
|
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: 43.96 E-value: 7.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1135 ENSVLKSDLGKIQLELGTSESRNE--VQRQEIEVLKRDKEQACFDLEELSTQTQKYKDEMSQLNcRILQLEGDSSGLHTQ 1212
Cdd:pfam17380 267 ENEFLNQLLHIVQHQKAVSERQQQekFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMD-RQAAIYAEQERMAME 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1213 KEENHAAIQVLMKKLEEAECREKQqgdqikhLKIELERVnEECQRLRLsqaeltgsleESQGQLHSVQLRLEAAQSQHdr 1292
Cdd:pfam17380 346 RERELERIRQEERKRELERIRQEE-------IAMEISRM-RELERLQM----------ERQQKNERVRQELEAARKVK-- 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1293 ivqgLQEQmsqlvpgarvaELQHLLSLREEEAERLNAQQEEYKQ-QLKAREDQVEEAEARLHNVEWLLQEKVEELRKQFE 1371
Cdd:pfam17380 406 ----ILEE-----------ERQRKIQQQKVEMEQIRAEQEEARQrEVRRLEEERAREMERVRLEEQERQQQVERLRQQEE 470
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1958766557 1372 KNTRSDLLLKELYVENAHLMKAVQLTEEKQRGAEKKNCVLEEKVRAL 1418
Cdd:pfam17380 471 ERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKL 517
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
381-578 |
1.15e-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: 43.52 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 381 YRQELNFHQGQVEQLVQERDKARQDLEKAEKRNLDFVREMDDCHSALEQLtEKKIKHLE---QEYRGRLSLLRSEVE--- 454
Cdd:TIGR02169 707 LSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENV-KSELKELEariEELEEDLHKLEEALNdle 785
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 455 -MERELFWEQARRQRAVLEQDVGRLQAEETSLREKLTLALKENSRLQKEIIEVVEKLSDSEKLVLRLQSDLqfvlkDKLE 533
Cdd:TIGR02169 786 aRLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEI-----ENLN 860
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1958766557 534 PQSMELLAQEEQFTAILNDYELKCRDLQDRNDELQAELEGLRVRL 578
Cdd:TIGR02169 861 GKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKI 905
|
|
| EFh_parvalbumin_alpha |
cd16254 |
EF-hand, calcium binding motif, found in alpha-parvalbumin; Alpha-parvalbumin is cytosolic Ca2 ... |
201-259 |
1.19e-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: 39.81 E-value: 1.19e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958766557 201 QVQGIWHELGVGSSGHLNEQELAVVCRSIGLHG--LEKQELEELFSKLDRDGDGRVSLAEF 259
Cdd:cd16254 35 DVKKVFHILDKDKSGFIEEDELKFVLKGFSPDGrdLSDKETKALLAAGDKDGDGKIGIDEF 95
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
382-533 |
1.20e-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: 42.22 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 382 RQELNFHQGQVEQLVQERDKARQDLEKAEKRNLDFVREMDDCHSALEQLtEKKIKhleqEYRGRLSLLRSEVE---MERE 458
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEV-EARIK----KYEEQLGNVRNNKEyeaLQKE 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958766557 459 LfwEQARRQRAVLEQDVGRLQAEETSLREKLTLALKENSRLQKEIIEVVEKLsdsEKLVLRLQSDLQFVLKDKLE 533
Cdd:COG1579 98 I--ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEL---DEELAELEAELEELEAEREE 167
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1096-1408 |
1.21e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1096 ESEMNDVKTKLLQLEDVVRALEKADSrESYRAELQRLSEENSVLKSDLGKIQLELGTSESRNEVQRQEIEVLKRDKEQAC 1175
Cdd:COG4717 162 EEELEELEAELAELQEELEELLEQLS-LATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1176 fDLEELSTQTQkykdeMSQLNCRILQLEGDSSGLHTQKEENHAAIQV-----------LMKKLEEAECREKQQGDQIKHL 1244
Cdd:COG4717 241 -LEERLKEARL-----LLLIAAALLALLGLGGSLLSLILTIAGVLFLvlgllallfllLAREKASLGKEAEELQALPALE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1245 KIELERVNEECQRLRLSQAELTGSLEESQGQLHSVQLRLEAAQSQHDRI-VQGLQEQMSQLVPGARVAELQHLLSL--RE 1321
Cdd:COG4717 315 ELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELqLEELEQEIAALLAEAGVEDEEELRAAleQA 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1322 EEAERLNAQQEEYKQQLKAREDQVEEAEARLHNVEWL-----LQEKVEELRKQFEKNTRSdllLKELYVENAHLMKAVQL 1396
Cdd:COG4717 395 EEYQELKEELEELEEQLEELLGELEELLEALDEEELEeeleeLEEELEELEEELEELREE---LAELEAELEQLEEDGEL 471
|
330
....*....|..
