|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1135-1446 |
2.25e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 81.91 E-value: 2.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1135 EREKDDMETKLLHLEDVVRALEKHVDLRENDR---LEFHRLSEE-----NTLLKNDLGRVRQELEAAESTHDAQRKEIEV 1206
Cdd:COG1196 178 ERKLEATEENLERLEDILGELERQLEPLERQAekaERYRELKEElkeleAELLLLKLRELEAELEELEAELEELEAELEE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1207 LKKDKEKACSEMEVLNRQNQNYKDQLSQLNVRVLQLGQEASTHQAQNEEHRVTIQMLTQSLEEVVRSGQQQSDQIQKLRV 1286
Cdd:COG1196 258 LEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1287 ELECLNQEHQSLQLPWSELTQTLEESQDQVQGAHLRLRQAQAQHLQEVR--LVPQDRVAELHRLLsLQGEQARRRLDAQR 1364
Cdd:COG1196 338 ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEelLEALRAAAELAAQL-EELEEAEEALLERL 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1365 EEHEKQLKATEERVEEAEMILKNMEMLLQEKVDKLKEQFEKNTKSDLLLKELYVENAHLVRALQATEEKQRGAEKQSRLL 1444
Cdd:COG1196 417 ERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLL 496
|
..
gi 768013504 1445 EE 1446
Cdd:COG1196 497 LE 498
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1135-1459 |
6.29e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 73.94 E-value: 6.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1135 EREKDDMETKLLHLEDVVRALEKHVD-LRENDRL--EFHRLSEE-----NTLLKNDLGRVRQELEAAESTHDAQRKEIEV 1206
Cdd:TIGR02168 178 ERKLERTRENLDRLEDILNELERQLKsLERQAEKaeRYKELKAElreleLALLVLRLEELREELEELQEELKEAEEELEE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1207 LKKDKEKACSEMEVLNRQNQNYKDQLSQLNVRVLQLGQEASTHQAQNEEHRVTIQMLTQSLEEVVRSGQQQSDQIQKLRV 1286
Cdd:TIGR02168 258 LTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1287 ELECLNQEHQSLQLPWSELTQTLEESQDQVQGAHLRLRQAQAQHLQEVRlvpqdRVAELhrllslqgEQARRRLDAQREE 1366
Cdd:TIGR02168 338 ELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS-----KVAQL--------ELQIASLNNEIER 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1367 HEKQLKATEERVEEAEMILKNMEMLLQEKvdKLKEQFEKNTKSDLLLKELYVENAHLVRALQatEEKQRGAEKQSRLLEE 1446
Cdd:TIGR02168 405 LEARLERLEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLEEALE--ELREELEEAEQALDAA 480
|
330
....*....|...
gi 768013504 1447 KvRALNKLVSRIA 1459
Cdd:TIGR02168 481 E-RELAQLQARLD 492
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1134-1460 |
9.28e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 73.55 E-value: 9.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1134 LEREKDDMETKLLHLEDVVRALEKHVdlrENDRLEFHRLSEENTLLKNDLGRVRQELEAAESTHDAQRKEIEVLKKDKEK 1213
Cdd:TIGR02168 717 LRKELEELSRQISALRKDLARLEAEV---EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ 793
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1214 ACSEMEVLNRQNQNYKDQLSQLNVRVLQLGQEASTHQAQNEEHRVTIQMLTQSLEevvrsgqQQSDQIQKLRVELEclnq 1293
Cdd:TIGR02168 794 LKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIE-------ELSEDIESLAAEIE---- 862
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1294 ehqslqlpwsELTQTLEESQDQVQgAHLRLRQAQAQHLQEVRLVPQDRVAELHRLlslqgEQARRRLDAQREEHEKQLKA 1373
Cdd:TIGR02168 863 ----------ELEELIEELESELE-ALLNERASLEEALALLRSELEELSEELREL-----ESKRSELRRELEELREKLAQ 926
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1374 TEERVEEAEMilknmemllqeKVDKLKEQFekntksdlllkelyveNAHLVRALQATEEKQRGAEKQSRLLEEKVRALNK 1453
Cdd:TIGR02168 927 LELRLEGLEV-----------RIDNLQERL----------------SEEYSLTLEEAEALENKIEDDEEEARRRLKRLEN 979
|
....*..
gi 768013504 1454 LVSRIAP 1460
Cdd:TIGR02168 980 KIKELGP 986
|
|
| EF-hand_7 |
pfam13499 |
EF-hand domain pair; |
214-275 |
2.05e-11 |
|
EF-hand domain pair;
Pssm-ID: 463900 [Multi-domain] Cd Length: 67 Bit Score: 60.73 E-value: 2.05e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768013504 214 ESQIRGVWEELGVGSSGHLSEQELAVVCQSVGLQG-LEKEELEDLFNKLDQDGDGKVSLEEFQ 275
Cdd:pfam13499 1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEpLSDEEVEELFKEFDLDKDGRISFEEFL 63
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1067-1459 |
6.59e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 64.21 E-value: 6.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1067 RSWSRGTQEQASEQQARAEGALEPGCHkhsveVARRGSLPSHLQLADP-QGSWQEQLAAPEegetkiALEREKDDMETKL 1145
Cdd:PRK04863 293 RELYTSRRQLAAEQYRLVEMARELAEL-----NEAESDLEQDYQAASDhLNLVQTALRQQE------KIERYQADLEELE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1146 LHLEDVVRALEKHVDLRENDRLEFHRLSEENTLLKNDLGRVRQELEAAESTHDAQRKEIEVLkkDKEKACSEMEVLNRQN 1225
Cdd:PRK04863 362 ERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQAL--ERAKQLCGLPDLTADN 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1226 -----QNYKDQLSQLNVRVLQLGQEASTHQAQNEEHRVTIQMLTQSLEEVVRSGQQQSdQIQKLR--VELECLNQEHQSL 1298
Cdd:PRK04863 440 aedwlEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRSEAWDV-ARELLRrlREQRHLAEQLQQL 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1299 QLPWSELTQTLEESQDQVQgahlRLRQAQAQHLQEVrlvpqDRVAELHRLLSLQGEQ------ARRRLDAQREEHEKQLK 1372
Cdd:PRK04863 519 RMRLSELEQRLRQQQRAER----LLAEFCKRLGKNL-----DDEDELEQLQEELEARleslseSVSEARERRMALRQQLE 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1373 ATEERVEEAEmILKNMEMLLQEKVDKLKEQFEKNtksdlllkelyVENAHLVRAL-QATEEKQRGAEKQSRLLEEKVRAL 1451
Cdd:PRK04863 590 QLQARIQRLA-ARAPAWLAAQDALARLREQSGEE-----------FEDSQDVTEYmQQLLERERELTVERDELAARKQAL 657
|
....*...
gi 768013504 1452 NKLVSRIA 1459
Cdd:PRK04863 658 DEEIERLS 665
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1168-1451 |
1.12e-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: 63.16 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1168 EFHRLSEENTLLKNDLGRVRQELEAAESTHDAQRKEIEVLKKDKEKACSEMEVLNRQNQ-------NYKDQLSQLNVRVL 1240
Cdd:TIGR02169 689 ELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSsleqeieNVKSELKELEARIE 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1241 QLgqEASTHQAQNEEHRVTIQMLTQSLEEVVRSGQQQSDQIQKLRVELECLNQEHQSLQLPWSELTQTLEESQDQVQGAH 1320
Cdd:TIGR02169 769 EL--EEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLK 846
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1321 LRLRQ-AQAQHLQEVRLVPQDRVAELHRLLSLQGEQARRRLDAQREEHEKQLKATEERVEEAEMILKNMEMLLQEKVDKL 1399
Cdd:TIGR02169 847 EQIKSiEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKL 926
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 768013504 1400 KEQFEKNTKSDLLLKELYVENAHLVRALQATEEKQRgaekqsrlLEEKVRAL 1451
Cdd:TIGR02169 927 EALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQR--------VEEEIRAL 970
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
409-717 |
2.09e-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: 62.39 E-value: 2.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 409 VEQLARERDKARQDLERAEKRNLEFVKEMDDCHSTLEQLTEKKIKHLEqgYRERLSLLRSEVEAERELFWEQAHRQRAAL 488
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAER--YQALLKEKREYEGYELLKEKEALERQKEAI 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 489 EWDVGRLQAEEAGLREKLtlalkenSRLQKEIVEVVEKLSDSERLALKLQKDLEFVLKDKLEpqsaELLAQEERFAAVLK 568
Cdd:TIGR02169 243 ERQLASLEEELEKLTEEI-------SELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIG----ELEAEIASLERSIA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 569 EYELKCRDLQDRNDELQAELEGLWARLPKNRHSPSwSPDGRRRQLpglgpagISFLGNSAPVSIETELMMEQVKEHYQDL 648
Cdd:TIGR02169 312 EKERELEDAEERLAKLEAEIDKLLAEIEELEREIE-EERKRRDKL-------TEEYAELKEELEDLRAELEEVDKEFAET 383
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768013504 649 R---TQLETKVNYYEREIAALKRNF-----EKERKDMEQAR-RREVSVLEGQKADLEELHEKSQEVIWGLQEQLQDTA 717
Cdd:TIGR02169 384 RdelKDYREKLEKLKREINELKRELdrlqeELQRLSEELADlNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLA 461
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
378-714 |
3.15e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.00 E-value: 3.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 378 ALDNELMTVDSAVQQAALACYHQELSYQQGQVEQLARERDKARQDLERAEKRNLEFVKEMDDCHSTLEQLTEK--KIKHL 455
Cdd:TIGR02168 224 ELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEisRLEQQ 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 456 EQGYRERL-SLLRSEVEAERELfwEQAHRQRAALEWDVGRLQAEEAGLREKLTLALKENSRLQKEIVEVVEKLSDSERLA 534
Cdd:TIGR02168 304 KQILRERLaNLERQLEELEAQL--EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 535 LKLQKDLefvlkdklepqsAELLAQEERFAAVLKEYELKCRDLQDRNDELQAELEGLWARLPKNRHSPSwspdgrRRQLP 614
Cdd:TIGR02168 382 ETLRSKV------------AQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKEL------QAELE 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 615 glgpagisflgnsapvsiETELMMEQVKEHYQDLRTQLETKvnyyEREIAALKRNFEKERKDMEQARRRevsvLEGQKAD 694
Cdd:TIGR02168 444 ------------------ELEEELEELQEELERLEEALEEL----REELEEAEQALDAAERELAQLQAR----LDSLERL 497
|
330 340
....*....|....*....|
gi 768013504 695 LEELHEKSQEVIWGLQEQLQ 714
Cdd:TIGR02168 498 QENLEGFSEGVKALLKNQSG 517
|
|
| EFh |
cd00051 |
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ... |
228-275 |
4.50e-09 |
|
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: 54.09 E-value: 4.50e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 768013504 228 SSGHLSEQELAVVCQSVGLqGLEKEELEDLFNKLDQDGDGKVSLEEFQ 275
Cdd:cd00051 13 GDGTISADELKAALKSLGE-GLSEEEIDEMIREVDKDGDGKIDFEEFL 59
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1116-1402 |
4.96e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 61.24 E-value: 4.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1116 GSWQEQLAAPEEGETKIA-LEREKDDMETKLLHLEDVVRALEKhvdLRENDRLEFHRLSEENTL-LKNDLGRVRQELEAA 1193
Cdd:TIGR02169 230 KEKEALERQKEAIERQLAsLEEELEKLTEEISELEKRLEEIEQ---LLEELNKKIKDLGEEEQLrVKEKIGELEAEIASL 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1194 ESTHDAQRKEIEVLKKDKEKACSEMEVLNRQNQNYKDQLSQLNVRVLQLGQEASTHQAQNEEhrvtiqmLTQSLEEVVRS 1273
Cdd:TIGR02169 307 ERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELED-------LRAELEEVDKE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1274 GQQQSDQIQKLRVELECLNQEHQSLQLPWSELTQTLEESQDQVQGAHLRLRQAQAQH--LQEVRLVPQDRVAELhrllsl 1351
Cdd:TIGR02169 380 FAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKIneLEEEKEDKALEIKKQ------ 453
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 768013504 1352 qgEQARRRLDAQREEHEKQLKATEERVEEAEMILKNmemlLQEKVDKLKEQ 1402
Cdd:TIGR02169 454 --EWKLEQLAADLSKYEQELYDLKEEYDRVEKELSK----LQRELAEAEAQ 498
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1144-1449 |
1.12e-08 |
|
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: 59.75 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1144 KLLHLEDVVRALEKHVDLRENDRLEFHRLSEENTLLKNDLGRvRQELEAAESTHDAQRKEIEVLKKDKEKACSEmevlnR 1223
Cdd:pfam17380 273 QLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVER-RRKLEEAEKARQAEMDRQAAIYAEQERMAME-----R 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1224 QNQNYKDQLSQLNVRVLQLGQEASTHQAQNEEHRVTIQMLTQSLEEVVRsgqQQSDQIQKLRVELEclnQEHQSLQLPWS 1303
Cdd:pfam17380 347 ERELERIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVR---QELEAARKVKILEE---ERQRKIQQQKV 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1304 ELTQTLEESQDQVQGAHLRLRQAQAQHLQEVRLVPQDRVAELHRLLSLQGEQARRRLDAQREEHEKQLKATEER-VEEAE 1382
Cdd:pfam17380 421 EMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRkILEKE 500
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768013504 1383 MILKNMEMLLQEKVDKLKEQFEKNTKSDLLLKELYVENAHLVRALQATEEKQRGAEKQSRLLEEKVR 1449
Cdd:pfam17380 501 LEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSR 567
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1115-1366 |
2.47e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.79 E-value: 2.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1115 QGSWQEQLAAPEEGETKIA-LEREKDDMETKLLHLEDVVRALEKHVDLRENDRLEFH-----------RLSEENTLLKND 1182
Cdd:COG1196 238 EAELEELEAELEELEAELEeLEAELAELEAELEELRLELEELELELEEAQAEEYELLaelarleqdiaRLEERRRELEER 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1183 LGRVRQELEAAESTHDAQRKEIEVLKKDKEKACSEMEVLNRQNQNYKDQLSQLNVRVLQLGQEASTHQAQNEEHRVTIQM 1262
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1263 LTQSLEEVVRSGQQQSDQIQKLRVELECLNQEHQSLQLPWSELTQTLEESQDQVQGAHLRLRQAQAQHLQEVRLVPQDRV 1342
Cdd:COG1196 398 LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA 477
|
250 260
....*....|....*....|....
