|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1052-1363 |
1.09e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 79.60 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1052 EREKDDMETKLLHLEDVVRALEKHVDLRENDR---LEFHRLSEE-----NTLLKNDLGRVRQELEAAESTHDAQRKEIEV 1123
Cdd:COG1196 178 ERKLEATEENLERLEDILGELERQLEPLERQAekaERYRELKEElkeleAELLLLKLRELEAELEELEAELEELEAELEE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1124 LKKDKEKACSEMEVLNRQNQNYKDQLSQLNVRVLQLGQEASTHQAQNEEHRVTIQMLTQSLEEVVRSGQQQSDQIQKLRV 1203
Cdd:COG1196 258 LEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1204 ELECLNQEHQSLQLPWSELTQTLEESQDQVQGAHLRLRQAQAQHLQEVR--LVPQDRVAELHRLLsLQGEQARRRLDAQR 1281
Cdd:COG1196 338 ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEelLEALRAAAELAAQL-EELEEAEEALLERL 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1282 EEHEKQLKATEERVEEAEMILKNMEMLLQEKVDKLKEQFEKNTKSDLLLKELYVENAHLVRALQATEEKQRGAEKQSRLL 1361
Cdd:COG1196 417 ERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLL 496
|
..
gi 55749678 1362 EE 1363
Cdd:COG1196 497 LE 498
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1052-1376 |
3.40e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 71.63 E-value: 3.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1052 EREKDDMETKLLHLEDVVRALEKHVD-LRENDRL--EFHRLSEE-----NTLLKNDLGRVRQELEAAESTHDAQRKEIEV 1123
Cdd:TIGR02168 178 ERKLERTRENLDRLEDILNELERQLKsLERQAEKaeRYKELKAElreleLALLVLRLEELREELEELQEELKEAEEELEE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1124 LKKDKEKACSEMEVLNRQNQNYKDQLSQLNVRVLQLGQEASTHQAQNEEHRVTIQMLTQSLEEVVRSGQQQSDQIQKLRV 1203
Cdd:TIGR02168 258 LTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1204 ELECLNQEHQSLQLPWSELTQTLEESQDQVQGAHLRLRQAQAQHLQEVRlvpqdRVAELhrllslqgEQARRRLDAQREE 1283
Cdd:TIGR02168 338 ELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS-----KVAQL--------ELQIASLNNEIER 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1284 HEKQLKATEERVEEAEMILKNMEMLLQEKvdKLKEQFEKNTKSDLLLKELYVENAHLVRALQatEEKQRGAEKQSRLLEE 1363
Cdd:TIGR02168 405 LEARLERLEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLEEALE--ELREELEEAEQALDAA 480
|
330
....*....|...
gi 55749678 1364 KvRALNKLVSRIA 1376
Cdd:TIGR02168 481 E-RELAQLQARLD 492
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1051-1377 |
5.59e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 70.86 E-value: 5.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1051 LEREKDDMETKLLHLEDVVRALEKHVdlrENDRLEFHRLSEENTLLKNDLGRVRQELEAAESTHDAQRKEIEVLKKDKEK 1130
Cdd:TIGR02168 717 LRKELEELSRQISALRKDLARLEAEV---EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ 793
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1131 ACSEMEVLNRQNQNYKDQLSQLNVRVLQLGQEASTHQAQNEEHRVTIQMLTQSLEevvrsgqQQSDQIQKLRVELEclnq 1210
Cdd:TIGR02168 794 LKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIE-------ELSEDIESLAAEIE---- 862
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1211 ehqslqlpwsELTQTLEESQDQVQgAHLRLRQAQAQHLQEVRLVPQDRVAELHRLlslqgEQARRRLDAQREEHEKQLKA 1290
Cdd:TIGR02168 863 ----------ELEELIEELESELE-ALLNERASLEEALALLRSELEELSEELREL-----ESKRSELRRELEELREKLAQ 926
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1291 TEERVEEAEMilknmemllqeKVDKLKEQFekntksdlllkelyveNAHLVRALQATEEKQRGAEKQSRLLEEKVRALNK 1370
Cdd:TIGR02168 927 LELRLEGLEV-----------RIDNLQERL----------------SEEYSLTLEEAEALENKIEDDEEEARRRLKRLEN 979
|
....*..
gi 55749678 1371 LVSRIAP 1377
Cdd:TIGR02168 980 KIKELGP 986
|
|
| EF-hand_7 |
pfam13499 |
EF-hand domain pair; |
198-259 |
4.70e-11 |
|
EF-hand domain pair;
Pssm-ID: 463900 [Multi-domain] Cd Length: 67 Bit Score: 59.57 E-value: 4.70e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 55749678 198 ESQIRGVWEELGVGSSGHLSEQELAVVCQSVGLQG-LEKEELEDLFNKLDQDGDGKVSLEEFQ 259
Cdd:pfam13499 1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEpLSDEEVEELFKEFDLDKDGRISFEEFL 63
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
984-1376 |
3.00e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 61.90 E-value: 3.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 984 RSWSRGTQEQASEQQARAEGALEPGCHkhsveVARRGSLPSHLQLADP-QGSWQEQLAAPEegetkiALEREKDDMETKL 1062
Cdd:PRK04863 293 RELYTSRRQLAAEQYRLVEMARELAEL-----NEAESDLEQDYQAASDhLNLVQTALRQQE------KIERYQADLEELE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1063 LHLEDVVRALEKHVDLRENDRLEFHRLSEENTLLKNDLGRVRQELEAAESTHDAQRKEIEVLkkDKEKACSEMEVLNRQN 1142
Cdd:PRK04863 362 ERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQAL--ERAKQLCGLPDLTADN 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1143 -----QNYKDQLSQLNVRVLQLGQEASTHQAQNEEHRVTIQMLTQSLEEVVRSGQQQSdQIQKLR--VELECLNQEHQSL 1215
Cdd:PRK04863 440 aedwlEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRSEAWDV-ARELLRrlREQRHLAEQLQQL 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1216 QLPWSELTQTLEESQDQVQgahlRLRQAQAQHLQEVrlvpqDRVAELHRLLSLQGEQ------ARRRLDAQREEHEKQLK 1289
Cdd:PRK04863 519 RMRLSELEQRLRQQQRAER----LLAEFCKRLGKNL-----DDEDELEQLQEELEARleslseSVSEARERRMALRQQLE 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1290 ATEERVEEAEmILKNMEMLLQEKVDKLKEQFEKNtksdlllkelyVENAHLVRAL-QATEEKQRGAEKQSRLLEEKVRAL 1368
Cdd:PRK04863 590 QLQARIQRLA-ARAPAWLAAQDALARLREQSGEE-----------FEDSQDVTEYmQQLLERERELTVERDELAARKQAL 657
|
....*...