gi 1958766557 1397 TEEKQRGAEKKN 1408
Cdd:COG4717 472 AELLQELEELKA 483
|
|
| EFh_parvalbumin_like |
cd16251 |
EF-hand, calcium binding motif, found in parvalbumin-like EF-hand family; The family includes ... |
195-260 |
1.29e-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: 1.29e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958766557 195 FNTPENQVQGIWHELGVGSSGHLNEQELAVVCRSIGLHG--LEKQELEELFSKLDRDGDGRVSLAEFQ 260
Cdd:cd16251 29 KQKSEDQIKKVFQILDKDKSGFIEEEELKYILKGFSIAGrdLTDEETKALLAAGDTDGDGKIGVEEFA 96
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
374-574 |
1.35e-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: 43.51 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 374 QQAALACYRQELNFHQGQVEQLVQERDKARQDLEKAEKRNLDFVREMDDCHSALEQLTEKKIKHLEQeyrgrLSLLRSEV 453
Cdd:TIGR02168 822 LRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEA-----LALLRSEL 896
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 454 EmerelfweQARRQRAVLEQDVGRLQAEETSLREKLTLALKENSRLQKEIIEVVEKLSDSEKLVLRLQSDLQFVLKDKLE 533
Cdd:TIGR02168 897 E--------ELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEE 968
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1958766557 534 PQSMELLAQEEQFTAI-------LNDYElkcrDLQDRNDELQAELEGL 574
Cdd:TIGR02168 969 EARRRLKRLENKIKELgpvnlaaIEEYE----ELKERYDFLTAQKEDL 1012
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1096-1426 |
1.42e-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: 43.29 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1096 ESEMNDVKTKLLQLEDVVRALEKA-DSRESYRAElqRLSEENSVLKSDLGKIQ--LELGTSESRNEVQRQEIEVlkrdKE 1172
Cdd:pfam12128 353 QSELENLEERLKALTGKHQDVTAKyNRRRSKIKE--QNNRDIAGIKDKLAKIReaRDRQLAVAEDDLQALESEL----RE 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1173 QACFDLEELSTQTQKYKDEMSQLNCRILQLEGdSSGLHTQKEENHAAIQVLMKKLEEAECREKQQGDQIKHLKIELERVN 1252
Cdd:pfam12128 427 QLEAGKLEFNEEEYRLKSRLGELKLRLNQATA-TPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQAS 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1253 EECQRLRLSQAELTGSLEESQGQL----HSVQ--LRLEAAQ-SQH-DRIVQGLQEQMSQLVP---GARVAELQHLLSLRE 1321
Cdd:pfam12128 506 EALRQASRRLEERQSALDELELQLfpqaGTLLhfLRKEAPDwEQSiGKVISPELLHRTDLDPevwDGSVGGELNLYGVKL 585
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1322 EeAERLNAQQ-EEYKQQLKAREDQVEEAEARLHNVEWLLQEKVEELRKQFEKNTRSDLLLKELYvENAHLmKAVQLTEEK 1400
Cdd:pfam12128 586 D-LKRIDVPEwAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTAL-KNARL-DLRRLFDEK 662
|
330 340
....*....|....*....|....*.