gi 768013504 1343 AELHRLLSLQGEQARRRLDAQREE 1366
Cdd:COG1196 478 ALAELLEELAEAAARLLLLLEAEA 501
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1141-1458 |
4.65e-08 |
|
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: 57.72 E-value: 4.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1141 METKLLHLEDVVRALEKHVDLrENDRL------------EFHRLSEENTLLKNDLGRVRQELEAAESTHDAQRK------ 1202
Cdd:TIGR04523 216 LESQISELKKQNNQLKDNIEK-KQQEInektteisntqtQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKqlnqlk 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1203 -EIEVLKKDKEKACS------------EMEVLNRQNQNYKDQLSQLNVRVLQLGQEASTHQAQNEEHRVTIQMLTQSLEE 1269
Cdd:TIGR04523 295 sEISDLNNQKEQDWNkelkselknqekKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEK 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1270 VVRSGQQQSDQIQKLRVELECLNQEHQSLQlpwsELTQTLEESQDQVQGAHLRLRQaQAQHLQEVRLVPQDRVAELHRLL 1349
Cdd:TIGR04523 375 LKKENQSYKQEIKNLESQINDLESKIQNQE----KLNQQKDEQIKKLQQEKELLEK-EIERLKETIIKNNSEIKDLTNQD 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1350 SlQGEQARRRLDAQREEHEKQLKATEERVEEAEMILKNMEMLLQEKVDKLKEQFEKNTKSDLLLKELyvenahlvralqa 1429
Cdd:TIGR04523 450 S-VKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDL------------- 515
|
330 340
....*....|....*....|....*....
gi 768013504 1430 teekqrgaEKQSRLLEEKVRALNKLVSRI 1458
Cdd:TIGR04523 516 --------TKKISSLKEKIEKLESEKKEK 536
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
379-591 |
5.34e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.64 E-value: 5.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 379 LDNELMTVDSAVQQAALACYHQELSYQQGQVEQLARERDKARQDLERAEKRNLEFVKEMDDCHSTLEQLTEKKIKHLEQg 458
Cdd:COG1196 225 LEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD- 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 459 yRERLSLLRSEVEAERelfwEQAHRQRAALEWDVGRLQAEEAGLREKLTLALKENSRLQKEIVEVVEKLSDSERLALKLQ 538
Cdd:COG1196 304 -IARLEERRRELEERL----EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 768013504 539 KDLEFVLKDKLEPQSAELLAQEErfaavLKEYELKCRDLQDRNDELQAELEGL 591
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQ-----LEELEEAEEALLERLERLEEELEEL 426
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
357-591 |
5.62e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.76 E-value: 5.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 357 EILQSLDFSVDEKVNLLELTW-ALDNELMTVDS--AVQQAALACYHQELSYQQGQVEQLARERDKARQDLERAEKRNLEF 433
Cdd:TIGR02168 270 EELRLEVSELEEEIEELQKELyALANEISRLEQqkQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEEL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 434 VKEMDDChstLEQLTEKKIKhleqgyRERLSLLRSEVEAErelfWEQAHRQRAALEWDVGRLQAEEAGLREKLTLALKEN 513
Cdd:TIGR02168 350 KEELESL---EAELEELEAE------LEELESRLEELEEQ----LETLRSKVAQLELQIASLNNEIERLEARLERLEDRR 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768013504 514 SRLQKEIVEVVEKLSDSERLALKLQKDLEFVLKDKLEPQSAELLAQEERFAAVLKEYELKCRDLQDRNDELQAELEGL 591
Cdd:TIGR02168 417 ERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSL 494
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1179-1458 |
1.50e-07 |
|
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: 56.18 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1179 LKNDLGRVRQELEAAESTHDAQRKEIEvlkkdkEKAcSEMEVLNRQNQNYKDQLSQLNVRVLQLGQEASTHQAQNEEHRV 1258
Cdd:TIGR04523 340 LNEQISQLKKELTNSESENSEKQRELE------EKQ-NEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDE 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1259 TIQMLTQSLEEVVRSGQQQSDQIQKLRVELECLNQEHQSLQLPWSELTQTLEESQDQVQ---GAHLRLRQAQAQHLQEVR 1335
Cdd:TIGR04523 413 QIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKvlsRSINKIKQNLEQKQKELK 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1336 LVPQD-------------RVAELHRLLSlQGEQARRRLDAQREEHEKQLKATEERVEEAEMILKNMEML-----LQEKVD 1397
Cdd:TIGR04523 493 SKEKElkklneekkeleeKVKDLTKKIS-SLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEkeideKNKEIE 571
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768013504 1398 KLKEQFE----KNTKSDLLLKELYVENAHLVRALQATEEKQRGAEKQSRLLEEKVRALNKLVSRI 1458
Cdd:TIGR04523 572 ELKQTQKslkkKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNI 636
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
400-613 |
1.98e-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: 1.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 400 QELSYQQGQVEQLARERDKARQDLERAEKRNLEFVKEMDDCHSTLEQLTEK---KIKHLEQGYRERLSLLRSEVEAEREl 476
Cdd:COG1196 302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEleeAEAELAEAEEALLEAEAELAEAEEE- 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 477 fWEQAHRQRAALEWDVGRLQAEEAGLREKLTLALKENSRLQKEIVEVVEKLSDSERLALKLQKDLEFVLKDKLEpQSAEL 556
Cdd:COG1196 381 -LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE-LEEEE 458
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 768013504 557 LAQEERFAAVLKEYELKCRDLQDRNDELQAELEGLWARLPKNRHSPSWSPDGRRRQL 613
Cdd:COG1196 459 EALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALL 515
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1166-1429 |
3.79e-07 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 54.75 E-value: 3.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1166 RLEFHRLSEENTLLKNDLG--RVRQELEAAESTHDAQ-----------RKEIEVLKK---DKEKACSEMEVLNRQNQNYK 1229
Cdd:pfam05557 6 ESKARLSQLQNEKKQMELEhkRARIELEKKASALKRQldresdrnqelQKRIRLLEKreaEAEEALREQAELNRLKKKYL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1230 DQLSQLnvrvlqlgqeASTHQAQNEEHRVTIQMLTQSLEEVVRSGQQQSDQIQKLRVELECLNQEHQSLQLPWSELTQ-- 1307
Cdd:pfam05557 86 EALNKK----------LNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQlr 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1308 -TLEESQDQVQGAHLRLR------QAQAQHLQEVRlvpqDRVAELHRLLSLQGEQARRRldaqreEHEKQLKATEERVEe 1380
Cdd:pfam05557 156 qNLEKQQSSLAEAEQRIKelefeiQSQEQDSEIVK----NSKSELARIPELEKELERLR------EHNKHLNENIENKL- 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 768013504 1381 aemilknmemLLQEKVDKLKEQFEKNTKSDLLLKELYVENAHLVRALQA 1429
Cdd:pfam05557 225 ----------LLKEEVEDLKRKLEREEKYREEAATLELEKEKLEQELQS 263
|
|
| EF-hand_8 |
pfam13833 |
EF-hand domain pair; |
228-274 |
4.00e-07 |
|
EF-hand domain pair;
Pssm-ID: 404678 [Multi-domain] Cd Length: 54 Bit Score: 48.08 E-value: 4.00e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 768013504 228 SSGHLSEQELAVVCQSVGLQGLEKEELEDLFNKLDQDGDGKVSLEEF 274
Cdd:pfam13833 1 EKGVITREELKRALALLGLKDLSEDEVDILFREFDTDGDGYISFDEF 47
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1179-1408 |
4.65e-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: 54.00 E-value: 4.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1179 LKNDLGRVRQELEAAESTHDAQRKEIEVLKKDKEKACSEMEVLNRQNQNYKDQLSQLNVRVLQLGQEASTHQAQNEEHR- 1257
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKe 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1258 ------VTIQMLTQSLEEVVRSGQQQSDQIQKLRVELECLNQEHQslqlpwsELTQTLEESQDQVQgahlRLRQAQAQHL 1331
Cdd:COG4942 105 elaellRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARR-------EQAEELRADLAELA----ALRAELEAER 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768013504 1332 QEVRLVPQDRVAELHRLLSLQGEQAR--RRLDAQREEHEKQLKATEERVEEaemilknmemlLQEKVDKLKEQFEKNTK 1408
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKllARLEKELAELAAELAELQQEAEE-----------LEALIARLEAEAAAAAE 241
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
382-706 |
5.37e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.68 E-value: 5.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 382 ELMTVDSAVQQAALACYHQELSYQQGQVEQLARERDKARQ-------DLERAEKRNLEFVKEMDDCHSTLEQLTEKKIKH 454
Cdd:TIGR02168 687 EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRqisalrkDLARLEAEVEQLEERIAQLSKELTELEAEIEEL 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 455 LEQGYRERLSLLRSEVE-AERELFWEQAHRQRAALEWDVGRLQAEEAGLREK---------------------LTLALKE 512
Cdd:TIGR02168 767 EERLEEAEEELAEAEAEiEELEAQIEQLKEELKALREALDELRAELTLLNEEaanlrerleslerriaaterrLEDLEEQ 846
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 513 NSRLQKEIVEVVEKLSDSERLALKLQKDLEFVL--KDKLEPQSAELLAQEERFAAVLKEYELKCRDLQDRNDELQAELEG 590
Cdd:TIGR02168 847 IEELSEDIESLAAEIEELEELIEELESELEALLneRASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQ 926
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 591 LWARLPKNRhspswspdGRRRQLpglgpagisflgnSAPVSIETELMMEQVKEHYQDL---RTQLETKVNYYEREIAALK 667
Cdd:TIGR02168 927 LELRLEGLE--------VRIDNL-------------QERLSEEYSLTLEEAEALENKIeddEEEARRRLKRLENKIKELG 985
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 768013504 668 R-NFEKERKDMEQARRREvsVLEGQKADLEELHEKSQEVI 706
Cdd:TIGR02168 986 PvNLAAIEEYEELKERYD--FLTAQKEDLTEAKETLEEAI 1023
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
408-729 |
1.28e-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: 53.15 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 408 QVEQLARERDKA-RQDLERAEKRNLEF---VKEMDDCHSTLEQlTEKKIKHLEQ---GYRERLSLLRSEVEAERELFWEQ 480
Cdd:TIGR02169 199 QLERLRREREKAeRYQALLKEKREYEGyelLKEKEALERQKEA-IERQLASLEEeleKLTEEISELEKRLEEIEQLLEEL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 481 AHRQRA-------ALEWDVGRLQAEEAGLREKLTLALKENSRLQKEIVEVVEKLSDSERLALKLQKDLE--FVLKDKLEP 551
Cdd:TIGR02169 278 NKKIKDlgeeeqlRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEeeRKRRDKLTE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 552 QSAELLAQEERFAAVLKEYELKCRDLQDRNDELQAELEGLwarlpKNRHSPSWSPDGRRRQLPGLGPAGISFLGNSAPVS 631
Cdd:TIGR02169 358 EYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKL-----KREINELKRELDRLQEELQRLSEELADLNAAIAGI 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 632 IETELMMEQVKEHYQDlrtqletkvnyyerEIAALKRNFEKERKDMEQARRREVSVLEGQKADLEELHEKSQEViwglqE 711
Cdd:TIGR02169 433 EAKINELEEEKEDKAL--------------EIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQREL-----A 493
|
330
....*....|....*...
gi 768013504 712 QLQDTARGPEPEQMGLAP 729
Cdd:TIGR02169 494 EAEAQARASEERVRGGRA 511
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1187-1381 |
1.41e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.46 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1187 RQELEAAESTHDAQRKEIEVLKKDKEKACSEME-------VLNRQNQNYKDQLSQLNVRVLQLGQEASTHQAQNEEHR-- 1257
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAalerriaALARRIRALEQELAALEAELAELEKEIAELRAELEAQKee 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1258 -----VTIQML-----------TQSLEEVVRSG-------QQQSDQIQKLRVELECLNQEHQSLQlpwsELTQTLEESQD 1314
Cdd:COG4942 106 laellRALYRLgrqpplalllsPEDFLDAVRRLqylkylaPARREQAEELRADLAELAALRAELE----AERAELEALLA 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768013504 1315 QVQGAHLRLRQAQAQHLQEVRLVPQDRVAELHRLLSLQgeQARRRLDAQREEHEKQLKATEERVEEA 1381
Cdd:COG4942 182 ELEEERAALEALKAERQKLLARLEKELAELAAELAELQ--QEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1165-1417 |
2.11e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 52.32 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1165 DRLEFHRLSEENTLLKNDLGRVRQELeaaeSTHDAQRKEIEvlkkdkEKACSEMEVLNRQNQNYKDQLSQLNVRVLQLGQ 1244
Cdd:PHA02562 158 DLLDISVLSEMDKLNKDKIRELNQQI----QTLDMKIDHIQ------QQIKTYNKNIEEQRKKNGENIARKQNKYDELVE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1245 EASTHQAQNEEhrvtiqmLTQSLEEVVRSGQQQSDQIQKLRVELECLNQEHQSLQlpwSEL------------TQTLEES 1312
Cdd:PHA02562 228 EAKTIKAEIEE-------LTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQ---KVIkmyekggvcptcTQQISEG 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1313 QDQVQGAHLRLRQAQAQHLQEvrlvpQDRVAELHRLLSLQGEQARRRLDAQRE-EHEKQLKATEerVEEAEMILKNMEML 1391
Cdd:PHA02562 298 PDRITKIKDKLKELQHSLEKL-----DTAIDELEEIMDEFNEQSKKLLELKNKiSTNKQSLITL--VDKAKKVKAAIEEL 370
|
250 260 270
....*....|....*....|....*....|....