gi 55749678 1369 NKLVSRIA 1376
Cdd:PRK04863 658 DEEIERLS 665
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1085-1368 |
4.39e-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: 4.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1085 EFHRLSEENTLLKNDLGRVRQELEAAESTHDAQRKEIEVLKKDKEKACSEMEVLNRQNQ-------NYKDQLSQLNVRVL 1157
Cdd:TIGR02169 689 ELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSsleqeieNVKSELKELEARIE 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1158 QLgqEASTHQAQNEEHRVTIQMLTQSLEEVVRSGQQQSDQIQKLRVELECLNQEHQSLQLPWSELTQTLEESQDQVQGAH 1237
Cdd:TIGR02169 769 EL--EEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLK 846
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1238 LRLRQ-AQAQHLQEVRLVPQDRVAELHRLLSLQGEQARRRLDAQREEHEKQLKATEERVEEAEMILKNMEMLLQEKVDKL 1316
Cdd:TIGR02169 847 EQIKSiEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKL 926
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 55749678 1317 KEQFEKNTKSDLLLKELYVENAHLVRALQATEEKQRgaekqsrlLEEKVRAL 1368
Cdd:TIGR02169 927 EALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQR--------VEEEIRAL 970
|
|
| EFh |
cd00051 |
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ... |
212-259 |
7.06e-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: 53.32 E-value: 7.06e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 55749678 212 SSGHLSEQELAVVCQSVGLqGLEKEELEDLFNKLDQDGDGKVSLEEFQ 259
Cdd:cd00051 13 GDGTISADELKAALKSLGE-GLSEEEIDEMIREVDKDGDGKIDFEEFL 59
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
393-701 |
1.02e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.08 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 393 VEQLARERDKARQDLERAEKRNLEFVKEMDDCHSTLEQLTEKKIKHLEqgYRERLSLLRSEVEAERELFWEQAHRQRAAL 472
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAER--YQALLKEKREYEGYELLKEKEALERQKEAI 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 473 EWDVGRLQAEEAGLREKLtlalkenSRLQKEIVEVVEKLSDSERLALKLQKDLEFVLKDKLEpqsaELLAQEERFAAVLK 552
Cdd:TIGR02169 243 ERQLASLEEELEKLTEEI-------SELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIG----ELEAEIASLERSIA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 553 EYELKCRDLQDRNDELQAELEGLWARLPKNRHSPSwSPDGRRRQLpglgpagISFLGNSAPVSIETELMMEQVKEHYQDL 632
Cdd:TIGR02169 312 EKERELEDAEERLAKLEAEIDKLLAEIEELEREIE-EERKRRDKL-------TEEYAELKEELEDLRAELEEVDKEFAET 383
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 55749678 633 R---TQLETKVNYYEREIAALKRNF-----EKERKDMEQAR-RREVSVLEGQKADLEELHEKSQEVIWGLQEQLQDTA 701
Cdd:TIGR02169 384 RdelKDYREKLEKLKREINELKRELdrlqeELQRLSEELADlNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLA 461
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
362-698 |
1.67e-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: 59.30 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 362 ALDNELMTVDSAVQQAALACYHQELSYQQGQVEQLARERDKARQDLERAEKRNLEFVKEMDDCHSTLEQLTEK--KIKHL 439
Cdd:TIGR02168 224 ELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEisRLEQQ 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 440 EQGYRERL-SLLRSEVEAERELfwEQAHRQRAALEWDVGRLQAEEAGLREKLTLALKENSRLQKEIVEVVEKLSDSERLA 518
Cdd:TIGR02168 304 KQILRERLaNLERQLEELEAQL--EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 519 LKLQKDLefvlkdklepqsAELLAQEERFAAVLKEYELKCRDLQDRNDELQAELEGLWARLPKNRHSPSwspdgrRRQLP 598
Cdd:TIGR02168 382 ETLRSKV------------AQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKEL------QAELE 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 599 glgpagisflgnsapvsiETELMMEQVKEHYQDLRTQLETKvnyyEREIAALKRNFEKERKDMEQARRRevsvLEGQKAD 678
Cdd:TIGR02168 444 ------------------ELEEELEELQEELERLEEALEEL----REELEEAEQALDAAERELAQLQAR----LDSLERL 497
|
330 340
....*....|....*....|
gi 55749678 679 LEELHEKSQEVIWGLQEQLQ 698
Cdd:TIGR02168 498 QENLEGFSEGVKALLKNQSG 517
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1033-1319 |
2.01e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 59.31 E-value: 2.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1033 GSWQEQLAAPEEGETKIA-LEREKDDMETKLLHLEDVVRALEKhvdLRENDRLEFHRLSEENTL-LKNDLGRVRQELEAA 1110
Cdd:TIGR02169 230 KEKEALERQKEAIERQLAsLEEELEKLTEEISELEKRLEEIEQ---LLEELNKKIKDLGEEEQLrVKEKIGELEAEIASL 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1111 ESTHDAQRKEIEVLKKDKEKACSEMEVLNRQNQNYKDQLSQLNVRVLQLGQEASTHQAQNEEhrvtiqmLTQSLEEVVRS 1190
Cdd:TIGR02169 307 ERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELED-------LRAELEEVDKE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1191 GQQQSDQIQKLRVELECLNQEHQSLQLPWSELTQTLEESQDQVQGAHLRLRQAQAQH--LQEVRLVPQDRVAELhrllsl 1268
Cdd:TIGR02169 380 FAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKIneLEEEKEDKALEIKKQ------ 453
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 55749678 1269 qgEQARRRLDAQREEHEKQLKATEERVEEAEMILKNmemlLQEKVDKLKEQ 1319
Cdd:TIGR02169 454 --EWKLEQLAADLSKYEQELYDLKEEYDRVEKELSK----LQRELAEAEAQ 498
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1061-1366 |
2.68e-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: 58.60 E-value: 2.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1061 KLLHLEDVVRALEKHVDLRENDRLEFHRLSEENTLLKNDLGRvRQELEAAESTHDAQRKEIEVLKKDKEKACSEmevlnR 1140
Cdd:pfam17380 273 QLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVER-RRKLEEAEKARQAEMDRQAAIYAEQERMAME-----R 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1141 QNQNYKDQLSQLNVRVLQLGQEASTHQAQNEEHRVTIQMLTQSLEEVVRsgqQQSDQIQKLRVELEclnQEHQSLQLPWS 1220
Cdd:pfam17380 347 ERELERIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVR---QELEAARKVKILEE---ERQRKIQQQKV 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1221 ELTQTLEESQDQVQGAHLRLRQAQAQHLQEVRLVPQDRVAELHRLLSLQGEQARRRLDAQREEHEKQLKATEER-VEEAE 1299
Cdd:pfam17380 421 EMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRkILEKE 500
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 55749678 1300 MILKNMEMLLQEKVDKLKEQFEKNTKSDLLLKELYVENAHLVRALQATEEKQRGAEKQSRLLEEKVR 1366
Cdd:pfam17380 501 LEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSR 567
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1043-1283 |
7.48e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.25 E-value: 7.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1043 EEGETKIALEREKDDMETKLLHLEDVVRALEKHVDLRENDRLEFH-----------RLSEENTLLKNDLGRVRQELEAAE 1111
Cdd:COG1196 250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLaelarleqdiaRLEERRRELEERLEELEEELAELE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1112 STHDAQRKEIEVLKKDKEKACSEMEVLNRQNQNYKDQLSQLNVRVLQLGQEASTHQAQNEEHRVTIQMLTQSLEEVVRSG 1191
Cdd:COG1196 330 EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1192 QQQSDQIQKLRVELECLNQEHQSLQLPWSELTQTLEESQDQVQGAHLRLRQAQAQHLQEVRLVPQDRVAELHRLLSLQGE 1271
Cdd:COG1196 410 EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
|
250
....*....|..