gi 1958766557 1401 QRGAEKKNCVLEEKVRALNKLISKMA 1426
Cdd:pfam12128 663 QSEKDKKNKALAERKDSANERLNSLE 688
|
|
| EF-hand_6 |
pfam13405 |
EF-hand domain; |
238-263 |
1.44e-03 |
|
EF-hand domain;
Pssm-ID: 463869 [Multi-domain] Cd Length: 30 Bit Score: 37.54 E-value: 1.44e-03
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1098-1300 |
1.45e-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: 43.12 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1098 EMNDVKTKLLQLEDVVRALEKadSRESYRAELQRLSEENSVLKSDLGKIQLELGT-------SESRNEVQRQEIEVLKRD 1170
Cdd:TIGR02168 310 RLANLERQLEELEAQLEELES--KLDELAEELAELEEKLEELKEELESLEAELEEleaeleeLESRLEELEEQLETLRSK 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1171 KEQACFDLEELSTQTQKYKDEMSQLNCRILQLEGDSSGLHTQKEEnhAAIQVLMKKLEEAECREKQQGDQIKHLKIELER 1250
Cdd:TIGR02168 388 VAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE--AELKELQAELEELEEELEELQEELERLEEALEE 465
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1251 VNEECQRLRLSQAELTGSLEESQGQLHSVQLRLEAAQSQHDRIVQGLQEQ 1300
Cdd:TIGR02168 466 LREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQ 515
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
374-577 |
1.55e-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: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 374 QQAALACYRQELNFHQGQVEQLVQERDKARQDLEKAEKRNLDFVREMDDCHSALEQLTE--KKIKHLEQEYRGRLSLLRS 451
Cdd:TIGR02169 810 IEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEelEELEAALRDLESRLGDLKK 889
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 452 EV-EMERELFWEQARRQRAVLEQDVGRLQAEEtsLREKLTLALKENS---RLQKEIIEVVEKLSDSEKLVLRLQSDLQFV 527
Cdd:TIGR02169 890 ERdELEAQLRELERKIEELEAQIEKKRKRLSE--LKAKLEALEEELSeieDPKGEDEEIPEEELSLEDVQAELQRVEEEI 967
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1958766557 528 lkDKLEPQSMellAQEEQFTAILNDYElkcrDLQDRNDELQAELEGLRVR 577
Cdd:TIGR02169 968 --RALEPVNM---LAIQEYEEVLKRLD----ELKEKRAKLEEERKAILER 1008
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
331-495 |
1.67e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 331 AQEGIQNGREILQSLDFNVDEKVNLLELTWALDN------ELLTVDGVIQQAalacyRQELNFHQGQVEQLVQERDKARQ 404
Cdd:COG4913 639 ELDALQERREALQRLAEYSWDEIDVASAEREIAEleaeleRLDASSDDLAAL-----EEQLEELEAELEELEEELDELKG 713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 405 DLEKAEKRNLDFVREMDDCHSALEQLTEKKIKHLEQEYRGRLsllrsevemERELFWEQARRQRAVLEQDVGRLQAEETS 484
Cdd:COG4913 714 EIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERF---------AAALGDAVERELRENLEERIDALRARLNR 784
|
170
....*....|.
gi 1958766557 485 LREKLTLALKE 495
Cdd:COG4913 785 AEEELERAMRA 795
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1086-1417 |
1.87e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1086 QEAKVMSVMSESEMNDVKTKLLQLEDVVRALEKADSRESYRAELQRLSEENSVLK-----SDLGKIQLELGTSESRN-EV 1159
Cdd:PTZ00121 1101 EEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEiarkaEDARKAEEARKAEDAKKaEA 1180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1160 QRQEIEVLKRDKEQACFDLEELStQTQKYKDEMSQLNCRILQLEgdssglhtQKEENHAAIQVLMKKLEEAECREKQQGD 1239
Cdd:PTZ00121 1181 ARKAEEVRKAEELRKAEDARKAE-AARKAEEERKAEEARKAEDA--------KKAEAVKKAEEAKKDAEEAKKAEEERNN 1251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1240 QiKHLKIELERVNEECQRLRLSQAELTGSLEESQgQLHSVQLRLEAAQSQHDRIVQGLQEQMSQlvpGARVAELQHLLSL 1319
Cdd:PTZ00121 1252 E-EIRKFEEARMAHFARRQAAIKAEEARKADELK-KAEEKKKADEAKKAEEKKKADEAKKKAEE---AKKADEAKKKAEE 1326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1320 REEEAERLNAQQEEYKQ-------QLKAREDQVEEAEARLHNVEWLLQE---KVEELRKQFEKNTRSDLLLKELYvENAH 1389
Cdd:PTZ00121 1327 AKKKADAAKKKAEEAKKaaeaakaEAEAAADEAEAAEEKAEAAEKKKEEakkKADAAKKKAEEKKKADEAKKKAE-EDKK 1405
|
330 340
....*....|....*....|....*...