gi 768013504 1392 LQEKVD------KLKEQFEK--NTKSDlLLKELY 1417
Cdd:PHA02562 371 QAEFVDnaeelaKLQDELDKivKTKSE-LVKEKY 403
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1199-1458 |
2.77e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.37 E-value: 2.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1199 AQRKEIEVLKKDKEKACSEMEVLNRQNQNYKDQLSQLNvrvlqlgQEASTHQAQNEEHRVTIQMLTQSLEEVVRSGQQQS 1278
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELE-------EELEQLRKELEELSRQISALRKDLARLEAEVEQLE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1279 DQIQKLRVELECLNQEHQslqlpwsELTQTLEESQD--QVQGAHLRLRQAQAQHLQEVRLVPQDRVAELHRLLSLQGEQA 1356
Cdd:TIGR02168 747 ERIAQLSKELTELEAEIE-------ELEERLEEAEEelAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1357 rRRLDAQREEHEKQLKATEERVEEAEMILKNME---MLLQEKVDKLKEQFEK-NTKSDLLLKELYVENAHLVRA---LQA 1429
Cdd:TIGR02168 820 -ANLRERLESLERRIAATERRLEDLEEQIEELSediESLAAEIEELEELIEElESELEALLNERASLEEALALLrseLEE 898
|
250 260
....*....|....*....|....*....
gi 768013504 1430 TEEKQRGAEKQSRLLEEKVRALNKLVSRI 1458
Cdd:TIGR02168 899 LSEELRELESKRSELRRELEELREKLAQL 927
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
408-679 |
2.90e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.22 E-value: 2.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 408 QVEQLARERDKARQDLERAEKRnlefVKEMDDCHSTLEQLtekkikhleqgyreRLSLLRSEVEAERELFWEQAHRQRAA 487
Cdd:COG4913 611 KLAALEAELAELEEELAEAEER----LEALEAELDALQER--------------REALQRLAEYSWDEIDVASAEREIAE 672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 488 LE----------WDVGRLQAEEAGLREKLTLALKENSRLQKEIVEVVEKLSDSERLALKLQKDLEFVLKDKLEPQSAELl 557
Cdd:COG4913 673 LEaelerldassDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALL- 751
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 558 aqEERFAAVLKE--YELKCRDLQDRNDELQAELEGLWARLPK--NRHSPSWSPDgrrrqlpgLGPAGISFLGNSAPVSIE 633
Cdd:COG4913 752 --EERFAAALGDavERELRENLEERIDALRARLNRAEEELERamRAFNREWPAE--------TADLDADLESLPEYLALL 821
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 768013504 634 TELMMEQVKEHYQDLRTQLETKVnyyEREIAALKRNFEKERKDMEQ 679
Cdd:COG4913 822 DRLEEDGLPEYEERFKELLNENS---IEFVADLLSKLRRAIREIKE 864
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1120-1449 |
5.16e-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: 5.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1120 EQLAAPEEGETKIALEREK-DDMETKLLHLEDVVRALEKHVDLRENDR---LEFHRLSE-----ENTLLKNDLGRVRQEL 1190
Cdd:TIGR02169 160 DEIAGVAEFDRKKEKALEElEEVEENIERLDLIIDEKRQQLERLRRERekaERYQALLKekreyEGYELLKEKEALERQK 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1191 EAAESTHDAQRKEIEVLKKDKEKACSEMEVLNRqnqnykdQLSQLNVRVLQLGQ-EASTHQAQNEEHRVTIQMLTQSLEE 1269
Cdd:TIGR02169 240 EAIERQLASLEEELEKLTEEISELEKRLEEIEQ-------LLEELNKKIKDLGEeEQLRVKEKIGELEAEIASLERSIAE 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1270 VVRSGQQQSDQIQKLRVELECLNQEHQ--------------SLQLPWSELTQTLEESQDQVQ---GAHLRLRQAQAQHLQ 1332
Cdd:TIGR02169 313 KERELEDAEERLAKLEAEIDKLLAEIEelereieeerkrrdKLTEEYAELKEELEDLRAELEevdKEFAETRDELKDYRE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1333 EVRLVpQDRVAELHRLLSLQGEQArRRLDAQREEHEKQLKATEERVEEAEMILKNMEMLLQEKVDKLKEQFEKNTKSDLL 1412
Cdd:TIGR02169 393 KLEKL-KREINELKRELDRLQEEL-QRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQE 470
|
330 340 350
....*....|....*....|....*....|....*..
gi 768013504 1413 LKELYVENAHLVRALQATEEKQRGAEKQSRLLEEKVR 1449
Cdd:TIGR02169 471 LYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVR 507
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
408-718 |
5.48e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.09 E-value: 5.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 408 QVEQLARERDKAR--QDL--ERAEKRNLEFVKEMDDCHSTLEQLTEKKIKHLEQgyRERLSLLRSEVEAERElfweQAHR 483
Cdd:COG1196 201 QLEPLERQAEKAEryRELkeELKELEAELLLLKLRELEAELEELEAELEELEAE--LEELEAELAELEAELE----ELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 484 QRAALEWDVGRLQAEEAGLREKLtlalkenSRLQKEIVEVVEKLSDSERLALKLQKDLEfVLKDKLEPQSAELLAQEERF 563
Cdd:COG1196 275 ELEELELELEEAQAEEYELLAEL-------ARLEQDIARLEERRRELEERLEELEEELA-ELEEELEELEEELEELEEEL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 564 AAVLKEYELKCRDLQDRNDELQAELEglwARLPKNRHSpswspDGRRRQLpglgpagiSFLGNSAPVSIETELMMEQVKE 643
Cdd:COG1196 347 EEAEEELEEAEAELAEAEEALLEAEA---ELAEAEEEL-----EELAEEL--------LEALRAAAELAAQLEELEEAEE 410
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768013504 644 HYQDLRTQLETKVNYYEREIAALKRNFEKERKDMEQARRREVSVLEgQKADLEELHEKSQEVIWGLQEQLQDTAR 718
Cdd:COG1196 411 ALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE-EEEALLELLAELLEEAALLEAALAELLE 484
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1230-1462 |
6.38e-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: 6.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1230 DQLSQLNVRVLQLGQEASTHQAQNEEHRVTIQMLTQSLEEVVRSGQQQSDQIQKLRVELECLNQEHQSLQLPWSELTQTL 1309
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1310 EESQDQVqGAHLRLRQAQAQHLQEVRLVPQDRVAELHRLLSLQGEQARrrldaQREEHEKQLKATEERVEEAEMILKNME 1389
Cdd:COG4942 100 EAQKEEL-AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAP-----ARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768013504 1390 MLLQEKVDKLKEQFEKntksdllLKELYVENAHLVRALQATEEKQRgaeKQSRLLEEKVRALNKLVSRIAPAA 1462
Cdd:COG4942 174 AELEALLAELEEERAA-------LEALKAERQKLLARLEKELAELA---AELAELQQEAEELEALIARLEAEA 236
|
|
| FRQ1 |
COG5126 |
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
207-274 |
6.64e-06 |
|
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 47.09 E-value: 6.64e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768013504 207 SPSFDTPESQIRGVWEELGVGSSGHLSEQELAVVCQSVGLqglEKEELEDLFNKLDQDGDGKVSLEEF 274
Cdd:COG5126 61 SLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTALGV---SEEEADELFARLDTDGDGKISFEEF 125
|
|
| FRQ1 |
COG5126 |
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
218-278 |
9.38e-06 |
|
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 46.71 E-value: 9.38e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768013504 218 RGVWEELGVGSSGHLSEQELAVVCQSVGLQGLEkEELEDLFNKLDQDGDGKVSLEEFQLGL 278
Cdd:COG5126 36 ATLFSEADTDGDGRISREEFVAGMESLFEATVE-PFARAAFDLLDTDGDGKISADEFRRLL 95
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1180-1454 |
1.01e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.45 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1180 KNDLGRVRQELEAAESTHDAQRKEIEVLKKDKEKAcsemevlnrqnQNYKDQLSQL-NVRVLQLGQEASTHQAQNEEHRV 1258
Cdd:TIGR02169 176 LEELEEVEENIERLDLIIDEKRQQLERLRREREKA-----------ERYQALLKEKrEYEGYELLKEKEALERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1259 TIQMLTQSLEEVVRSGQQQSDQIQKLRVELECLN--------QEHQSLQLPWSELTQTLEESQDQVQGAHLRLRQAQAQH 1330
Cdd:TIGR02169 245 QLASLEEELEKLTEEISELEKRLEEIEQLLEELNkkikdlgeEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERL 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1331 lqevrlvpQDRVAELHRLLSlQGEQARRRLDAQReeheKQLKATEERVEEAEMILKNMEMLLQEKVDKLKEQFEK----N 1406
Cdd:TIGR02169 325 --------AKLEAEIDKLLA-EIEELEREIEEER----KRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDElkdyR 391
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 768013504 1407 TKSDLLLKELYVENAHLVRALqatEEKQRGAEKQSRLLEEKVRALNKL 1454
Cdd:TIGR02169 392 EKLEKLKREINELKRELDRLQ---EELQRLSEELADLNAAIAGIEAKI 436
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1048-1456 |
1.26e-05 |
|
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: 50.12 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1048 AASCRGQAERLQaiqeerarswsrgTQEQASEQQARAEGALEPgCHKHSVEvARRGSLPSHLQLA-----DPQGSWQEQL 1122
Cdd:pfam15921 287 ASSARSQANSIQ-------------SQLEIIQEQARNQNSMYM-RQLSDLE-STVSQLRSELREAkrmyeDKIEELEKQL 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1123 AAPEEGETKIALEREKDDMETKllHLEDVVRALEKHVDLREND----RLEFHRLSEENTLLKNDLGRVRQELEaaESTHD 1198
Cdd:pfam15921 352 VLANSELTEARTERDQFSQESG--NLDDQLQKLLADLHKREKElsleKEQNKRLWDRDTGNSITIDHLRRELD--DRNME 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1199 AQRKEiEVLKKDKEKACSEMEVLNRQNQNYKDQLSQLNVRVLQLG----------QEASTHQAQNEEHRVTIQMLTQSLE 1268
Cdd:pfam15921 428 VQRLE-ALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLEstkemlrkvvEELTAKKMTLESSERTVSDLTASLQ 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1269 EVVRSGQQQSDQIQKLRVELECLNQEHQSLqlpwseltqtleesqdQVQGAHLRLRQAQAQHLQeVRLVPQDRVAELHR- 1347
Cdd:pfam15921 507 EKERAIEATNAEITKLRSRVDLKLQELQHL----------------KNEGDHLRNVQTECEALK-LQMAEKDKVIEILRq 569
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1348 ----LLSLQGEQARRRLDAQREEHEKQLKATEERVEeaemiLKNMEMLLQEKVDKLKEQFEKntKSDLLLKELYVENAHL 1423
Cdd:pfam15921 570 qienMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLE-----LQEFKILKDKKDAKIRELEAR--VSDLELEKVKLVNAGS 642
|
410 420 430
....*....|....*....|....*....|...
gi 768013504 1424 VRALQATEEKQrgaeKQSRLLEEKVRALNKLVS 1456
Cdd:pfam15921 643 ERLRAVKDIKQ----ERDQLLNEVKTSRNELNS 671
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1182-1454 |
1.35e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 50.05 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1182 DLGRVRQELEAAESTHDAQRKEI-EVLK----------------KDKEKACSEMEVLNRQNQNYKDQLSQ---------- 1234
Cdd:PRK10929 24 DEKQITQELEQAKAAKTPAQAEIvEALQsalnwleerkgsleraKQYQQVIDNFPKLSAELRQQLNNERDeprsvppnms 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1235 ---LNVRVLQLGQE--ASTHQAQNEEHRvtIQMLTQSLEEVvrsGQQQSDqIQKLrvelecLNQEHQSLQLPWSELTqTL 1309
Cdd:PRK10929 104 tdaLEQEILQVSSQllEKSRQAQQEQDR--AREISDSLSQL---PQQQTE-ARRQ------LNEIERRLQTLGTPNT-PL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1310 EESQDQVQGAHLRLRQAQAQHLQEVRLVPQDRvAELHRLLSLQGEQARRRLDAQREEHEKQLKAteERVEEAEMILKNME 1389
Cdd:PRK10929 171 AQAQLTALQAESAALKALVDELELAQLSANNR-QELARLRSELAKKRSQQLDAYLQALRNQLNS--QRQREAERALESTE 247
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768013504 1390 MLLQEKVD---KLKEQFEKNtksdlllKELYVENAHLVRALQATEEKQRGAEKQSrlleEKVR-ALNKL 1454
Cdd:PRK10929 248 LLAEQSGDlpkSIVAQFKIN-------RELSQALNQQAQRMDLIASQQRQAASQT----LQVRqALNTL 305
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
356-595 |
1.51e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.94 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 356 REILQSLDFSVDEKVNLLEltwALDNELMTVDSAVQQAALACYHQELSYQ--QGQVEQLARERDKARQDLERAEKRNLEF 433
Cdd:COG1196 238 EAELEELEAELEELEAELE---ELEAELAELEAELEELRLELEELELELEeaQAEEYELLAELARLEQDIARLEERRREL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 434 VKEMDDCHSTLEQLTEKKIKHLEQ--GYRERLSLLRSEVEAERELFWEQAHRQRAALEwDVGRLQAEEAGLREKLTLALK 511
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEEleELEEELEEAEEELEEAEAELAEAEEALLEAEA-ELAEAEEELEELAEELLEALR 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 512 ENSRLQKEIVEVVEKLSDSERLALKLQKDLEFVLKD--KLEPQSAELLAQEERFAAVLKEYELKCRDLQDRNDELQAELE 589
Cdd:COG1196 394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEAlaELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
....*.