gi 55749678 1272 QARRRLDAQREE 1283
Cdd:COG1196 490 AARLLLLLEAEA 501
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
363-575 |
1.60e-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: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 363 LDNELMTVDSAVQQAALACYHQELSYQQGQVEQLARERDKARQDLERAEKRNLEFVKEMDDCHSTLEQLTEKKIKHLEQg 442
Cdd:COG1196 225 LEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD- 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 443 yRERLSLLRSEVEAERelfwEQAHRQRAALEWDVGRLQAEEAGLREKLTLALKENSRLQKEIVEVVEKLSDSERLALKLQ 522
Cdd:COG1196 304 -IARLEERRRELEERL----EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 55749678 523 KDLEFVLKDKLEPQSAELLAQEErfaavLKEYELKCRDLQDRNDELQAELEGL 575
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQ-----LEELEEAEEALLERLERLEEELEEL 426
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
341-575 |
1.85e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.83 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 341 EILQSLDFSVDEKVNLLELTW-ALDNELMTVDS--AVQQAALACYHQELSYQQGQVEQLARERDKARQDLERAEKRNLEF 417
Cdd:TIGR02168 270 EELRLEVSELEEEIEELQKELyALANEISRLEQqkQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEEL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 418 VKEMDDChstLEQLTEKKIKhleqgyRERLSLLRSEVEAErelfWEQAHRQRAALEWDVGRLQAEEAGLREKLTLALKEN 497
Cdd:TIGR02168 350 KEELESL---EAELEELEAE------LEELESRLEELEEQ----LETLRSKVAQLELQIASLNNEIERLEARLERLEDRR 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 55749678 498 SRLQKEIVEVVEKLSDSERLALKLQKDLEFVLKDKLEPQSAELLAQEERFAAVLKEYELKCRDLQDRNDELQAELEGL 575
Cdd:TIGR02168 417 ERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSL 494
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
392-1110 |
3.21e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.94 E-value: 3.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 392 QVEQLARERDKAR--QDL--ERAEKRNLEFVKEMDDCHSTLEQLTEKKIKHLEQgyRERLSLLRSEVEAERElfweQAHR 467
Cdd:COG1196 201 QLEPLERQAEKAEryRELkeELKELEAELLLLKLRELEAELEELEAELEELEAE--LEELEAELAELEAELE----ELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 468 QRAALEWDVGRLQAEEAGLREKLtlalkenSRLQKEIVEVVEKLSDSERLALKLQKDLEfvlkdklepqsaELLAQEERF 547
Cdd:COG1196 275 ELEELELELEEAQAEEYELLAEL-------ARLEQDIARLEERRRELEERLEELEEELA------------ELEEELEEL 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 548 AAVLKEYELKCRDLQDRNDELQAELEGLWARLPKnrhspswspdgrrrqlpglgpagisflgnsapVSIETELMMEQVKE 627
Cdd:COG1196 336 EEELEELEEELEEAEEELEEAEAELAEAEEALLE--------------------------------AEAELAEAEEELEE 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 628 HYQDLRTQLETKVNyYEREIAALKRNFEKERKDMEQARRREVSVLEGQKADLEELHEKSQEviwgLQEQLQDTARgpepe 707
Cdd:COG1196 384 LAEELLEALRAAAE-LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA----LEEAAEEEAE----- 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 708 qmglapccTQALCGLALRHHSHLQQIRREAEAELSGELSGLGALPARRDLTLELEEPPQGPLprGSQRSEQLELERALKL 787
Cdd:COG1196 454 --------LEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFL--EGVKAALLLAGLRGLA 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 788 QPCASEKRAQMCVSLALEEEELELARGKRVDGPSLEAEMQALPKDglvagsGQEGTRGLLPLRPGCGERPLAWLAPGDGR 867
Cdd:COG1196 524 GAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKA------AKAGRATFLPLDKIRARAALAAALARGAI 597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 868 ESEEAAGAGPRRRQAQDTEATQSPAPAPAPASHGPSERWSRMQPCGVDGDIVPKEPEpfGASAAGLEQPGARELPLLGTE 947
Cdd:COG1196 598 GAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGE--GGSAGGSLTGGSRRELLAALL 675
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 948 RDASQTQprmwepplrpAASCRGQAERLQAIQEERARSWSRGTQEQASEQQARAEGALEpgchKHSVEVARRGSLPSHLQ 1027
Cdd:COG1196 676 EAEAELE----------ELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEE----ALEEQLEAEREELLEEL 741
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1028 LADPQGSWQEQLAAPEEGETKIALEREKDDMETKLLHLEDV-VRALEKHVDLREndRLEFhrLSEEntllKNDLGRVRQE 1106
Cdd:COG1196 742 LEEEELLEEEALEELPEPPDLEELERELERLEREIEALGPVnLLAIEEYEELEE--RYDF--LSEQ----REDLEEARET 813
|
....
gi 55749678 1107 LEAA 1110
Cdd:COG1196 814 LEEA 817
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1058-1375 |
3.57e-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: 55.03 E-value: 3.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1058 METKLLHLEDVVRALEKHVDLrENDRL------------EFHRLSEENTLLKNDLGRVRQELEAAESTHDAQRK------ 1119
Cdd:TIGR04523 216 LESQISELKKQNNQLKDNIEK-KQQEInektteisntqtQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKqlnqlk 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1120 -EIEVLKKDKEKACS------------EMEVLNRQNQNYKDQLSQLNVRVLQLGQEASTHQAQNEEHRVTIQMLTQSLEE 1186
Cdd:TIGR04523 295 sEISDLNNQKEQDWNkelkselknqekKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEK 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1187 VVRSGQQQSDQIQKLRVELECLNQEHQSLQlpwsELTQTLEESQDQVQGAHLRLRQaQAQHLQEVRLVPQDRVAELHRLL 1266
Cdd:TIGR04523 375 LKKENQSYKQEIKNLESQINDLESKIQNQE----KLNQQKDEQIKKLQQEKELLEK-EIERLKETIIKNNSEIKDLTNQD 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1267 SlQGEQARRRLDAQREEHEKQLKATEERVEEAEMILKNMEMLLQEKVDKLKEQFEKNTKSDLLLKELyvenahlvralqa 1346
Cdd:TIGR04523 450 S-VKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDL------------- 515
|
330 340
....*....|....*....|....*....
gi 55749678 1347 teekqrgaEKQSRLLEEKVRALNKLVSRI 1375
Cdd:TIGR04523 516 --------TKKISSLKEKIEKLESEKKEK 536
|
|
| EF-hand_8 |
pfam13833 |
EF-hand domain pair; |
212-258 |
5.11e-07 |
|
EF-hand domain pair;
Pssm-ID: 404678 [Multi-domain] Cd Length: 54 Bit Score: 47.69 E-value: 5.11e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 55749678 212 SSGHLSEQELAVVCQSVGLQGLEKEELEDLFNKLDQDGDGKVSLEEF 258
Cdd:pfam13833 1 EKGVITREELKRALALLGLKDLSEDEVDILFREFDTDGDGYISFDEF 47
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
384-597 |
5.91e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.17 E-value: 5.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 384 QELSYQQGQVEQLARERDKARQDLERAEKRNLEFVKEMDDCHSTLEQLTEK---KIKHLEQGYRERLSLLRSEVEAEREl 460
Cdd:COG1196 302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEleeAEAELAEAEEALLEAEAELAEAEEE- 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 461 fWEQAHRQRAALEWDVGRLQAEEAGLREKLTLALKENSRLQKEIVEVVEKLSDSERLALKLQKDLEFVLKDKLEpQSAEL 540
Cdd:COG1196 381 -LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE-LEEEE 458
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 55749678 541 LAQEERFAAVLKEYELKCRDLQDRNDELQAELEGLWARLPKNRHSPSWSPDGRRRQL 597
Cdd:COG1196 459 EALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALL 515
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1096-1375 |
8.88e-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: 53.49 E-value: 8.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1096 LKNDLGRVRQELEAAESTHDAQRKEIEvlkkdkEKAcSEMEVLNRQNQNYKDQLSQLNVRVLQLGQEASTHQAQNEEHRV 1175
Cdd:TIGR04523 340 LNEQISQLKKELTNSESENSEKQRELE------EKQ-NEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDE 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1176 TIQMLTQSLEEVVRSGQQQSDQIQKLRVELECLNQEHQSLQLPWSELTQTLEESQDQVQGAHLRLRQAQaQHLQEVRLVP 1255
Cdd:TIGR04523 413 QIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIK-QNLEQKQKEL 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1256 QDRVAELHRLLS-----------LQGEQAR-----RRLDAQREEHEKQLKATEERVEEAEMILKNMEML-----LQEKVD 1314
Cdd:TIGR04523 492 KSKEKELKKLNEekkeleekvkdLTKKISSlkekiEKLESEKKEKESKISDLEDELNKDDFELKKENLEkeideKNKEIE 571
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 55749678 1315 KLKEQFE----KNTKSDLLLKELYVENAHLVRALQATEEKQRGAEKQSRLLEEKVRALNKLVSRI 1375
Cdd:TIGR04523 572 ELKQTQKslkkKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNI 636
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1096-1325 |
1.54e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.07 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1096 LKNDLGRVRQELEAAESTHDAQRKEIEVLKKDKEKACSEMEVLNRQNQNYKDQLSQLNVRVLQLGQEASTHQAQNEEHR- 1174