gi 1958766557 1390 LMKAVQLTEEKQRGAEKKNCVLEEKVRA 1417
Cdd:PTZ00121 1406 KADELKKAAAAKKKADEAKKKAEEKKKA 1433
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
391-586 |
1.93e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 391 QVEQLVQERDK---ARQDLEKAEKRnLDFVREMDDCHSALEQLTEKkIKHLEQEyRGRLSLLRSEVEM---ERELfwEQA 464
Cdd:COG4913 226 AADALVEHFDDlerAHEALEDAREQ-IELLEPIRELAERYAAARER-LAELEYL-RAALRLWFAQRRLellEAEL--EEL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 465 RRQRAVLEQDVGRLQAEETSLREK---LTLALKENS-----RLQKEIIEVVEKLSDSEKLVLRLQSDLQFV-LKDKLEPQ 535
Cdd:COG4913 301 RAELARLEAELERLEARLDALREEldeLEAQIRGNGgdrleQLEREIERLERELEERERRRARLEALLAALgLPLPASAE 380
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958766557 536 SMELLAQE-----EQFTAILNDYELKCRDLQDRNDELQAELEGLRVRLPRSRQSPS 586
Cdd:COG4913 381 EFAALRAEaaallEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKS 436
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1097-1406 |
2.18e-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: 42.73 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1097 SEMNDVKTK---LLQLEDVVRALEKADS-RESYRAELQRLSEENSVLKSDLGK---IQLELGTSESRNEVQRQ------- 1162
Cdd:TIGR00606 166 SEGKALKQKfdeIFSATRYIKALETLRQvRQTQGQKVQEHQMELKYLKQYKEKaceIRDQITSKEAQLESSREivksyen 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1163 EIEVLK-RDKEqacfdLEELSTQTQKYKDEMSQLNCRILQLEGDSSGLHTQKEENHAAIQVLMKKLEEAECRE-KQQGDQ 1240
Cdd:TIGR00606 246 ELDPLKnRLKE-----IEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTvREKERE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1241 IKHLKIELERVNEECQRLRLSQAEL-----TGSLEESQGQLH---------SVQLRLEAAQSQHD-----------RIVQ 1295
Cdd:TIGR00606 321 LVDCQRELEKLNKERRLLNQEKTELlveqgRLQLQADRHQEHirardsliqSLATRLELDGFERGpfserqiknfhTLVI 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1296 GLQEQMSQLVpGARVAELQHLLSLREEEAERLNAQQEEYKQQLKAREDQVEEAEARLHNVEWLLQ----------EKVEE 1365
Cdd:TIGR00606 401 ERQEDEAKTA-AQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQqlegssdrilELDQE 479
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1958766557 1366 LRK------QFEKNTRSDLLLKE-LYVENAHLMKAVQLTEEKQRGAEK 1406
Cdd:TIGR00606 480 LRKaerelsKAEKNSLTETLKKEvKSLQNEKADLDRKLRKLDQEMEQL 527
|
|
| EF-hand_7 |
pfam13499 |
EF-hand domain pair; |
11-71 |
2.19e-03 |
|
EF-hand domain pair;
Pssm-ID: 463900 [Multi-domain] Cd Length: 67 Bit Score: 38.00 E-value: 2.19e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958766557 11 SRLRDVYSSCDTTGTGFLDQEELTQLCTKLGLEEQLP--ALLHILL-----GDGrlaRVNFEEFKEGF 71
Cdd:pfam13499 2 EKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEPLSdeEVEELFKefdldKDG---RISFEEFLELY 66
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1178-1352 |
2.35e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 42.48 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1178 LEELSTQTQKYKDEMSQLNCRILQLEGDSSGLhTQKEENHAAIQVLMKKLEEAecREKQQGDQIKHLKIELERVNEECQR 1257
Cdd:PRK10246 218 VQSLTASLQVLTDEEKQLLTAQQQQQQSLNWL-TRLDELQQEASRRQQALQQA--LAAEEKAQPQLAALSLAQPARQLRP 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1258 LRLSQAELTGSLEESQGQLHSVQLRLEAAQSQHDRIVQGLQEQMSQLvpgarVAELQHLLS-LREEEAERL--------- 1327
Cdd:PRK10246 295 HWERIQEQSAALAHTRQQIEEVNTRLQSTMALRARIRHHAAKQSAEL-----QAQQQSLNTwLAEHDRFRQwnnelagwr 369
|
170 180
....*....|....*....|....*..