gi 768013504 590 GLWARL 595
Cdd:COG1196 474 LLEAAL 479
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1045-1419 |
1.68e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.75 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1045 LRPAASCRGQAERLQAIQEE--RARSWSRGTQE--QASEQQARAEGALEPGCHKHSVEVARRGSLPShlQLADPQGSWQE 1120
Cdd:PTZ00121 1410 LKKAAAAKKKADEAKKKAEEkkKADEAKKKAEEakKADEAKKKAEEAKKAEEAKKKAEEAKKADEAK--KKAEEAKKADE 1487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1121 QLAAPEEGETKIALEREKDDMETKLLHLE--------DVVRALEKHVDLRENDRLEFHRLSEE----NTLLKNDLGRVRQ 1188
Cdd:PTZ00121 1488 AKKKAEEAKKKADEAKKAAEAKKKADEAKkaeeakkaDEAKKAEEAKKADEAKKAEEKKKADElkkaEELKKAEEKKKAE 1567
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1189 ELEAAESTHDAQRKEIEVLKKDKEKACSEMEVLNRQNQNYKDQlsqlNVRVLQLGQEASTHQAQNEEHRVTIQMLTQSLE 1268
Cdd:PTZ00121 1568 EAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE----EAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEA 1643
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1269 EVVRSGQQQSDQIQKLRVELECLNQEHQSLQLPWSELTQtlEESQDQVQGAHLRLRQAQAQHLQEVRLVPQDRVAELHRL 1348
Cdd:PTZ00121 1644 EEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKK--AEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEEL 1721
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768013504 1349 LSLQGEQARRRLDAQREEHEKQLKATEERVEEAEmilknmemllQEKVDKLKEQFEKNTKSDLLLKELYVE 1419
Cdd:PTZ00121 1722 KKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE----------KKKIAHLKKEEEKKAEEIRKEKEAVIE 1782
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1054-1456 |
1.88e-05 |
|
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: 49.45 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1054 QAERLQAIQEERARSWSRGTQEQASEQQARAEGALEPGchKHSVEVARRGSLPSHL---QLADPQGSWQEQLAAPEEGET 1130
Cdd:pfam12128 600 EELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKA--SREETFARTALKNARLdlrRLFDEKQSEKDKKNKALAERK 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1131 KIALEREKD-DMETKLLHLEDVVRALEKHVDLRENDRLEFHRLSEENTLLKNDLGRVRQELEAAESTHDAQRKEIEvlkk 1209
Cdd:pfam12128 678 DSANERLNSlEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALE---- 753
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1210 dkekacsemevlnrqnQNYKDQLSQLNV---RVLQLGQEasthqaqneehrvtIQMLTQSLEEVVRSGQQQSDQIQKLRv 1286
Cdd:pfam12128 754 ----------------TWYKRDLASLGVdpdVIAKLKRE--------------IRTLERKIERIAVRRQEVLRYFDWYQ- 802
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1287 elECLNQEHQSLQLPWSELTQTLEESQDQV--QGAHLRLRQAQAQHLQEVRLVPQDRVAELHRLL-SLQGEQARRRLDAQ 1363
Cdd:pfam12128 803 --ETWLQRRPRLATQLSNIERAISELQQQLarLIADTKLRRAKLEMERKASEKQQVRLSENLRGLrCEMSKLATLKEDAN 880
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1364 REEHEKQLKATEERVEEAEMILKNMEMLLQEKVDKLKEQFEKNTKSDL------LLKELYVENAHLVRALQATEEKQRGA 1437
Cdd:pfam12128 881 SEQAQGSIGERLAQLEDLKLKRDYLSESVKKYVEHFKNVIADHSGSGLaetwesLREEDHYQNDKGIRLLDYRKLVPYLE 960
|
410
....*....|....*....
gi 768013504 1438 EKQSRLLEEKVRALNKLVS 1456
Cdd:pfam12128 961 QWFDVRVPQSIMVLREQVS 979
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1054-1451 |
3.38e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.78 E-value: 3.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1054 QAERLQAIQEERARSWSRGTQEQASEQQARAEGALEpgchKHSVEVARRGSLPSHLQLADPQGSWQEQLAApEEGETKIA 1133
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ----LEELEEAEEALLERLERLEEELEELEEALAE-LEEEEEEE 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1134 LEREKDDMETKLLHLEDVVRALEKHVDLRENDRLEFHRLSEENTLLKNDLGRVRQELEAAESTHDAQRKEIEVLKKDKEK 1213
Cdd:COG1196 441 EEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLR 520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1214 ACSEMEVLNRQNQNYKDQ---------LSQLNVRVLQLGQEASTHQAQNEEHRVTIQMLTQSLEEVVRSGQQQSDQIQKL 1284
Cdd:COG1196 521 GLAGAVAVLIGVEAAYEAaleaalaaaLQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAA 600
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1285 RVELECLNQEHQSLQLP-----------------WSELTQTLEESQDQVQGAHLRLRQAQAQHLQEVRlvpqdRVAELHR 1347
Cdd:COG1196 601 VDLVASDLREADARYYVlgdtllgrtlvaarleaALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRR-----ELLAALL 675
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1348 LLSLQGEQARRRLDAQREEHEKQLKATEERVEEAEMILKNMEMLLQEKVDKLKEQFEKNTKSDLLLKELYVENAHLVRAL 1427
Cdd:COG1196 676 EAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEE 755
|
410 420
....*....|....*....|....
gi 768013504 1428 QATEEKQRGAEKQSRLLEEKVRAL 1451
Cdd:COG1196 756 LPEPPDLEELERELERLEREIEAL 779
|
|
| EFh_parvalbumin_like |
cd16251 |
EF-hand, calcium binding motif, found in parvalbumin-like EF-hand family; The family includes ... |
214-275 |
3.44e-05 |
|
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: 44.06 E-value: 3.44e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768013504 214 ESQIRGVWEELGVGSSGHLSEQELAVVCQSVGLQG--LEKEELEDLFNKLDQDGDGKVSLEEFQ 275
Cdd:cd16251 33 EDQIKKVFQILDKDKSGFIEEEELKYILKGFSIAGrdLTDEETKALLAAGDTDGDGKIGVEEFA 96
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1188-1462 |
3.71e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.97 E-value: 3.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1188 QELEAAESTHDAQRKEIEVLKKDKEKACSEMEVLNRQNQNYKDQLSQLNVRVLQLGQEASTHQAQNEEHRVTIQMLTQSL 1267
Cdd:COG4372 31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1268 EEVVRSGQQQSDQIQKLRVELECLNQEHQSLQLPWSELTQTLEESQDQVQGAHLRLRQAQAQHLQEVRLVPQDRVAELHR 1347
Cdd:COG4372 111 EELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1348 LLSLQGEQARRRLDAQREEHEKQLKATEERVEEAEMILKNMEMLLQEKVDKLKEQFEKNTKSDLLLKELYVENAHLVRAL 1427
Cdd:COG4372 191 EANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVE 270
|
250 260 270
....*....|....*....|....*....|....*
gi 768013504 1428 QATEEKQRGAEKQSRLLEEKVRALNKLVSRIAPAA 1462
Cdd:COG4372 271 KDTEEEELEIAALELEALEEAALELKLLALLLNLA 305
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1197-1462 |
4.89e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.14 E-value: 4.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1197 HDAQRKEIEVLKKDKEKACS---EMEVLNRQNQNYKDQLSQLNVRVLQLGQEASTHQAQNEEHRVTIQMLTQSLEEVVRS 1273
Cdd:TIGR02169 659 SRAPRGGILFSRSEPAELQRlreRLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKER 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1274 GQQQSDQIQKLRVELECLNQEHQSLQLPWSELTQTLEESQDQVQGAHLRLRQAQAQHLQ-EVRLVPQDRVAELHRLLSLQ 1352
Cdd:TIGR02169 739 LEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQaELSKLEEEVSRIEARLREIE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1353 GEQARRRLDAQREEHEKQ-LKATEERVEEAEMILKNMEMLLQEKVDKLKEQFEKNTKSdllLKELYVENAHLVRALQATE 1431
Cdd:TIGR02169 819 QKLNRLTLEKEYLEKEIQeLQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAA---LRDLESRLGDLKKERDELE 895
|
250 260 270
....*....|....*....|....*....|.
gi 768013504 1432 EKQRGAEKQSRLLEEKVRALNKLVSRIAPAA 1462
Cdd:TIGR02169 896 AQLRELERKIEELEAQIEKKRKRLSELKAKL 926
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1059-1462 |
5.02e-05 |
|
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: 48.02 E-value: 5.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1059 QAIQEERARswsRGTQEQ-ASEQQARAEGALEPGCHKhsvevARRGSLPSHLQLA-DPQGSWQEQLAAPEegetkiALER 1136
Cdd:COG3096 286 RALELRREL---FGARRQlAEEQYRLVEMARELEELS-----ARESDLEQDYQAAsDHLNLVQTALRQQE------KIER 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1137 EKDDMETKLLHLEDVVRALEKHVDLRENDRLEFHRLSEENTLLKNDLGRVRQELEAAESTHDAQRKEIEVLkkDKEKACS 1216
Cdd:COG3096 352 YQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQAVQAL--EKARALC 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1217 EMEVLNRQN-----QNYKDQLSQLNVRVLQLGQEASTHQAQNEEHRVTIQMLTQSLEEVVRS--GQQQSDQIQKLRvELE 1289
Cdd:COG3096 430 GLPDLTPENaedylAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIAGEVERSqaWQTARELLRRYR-SQQ 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1290 CLNQEHQSLQLPWSELTQtLEESQDQVQgahlRLRQAQAQHLQEVRlvpqDRVAELHRLLSlqgeqarrRLDAQREEHEK 1369
Cdd:COG3096 509 ALAQRLQQLRAQLAELEQ-RLRQQQNAE----RLLEEFCQRIGQQL----DAAEELEELLA--------ELEAQLEELEE 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1370 QLkateERVEEAEMILKNMEMLLQEKVDKLKEQFEKNTKSDLLLKEL------YVENAHLV-RALQATEEKQRGAEKQSR 1442
Cdd:COG3096 572 QA----AEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERLreqsgeALADSQEVtAAMQQLLEREREATVERD 647
|
410 420
....*....|....*....|
gi 768013504 1443 LLEEKVRALNKLVSRIAPAA 1462
Cdd:COG3096 648 ELAARKQALESQIERLSQPG 667
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1265-1465 |
6.10e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.74 E-value: 6.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1265 QSLEEVVRSGQQQSDQIQKLRVELECLNQEHQSLQLPWSELTQTLEESQDQVQGAHLRLRQAQAQHLQEvrlvpQDRVAE 1344
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL-----EERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1345 LHRLLSLQGEQaRRRLDAQREEHEKQLKATEERVEEaemilknmemlLQEKVDKLKEQFEKNTKS-DLLLKELYVENAHL 1423
Cdd:TIGR02168 752 LSKELTELEAE-IEELEERLEEAEEELAEAEAEIEE-----------LEAQIEQLKEELKALREAlDELRAELTLLNEEA 819
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 768013504 1424 VRALQATEEKQRGAEKQSRLLEEKVRALNKLVSRIAPAALSV 1465
Cdd:TIGR02168 820 ANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEI 861
|
|
| EF-hand_5 |
pfam13202 |
EF hand; |
254-275 |
6.24e-05 |
|
EF hand;
Pssm-ID: 433035 [Multi-domain] Cd Length: 25 Bit Score: 41.15 E-value: 6.24e-05
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1052-1407 |
6.43e-05 |
|
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: 47.43 E-value: 6.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1052 RGQAERLQAIQEERARSWSRGTQEQASEQQARAegalepgchkhsvEVARRGSLPSHlqladpqgswQEQLAAPEEGE-T 1130
Cdd:pfam17380 295 KMEQERLRQEKEEKAREVERRRKLEEAEKARQA-------------EMDRQAAIYAE----------QERMAMERERElE 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1131 KIALEREKDDMETklLHLEDVVRALEKhvdLRENDRLEFHRLSeentllKNDlgRVRQELEAAesthdaqrKEIEVLKKD 1210
Cdd:pfam17380 352 RIRQEERKRELER--IRQEEIAMEISR---MRELERLQMERQQ------KNE--RVRQELEAA--------RKVKILEEE 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1211 KEKACSEMEVLNRQNQNYKDQLSQLNVRVLQLGQEASTHQAQNEEHRVTIQM-LTQSLEEVVRSGQQQSDQIQKLRVELE 1289
Cdd:pfam17380 411 RQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVeRLRQQEEERKRKKLELEKEKRDRKRAE 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1290 CLNQEHQSLQLPWSELTQTLEESQDQVQGAHLRLRQAQAQHLQEVRLVPQDRvaelhrllslqgeQARRRLDAQREEHEK 1369
Cdd:pfam17380 491 EQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEER-------------RKQQEMEERRRIQEQ 557
|
330 340 350
....*....|....*....|....*....|....*....