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKe 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1175 ------VTIQMLTQSLEEVVRSGQQQSDQIQKLRVELECLNQEHQslqlpwsELTQTLEESQDQVQgahlRLRQAQAQHL 1248
Cdd:COG4942 105 elaellRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARR-------EQAEELRADLAELA----ALRAELEAER 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 55749678 1249 QEVRLVPQDRVAELHRLLSLQGEQAR--RRLDAQREEHEKQLKATEERVEEaemilknmemlLQEKVDKLKEQFEKNTK 1325
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKllARLEKELAELAAELAELQQEAEE-----------LEALIARLEAEAAAAAE 241
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1083-1346 |
2.49e-06 |
|
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: 52.05 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1083 RLEFHRLSEENTLLKNDLG--RVRQELEAAESTHDAQ-----------RKEIEVLKK---DKEKACSEMEVLNRQNQNYK 1146
Cdd:pfam05557 6 ESKARLSQLQNEKKQMELEhkRARIELEKKASALKRQldresdrnqelQKRIRLLEKreaEAEEALREQAELNRLKKKYL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1147 DQLSQLnvrvlqlgqeASTHQAQNEEHRVTIQMLTQSLEEVVRSGQQQSDQIQKLRVELECLNQEHQSLQLPWSELTQ-- 1224
Cdd:pfam05557 86 EALNKK----------LNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQlr 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1225 -TLEESQDQVQGAHLRLR------QAQAQHLQEVRlvpqDRVAELHRLLSLQGEQARRRldaqreEHEKQLKATEERVEe 1297
Cdd:pfam05557 156 qNLEKQQSSLAEAEQRIKelefeiQSQEQDSEIVK----NSKSELARIPELEKELERLR------EHNKHLNENIENKL- 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 55749678 1298 aemilknmemLLQEKVDKLKEQFEKNTKSDLLLKELYVENAHLVRALQA 1346
Cdd:pfam05557 225 ----------LLKEEVEDLKRKLEREEKYREEAATLELEKEKLEQELQS 263
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
366-690 |
3.20e-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: 51.98 E-value: 3.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 366 ELMTVDSAVQQAALACYHQELSYQQGQVEQLARERDKARQ-------DLERAEKRNLEFVKEMDDCHSTLEQLTEKKIKH 438
Cdd:TIGR02168 687 EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRqisalrkDLARLEAEVEQLEERIAQLSKELTELEAEIEEL 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 439 LEQGYRERLSLLRSEVE-AERELFWEQAHRQRAALEWDVGRLQAEEAGLREK---------------------LTLALKE 496
Cdd:TIGR02168 767 EERLEEAEEELAEAEAEiEELEAQIEQLKEELKALREALDELRAELTLLNEEaanlrerleslerriaaterrLEDLEEQ 846
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 497 NSRLQKEIVEVVEKLSDSERLALKLQKDLEFVL--KDKLEPQSAELLAQEERFAAVLKEYELKCRDLQDRNDELQAELEG 574
Cdd:TIGR02168 847 IEELSEDIESLAAEIEELEELIEELESELEALLneRASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQ 926
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 575 LWARLPKNRhspswspdGRRRQLpglgpagisflgnSAPVSIETELMMEQVKEHYQDL---RTQLETKVNYYEREIAALK 651
Cdd:TIGR02168 927 LELRLEGLE--------VRIDNL-------------QERLSEEYSLTLEEAEALENKIeddEEEARRRLKRLENKIKELG 985
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 55749678 652 R-NFEKERKDMEQARRREvsVLEGQKADLEELHEKSQEVI 690
Cdd:TIGR02168 986 PvNLAAIEEYEELKERYD--FLTAQKEDLTEAKETLEEAI 1023
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1082-1334 |
4.18e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 51.17 E-value: 4.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1082 DRLEFHRLSEENTLLKNDLGRVRQELeaaeSTHDAQRKEIEvlkkdkEKACSEMEVLNRQNQNYKDQLSQLNVRVLQLGQ 1161
Cdd:PHA02562 158 DLLDISVLSEMDKLNKDKIRELNQQI----QTLDMKIDHIQ------QQIKTYNKNIEEQRKKNGENIARKQNKYDELVE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1162 EASTHQAQNEEhrvtiqmLTQSLEEVVRSGQQQSDQIQKLRVELECLNQEHQSLQlpwSEL------------TQTLEES 1229
Cdd:PHA02562 228 EAKTIKAEIEE-------LTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQ---KVIkmyekggvcptcTQQISEG 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1230 QDQVQGAHLRLRQAQAQHLQEvrlvpQDRVAELHRLLSLQGEQARRRLDAQRE-EHEKQLKATEerVEEAEMILKNMEML 1308
Cdd:PHA02562 298 PDRITKIKDKLKELQHSLEKL-----DTAIDELEEIMDEFNEQSKKLLELKNKiSTNKQSLITL--VDKAKKVKAAIEEL 370
|
250 260 270
....*....|....*....|....*....|....
gi 55749678 1309 LQEKVD------KLKEQFEK--NTKSDlLLKELY 1334
Cdd:PHA02562 371 QAEFVDnaeelaKLQDELDKivKTKSE-LVKEKY 403
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1104-1298 |
5.20e-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: 50.53 E-value: 5.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1104 RQELEAAESTHDAQRKEIEVLKKDKEKACSEME-------VLNRQNQNYKDQLSQLNVRVLQLGQEASTHQAQNEEHR-- 1174
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAalerriaALARRIRALEQELAALEAELAELEKEIAELRAELEAQKee 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1175 -----VTIQML-----------TQSLEEVVRSG-------QQQSDQIQKLRVELECLNQEHQSLQlpwsELTQTLEESQD 1231
Cdd:COG4942 106 laellRALYRLgrqpplalllsPEDFLDAVRRLqylkylaPARREQAEELRADLAELAALRAELE----AERAELEALLA 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 55749678 1232 QVQGAHLRLRQAQAQHLQEVRLVPQDRVAELHRLLSLQgeQARRRLDAQREEHEKQLKATEERVEEA 1298
Cdd:COG4942 182 ELEEERAALEALKAERQKLLARLEKELAELAAELAELQ--QEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
392-713 |
5.91e-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: 5.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 392 QVEQLARERDKA-RQDLERAEKRNLEFVKEMDDCHSTLEQL--TEKKIKHLEQ---GYRERLSLLRSEVEAERELFWEQA 465
Cdd:TIGR02169 199 QLERLRREREKAeRYQALLKEKREYEGYELLKEKEALERQKeaIERQLASLEEeleKLTEEISELEKRLEEIEQLLEELN 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 466 HRQRA-------ALEWDVGRLQAEEAGLREKLTLALKENSRLQKEIVEVVEKLSDSERLALKLQKDLE--FVLKDKLEPQ 536
Cdd:TIGR02169 279 KKIKDlgeeeqlRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEeeRKRRDKLTEE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 537 SAELLAQEERFAAVLKEYELKCRDLQDRNDELQAELEGLwarlpKNRHSPSWSPDGRRRQLPGLGPAGISFLGNSAPVSI 616
Cdd:TIGR02169 359 YAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKL-----KREINELKRELDRLQEELQRLSEELADLNAAIAGIE 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 617 ETELMMEQVKEHYQDlrtqletkvnyyerEIAALKRNFEKERKDMEQARRREVSVLEGQKADLEELHEKSQEViwglqEQ 696
Cdd:TIGR02169 434 AKINELEEEKEDKAL--------------EIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQREL-----AE 494
|
330
....*....|....*..
gi 55749678 697 LQDTARGPEPEQMGLAP 713
Cdd:TIGR02169 495 AEAQARASEERVRGGRA 511
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
392-579 |
8.85e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 8.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 392 QVEQLARERDKARQDLERAEKRnlefVKEMDDCHSTLEQLtekkikhleqgyreRLSLLRSEVEAERELFWEQAHRQRAA 471
Cdd:COG4913 611 KLAALEAELAELEEELAEAEER----LEALEAELDALQER--------------REALQRLAEYSWDEIDVASAEREIAE 672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 472 LE----------WDVGRLQAEEAGLREKLTLALKENSRLQKEIVEVVEKLSDSERLALKLQKDLEFVLKDKLEPQSAELl 541
Cdd:COG4913 673 LEaelerldassDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALL- 751
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 55749678 542 aqEERFAAVLKE--YELKCRDLQDRNDELQAELEGLWARL 579
Cdd:COG4913 752 --EERFAAALGDavERELRENLEERIDALRARLNRAEEEL 789
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1116-1375 |
1.06e-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: 50.06 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1116 AQRKEIEVLKKDKEKACSEMEVLNRQNQNYKDQLSQLNvrvlqlgQEASTHQAQNEEHRVTIQMLTQSLEEVVRSGQQQS 1195
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELE-------EELEQLRKELEELSRQISALRKDLARLEAEVEQLE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1196 DQIQKLRVELECLNQEHQslqlpwsELTQTLEESQD--QVQGAHLRLRQAQAQHLQEVRLVPQDRVAELHRLLSLQGE-- 1271
Cdd:TIGR02168 747 ERIAQLSKELTELEAEIE-------ELEERLEEAEEelAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEea 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1272 -QARRRLDAQREEHEKQLKATEERVEEAEMILKNMEML------LQEKVDKLKEQFEKNTKsdlLLKELYVENAHLVRAL 1344
Cdd:TIGR02168 820 aNLRERLESLERRIAATERRLEDLEEQIEELSEDIESLaaeieeLEELIEELESELEALLN---ERASLEEALALLRSEL 896
|
250 260 270
....*....|....*....|....*....|.