gi 1958766557 1328 --NAQQEEYKQQLKAREDQVEEAEARL 1352
Cdd:PRK10246 370 aqFSQQTSDREQLRQWQQQLTHAEQKL 396
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
332-571 |
3.06e-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: 42.13 E-value: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 332 QEGIQNGREILQSLDFNVDEKVNlleltwALDNELLTVDGVIQQAalacyRQELNFHQGQVEQLVQER-DKARQDLEkae 410
Cdd:pfam12128 282 QETSAELNQLLRTLDDQWKEKRD------ELNGELSAADAAVAKD-----RSELEALEDQHGAFLDADiETAAADQE--- 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 411 krNLDFVR-EMDDCHSALEQLTEKkIKHLEQEYRGRLSLLRSE-------VEMERELFWEQARRQRAVLEQDvgrLQAEE 482
Cdd:pfam12128 348 --QLPSWQsELENLEERLKALTGK-HQDVTAKYNRRRSKIKEQnnrdiagIKDKLAKIREARDRQLAVAEDD---LQALE 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 483 TSLREKLTLALKENSRLQKEII-----------------EVVEKLSDSEKLVLRLQSDLQFVLKDKLEPQSMELLAQE-- 543
Cdd:pfam12128 422 SELREQLEAGKLEFNEEEYRLKsrlgelklrlnqatatpELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKrr 501
|
250 260
....*....|....*....|....*...
gi 1958766557 544 EQFTAILNDYELKCRDLQDRNDELQAEL 571
Cdd:pfam12128 502 DQASEALRQASRRLEERQSALDELELQL 529
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1258-1369 |
3.75e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 41.19 E-value: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1258 LRLSQAELTGSLEESQGQLHSVQLRLEAAQSQhdrivQGLQEQMSQLVpgARVAELQHLLSLREEEAERLNA-QQEEY-- 1334
Cdd:COG1566 74 ARLDPTDLQAALAQAEAQLAAAEAQLARLEAE-----LGAEAEIAAAE--AQLAAAQAQLDLAQRELERYQAlYKKGAvs 146
|
90 100 110
....*....|....*....|....*....|....*
gi 1958766557 1335 KQQLKAREDQVEEAEARLHNvewlLQEKVEELRKQ 1369
Cdd:COG1566 147 QQELDEARAALDAAQAQLEA----AQAQLAQAQAG 177
|
|
| EF-hand_5 |
pfam13202 |
EF hand; |
239-260 |
4.02e-03 |
|
EF hand;
Pssm-ID: 433035 [Multi-domain] Cd Length: 25 Bit Score: 36.14 E-value: 4.02e-03
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1119-1425 |
4.54e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 41.43 E-value: 4.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1119 ADSRESYRAELQRLSEENSVLKSDLGKIQLEL-----GTSESRNEVQRQEIEVL----------KRDKEQ-ACFDLEELS 1182
Cdd:PLN02939 55 APKQRSSNSKLQSNTDENGQLENTSLRTVMELpqkstSSDDDHNRASMQRDEAIaaidneqqtnSKDGEQlSDFQLEDLV 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1183 TQTQKYKDEMSQLNCRILQLEGDSSGLHTQKEENHAAIQVLMKKLEEAECREKQQ----------GDQIKHLKIEL---- 1248