gi 768013504 1370 QLKATEERvEEAEMILKNMEMLLQ-EKVDKLKEQFEKNT 1407
Cdd:pfam17380 558 MRKATEER-SRLEAMEREREMMRQiVESEKARAEYEATT 595
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1052-1447 |
8.97e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.44 E-value: 8.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1052 RGQAERLQAIQEERARSwsRGTQEQASEQQARAEGALEPGCHKHSVEVARRGSlpSHLQLADPQGSWQEQLAAPEEGETK 1131
Cdd:PTZ00121 1377 KKKADAAKKKAEEKKKA--DEAKKKAEEDKKKADELKKAAAAKKKADEAKKKA--EEKKKADEAKKKAEEAKKADEAKKK 1452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1132 IALEREKDDMETKLLHLEDVVRALEKHVDLRENDrlEFHRLSEENTLLKNDLGRVRQELEAAESTHDAQ-RKEIEVLKKD 1210
Cdd:PTZ00121 1453 AEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKAD--EAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEeAKKADEAKKA 1530
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1211 KEKACSEmEVLNRQNQNYKDQLSQLNvRVLQLGQEASTHQAQNEEHRVtiQMLTQSLEEVVRSGQQQSDQIQKLRVELEC 1290
Cdd:PTZ00121 1531 EEAKKAD-EAKKAEEKKKADELKKAE-ELKKAEEKKKAEEAKKAEEDK--NMALRKAEEAKKAEEARIEEVMKLYEEEKK 1606
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1291 LNQEhqslQLPWSELTQTLEESQDQVQGAHLRLRQAQAQHLQEVRLVPQDRVAElhRLLSLQGEQARRRLDAQREEHEKQ 1370
Cdd:PTZ00121 1607 MKAE----EAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAE--EENKIKAAEEAKKAEEDKKKAEEA 1680
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768013504 1371 LKATEERVEEAEMILKNMEMllQEKVDKLKEQF-EKNTKSDLLLKELYVENAHLVRALQATEEKQRGAEKQSRLLEEK 1447
Cdd:PTZ00121 1681 KKAEEDEKKAAEALKKEAEE--AKKAEELKKKEaEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEK 1756
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1133-1299 |
1.03e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1133 ALEREKDDMETKLLHLEDVVRALEKHVDLREN---------------DRLEFHRLSEENTLLKNDLGRVRQELEAAESTH 1197
Cdd:COG4913 239 RAHEALEDAREQIELLEPIRELAERYAAARERlaeleylraalrlwfAQRRLELLEAELEELRAELARLEAELERLEARL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1198 DAQRKEIEVLK--------KDKEKACSEMEVLNRQNQNYKDQLSQLNVRVLQLGQEASTHQAQNEEHRVTIQMLTQSLEE 1269
Cdd:COG4913 319 DALREELDELEaqirgnggDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEE 398
|
170 180 190
....*....|....*....|....*....|....
gi 768013504 1270 VVRSGQQQ----SDQIQKLRVELECLNQEHQSLQ 1299
Cdd:COG4913 399 ELEALEEAlaeaEAALRDLRRELRELEAEIASLE 432
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
392-532 |
1.05e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 392 QAALACYHQELSYQQGQVEQLARERDKARQDLERAEKRNLEF-VKEMDDCHSTLEQLTEKK--IKHLEQGYRERLSLLRS 468
Cdd:COG4913 294 EAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELeeRERRRARLEALLAALGL 373
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768013504 469 EVEAERELFWEQAHRQRAALEwdvgRLQAEEAGLREKLTLALKENSRLQKEIVEVVEKLSDSER 532
Cdd:COG4913 374 PLPASAEEFAALRAEAAALLE----ALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
399-591 |
1.22e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.98 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 399 HQELSYQQGQVEQLARERDKARQDLERAE------KRNLEFVK-EMDDCHSTLEQLTEKKIKhleqgYRERLSLLRSEve 471
Cdd:TIGR02169 715 SRKIGEIEKEIEQLEQEEEKLKERLEELEedlsslEQEIENVKsELKELEARIEELEEDLHK-----LEEALNDLEAR-- 787
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 472 aERELFWEQAHRQRAALEWDVGRLQAEEAGLREKLTLALKENSRLQKEIVEVVEklsdsERLALKLQKDLEFVLKDKLEP 551
Cdd:TIGR02169 788 -LSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQE-----QRIDLKEQIKSIEKEIENLNG 861
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 768013504 552 QSAELLAQEERFAAVLKEYELKCRDLQDRNDELQAELEGL 591
Cdd:TIGR02169 862 KKEELEEELEELEAALRDLESRLGDLKKERDELEAQLREL 901
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1188-1459 |
1.37e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 46.50 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1188 QELEAAESTHDAQRKEIEVLKKDKEKACSEMEVLNRQNQNYK---DQLSQLNVRVLQLGQEasthqaqNEEHRVTIQMLT 1264
Cdd:TIGR00618 542 TSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKediPNLQNITVRLQDLTEK-------LSEAEDMLACEQ 614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1265 QSLEEvvrsgqQQSDQIQKLRVELEcLNQEHQSLQLPWSELTQTLEE-SQDQVQGAHLRLRQAQAQHLQEVRLVPQdrvA 1343
Cdd:TIGR00618 615 HALLR------KLQPEQDLQDVRLH-LQQCSQELALKLTALHALQLTlTQERVREHALSIRVLPKELLASRQLALQ---K 684
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1344 ELHRLLSLQG--EQARRRLDAQREEHEKQLKATEERVEEAEMI------LKNMEMLLQEKVDKLKEQFekntksDLLLKE 1415
Cdd:TIGR00618 685 MQSEKEQLTYwkEMLAQCQTLLRELETHIEEYDREFNEIENASsslgsdLAAREDALNQSLKELMHQA------RTVLKA 758
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 768013504 1416 LyvENAHLVRALQATEEKQRGAEKQ--SRLLEEKVRALNKLVSRIA 1459
Cdd:TIGR00618 759 R--TEAHFNNNEEVTAALQTGAELShlAAEIQFFNRLREEDTHLLK 802
|
|
| EF-hand_1 |
pfam00036 |
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ... |
253-278 |
1.48e-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: 40.08 E-value: 1.48e-04
10 20
....*....|....*....|....*.
gi 768013504 253 ELEDLFNKLDQDGDGKVSLEEFQLGL 278
Cdd:pfam00036 1 ELKEIFRLFDKDGDGKIDFEEFKELL 26
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1130-1458 |
1.48e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.55 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1130 TKIALErEKDDMETKLLhLEDVVRALEKhvDLRENDRLEFHRLSEentlLKNDlgrvRQELEAAESTHDAQRKEIEVLKK 1209
Cdd:TIGR04523 106 SKINSE-IKNDKEQKNK-LEVELNKLEK--QKKENKKNIDKFLTE----IKKK----EKELEKLNNKYNDLKKQKEELEN 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1210 DKEKACSEMEVLNRQNQNYKDQLSQLNVRVLQLgqeasthQAQNEEHRvtiqMLTQSLEEVVRSGQQQSDQIQKLRVELE 1289
Cdd:TIGR04523 174 ELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNL-------KKKIQKNK----SLESQISELKKQNNQLKDNIEKKQQEIN 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1290 CLNQEHQSLQLPWSELTQTLEESQDQVQGAHLRLRQAQAQHLQEvrlvpQDRVAELHRLLSLQGEQARRRLDaqrEEHEK 1369
Cdd:TIGR04523 243 EKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKEL-----EKQLNQLKSEISDLNNQKEQDWN---KELKS 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1370 QLKATEERVEEAEMILKNMEmllqEKVDKLKEQFEKNTKSdllLKELYVENAHLVRALqatEEKQRGAEKQSRLLEEKVR 1449
Cdd:TIGR04523 315 ELKNQEKKLEEIQNQISQNN----KIISQLNEQISQLKKE---LTNSESENSEKQREL---EEKQNEIEKLKKENQSYKQ 384
|
....*....
gi 768013504 1450 ALNKLVSRI 1458
Cdd:TIGR04523 385 EIKNLESQI 393
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1189-1454 |
1.80e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 45.29 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1189 ELEAAESTHDAQRKEIEVLKKDKEKacsemevLNRQNQNYKDQLSQLNVRVLQLGQEASTHQAQNEEHRVTIQMLTQSLE 1268
Cdd:COG1340 9 SLEELEEKIEELREEIEELKEKRDE-------LNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1269 EVVRSGQQQSDQIQKLRVELECLNQEHQSL--------QLPWSELTQTL---EESQ--DQVQGAHLRLRQAQAQHLQEVR 1335
Cdd:COG1340 82 ELNEKLNELREELDELRKELAELNKAGGSIdklrkeieRLEWRQQTEVLspeEEKElvEKIKELEKELEKAKKALEKNEK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1336 LvpQDRVAELhRLLSLQGEQARRRLDAQREEHEKQLKATEERVEEAEMILKNMEML------LQEKVDKLKEQFEKntks 1409
Cdd:COG1340 162 L--KELRAEL-KELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELhkeiveAQEKADELHEEIIE---- 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 768013504 1410 dllLKELYVENAHLVRALQATEEKQRGAEKQSRLLEEKVRALNKL 1454
Cdd:COG1340 235 ---LQKELRELRKELKKLRKKQRALKREKEKEELEEKAEEIFEKL 276
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1133-1318 |
2.07e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.21 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1133 ALEREKDDMETKLLHLE-DVVRALEKHVDLR---ENDRLEFHRLSEENTLLKNDLGRVRQELEAAESTHDAQRKEIEVLK 1208
Cdd:TIGR02169 312 EKERELEDAEERLAKLEaEIDKLLAEIEELEreiEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYR 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1209 KDKEKACSEMEVLNRQNQNYKDQLSQLNVRVLQLGQE-ASTHQAQNE------EHRVTIQMLTQSLEEVVRSGQQQSDQI 1281
Cdd:TIGR02169 392 EKLEKLKREINELKRELDRLQEELQRLSEELADLNAAiAGIEAKINEleeekeDKALEIKKQEWKLEQLAADLSKYEQEL 471
|
170 180 190
....*....|....*....|....*....|....*..
gi 768013504 1282 QKLRVELECLNQEHQSLQLPWSELTQTLEESQDQVQG 1318
Cdd:TIGR02169 472 YDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRG 508
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1046-1448 |
2.18e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 46.05 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1046 RPAASCRGQAERL--QAIQEERARSWSRGTQEQASEQQARAEGALEPGCHKHSVEVARRGSLPS--HLQLADPQGSwQEQ 1121
Cdd:PLN02939 30 RLAVSCRARRRGFssQQKKKRGKNIAPKQRSSNSKLQSNTDENGQLENTSLRTVMELPQKSTSSddDHNRASMQRD-EAI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1122 LAAPEEgetkiALEREKDDMETKLLHLEDVVRALekhvdlrendrlefhRLSEENTLLKNDlGRVR--QELEAAESTHDA 1199
Cdd:PLN02939 109 AAIDNE-----QQTNSKDGEQLSDFQLEDLVGMI---------------QNAEKNILLLNQ-ARLQalEDLEKILTEKEA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1200 QRKEIEVLKKDKEKACSEM----------EVLNRQNQNYKDQLSQLNVR----VLQLGQEASTHQAQNEEHRVTIQMLTQ 1265
Cdd:PLN02939 168 LQGKINILEMRLSETDARIklaaqekihvEILEEQLEKLRNELLIRGATeglcVHSLSKELDVLKEENMLLKDDIQFLKA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1266 SLEEVVRSGQQqsdqiqklrveLECLNQEHQSLQLPWSELTQTLEESQDQVqgahLRLRQAQAQHLQEvrlvpqdRVAEL 1345
Cdd:PLN02939 248 ELIEVAETEER-----------VFKLEKERSLLDASLRELESKFIVAQEDV----SKLSPLQYDCWWE-------KVENL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1346 HRLLSL---QGEQARRRLDaQREEHEKQLKATEERVEEAEMILKNMEM--LLQEKVDKLKEQFEKNTKSDLLLKELYven 1420
Cdd:PLN02939 306 QDLLDRatnQVEKAALVLD-QNQDLRDKVDKLEASLKEANVSKFSSYKveLLQQKLKLLEERLQASDHEIHSYIQLY--- 381
|
410 420
....*....|....*....|....*...
gi 768013504 1421 AHLVRALQATEEKQRgAEKQSRLLEEKV 1448
Cdd:PLN02939 382 QESIKEFQDTLSKLK-EESKKRSLEHPA 408
|
|
| EFh |
smart00054 |
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ... |
253-274 |
2.38e-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: 39.67 E-value: 2.38e-04
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1198-1381 |
2.48e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1198 DAQRKeIEVLKKDKEKACSEMEVLNRQNQNYKDQLSQLNVR--VLQLGQEASTHQAQNEEHRVTIQMLTQSLEEVVRSgq 1275
Cdd:COG4913 607 DNRAK-LAALEAELAELEEELAEAEERLEALEAELDALQERreALQRLAEYSWDEIDVASAEREIAELEAELERLDAS-- 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1276 qqSDQIQKLRVELECLNQEHQSLQLPWSELTQTLEESQDQVQGAHLRLRQAQAQHLQEVRLVPQDRVAEL-HRLLSLQGE 1354
Cdd:COG4913 684 --SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLeERFAAALGD 761
|
170 180 190
....*....|....*....|....*....|.
gi 768013504 1355 ----QARRRLDAQREEHEKQLKATEERVEEA 1381
Cdd:COG4913 762 averELRENLEERIDALRARLNRAEEELERA 792
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1161-1394 |
2.54e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.78 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1161 LRENDRLEFHRLSEENTLLKNDLGRVRQELEAAEsthdaqrKEIEVLKKDkekacSEMEVLNRQNQNYKDQLSQLNVRVL 1240
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAE-------AALEEFRQK-----NGLVDLSEEAKLLLQQLSELESQLA 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1241 QLGQEASTHQAQNEEHRVTIQMLTQSLEEVVRSGQQQS--DQIQKLRVELeclnqehqslqlpwSELTQTLEESQDQVQG 1318
Cdd:COG3206 230 EARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQlrAQLAELEAEL--------------AELSARYTPNHPDVIA 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1319 AHLRLRQAQAQHLQEVRLVPQDRVAELhRLLSLQGEQARRRLDAQRE------EHEKQLKATEERVEEAEMILKNMEMLL 1392
Cdd:COG3206 296 LRAQIAALRAQLQQEAQRILASLEAEL-EALQAREASLQAQLAQLEArlaelpELEAELRRLEREVEVARELYESLLQRL 374
|
..