gi 55749678 1345 QATEEKQRGAEKQSRLLEEKVRALNKLVSRI 1375
Cdd:TIGR02168 897 EELSEELRELESKRSELRRELEELREKLAQL 927
|
|
| FRQ1 |
COG5126 |
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
212-258 |
1.10e-05 |
|
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 46.32 E-value: 1.10e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 55749678 212 SSGHLSEQELAVVCQSVGLqglEKEELEDLFNKLDQDGDGKVSLEEF 258
Cdd:COG5126 82 GDGKISADEFRRLLTALGV---SEEEADELFARLDTDGDGKISFEEF 125
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1147-1381 |
1.48e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.99 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1147 DQLSQLNVRVLQLGQEASTHQAQNEEHRVTIQMLTQSLEEVVRSGQQQSDQIQKLRVELECLNQEHQSLQLPWSELTQTL 1226
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1227 EESQDQVqGAHLRLRQAQAQHLQEVRLVPQDRVAELHRLLSLQGEQARRRLDaQREEHEKQLKATEERVEEAEMILKNME 1306
Cdd:COG4942 100 EAQKEEL-AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARRE-QAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 55749678 1307 MLLQEKVDKLKEQFEKNTKSDLLLKELYVENAHLVRALQATEEKQRGAEKQSRLLEEKVRALNKLVSRIAPAALS 1381
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| FRQ1 |
COG5126 |
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
202-262 |
1.57e-05 |
|
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 45.94 E-value: 1.57e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 55749678 202 RGVWEELGVGSSGHLSEQELAVVCQSVGLQGLEkEELEDLFNKLDQDGDGKVSLEEFQLGL 262
Cdd:COG5126 36 ATLFSEADTDGDGRISREEFVAGMESLFEATVE-PFARAAFDLLDTDGDGKISADEFRRLL 95
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1037-1366 |
2.27e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 49.30 E-value: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1037 EQLAAPEEGETKIALEREK-DDMETKLLHLEDVVRALEKHVDLRENDR---LEFHRLSE-----ENTLLKNDLGRVRQEL 1107
Cdd:TIGR02169 160 DEIAGVAEFDRKKEKALEElEEVEENIERLDLIIDEKRQQLERLRRERekaERYQALLKekreyEGYELLKEKEALERQK 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1108 EAAESTHDAQRKEIEVLKKDKEKACSEMEVLNRqnqnykdQLSQLNVRVLQLGQ-EASTHQAQNEEHRVTIQMLTQSLEE 1186
Cdd:TIGR02169 240 EAIERQLASLEEELEKLTEEISELEKRLEEIEQ-------LLEELNKKIKDLGEeEQLRVKEKIGELEAEIASLERSIAE 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1187 VVRSGQQQSDQIQKLRVELECLNQEHQ--------------SLQLPWSELTQTLEESQDQVQ---GAHLRLRQAQAQHLQ 1249
Cdd:TIGR02169 313 KERELEDAEERLAKLEAEIDKLLAEIEelereieeerkrrdKLTEEYAELKEELEDLRAELEevdKEFAETRDELKDYRE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1250 EVRLVpQDRVAELHRLLSLQGEQArRRLDAQREEHEKQLKATEERVEEAEMILKNMEMLLQEKVDKLKEQFEKNTKSDLL 1329
Cdd:TIGR02169 393 KLEKL-KREINELKRELDRLQEEL-QRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQE 470
|
330 340 350
....*....|....*....|....*....|....*..
gi 55749678 1330 LKELYVENAHLVRALQATEEKQRGAEKQSRLLEEKVR 1366
Cdd:TIGR02169 471 LYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVR 507
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1099-1371 |
2.64e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 48.90 E-value: 2.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1099 DLGRVRQELEAAESTHDAQRKEI-EVLK----------------KDKEKACSEMEVLNRQNQNYKDQLSQ---------- 1151
Cdd:PRK10929 24 DEKQITQELEQAKAAKTPAQAEIvEALQsalnwleerkgsleraKQYQQVIDNFPKLSAELRQQLNNERDeprsvppnms 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1152 ---LNVRVLQLGQE--ASTHQAQNEEHRvtIQMLTQSLEEVvrsGQQQSDqIQKLrvelecLNQEHQSLQLPWSELTqTL 1226
Cdd:PRK10929 104 tdaLEQEILQVSSQllEKSRQAQQEQDR--AREISDSLSQL---PQQQTE-ARRQ------LNEIERRLQTLGTPNT-PL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1227 EESQDQVQGAHLRLRQAQAQHLQEVRLVPQDRvAELHRLLSLQGEQARRRLDAQREEHEKQLKAteERVEEAEMILKNME 1306
Cdd:PRK10929 171 AQAQLTALQAESAALKALVDELELAQLSANNR-QELARLRSELAKKRSQQLDAYLQALRNQLNS--QRQREAERALESTE 247
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 55749678 1307 MLLQEKVD---KLKEQFEKNtksdlllKELYVENAHLVRALQATEEKQRGAEKQSrlleEKVR-ALNKL 1371
Cdd:PRK10929 248 LLAEQSGDlpkSIVAQFKIN-------RELSQALNQQAQRMDLIASQQRQAASQT----LQVRqALNTL 305
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
376-786 |
2.86e-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: 2.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 376 QAALACYHQELSYQQGQVEQLARERDKARQDLERAEKRNLEFVKEMDDCHSTLEQLTEKKIKHLEqgyrERLSLLRSEVE 455
Cdd:COG1196 357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE----ELEELEEALAE 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 456 AERELfwEQAHRQRAALEWDVGRLQAEEAGLREKLTLALKENSRLQKEIVEVVEKLSDSERLALKLQK-------DLEFV 528
Cdd:COG1196 433 LEEEE--EEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEaeadyegFLEGV 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 529 LKDKLEPQS-------AELLAQEERFAAVLKEYEL-KCRDLQDRNDELQAELEGLWARLPKNRHS--PSWSPDGRRRQLP 598
Cdd:COG1196 511 KAALLLAGLrglagavAVLIGVEAAYEAALEAALAaALQNIVVEDDEVAAAAIEYLKAAKAGRATflPLDKIRARAALAA 590
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 599 GLGPAGISFLGNSAPVSIETELMMEQVKEHYQDLRTQLETKVNYYEREIAALKRNFEKERKDMEQARRREVSVLEGQKAD 678
Cdd:COG1196 591 ALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRREL 670
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 679 LEELHEKSQEVIwGLQEQLQDTARGPEPEQMGLAPCCTQALCGLALRHHSHLQQIRREAEAELSGELSGLGALPARRDLT 758
Cdd:COG1196 671 LAALLEAEAELE-ELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLE 749
|
410 420
....*....|....*....|....*...