Cdd:PLN02939 135 GMIQNAEKNILLLNQARLQALEDLEKILTEKEALQGKINILEMRLSETDARIKLAaqekihveilEEQLEKLRNELlirg 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1249 -------ERVNEECQRLRLSQAELTGSLEESQGQLHSVQ------LRLEAAQSQHDRIVQGL-------QEQMSQLVP-- 1306
Cdd:PLN02939 215 ateglcvHSLSKELDVLKEENMLLKDDIQFLKAELIEVAeteervFKLEKERSLLDASLRELeskfivaQEDVSKLSPlq 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1307 ----GARVAELQHLLSLREEEAERLNAQQEEYkQQLKAREDQVEE--AEARLHN-----VEwLLQEKVEELRKQFEKNTR 1375
Cdd:PLN02939 295 ydcwWEKVENLQDLLDRATNQVEKAALVLDQN-QDLRDKVDKLEAslKEANVSKfssykVE-LLQQKLKLLEERLQASDH 372
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1376 SDLLLKELYVEnahlmkavqLTEEKQRGAEKknCVLEEKVRALNKLISKM 1425
Cdd:PLN02939 373 EIHSYIQLYQE---------SIKEFQDTLSK--LKEESKKRSLEHPADDM 411
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
399-578 |
4.86e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.46 E-value: 4.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 399 RDKARQDLEKAEkRNL----DFVREMDdchSALEQLTE--------KKIKHLEQEYRGRLSLLRsevemerelfWEQARR 466
Cdd:COG1196 174 KEEAERKLEATE-ENLerleDILGELE---RQLEPLERqaekaeryRELKEELKELEAELLLLK----------LRELEA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 467 QRAVLEQDVGRLQAEETSLREKLTLALKENSRLQKEIIEVVEKLSDSEKLVLRLQSDLQfvlkdKLEPQSMELLAQEEQF 546
Cdd:COG1196 240 ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA-----RLEQDIARLEERRREL 314
|
170 180 190
....*....|....*....|....*....|..
gi 1958766557 547 TAILNDYELKCRDLQDRNDELQAELEGLRVRL 578
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEEL 346
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1260-1420 |
5.17e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.72 E-value: 5.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1260 LSQaELTG---SLEESQGQLH--SVQLRLEAAQSQhdrivqGLQEQMSQLVPGARVAE-----LQHLLSLREEEAERLNA 1329
Cdd:PRK09039 44 LSR-EISGkdsALDRLNSQIAelADLLSLERQGNQ------DLQDSVANLRASLSAAEaersrLQALLAELAGAGAAAEG 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1330 QQEEYKQQLKAREDQVEEAEARLHnvewLLQEKVEELRKQFekntrsdlllkelyvenAHLMKAVQLTEEKQRGAEKK-- 1407
Cdd:PRK09039 117 RAGELAQELDSEKQVSARALAQVE----LLNQQIAALRRQL-----------------AALEAALDASEKRDRESQAKia 175
|
170
....*....|....*....