gi 768013504 1393 QE 1394
Cdd:COG3206 375 EE 376
|
|
| EF-hand_6 |
pfam13405 |
EF-hand domain; |
253-278 |
3.35e-04 |
|
EF-hand domain;
Pssm-ID: 463869 [Multi-domain] Cd Length: 30 Bit Score: 39.08 E-value: 3.35e-04
10 20
....*....|....*....|....*.
gi 768013504 253 ELEDLFNKLDQDGDGKVSLEEFQLGL 278
Cdd:pfam13405 1 ELREAFKLFDKDGDGKISLEELRKAL 26
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1136-1451 |
3.70e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.17 E-value: 3.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1136 REKDDMETKLLHLEDVV-RALEKHVDLRENDRlEFHRLSEENTLLKNDLgRVRQELEA-AESTH---DAQRKEIEVLKKD 1210
Cdd:pfam01576 2 RQEEEMQAKEEELQKVKeRQQKAESELKELEK-KHQQLCEEKNALQEQL-QAETELCAeAEEMRarlAARKQELEEILHE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1211 KEKACSEMEVLNRQNQNYKDQLSQlNVRVL--QLGQEASTHQAQNEEhRVTIQMLTQSLEEVVRSGQQQSDQIQKlrvel 1288
Cdd:pfam01576 80 LESRLEEEEERSQQLQNEKKKMQQ-HIQDLeeQLDEEEAARQKLQLE-KVTTEAKIKKLEEDILLLEDQNSKLSK----- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1289 eclnqEHQSLQLPWSELTQTLEESQDQVQG-AHLRLRQAQAQHLQEVRLVPQDRvaelhrlLSLQGEQARRRLDAQREEH 1367
Cdd:pfam01576 153 -----ERKLLEERISEFTSNLAEEEEKAKSlSKLKNKHEAMISDLEERLKKEEK-------GRQELEKAKRKLEGESTDL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1368 EKQLKATEERVEEAEMILKNMEMLLQEKVDKLKEQFEKNTKSDLLLKELYVENAHLVRALQATEEKQRGAEKQSRLLEEK 1447
Cdd:pfam01576 221 QEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEE 300
|
....
gi 768013504 1448 VRAL 1451
Cdd:pfam01576 301 LEAL 304
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1129-1452 |
4.02e-04 |
|
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: 45.04 E-value: 4.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1129 ETKIALEREKDDMETKLLHLEDVVRALEKHVDLRENDRLEFHRLSEentLLKNDLGRVRQELEAAESTHDAQRKEIEVLK 1208
Cdd:TIGR00606 688 QTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAP---GRQSIIDLKEKEIPELRNKLQKVNRDIQRLK 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1209 KDKEKACSEMEVLNRQNQNYKDQLSQLNVrvlqlgqeasthqaqneehrvtIQMLTQSLEEVVRSGQQQSDQIQKLRVEL 1288
Cdd:TIGR00606 765 NDIEEQETLLGTIMPEEESAKVCLTDVTI----------------------MERFQMELKDVERKIAQQAAKLQGSDLDR 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1289 EC--LNQEHQSLQLPWSELTQTLEESQDQVQGahlrlRQAQAQHLQEvrlvpqdRVAEL--HRLLSLQGEQARRRLDAQR 1364
Cdd:TIGR00606 823 TVqqVNQEKQEKQHELDTVVSKIELNRKLIQD-----QQEQIQHLKS-------KTNELksEKLQIGTNLQRRQQFEEQL 890
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1365 EEHEKQLK----ATEERVEEAEMILKNMEMLLQEKVDKLKEQFEKNTKSDLLLKELYVENAHLVRALQATEEK-QRGAEK 1439
Cdd:TIGR00606 891 VELSTEVQslirEIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKiQDGKDD 970
|
330
....*....|...
gi 768013504 1440 QSRLLEEKVRALN 1452
Cdd:TIGR00606 971 YLKQKETELNTVN 983
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1160-1459 |
4.28e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 45.21 E-value: 4.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1160 DLRENDRLEFHRLSEEntlLKNDLGRVRQELEAAESTHDAQRKEIEVLKKDKEKACSEMEVLNRQNQNYKDQLSQLNVRV 1239
Cdd:pfam12128 586 DLKRIDVPEWAASEEE---LRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEK 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1240 ----LQLGQEASTHQAQNEEHRVTIQ-MLTQSLEEVVRSGQQQSDQIQKLRVELeclnqehqslQLPWSELTQTLEESQD 1314
Cdd:pfam12128 663 qsekDKKNKALAERKDSANERLNSLEaQLKQLDKKHQAWLEEQKEQKREARTEK----------QAYWQVVEGALDAQLA 732
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1315 QVQGAHLRLRQAQAQHLQEVRlvpqdrvAELHRLLSLQG--EQARRRLDAQREEHEKQLKATEERVEEAEMILKNMEMLL 1392
Cdd:pfam12128 733 LLKAAIAARRSGAKAELKALE-------TWYKRDLASLGvdPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETW 805
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768013504 1393 QEKVDKLKEQFEKNTKSDLLLKELYVENAHLVRALQATEEKQRGA-EKQSRLLEEKVRALNKLVSRIA 1459
Cdd:pfam12128 806 LQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKAsEKQQVRLSENLRGLRCEMSKLA 873
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1119-1453 |
4.41e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.03 E-value: 4.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1119 QEQLAAPEEGETKIA-LEREKDDMETKLLHLEDVVRALEKHVDLRENDRLEfhrLSEENTLLKNDLGRVRQELEAAESTH 1197
Cdd:PRK02224 240 DEVLEEHEERREELEtLEAEIEDLRETIAETEREREELAEEVRDLRERLEE---LEEERDDLLAEAGLDDADAEAVEARR 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1198 DAQRKEIEVLKKDKEKACSEMEVLNRQNQNYKDQLSQLNVRVLQLGQEASTHQAQNEEHRVTIQMLTQSLEEVVRSGQQQ 1277
Cdd:PRK02224 317 EELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEEL 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1278 SDQIQKLRVELECLNQEHQSLQLPWSELTQTLEESQDQVQGAHLRLRQAQA-----------QHLQEVRLVP-----QDR 1341
Cdd:PRK02224 397 RERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEAlleagkcpecgQPVEGSPHVEtieedRER 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1342 VAELHRLLslqgEQARRRLDAQREEHE--KQLKATEERVEEAEMILKNMEMLLQEKVDKLKEQFEKntksdllLKELYVE 1419
Cdd:PRK02224 477 VEELEAEL----EDLEEEVEEVEERLEraEDLVEAEDRIERLEERREDLEELIAERRETIEEKRER-------AEELRER 545
|
330 340 350
....*....|....*....|....*....|....
gi 768013504 1420 NAHLVRALQATEEKQRGAEKQSRLLEEKVRALNK 1453
Cdd:PRK02224 546 AAELEAEAEEKREAAAEAEEEAEEAREEVAELNS 579
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1126-1453 |
5.14e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 5.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1126 EEGETKIALEREKDDMETKLLHLEDVVRALEKHVDLRENDRLEFHRLSEENTLLKNDLGRVRQELEAAESTHDAQRKEIE 1205
Cdd:PRK03918 197 EKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1206 VLKKD-------KEKAcSEMEVLNRQNQNYKDQLSQLNVRVLQLGQEASTHQAQ---NEEHRVTIQMLTQSLEEVVR--- 1272
Cdd:PRK03918 277 ELEEKvkelkelKEKA-EEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERikeLEEKEERLEELKKKLKELEKrle 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1273 ----------SGQQQSDQIQKLRVELECLNQEH------------QSLQLPWSELTQ---TLEESQDQVQGAHLRLRQAQ 1327
Cdd:PRK03918 356 eleerhelyeEAKAKKEELERLKKRLTGLTPEKlekeleelekakEEIEEEISKITArigELKKEIKELKKAIEELKKAK 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1328 AQHLQEVRLVPQDRVAELHRLLSLQGEQARRRLdAQREEHEKQLKATEERVE----EAEMILKNMEML-----LQEKVDK 1398
Cdd:PRK03918 436 GKCPVCGRELTEEHRKELLEEYTAELKRIEKEL-KEIEEKERKLRKELRELEkvlkKESELIKLKELAeqlkeLEEKLKK 514
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 768013504 1399 L-KEQFEKNTKSDLLLKELYVENAHLVRALQATEEKQRGAEKQSRLLEEKVRALNK 1453
Cdd:PRK03918 515 YnLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEE 570
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1172-1458 |
6.11e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.52 E-value: 6.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1172 LSEENTLLKNDLgrvRQELEAAESThDAQRKEIEVLKKDKEKACSEMEVLNRQNQNYKDQ-------------LSQLNVR 1238
Cdd:PRK11281 54 LEAEDKLVQQDL---EQTLALLDKI-DRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDndeetretlstlsLRQLESR 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1239 VLQLGQEASTHQ-------------------AQNE--EHRVTIQMLTQSLEEVVRSGQQQS-DQIQKLRVELECLNQ--E 1294
Cdd:PRK11281 130 LAQTLDQLQNAQndlaeynsqlvslqtqperAQAAlyANSQRLQQIRNLLKGGKVGGKALRpSQRVLLQAEQALLNAqnD 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1295 HQSLQLPWSELTQTLEESQDQVQGAHLRLRQAQAQHLQEVRlvpqdrvaelhrllslqgeqarrrldaqreeHEKQLKAT 1374
Cdd:PRK11281 210 LQRKSLEGNTQLQDLLQKQRDYLTARIQRLEHQLQLLQEAI-------------------------------NSKRLTLS 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1375 EERVEEAEmilkNMEMLLQEKVDKL-KEQFEKNTK-SDLLLK-----------ELYVENAhLVRALQATeekqrgaekqs 1441
Cdd:PRK11281 259 EKTVQEAQ----SQDEAARIQANPLvAQELEINLQlSQRLLKateklntltqqNLRVKNW-LDRLTQSE----------- 322
|
330
....*....|....*....
gi 768013504 1442 RLLEEKVRALNK--LVSRI 1458
Cdd:PRK11281 323 RNIKEQISVLKGslLLSRI 341
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
404-724 |
7.76e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 44.19 E-value: 7.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 404 YQQGQVEQLARERDKARQDLERAEKRNLEFVKEMDdchstleqlTEKKIKHLEQGYRERLSLLRSEVEAERELFWEQAHR 483
Cdd:pfam02463 139 VQGGKIEIIAMMKPERRLEIEEEAAGSRLKRKKKE---------ALKKLIEETENLAELIIDLEELKLQELKLKEQAKKA 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 484 QRAALEWDVGRLQAEEAGLREKLTLALKENSRLQKEIVEVVEKLSDSERLALKLQKDLEFVLKD------KLEPQSAELL 557
Cdd:pfam02463 210 LEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKEnkeeekEKKLQEEELK 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 558 AQEERFAAVLKEYELKCRDLQDRNDELQAELEGLwARLPKNRHSPSWSPDGRRRQLpglgpagISFLGNSAPVSIETELM 637
Cdd:pfam02463 290 LLAKEEEELKSELLKLERRKVDDEEKLKESEKEK-KKAEKELKKEKEEIEELEKEL-------KELEIKREAEEEEEEEL 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 638 MEQVKEHYQDLRTQLETKVNYYEREIAALKRNFE-KERKDMEQARRREVSVLEGQKADLEELHEKSQEVIWGLQEQLQDT 716
Cdd:pfam02463 362 EKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEeLELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIEL 441
|
....*...
gi 768013504 717 ARGPEPEQ 724
Cdd:pfam02463 442 KQGKLTEE 449
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1023-1448 |
9.12e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.95 E-value: 9.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1023 ELPLLGTERDA-SQTQPRMWEPPLRPAASCRGQAERLQAIQEERARSWSRGTQEQASEQQARAEgalepgCHKHSVEVAR 1101
Cdd:pfam15921 357 ELTEARTERDQfSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRE------LDDRNMEVQR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1102 RGSLPSHLQlADPQGSWQEQLAA---------------PEEGETKIALEREKDDMETKLLHLEDVVRALEK-HVDLREND 1165
Cdd:pfam15921 431 LEALLKAMK-SECQGQMERQMAAiqgkneslekvssltAQLESTKEMLRKVVEELTAKKMTLESSERTVSDlTASLQEKE 509
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1166 RlEFHRLSEENTLLKNDLGRVRQELEAAESTHDAQRK---EIEVLKKDKEKACSEMEVLNRQNQNykdqLSQLnvrVLQL 1242
Cdd:pfam15921 510 R-AIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNvqtECEALKLQMAEKDKVIEILRQQIEN----MTQL---VGQH 581
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1243 GQEASTHQAQNEEHRVTIQMLTQSLEEVVRSGQQQSDQIQKLRVELECLNQEHQSLQLPWSELTQTLEEsqdqvqgahlr 1322
Cdd:pfam15921 582 GRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKD----------- 650
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1323 LRQAQAQHLQEVRLVPQD--RVAELHRLLSLQGEQARRRLDAQREEHEKQLKATEERVEEAEMILKNMEM---------- 1390
Cdd:pfam15921 651 IKQERDQLLNEVKTSRNElnSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGsdghamkvam 730
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768013504 1391 --------------LLQEKVDKLKEQFEKNTKSDLLLKElyvENAHLVRALQ--ATEEKQRGAE-----KQSRLLEEKV 1448
Cdd:pfam15921 731 gmqkqitakrgqidALQSKIQFLEEAMTNANKEKHFLKE---EKNKLSQELStvATEKNKMAGElevlrSQERRLKEKV 806
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
393-595 |
1.37e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.49 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 393 AALACYHQELSYQQGQVEQLARERDKARQDLERAE---KRNLEFVKEMDDCHSTLEQLTEKKikhleqgyrerlsllrSE 469
Cdd:PRK02224 206 ERLNGLESELAELDEEIERYEEQREQARETRDEADevlEEHEERREELETLEAEIEDLRETI----------------AE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 470 VEAERELFWEQAHRQRAALEwdvgRLQAEEAGLREKLTL-------ALKENSRLQKEIVEVVEKLSDSERLALKLQKDLE 542
Cdd:PRK02224 270 TEREREELAEEVRDLRERLE----ELEEERDDLLAEAGLddadaeaVEARREELEDRDEELRDRLEECRVAAQAHNEEAE 345
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 768013504 543 FVLK--DKLEPQSAELLAQEERFAAVLKEYELKCRDLQDRNDELQAELEGLWARL 595
Cdd:PRK02224 346 SLREdaDDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERF 400
|
|
| XopAW |
NF041410 |
XopAW family type III secretion system calcium-binding effector; |
228-280 |
1.59e-03 |
|
XopAW family type III secretion system calcium-binding effector;
Pssm-ID: 469301 [Multi-domain] Cd Length: 227 Bit Score: 41.59 E-value: 1.59e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 768013504 228 SSGHLSEQELAVVCQS---VGLQGLEKEELEDLFNKLDQDGDGKVSLEEFQLGLFS 280
Cdd:NF041410 76 GDGSLSSDELAAAAPPpppPPDQAPSTELADDLLSALDTDGDGSISSDELSAGLTS 131
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1133-1289 |
1.65e-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: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1133 ALEREKDDMETKLLHLEDVVRALEKHVDLRENDRLEFHRLSEENTL------LKNDLGRVRQELEAAESTHD-------- 1198
Cdd:COG4913 614 ALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDeidvasAEREIAELEAELERLDASSDdlaaleeq 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1199 --AQRKEIEVLKKDKEKACSEMEVLNRQNQNYKDQLSQLNVRVLQLGQEASTHQAQNEEHRVTIQMLTQSLEEVVRSGQQ 1276
Cdd:COG4913 694 leELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEE 773
|
170
....*....|...