gi 55749678 759 LELEEPPQGPLPRGSQRSEQLELERALK 786
Cdd:COG1196 750 EEALEELPEPPDLEELERELERLEREIE 777
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
401-1320 |
3.44e-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: 48.51 E-value: 3.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 401 DKARQDLERAEkrnlEFVKEMDDCHSTLEQLTEKKIKHLEqgYRERLSLLRSEVEAERelfWEQAHRQRAALEWDVGRLQ 480
Cdd:TIGR02168 182 ERTRENLDRLE----DILNELERQLKSLERQAEKAERYKE--LKAELRELELALLVLR---LEELREELEELQEELKEAE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 481 AEEAglrekltlalkensRLQKEIVEVVEKLSDSERLALKLQKDLEFV---------LKDKLEPQSAELLAQEERFAAVL 551
Cdd:TIGR02168 253 EELE--------------ELTAELQELEEKLEELRLEVSELEEEIEELqkelyalanEISRLEQQKQILRERLANLERQL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 552 KEYELKCRDLQDRNDELQAELEGLWARLpknrhspswspdgrrrqlpglgpagisflgnsAPVSIETELMMEQVKEHYQD 631
Cdd:TIGR02168 319 EELEAQLEELESKLDELAEELAELEEKL--------------------------------EELKEELESLEAELEELEAE 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 632 LRtQLETKVNYYEREIAALKRNFEKERKDMEQArRREVSVLEGQKADLEELHEKSQEVIWGLQEQLQDTARGPEPEQMGL 711
Cdd:TIGR02168 367 LE-ELESRLEELEEQLETLRSKVAQLELQIASL-NNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEE 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 712 ApccTQALCGLALRHHSH------LQQIRREAEAELSGELSGLGALPARRDLTLELEEPPQGP----------------- 768
Cdd:TIGR02168 445 L---EEELEELQEELERLeealeeLREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFsegvkallknqsglsgi 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 769 LPRGSQRSE-QLELERALKLqpcASEKRAQMCVSLALEEEEL------ELARGKRVDGPSLEAEMQALPKDGLVAGSGQE 841
Cdd:TIGR02168 522 LGVLSELISvDEGYEAAIEA---ALGGRLQAVVVENLNAAKKaiaflkQNELGRVTFLPLDSIKGTEIQGNDREILKNIE 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 842 GTRGLLPLRPGCGERPLAWLAP--GDGRESEEAAGAGPRRRQaqdteatqspapapapasHGPSERWsrmqpCGVDGDIV 919
Cdd:TIGR02168 599 GFLGVAKDLVKFDPKLRKALSYllGGVLVVDDLDNALELAKK------------------LRPGYRI-----VTLDGDLV 655
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 920 PKEpepfGASAAGleqPGARELPLLGTER---DASQTQPRMwepplrpAASCRGQAERLQAIQEERARSWSRGTQEQASE 996
Cdd:TIGR02168 656 RPG----GVITGG---SAKTNSSILERRReieELEEKIEEL-------EEKIAELEKALAELRKELEELEEELEQLRKEL 721
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 997 QQARAE-GALEPGCHKHSVEVARRGSLPSHLQLADPQGSWQEQLAAPEEGETKIALEREKDDMETkllhLEDVVRALEkh 1075
Cdd:TIGR02168 722 EELSRQiSALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEE----LEAQIEQLK-- 795
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1076 vDLRENDRLEFHRLSEENTLLKNDLGRVRQELEAAESTHDAQRKEIEVLKKDKEKACSEMEVLNRQNQNYKDQLSQLNVR 1155
Cdd:TIGR02168 796 -EELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESE 874
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1156 VLQLGQEASTHQAQNEEHRVTIQMLTQSLEEVvrsgqqqSDQIQKLRVELECLNQEHQSLQLPWSELTQTLEESQDQVQG 1235
Cdd:TIGR02168 875 LEALLNERASLEEALALLRSELEELSEELREL-------ESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSE 947
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1236 AHLRLRQAQAQHLQEVRLVP---QDRVAELHRLLS------------LQGEQARRR-LDAQREEHEKQLKATEERVEEae 1299
Cdd:TIGR02168 948 EYSLTLEEAEALENKIEDDEeeaRRRLKRLENKIKelgpvnlaaieeYEELKERYDfLTAQKEDLTEAKETLEEAIEE-- 1025
|
970 980
....*....|....*....|.
gi 55749678 1300 mILKNMEMLLQEKVDKLKEQF 1320
Cdd:TIGR02168 1026 -IDREARERFKDTFDQVNENF 1045
|
|
| EFh_parvalbumin_like |
cd16251 |
EF-hand, calcium binding motif, found in parvalbumin-like EF-hand family; The family includes ... |
198-259 |
4.09e-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: 4.09e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 55749678 198 ESQIRGVWEELGVGSSGHLSEQELAVVCQSVGLQG--LEKEELEDLFNKLDQDGDGKVSLEEFQ 259
Cdd:cd16251 33 EDQIKKVFQILDKDKSGFIEEEELKYILKGFSIAGrdLTDEETKALLAAGDTDGDGKIGVEEFA 96
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
962-1336 |
4.27e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.21 E-value: 4.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 962 LRPAASCRGQAERLQAIQEE--RARSWSRGTQE--QASEQQARAEGALEPGCHKHSVEVARRGSLPShlQLADPQGSWQE 1037
Cdd:PTZ00121 1410 LKKAAAAKKKADEAKKKAEEkkKADEAKKKAEEakKADEAKKKAEEAKKAEEAKKKAEEAKKADEAK--KKAEEAKKADE 1487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1038 QLAAPEEGETKIALEREKDDMETKLLHLE--------DVVRALEKHVDLRENDRLEFHRLSEE----NTLLKNDLGRVRQ 1105
Cdd:PTZ00121 1488 AKKKAEEAKKKADEAKKAAEAKKKADEAKkaeeakkaDEAKKAEEAKKADEAKKAEEKKKADElkkaEELKKAEEKKKAE 1567
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1106 ELEAAESTHDAQRKEIEVLKKDKEKACSEMEVLNRQNQNYKDQlsqlNVRVLQLGQEASTHQAQNEEHRVTIQMLTQSLE 1185
Cdd:PTZ00121 1568 EAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE----EAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEA 1643
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1186 EVVRSGQQQSDQIQKLRVELECLNQEHQSLQLPWSELTQtlEESQDQVQGAHLRLRQAQAQHLQEVRLVPQDRVAELHRL 1265
Cdd:PTZ00121 1644 EEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKK--AEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEEL 1721
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 55749678 1266 LSLQGEQARRRLDAQREEHEKQLKATEERVEEAEmilknmemllQEKVDKLKEQFEKNTKSDLLLKELYVE 1336
Cdd:PTZ00121 1722 KKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE----------KKKIAHLKKEEEKKAEEIRKEKEAVIE 1782
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
340-579 |
4.55e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.01 E-value: 4.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 340 REILQSLDFSVDEKVNLLEltwALDNELMTVDSAVQQAALACYHQELSYQ--QGQVEQLARERDKARQDLERAEKRNLEF 417
Cdd:COG1196 238 EAELEELEAELEELEAELE---ELEAELAELEAELEELRLELEELELELEeaQAEEYELLAELARLEQDIARLEERRREL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 418 VKEMDDCHSTLEQLTEKKIKHLEQ--GYRERLSLLRSEVEAERELFWEQAHRQRAALEwDVGRLQAEEAGLREKLTLALK 495
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEEleELEEELEEAEEELEEAEAELAEAEEALLEAEA-ELAEAEEELEELAEELLEALR 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 496 ENSRLQKEIVEVVEKLSDSERLALKLQKDLEFVLKD--KLEPQSAELLAQEERFAAVLKEYELKCRDLQDRNDELQAELE 573
Cdd:COG1196 394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEAlaELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
....*.