gi 1958766557 1408 ------NCVLEEKVRALNK 1420
Cdd:PRK09039 176 dlgrrlNVALAQRVQELNR 194
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1086-1417 |
6.19e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 6.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1086 QEAKVMSVMSESEMNDVKTKLLQLEDVVRALEKADSRESYRAE-LQRLSEEnsVLKSDLGKIQLELGTSESrNEVQRQEI 1164
Cdd:PTZ00121 1339 EEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADaAKKKAEE--KKKADEAKKKAEEDKKKA-DELKKAAA 1415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1165 EVLKRDKEQACFDLEELSTQTQKYKDEMSQLNcrilqlEGDSSGLHTQKEENHAAIQVLMKKLEEAE--CREKQQGDQIK 1242
Cdd:PTZ00121 1416 AKKKADEAKKKAEEKKKADEAKKKAEEAKKAD------EAKKKAEEAKKAEEAKKKAEEAKKADEAKkkAEEAKKADEAK 1489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1243 HLKIELERVNEECQRlrlsQAELTGSLEESQgQLHSVQLRLEAAQSQHDRIVQGLQ--EQMSQLVPGARVAELQHLLSLR 1320
Cdd:PTZ00121 1490 KKAEEAKKKADEAKK----AAEAKKKADEAK-KAEEAKKADEAKKAEEAKKADEAKkaEEKKKADELKKAEELKKAEEKK 1564
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1321 EEEAERlnaQQEEYKQQLKAREDQVEEAE-ARLHNVEWLLQE----KVEELRKQFEKNTRSDLLLKELYVENAHLMKAVQ 1395
Cdd:PTZ00121 1565 KAEEAK---KAEEDKNMALRKAEEAKKAEeARIEEVMKLYEEekkmKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKK 1641
|
330 340
....*....|....*....|..
gi 1958766557 1396 LTEEKQRGAEKKNCVLEEKVRA 1417
Cdd:PTZ00121 1642 EAEEKKKAEELKKAEEENKIKA 1663
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
385-688 |
7.32e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 40.83 E-value: 7.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 385 LNFHQGQVEQLVQERDKARQDLEkaEKRNLDFVREMDDCHSALEQLTEKKIKhleqEYRGRLSLLRSEVE-MEREL---- 459
Cdd:COG5022 776 VIQHGFRLRRLVDYELKWRLFIK--LQPLLSLLGSRKEYRSYLACIIKLQKT----IKREKKLRETEEVEfSLKAEvliq 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 460 -FWEQARRQR--------AVLEQDVGRLQAEETSLRE-----KLTLALKE-NSRLQKEIIEVVEKLSDSEKLVLRLQSDL 524
Cdd:COG5022 850 kFGRSLKAKKrfsllkkeTIYLQSAQRVELAERQLQElkidvKSISSLKLvNLELESEIIELKKSLSSDLIENLEFKTEL 929
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 525 QFVLKDKL------EPQSMELLAQE----------------EQFTAILNDYELKCRDLQDRNDELQ------AELEGLRV 576
Cdd:COG5022 930 IARLKKLLnnidleEGPSIEYVKLPelnklhevesklketsEEYEDLLKKSTILVREGNKANSELKnfkkelAELSKQYG 1009
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 577 RLPRSRQSPsgtpgTHRRWTPGRGPADnlfvgeSIPVSLETEIKMQQMKEnyQELRMQLETKVNYYEKEIEVMKRnfekd 656
Cdd:COG5022 1010 ALQESTKQL-----KELPVEVAELQSA------SKIISSESTELSILKPL--QKLKGLLLLENNQLQARYKALKL----- 1071
|
330 340 350
....*....|....*....|....*....|..
gi 1958766557 657 KKEMEQAFQLEVSVLEGQKADLETLYAKSQEV 688
Cdd:COG5022 1072 RRENSLLDDKQLYQLESTENLLKTINVKDLEV 1103
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1264-1424 |
7.87e-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: 7.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1264 ELTGSLEESQGQLHSVQLRLEAAQSQHDRivqglqeqmsqlvpgARVAELQHLLSLREEEAERLNAQQEEYKQQLKARED 1343
Cdd:COG1196 217 ELKEELKELEAELLLLKLRELEAELEELE---------------AELEELEAELEELEAELAELEAELEELRLELEELEL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1344 QVEEAEARLHNVEWLLQEKVEELRKQFEKNTRSDLLLKELYVENAHLMKAVQLTEEKQRGAEKKNCVLEEKVRALNKLIS 1423
Cdd:COG1196 282 ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361
|
.