gi 768013504 1277 QSDQIQKLRVELE 1289
Cdd:COG4913 774 RIDALRARLNRAE 786
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1055-1366 |
1.81e-03 |
|
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: 43.02 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1055 AERLQAIQEERArswsrGTQEQASEQQARAEGALEpgchkhsvEVARRGSlpshlQLADPQ----------GSWQEQLAA 1124
Cdd:COG3096 360 TERLEEQEEVVE-----EAAEQLAEAEARLEAAEE--------EVDSLKS-----QLADYQqaldvqqtraIQYQQAVQA 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1125 PEE-----GETKIALEREKDDMET---KLLHLEDVVRALEKHVDLRENDRLEFHRLSEentLLKNDLGRV---------R 1187
Cdd:COG3096 422 LEKaralcGLPDLTPENAEDYLAAfraKEQQATEEVLELEQKLSVADAARRQFEKAYE---LVCKIAGEVersqawqtaR 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1188 QELEAAEStHDAQRKEIEVLKKdkekACSEMEVLNRQNQNYKDQLSQLNVRVLQLGQEASTHQAQNEEHRVTIQMLTQSL 1267
Cdd:COG3096 499 ELLRRYRS-QQALAQRLQQLRA----QLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQA 573
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1268 EEvvrSGQQQSDqiqkLRVELECLNQEHQSL--QLP-WSELTQTLEESQDQVqGAHLRLRQAQAQHLQevRLVPQDRVAE 1344
Cdd:COG3096 574 AE---AVEQRSE----LRQQLEQLRARIKELaaRAPaWLAAQDALERLREQS-GEALADSQEVTAAMQ--QLLEREREAT 643
|
330 340
....*....|....*....|..
gi 768013504 1345 LHRLLSlqgEQARRRLDAQREE 1366
Cdd:COG3096 644 VERDEL---AARKQALESQIER 662
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
404-594 |
1.85e-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: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 404 YQQGQVEQLARERDKARQDLERAEKRNLEFVKEMDDCHSTLEQLTEKkikhleqgyRERLSLLRSEVEAERElfweQAHR 483
Cdd:COG4913 264 YAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAE---------LERLEARLDALREELD----ELEA 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 484 QRAALEWD-VGRLQAEEAGLREKLTLALKENSRLQKEIVEVVEKLSDSERLALKLQKDLEfVLKDKLEPQSAELlaQEER 562
Cdd:COG4913 331 QIRGNGGDrLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAA-ALLEALEEELEAL--EEAL 407
|
170 180 190
....*....|....*....|....*....|..
gi 768013504 563 FAAVLKEyelkcRDLQDRNDELQAELEGLWAR 594
Cdd:COG4913 408 AEAEAAL-----RDLRRELRELEAEIASLERR 434
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1274-1453 |
2.39e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1274 GQQQSDQIQKLRVELECLNQEHQSLQLPWSELTQTLEESQDQ----------------VQGAHLRLRQAQAQhLQEVRLV 1337
Cdd:COG4913 605 GFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERrealqrlaeyswdeidVASAEREIAELEAE-LERLDAS 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1338 P------QDRVAELHRLLSlQGEQARRRLDAQREEHEKQLKATEERVEEAEMILKNMEMLL-QEKVDKLKEQFEKNTKSD 1410
Cdd:COG4913 684 SddlaalEEQLEELEAELE-ELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLArLELRALLEERFAAALGDA 762
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 768013504 1411 LLLKELyvenAHLVRALQATEEKQRGAEKQsrlLEEKVRALNK 1453
Cdd:COG4913 763 VERELR----ENLEERIDALRARLNRAEEE---LERAMRAFNR 798
|
|
| EFh |
cd00051 |
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ... |
253-288 |
2.44e-03 |
|
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: 37.53 E-value: 2.44e-03
10 20 30
....*....|....*....|....*....|....*.
gi 768013504 253 ELEDLFNKLDQDGDGKVSLEEFQLGLFSHEPALLLE 288
Cdd:cd00051 1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEE 36
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1125-1230 |
2.79e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.15 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1125 PEEGETKIALEREKDDMETKLLHLEDVVRALEKHV-DLREndrlEFHRLSEENTLLKNDLGRVRQELEA-AESTHDAQR- 1201
Cdd:COG2433 395 PEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVeELEA----ELEEKDERIERLERELSEARSEERReIRKDREISRl 470
|
90 100 110
....*....|....*....|....*....|
gi 768013504 1202 -KEIEVLKKDKEKACSEMEVLNRQNQNYKD 1230
Cdd:COG2433 471 dREIERLERELEEERERIEELKRKLERLKE 500
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1115-1457 |
2.90e-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: 42.34 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1115 QGSWQEQLAAPEEGETKIALEREK--DDMETKLLHLEDVVRALEKHVDLRENDRLEFHRLSEEntllknDLGRVRQELEA 1192
Cdd:TIGR00606 232 QLESSREIVKSYENELDPLKNRLKeiEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEK------VFQGTDEQLND 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1193 AESTHDAQRKEIEVLKKDKEKacsEMEVLNRQNQNYKDQLSQLNVRVLQLGQEASTHQAQNEEHRVTIQMLTQSLE---- 1268
Cdd:TIGR00606 306 LYHNHQRTVREKERELVDCQR---ELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLEldgf 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1269 --------------EVVRSGQQ-------------------QSDQIQKLRVELECLNQ----EHQSLQLPWSELTQTLEE 1311
Cdd:TIGR00606 383 ergpfserqiknfhTLVIERQEdeaktaaqlcadlqskerlKQEQADEIRDEKKGLGRtielKKEILEKKQEELKFVIKE 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1312 SQDQVQGAH--LRLRQAQAQHLQEVRLVPQDRVAE--LHRLLSLQGEQAR--RRLDAQREEHEKQLKATEERveeaemil 1385
Cdd:TIGR00606 463 LQQLEGSSDriLELDQELRKAERELSKAEKNSLTEtlKKEVKSLQNEKADldRKLRKLDQEMEQLNHHTTTR-------- 534
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768013504 1386 KNMEMLLQEKVDKLKEQFEKNTK-SDLLLKEL-YVENAhlvRALQATEEKQRGAEKQSRlleEKVRALNKLVSR 1457
Cdd:TIGR00606 535 TQMEMLTKDKMDKDEQIRKIKSRhSDELTSLLgYFPNK---KQLEDWLHSKSKEINQTR---DRLAKLNKELAS 602
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
391-614 |
4.41e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.29 E-value: 4.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 391 QQAALACYHQELSYQQGQVEQLARERDKARQDLERAEKRNLEFVKEMDDCHSTLEQLtEKKIKHLEQgyreRLSLLRSEV 470
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAAL-EAELAELEK----EIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 471 EAERELFWE-----QAHRQRAALEWDVGRLQAEEAGLREKLTLALKENSRLQ-KEIVEVVEKLSDSERLALKLQKDLEfV 544
Cdd:COG4942 100 EAQKEELAEllralYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQaEELRADLAELAALRAELEAERAELE-A 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768013504 545 LKDKLEPQSAELLAQEERFAAVL-------KEYELKCRDLQDRNDELQAELEGLWARL-PKNRHSPSWSPDGRRRQLP 614
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLarlekelAELAAELAELQQEAEELEALIARLEAEAaAAAERTPAAGFAALKGKLP 256
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
406-713 |
4.54e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 41.64 E-value: 4.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 406 QGQVEQLARERDKARQDLERAEK--RNLEFVKEMddCHSTLEQLTEKKIKhLEQGYRERLSLLRSEVEAERelfweqahr 483
Cdd:pfam15921 443 QGQMERQMAAIQGKNESLEKVSSltAQLESTKEM--LRKVVEELTAKKMT-LESSERTVSDLTASLQEKER--------- 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 484 qraALEwdvgRLQAEEAGLREKLTLALKENSRLQKEIVEVVEKLSDSERLALKL-QKDLEF-VLKDKLEPQSaELLAQEE 561
Cdd:pfam15921 511 ---AIE----ATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMaEKDKVIeILRQQIENMT-QLVGQHG 582
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 562 RFA-AVLKEYELKCRDLQDRNDELQaELEGLwarlpKNRHspswspDGRRRQLPG-----------LGPAGISFLGNSAP 629
Cdd:pfam15921 583 RTAgAMQVEKAQLEKEINDRRLELQ-EFKIL-----KDKK------DAKIRELEArvsdlelekvkLVNAGSERLRAVKD 650
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 630 VSIETELMMEQVKEHYQDLrtqletkvNYYEREIAALKRNFEKERKDMEQARRREVSVLEGQKADLEELHE--KSQE--- 704
Cdd:pfam15921 651 IKQERDQLLNEVKTSRNEL--------NSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNtlKSMEgsd 722
|
330
....*....|....
gi 768013504 705 -----VIWGLQEQL 713
Cdd:pfam15921 723 ghamkVAMGMQKQI 736
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
495-594 |
4.64e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 39.89 E-value: 4.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 495 LQAEEAGLREKLTLALKENSRLQKEIVEVVEKLSDSERLALKLQKDLEFVLKDK--LEPQSAELLAQEERFAAVLKEYEL 572
Cdd:pfam13851 31 LKEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLENYEKDKqsLKNLKARLKVLEKELKDLKWEHEV 110
|
90 100
....*....|....*....|..
gi 768013504 573 kcrdLQDRNDELQAELEGLWAR 594
Cdd:pfam13851 111 ----LEQRFEKVERERDELYDK 128
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1054-1454 |
4.85e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 4.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1054 QAERLQAIQEERARSWSRGTQE--QASEQQARAEGALEPGCHKHSVEVARRGSlpSHLQLADPQGSWQEQLAAPEEGETK 1131
Cdd:PTZ00121 1279 KADELKKAEEKKKADEAKKAEEkkKADEAKKKAEEAKKADEAKKKAEEAKKKA--DAAKKKAEEAKKAAEAAKAEAEAAA 1356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1132 IALEREKDDMETKLLHLEDVVRALE----KHVDLRENDrlEFHRLSEENtllKNDLGRVRQELEAAESTHDAQRKEIEVL 1207
Cdd:PTZ00121 1357 DEAEAAEEKAEAAEKKKEEAKKKADaakkKAEEKKKAD--EAKKKAEED---KKKADELKKAAAAKKKADEAKKKAEEKK 1431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1208 KKD--KEKACSEMEVLNRQNQNYKDQLSQLNVRVLQLGQEASTHQAQNEEHRvTIQMLTQSLEEVVRSGQQ--QSDQIQK 1283
Cdd:PTZ00121 1432 KADeaKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAK-KADEAKKKAEEAKKKADEakKAAEAKK 1510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1284 LRVELECLNQEHQSLQLPWSELTQTLEESQ--DQVQGAHLRLRQAQAQHLQEVRLVPQDRVAELHRLLSL-------QGE 1354
Cdd:PTZ00121 1511 KADEAKKAEEAKKADEAKKAEEAKKADEAKkaEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALrkaeeakKAE 1590
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1355 QARRRLDAQREEHEKQLKATEERVEEAEMIlKNMEMLLQEKVDKLKEQFEKNT-----KSDLLLKElyvENAHLVRA--- 1426
Cdd:PTZ00121 1591 EARIEEVMKLYEEEKKMKAEEAKKAEEAKI-KAEELKKAEEEKKKVEQLKKKEaeekkKAEELKKA---EEENKIKAaee 1666
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 768013504 1427 -------------LQATEEKQRGAEKQSRLLEEKVRALNKL 1454
Cdd:PTZ00121 1667 akkaeedkkkaeeAKKAEEDEKKAAEALKKEAEEAKKAEEL 1707
|
|
| EFh_PI-PLC |
cd15898 |
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ... |
216-281 |
4.97e-03 |
|
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) isozymes; PI-PLC isozymes are signaling enzymes that hydrolyze the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. This family corresponds to the four EF-hand motifs containing PI-PLC isozymes, including PI-PLC-beta (1-4), -gamma (1-2), -delta (1,3,4), -epsilon (1), -zeta (1), eta (1-2). Lower eukaryotes such as yeast and slime molds contain only delta-type isozymes. In contrast, other types of isoforms present in higher eukaryotes. This family also includes 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase 1 (PLC1) from fungi. Some homologs from plants contain only two atypical EF-hand motifs and they are not included. All PI-PLC isozymes except sperm-specific PI-PLC-zeta share a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C2 domain. PI-PLC-zeta lacks the PH domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. Most of EF-hand motifs found in PI-PLCs consist of a helix-loop-helix structure, but lack residues critical to metal binding. Moreover, the EF-hand region of most of PI-PLCs may have an important regulatory function, but it has yet to be identified. However, PI-PLC-zeta is a key exception. It is responsible for Ca2+ oscillations in fertilized oocytes and exhibits a high sensitivity to Ca2+ mediated through its EF-hand domain. In addition, PI-PLC-eta2 shows a canonical EF-loop directing Ca2+-sensitivity and thus can amplify transient Ca2+ signals. Also it appears that PI-PLC-delta1 can regulate the binding of PH domain to PIP2 in a Ca2+-dependent manner through its functionally important EF-hand domains. PI-PLCs can be activated by a variety of extracellular ligands, such as growth factors, hormones, cytokines and lipids. Their activation has been implicated in tumorigenesis and/or metastasis linked to migration, proliferation, growth, inflammation, angiogenesis and actin cytoskeleton reorganization. PI-PLC-beta isozymes are activated by G-protein coupled receptor (GPCR) through different mechanisms. However, PI-PLC-gamma isozymes are activated by receptor tyrosine kinase (RTK), such as Rho and Ras GTPases. In contrast, PI-PLC-epsilon are activated by both GPCR and RTK. PI-PLC-delta1 and PLC-eta 1 are activated by GPCR-mediated calcium mobilization. The activation mechanism for PI-PLC-zeta remains unclear.