gi 55749678 574 GLWARL 579
Cdd:COG1196 474 LLEAAL 479
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1097-1371 |
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 55749678 1097 KNDLGRVRQELEAAESTHDAQRKEIEVLKKDKEKAcsemevlnrqnQNYKDQLSQL-NVRVLQLGQEASTHQAQNEEHRV 1175
Cdd:TIGR02169 176 LEELEEVEENIERLDLIIDEKRQQLERLRREREKA-----------ERYQALLKEKrEYEGYELLKEKEALERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1176 TIQMLTQSLEEVVRSGQQQSDQIQKLRVELECLN--------QEHQSLQLPWSELTQTLEESQDQVQGAHLRLRQAQAQH 1247
Cdd:TIGR02169 245 QLASLEEELEKLTEEISELEKRLEEIEQLLEELNkkikdlgeEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERL 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1248 lqevrlvpQDRVAELHRLLSlQGEQARRRLDAQReeheKQLKATEERVEEAEMILKNMEMLLQEKVDKLKEQFEK----N 1323
Cdd:TIGR02169 325 --------AKLEAEIDKLLA-EIEELEREIEEER----KRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDElkdyR 391
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 55749678 1324 TKSDLLLKELYVENAHLVRALqatEEKQRGAEKQSRLLEEKVRALNKL 1371
Cdd:TIGR02169 392 EKLEKLKREINELKRELDRLQ---EELQRLSEELADLNAAIAGIEAKI 436
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
965-1373 |
7.48e-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: 47.42 E-value: 7.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 965 AASCRGQAERLQaiqeerarswsrgTQEQASEQQARAEGALEPgCHKHSVEvARRGSLPSHLQLA-----DPQGSWQEQL 1039
Cdd:pfam15921 287 ASSARSQANSIQ-------------SQLEIIQEQARNQNSMYM-RQLSDLE-STVSQLRSELREAkrmyeDKIEELEKQL 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1040 AAPEEGETKIALEREKDDMETKllHLEDVVRALEKHVDLREND----RLEFHRLSEENTLLKNDLGRVRQELEaaESTHD 1115
Cdd:pfam15921 352 VLANSELTEARTERDQFSQESG--NLDDQLQKLLADLHKREKElsleKEQNKRLWDRDTGNSITIDHLRRELD--DRNME 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1116 AQRKEiEVLKKDKEKACSEMEVLNRQNQNYKDQLSQLNVRVLQLG----------QEASTHQAQNEEHRVTIQMLTQSLE 1185
Cdd:pfam15921 428 VQRLE-ALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLEstkemlrkvvEELTAKKMTLESSERTVSDLTASLQ 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1186 EVVRSGQQQSDQIQKLRVELECLNQEHQSLqlpwseltqtleesqdQVQGAHLRLRQAQAQHLQeVRLVPQDRVAELHR- 1264
Cdd:pfam15921 507 EKERAIEATNAEITKLRSRVDLKLQELQHL----------------KNEGDHLRNVQTECEALK-LQMAEKDKVIEILRq 569
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1265 ----LLSLQGEQARRRLDAQREEHEKQLKATEERVEeaemiLKNMEMLLQEKVDKLKEQFEKntKSDLLLKELYVENAHL 1340
Cdd:pfam15921 570 qienMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLE-----LQEFKILKDKKDAKIRELEAR--VSDLELEKVKLVNAGS 642
|
410 420 430
....*....|....*....|....*....|...
gi 55749678 1341 VRALQATEEKQrgaeKQSRLLEEKVRALNKLVS 1373
Cdd:pfam15921 643 ERLRAVKDIKQ----ERDQLLNEVKTSRNELNS 671
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
971-1373 |
8.38e-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: 47.14 E-value: 8.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 971 QAERLQAIQEERARSWSRGTQEQASEQQARAEGALEPGchKHSVEVARRGSLPSHL---QLADPQGSWQEQLAAPEEGET 1047
Cdd:pfam12128 600 EELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKA--SREETFARTALKNARLdlrRLFDEKQSEKDKKNKALAERK 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1048 KIALEREKD-DMETKLLHLEDVVRALEKHVDLRENDRLEFHRLSEENTLLKNDLGRVRQELEAAESTHDAQRKEIEvlkk 1126
Cdd:pfam12128 678 DSANERLNSlEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALE---- 753
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1127 dkekacsemevlnrqnQNYKDQLSQLNV---RVLQLGQEasthqaqneehrvtIQMLTQSLEEVVRSGQQQSDQIQKLRv 1203
Cdd:pfam12128 754 ----------------TWYKRDLASLGVdpdVIAKLKRE--------------IRTLERKIERIAVRRQEVLRYFDWYQ- 802
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1204 elECLNQEHQSLQLPWSELTQTLEESQDQV--QGAHLRLRQAQAQHLQEVRLVPQDRVAELHRLL-SLQGEQARRRLDAQ 1280
Cdd:pfam12128 803 --ETWLQRRPRLATQLSNIERAISELQQQLarLIADTKLRRAKLEMERKASEKQQVRLSENLRGLrCEMSKLATLKEDAN 880
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1281 REEHEKQLKATEERVEEAEMILKNMEMLLQEKVDKLKEQFEKNTKSDL------LLKELYVENAHLVRALQATEEKQRGA 1354
Cdd:pfam12128 881 SEQAQGSIGERLAQLEDLKLKRDYLSESVKKYVEHFKNVIADHSGSGLaetwesLREEDHYQNDKGIRLLDYRKLVPYLE 960
|
410
....*....|....*....
gi 55749678 1355 EKQSRLLEEKVRALNKLVS 1373
Cdd:pfam12128 961 QWFDVRVPQSIMVLREQVS 979
|
|
| EF-hand_5 |
pfam13202 |
EF hand; |
238-259 |
8.63e-05 |
|
EF hand;
Pssm-ID: 433035 [Multi-domain] Cd Length: 25 Bit Score: 40.77 E-value: 8.63e-05
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1114-1379 |
1.18e-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: 46.60 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1114 HDAQRKEIEVLKKDKEKACS---EMEVLNRQNQNYKDQLSQLNVRVLQLGQEASTHQAQNEEHRVTIQMLTQSLEEVVRS 1190
Cdd:TIGR02169 659 SRAPRGGILFSRSEPAELQRlreRLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKER 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1191 GQQQSDQIQKLRVELECLNQEHQSLQLPWSELTQTLEESQDQVQGAHLRLRQAQAQHLQ-EVRLVPQDRVAELHRLLSLQ 1269
Cdd:TIGR02169 739 LEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQaELSKLEEEVSRIEARLREIE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1270 GEQARRRLDAQREEHEKQ-LKATEERVEEAEMILKNMEMLLQEKVDKLKEQFEKNTKSdllLKELYVENAHLVRALQATE 1348
Cdd:TIGR02169 819 QKLNRLTLEKEYLEKEIQeLQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAA---LRDLESRLGDLKKERDELE 895
|
250 260 270
....*....|....*....|....*....|.
gi 55749678 1349 EKQRGAEKQSRLLEEKVRALNKLVSRIAPAA 1379
Cdd:TIGR02169 896 AQLRELERKIEELEAQIEKKRKRLSELKAKL 926
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
971-1368 |
1.23e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.85 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 971 QAERLQAIQEERARSWSRGTQEQASEQQARAEGALEpgchKHSVEVARRGSLPSHLQLADPQGSWQEQLAApEEGETKIA 1050
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ----LEELEEAEEALLERLERLEEELEELEEALAE-LEEEEEEE 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1051 LEREKDDMETKLLHLEDVVRALEKHVDLRENDRLEFHRLSEENTLLKNDLGRVRQELEAAESTHDAQRKEIEVLKKDKEK 1130
Cdd:COG1196 441 EEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLR 520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1131 ACSEMEVLNRQNQNYKDQ---------LSQLNVRVLQLGQEASTHQAQNEEHRVTIQMLTQSLEEVVRSGQQQSDQIQKL 1201
Cdd:COG1196 521 GLAGAVAVLIGVEAAYEAaleaalaaaLQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAA 600
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1202 RVELECLNQEHQSLQLP-----------------WSELTQTLEESQDQVQGAHLRLRQAQAQHLQEVRlvpqdRVAELHR 1264
Cdd:COG1196 601 VDLVASDLREADARYYVlgdtllgrtlvaarleaALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRR-----ELLAALL 675
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1265 LLSLQGEQARRRLDAQREEHEKQLKATEERVEEAEMILKNMEMLLQEKVDKLKEQFEKNTKSDLLLKELYVENAHLVRAL 1344
Cdd:COG1196 676 EAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEE 755
|
410 420
....*....|....*....|....
gi 55749678 1345 QATEEKQRGAEKQSRLLEEKVRAL 1368
Cdd:COG1196 756 LPEPPDLEELERELERLEREIEAL 779
|
|
| EF-hand_1 |
pfam00036 |
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ... |
237-262 |
1.39e-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: 1.39e-04
10 20
....*....|....*....|....*.