gi 1958766557 1424 K 1424
Cdd:COG1196 362 E 362
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1096-1388 |
8.27e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 8.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1096 ESEMNDVKTKLLQLEDVVRALEKA-----DSRESYRAELQRLSEENSVLKSDLGKIQLELGTSESR-NEVQR-------- 1161
Cdd:PRK02224 376 REAVEDRREEIEELEEEIEELRERfgdapVDLGNAEDFLEELREERDELREREAELEATLRTARERvEEAEAlleagkcp 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1162 ---QEIE------VLKRDKEQacfdLEELSTQTQKYKDEMSQLNCRILQLEgdssglhtqkeenhaAIQVLMKKLEEAEC 1232
Cdd:PRK02224 456 ecgQPVEgsphveTIEEDRER----VEELEAELEDLEEEVEEVEERLERAE---------------DLVEAEDRIERLEE 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1233 REKQQGDQIKHLKIELERVNEECQRLRLSQAELTGSLEESQGQLHSVQLRLEAAQSQHDRIVQGLQEQMSQLVPGARVAE 1312
Cdd:PRK02224 517 RREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRT 596
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1313 LQHLLSLREEEAERLN-------AQQEEYKQQLKAR------------EDQVEEAEARLHNVEWLLQEKVEELRKQFEKn 1373
Cdd:PRK02224 597 LLAAIADAEDEIERLRekrealaELNDERRERLAEKrerkreleaefdEARIEEAREDKERAEEYLEQVEEKLDELREE- 675
|
330
....*....|....*
gi 1958766557 1374 tRSDLLLKELYVENA 1388
Cdd:PRK02224 676 -RDDLQAEIGAVENE 689
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
383-679 |
8.28e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.77 E-value: 8.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 383 QELNFHQGQVEQLVQERDKARQDLEKAEKRnldfvremddchsaLEQlTEKKIKHLE---QEYRGRLSLLRSEVE----- 454
Cdd:TIGR04523 246 TEISNTQTQLNQLKDEQNKIKKQLSEKQKE--------------LEQ-NNKKIKELEkqlNQLKSEISDLNNQKEqdwnk 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 455 --------MERELfwEQARRQRAVLEQDVGRLQAEETSLREKLTLALKENSRLQKEIievVEKLSDSEKLVLRLQSDLQF 526
Cdd:TIGR04523 311 elkselknQEKKL--EEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQREL---EEKQNEIEKLKKENQSYKQE 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 527 VLKDKLEPQSMELLAQEEQFTAILNDYELKcrDLQDRNDELQAELEGLRvrlprsrqspsgtpgthrrwtpgrgpADNLF 606
Cdd:TIGR04523 386 IKNLESQINDLESKIQNQEKLNQQKDEQIK--KLQQEKELLEKEIERLK--------------------------ETIIK 437
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958766557 607 VGESIPvSLETEIKMQQMK-ENYQELRMQLETKVNYYEKEIEVMKRNFEKDKKEMEQAFQlEVSVLEGQKADLE 679
Cdd:TIGR04523 438 NNSEIK-DLTNQDSVKELIiKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEK-ELKKLNEEKKELE 509
|
|
| TACC_C |
pfam05010 |
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ... |
1101-1284 |
9.12e-03 |
|
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.
Pssm-ID: 461517 [Multi-domain] Cd Length: 201 Bit Score: 39.27 E-value: 9.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1101 DVKTKLLQLEDVVRALEKADSRESYRAELQRLSEENSVLKSDLGKIQLELGTSESRNEVQRQEIEVLKRDKEQACFDLEE 1180
Cdd:pfam05010 7 DAALEKARNEIEEKELEINELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEHAEIQKVLEEKDQALADLNS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958766557 1181 LSTqtqkykdEMSQLNCRILQLEGDSSGLHTQKEenhaaiqVLMKKLEEAECREKQQGDQIKHLKI----ELERVNEECQ 1256
Cdd:pfam05010 87 VEK-------SFSDLFKRYEKQKEVISGYKKNEE-------SLKKCAQDYLARIKKEEQRYQALKAhaeeKLDQANEEIA 152
|
170 180 190
....*....|....*....|....*....|..
gi 1958766557 1257 RLRLS----QAELTGSLEESQGQLHSVQLRLE 1284
Cdd:pfam05010 153 QVRSKakaeTAALQASLRKEQMKVQSLERQLE 184
|
|
| |