Pssm-ID: 320029 [Multi-domain] Cd Length: 137 Bit Score: 38.80 E-value: 4.97e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768013504 216 QIRGVWEELGVGSSGHLSEQELAVVCQSVGLQgLEKEELEDLFNKLDQDGDGKVSLEEFQLGLFSH 281
Cdd:cd15898 1 WLRRQWIKADKDGDGKLSLKEIKKLLKRLNIR-VSEKELKKLFKEVDTNGDGTLTFDEFEELYKSL 65
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
401-591 |
5.90e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 5.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 401 ELSYQQGQVEQLARERDKARQDLERAEKRNLEFVKEMDDCHSTLEQL------TEKKIKHLEQgYRERLSLLRSEVEAER 474
Cdd:PRK03918 218 ELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELeerieeLKKEIEELEE-KVKELKELKEKAEEYI 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 475 EL--FWEQAHRQRAALEWDVGRLQAEEAGLREKLTLALKENSR---LQKEIVEVVEKLSDSERLALKLQKDLEfvLKDKL 549
Cdd:PRK03918 297 KLseFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERleeLKKKLKELEKRLEELEERHELYEEAKA--KKEEL 374
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 768013504 550 EPQSAELLAQE-ERFAAVLKEYELKCRDLQDRNDELQAELEGL 591
Cdd:PRK03918 375 ERLKKRLTGLTpEKLEKELEELEKAKEEIEEEISKITARIGEL 417
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1117-1389 |
6.24e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 41.10 E-value: 6.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1117 SWQEQLAAPEEGETKIALEREKDDMETKLLH-LEDVVRALEKhvdlrendRLEFHRLSEENTLLKNDLGRVRQELEAAES 1195
Cdd:COG5185 313 SLEEQLAAAEAEQELEESKRETETGIQNLTAeIEQGQESLTE--------NLEAIKEEIENIVGEVELSKSSEELDSFKD 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1196 THDAQRKEIEVLKKDKEKacsemevlnrQNQNYKDQLSQlnvrvlqlgqEASTHQAQNEEHRVTIQMLTQSLEEVVRSGQ 1275
Cdd:COG5185 385 TIESTKESLDEIPQNQRG----------YAQEILATLED----------TLKAADRQIEELQRQIEQATSSNEEVSKLLN 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1276 QQSDQIQKLRVELEclNQEHQSLQLPWSELTQTLEESQDQVQGAHLRLRQAQAQHLQEVRLVPQDRVAELHRLLSLQGEQ 1355
Cdd:COG5185 445 ELISELNKVMREAD--EESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQV 522
|
250 260 270
....*....|....*....|....*....|....
gi 768013504 1356 ARRRLDAQREEHEKQLKATEERVEEAEMILKNME 1389
Cdd:COG5185 523 AESLKDFMRARGYAHILALENLIPASELIQASNA 556
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1119-1299 |
6.92e-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: 41.20 E-value: 6.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1119 QEQLAA--PEEGETKIALEREKDDMETKLLHLEDVVRALEKHVDLRENDRLEFHRLSEENTLLKNDLGRVRQELEAAEST 1196
Cdd:TIGR02168 336 AEELAEleEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDR 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1197 HDAQRKEIEVLKKDKEKAcsemevlnrqnqnykdQLSQLNVRVLQLGQEASTHQAQNEEHRVTIQMLTQSLEEVVRSGQQ 1276
Cdd:TIGR02168 416 RERLQQEIEELLKKLEEA----------------ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDA 479
|
170 180
....*....|....*....|...
gi 768013504 1277 QSDQIQKLRVELECLNQEHQSLQ 1299
Cdd:TIGR02168 480 AERELAQLQARLDSLERLQENLE 502
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1368-1453 |
7.18e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.97 E-value: 7.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1368 EKQLKATEERVEEAEMILKNMEML---LQEKVDKLKEQFEKnTKSDL------LLKELYVENAHLVRALQATEEKQRGAE 1438
Cdd:PRK00409 526 EELERELEQKAEEAEALLKEAEKLkeeLEEKKEKLQEEEDK-LLEEAekeaqqAIKEAKKEADEIIKELRQLQKGGYASV 604
|
90
....*....|....*
gi 768013504 1439 KqSRLLEEKVRALNK 1453
Cdd:PRK00409 605 K-AHELIEARKRLNK 618
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1362-1451 |
7.20e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 40.25 E-value: 7.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1362 AQREEHEKQLKATEERVEEAEMILKNMEMLLQEKVDKLKEQFEKNTKSdlLLKELyvENAHLVRALQATEEKQRGAEKQS 1441
Cdd:cd16269 205 AKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKMEEEREN--LLKEQ--ERALESKLKEQEALLEEGFKEQA 280
|
90
....*....|
gi 768013504 1442 RLLEEKVRAL 1451
Cdd:cd16269 281 ELLQEEIRSL 290
|
|
| EFh_parvalbumins |
cd16253 |
EF-hand, calcium binding motif, found in parvalbumins; Parvalbumins are small, acidic, ... |
216-275 |
7.49e-03 |
|
EF-hand, calcium binding motif, found in parvalbumins; 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: 319996 [Multi-domain] Cd Length: 101 Bit Score: 37.54 E-value: 7.49e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768013504 216 QIRGVWEELGVGSSGHLSEQELAVV--CQSVGLQGLEKEELEDLFNKLDQDGDGKVSLEEFQ 275
Cdd:cd16253 35 DIKKVFNILDQDKSGFIEEEELKLFlkNFSDGARVLSDKETKNFLAAGDSDGDGKIGVDEFK 96
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1055-1461 |
7.62e-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: 40.98 E-value: 7.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1055 AERLQAIQEERARSWSRGTQEQASEQQARAEGALEPGCHKHSVEVARrgslpSHLQLADPQgswqeQLAAPEEGETKIAL 1134
Cdd:pfam12128 275 ASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDR-----SELEALEDQ-----HGAFLDADIETAAA 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1135 EREK-DDMETKLLHLEDVVRALE-KHVDL-RENDRLEFHRLSEENTllknDLGRVRQELEAAESTHDAQRKEIEvlkKDK 1211
Cdd:pfam12128 345 DQEQlPSWQSELENLEERLKALTgKHQDVtAKYNRRRSKIKEQNNR----DIAGIKDKLAKIREARDRQLAVAE---DDL 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1212 EKACSEM-EVLNRQNQNYKDQLSQLNVRVlqlgqeasthqaqnEEHRVTIQMLTQSLEEVVRSGQQQsDQIQKLRVELEC 1290
Cdd:pfam12128 418 QALESELrEQLEAGKLEFNEEEYRLKSRL--------------GELKLRLNQATATPELLLQLENFD-ERIERAREEQEA 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1291 LNQEHQSLQLPWSELTQTLEESQDQVQGAHLRLRQaQAQHLQEVRLVPQDRVAELHRLLSLQG---EQARRRLDAQreeh 1367
Cdd:pfam12128 483 ANAEVERLQSELRQARKRRDQASEALRQASRRLEE-RQSALDELELQLFPQAGTLLHFLRKEApdwEQSIGKVISP---- 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 1368 eKQLKATEERVEEAEMILKNMEMLLQEKVDKlkEQFEKNTKSDLLlKELYVENAHLVRALQATEEKQRGAEKQSRLLEEK 1447
Cdd:pfam12128 558 -ELLHRTDLDPEVWDGSVGGELNLYGVKLDL--KRIDVPEWAASE-EELRERLDKAEEALQSAREKQAAAEEQLVQANGE 633
|
410
....*....|....
gi 768013504 1448 VRALNKLVSRIAPA 1461
Cdd:pfam12128 634 LEKASREETFARTA 647
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
460-594 |
8.07e-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: 39.52 E-value: 8.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 460 RERLSLLRSEVEAERELFwEQAHRQRAALEWDVGRLQAEEAGLREKLTLA--LKENSRLQKEIvevveklsDSERLALKL 537
Cdd:COG1579 37 EDELAALEARLEAAKTEL-EDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnNKEYEALQKEI--------ESLKRRISD 107
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 768013504 538 QKDLEFVLKDKLEPQSAELLAQEERFAAVLKEYELKCRDLQDRNDELQAELEGLWAR 594
Cdd:COG1579 108 LEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
|
| PTZ00184 |
PTZ00184 |
calmodulin; Provisional |
230-274 |
8.78e-03 |
|
calmodulin; Provisional
Pssm-ID: 185504 [Multi-domain] Cd Length: 149 Bit Score: 38.59 E-value: 8.78e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 768013504 230 GHLSEQELAVVCQSVGlQGLEKEELEDLFNKLDQDGDGKVSLEEF 274
Cdd:PTZ00184 99 GFISAAELRHVMTNLG-EKLTDEEVDEMIREADVDGDGQINYEEF 142
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
511-718 |
9.85e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.13 E-value: 9.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 511 KENSRLQKEIVEVVEKLSDSERLALKLQKDLEfvlkdKLEPQSAELLAQEERFAAVLKEYELKCRDLQDRNDELQAELEG 590
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLA-----ALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 591 LWARLpknrhspswSPDGRRRQLPGLGPAGISFLGNSAPVSIETELM-MEQVKEHYQDLRTQLETKVNyyerEIAALKRN 669
Cdd:COG4942 102 QKEEL---------AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQyLKYLAPARREQAEELRADLA----ELAALRAE 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 768013504 670 FEKERKDMEQARRRevsvLEGQKADLEELHEKSQEVIWGLQEQLQDTAR 718
Cdd:COG4942 169 LEAERAELEALLAE----LEEERAALEALKAERQKLLARLEKELAELAA 213
|
|
| EFh_parvalbumin_beta |
cd16255 |
EF-hand, calcium binding motif, found in beta-parvalbumin; Beta-parvalbumin, also termed ... |
187-275 |
9.91e-03 |
|
EF-hand, calcium binding motif, found in beta-parvalbumin; Beta-parvalbumin, also termed Oncomodulin-1 (OM), is a small calcium-binding protein that is expressed in hepatomas, as well as in the blastocyst and the cytotrophoblasts of the placenta. It is also found to be expressed in the cochlear outer hair cells of the organ of Corti and frequently expressed in neoplasms. Mammalian beta-parvalbumin is secreted by activated macrophages and neutrophils. It may function as a tissue-specific Ca2+-dependent regulatory protein, and may also serve as a specialized cytosolic Ca2+ buffer. Beta-parvalbumin acts as a potent growth-promoting signal between the innate immune system and neurons in vivo. It has high and specific affinity for its receptor on retinal ganglion cells (RGC) and functions as the principal mediator of optic nerve regeneration. It exerts its effects in a cyclic adenosine monophosphate (cAMP)-dependent manner and can further elevate intracellular cAMP levels. Moreover, beta-parvalbumin is associated with efferent function and outer hair cell electromotility, and can identify different hair cell types in the mammalian inner ear. Beta-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+. The EF site displays a high-affinity for Ca2+/Mg2+, and the CD site is a low-affinity Ca2+-specific site. In addition, beta-parvalbumin is distinguished from other parvalbumins by its unusually low isoelectric point (pI = 3.1) and sequence eccentricities (e.g., Y57-L58-D59 instead of F57-I58-E59).
Pssm-ID: 319998 [Multi-domain] Cd Length: 101 Bit Score: 37.02 E-value: 9.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768013504 187 AQGQLQTWDSEDFGSPQKSCSPSFDTPEsQIRGVWEELGVGSSGHLSEQELAVVCQ--SVGLQGLEKEELEDLFNKLDQD 264
Cdd:cd16255 7 ALSQCQAADSFNFKKFFATSGLSKKSAD-DVKKVFEIIDQDKSGFIEEEELKLFLQnfSSGARELTDAETKAFLKAGDSD 85
|
90
....*....|.
gi 768013504 265 GDGKVSLEEFQ 275
Cdd:cd16255 86 GDGKIGVEEFQ 96
|
|
| |