gi 55749678 237 ELEDLFNKLDQDGDGKVSLEEFQLGL 262
Cdd:pfam00036 1 ELKEIFRLFDKDGDGKIDFEEFKELL 26
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1182-1382 |
1.74e-04 |
|
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: 46.20 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1182 QSLEEVVRSGQQQSDQIQKLRVELECLNQEHQSLQLPWSELTQTLEESQDQVQGAHLRLRQAQAQHLQEvrlvpQDRVAE 1261
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL-----EERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1262 LHRLLSLQGEQaRRRLDAQREEHEKQLKATEERVEEaemilknmemlLQEKVDKLKEQFEKNTKS-DLLLKELYVENAHL 1340
Cdd:TIGR02168 752 LSKELTELEAE-IEELEERLEEAEEELAEAEAEIEE-----------LEAQIEQLKEELKALREAlDELRAELTLLNEEA 819
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 55749678 1341 VRALQATEEKQRGAEKQSRLLEEKVRALNKLVSRIAPAALSV 1382
Cdd:TIGR02168 820 ANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEI 861
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
376-516 |
1.99e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 376 QAALACYHQELSYQQGQVEQLARERDKARQDLERAEKRNLEF-VKEMDDCHSTLEQLTEKK--IKHLEQGYRERLSLLRS 452
Cdd:COG4913 294 EAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELeeRERRRARLEALLAALGL 373
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 55749678 453 EVEAERELFWEQAHRQRAALEwdvgRLQAEEAGLREKLTLALKENSRLQKEIVEVVEKLSDSER 516
Cdd:COG4913 374 PLPASAEEFAALRAEAAALLE----ALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| EFh |
smart00054 |
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ... |
237-258 |
2.25e-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: 2.25e-04
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
976-1379 |
2.33e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 45.71 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 976 QAIQEERARswsRGTQEQ-ASEQQARAEGALEPGCHKhsvevARRGSLPSHLQLA-DPQGSWQEQLAAPEegetkiALER 1053
Cdd:COG3096 286 RALELRREL---FGARRQlAEEQYRLVEMARELEELS-----ARESDLEQDYQAAsDHLNLVQTALRQQE------KIER 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1054 EKDDMETKLLHLEDVVRALEKHVDLRENDRLEFHRLSEENTLLKNDLGRVRQELEAAESTHDAQRKEIEVLkkDKEKACS 1133
Cdd:COG3096 352 YQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQAVQAL--EKARALC 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1134 EMEVLNRQN-----QNYKDQLSQLNVRVLQLGQEASTHQAQNEEHRVTIQMLTQSLEEVVRS--GQQQSDQIQKLRvELE 1206
Cdd:COG3096 430 GLPDLTPENaedylAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIAGEVERSqaWQTARELLRRYR-SQQ 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1207 CLNQEHQSLQLPWSELTQtLEESQDQVQgahlRLRQAQAQHLQEVRlvpqDRVAELHRLLSlqgeqarrRLDAQREEHEK 1286
Cdd:COG3096 509 ALAQRLQQLRAQLAELEQ-RLRQQQNAE----RLLEEFCQRIGQQL----DAAEELEELLA--------ELEAQLEELEE 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1287 QLKATEERVEEAEMILKNMEMLLQEKVDKLKEQFEKNTKSDLLLKEL--YVENAHLV-RALQATEEKQRGAEKQSRLLEE 1363
Cdd:COG3096 572 QAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSgeALADSQEVtAAMQQLLEREREATVERDELAA 651
|
410
....*....|....*.
gi 55749678 1364 KVRALNKLVSRIAPAA 1379
Cdd:COG3096 652 RKQALESQIERLSQPG 667
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1050-1216 |
2.44e-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: 2.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1050 ALEREKDDMETKLLHLEDVVRALEKHVDLREN---------------DRLEFHRLSEENTLLKNDLGRVRQELEAAESTH 1114
Cdd:COG4913 239 RAHEALEDAREQIELLEPIRELAERYAAARERlaeleylraalrlwfAQRRLELLEAELEELRAELARLEAELERLEARL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1115 DAQRKEIEVLK--------KDKEKACSEMEVLNRQNQNYKDQLSQLNVRVLQLGQEASTHQAQNEEHRVTIQMLTQSLEE 1186
Cdd:COG4913 319 DALREELDELEaqirgnggDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEE 398
|
170 180 190
....*....|....*....|....*....|....
gi 55749678 1187 VVRSGQQQ----SDQIQKLRVELECLNQEHQSLQ 1216
Cdd:COG4913 399 ELEALEEAlaeaEAALRDLRRELRELEAEIASLE 432
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
969-1324 |
2.51e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 45.50 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 969 RGQAERLQAIQEERARSWSRGTQEQASEQQARAegalepgchkhsvEVARRGSLPSHlqladpqgswQEQLAAPEEGE-T 1047
Cdd:pfam17380 295 KMEQERLRQEKEEKAREVERRRKLEEAEKARQA-------------EMDRQAAIYAE----------QERMAMERERElE 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1048 KIALEREKDDMETklLHLEDVVRALEKhvdLRENDRLEFHRLSeentllKNDlgRVRQELEAAesthdaqrKEIEVLKKD 1127
Cdd:pfam17380 352 RIRQEERKRELER--IRQEEIAMEISR---MRELERLQMERQQ------KNE--RVRQELEAA--------RKVKILEEE 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1128 KEKACSEMEVLNRQNQNYKDQLSQLNVRVLQLGQEASTHQAQNEEHRVTIQM-LTQSLEEVVRSGQQQSDQIQKLRVELE 1206
Cdd:pfam17380 411 RQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVeRLRQQEEERKRKKLELEKEKRDRKRAE 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1207 CLNQEHQSLQLPWSELTQTLEESQDQVQGAHLRLRQAQAQHLQEVRLVPQDRvaelhrllslqgeQARRRLDAQREEHEK 1286
Cdd:pfam17380 491 EQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEER-------------RKQQEMEERRRIQEQ 557
|
330 340 350
....*....|....*....|....*....|....*....
gi 55749678 1287 QLKATEERvEEAEMILKNMEMLLQ-EKVDKLKEQFEKNT 1324
Cdd:pfam17380 558 MRKATEER-SRLEAMEREREMMRQiVESEKARAEYEATT 595
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
969-1364 |
2.61e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 2.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 969 RGQAERLQAIQEERARSwsRGTQEQASEQQARAEGALEPGCHKHSVEVARRGSlpSHLQLADPQGSWQEQLAAPEEGETK 1048
Cdd:PTZ00121 1377 KKKADAAKKKAEEKKKA--DEAKKKAEEDKKKADELKKAAAAKKKADEAKKKA--EEKKKADEAKKKAEEAKKADEAKKK 1452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1049 IALEREKDDMETKLLHLEDVVRALEKHVDLRENDrlEFHRLSEENTLLKNDLGRVRQELEAAESTHDAQ-RKEIEVLKKD 1127
Cdd:PTZ00121 1453 AEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKAD--EAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEeAKKADEAKKA 1530
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1128 KEKACSEmEVLNRQNQNYKDQLSQLNvRVLQLGQEASTHQAQNEEHRVtiQMLTQSLEEVVRSGQQQSDQIQKLRVELEC 1207
Cdd:PTZ00121 1531 EEAKKAD-EAKKAEEKKKADELKKAE-ELKKAEEKKKAEEAKKAEEDK--NMALRKAEEAKKAEEARIEEVMKLYEEEKK 1606
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1208 LNQEhqslQLPWSELTQTLEESQDQVQGAHLRLRQAQAQHLQEVRLVPQDRVAElhRLLSLQGEQARRRLDAQREEHEKQ 1287
Cdd:PTZ00121 1607 MKAE----EAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAE--EENKIKAAEEAKKAEEDKKKAEEA 1680
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 55749678 1288 LKATEERVEEAEMILKNMEMllQEKVDKLKEQF-EKNTKSDLLLKELYVENAHLVRALQATEEKQRGAEKQSRLLEEK 1364
Cdd:PTZ00121 1681 KKAEEDEKKAAEALKKEAEE--AKKAEELKKKEaEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEK 1756
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1105-1379 |
3.13e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.89 E-value: 3.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1105 QELEAAESTHDAQRKEIEVLKKDKEKACSEMEVLNRQNQNYKDQLSQLNVRVLQLGQEASTHQAQNEEHRVTIQMLTQSL 1184
Cdd:COG4372 31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1185 EEVVRSGQQQSDQIQKLRVELECLNQEHQSLQLPWSELTQTLEESQDQVQGAHLRLRQAQAQHLQEVRLVPQDRVAELHR 1264
Cdd:COG4372 111 EELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1265 LLSLQGEQARRRLDAQREEHEKQLKATEERVEEAEMILKNMEMLLQEKVDKLKEQFEKNTKSDLLLKELYVENAHLVRAL 1344
Cdd:COG4372 191 EANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVE 270
|
250 260 270
....*....|....*....|....*....|....*
gi 55749678 1345 QATEEKQRGAEKQSRLLEEKVRALNKLVSRIAPAA 1379
Cdd:COG4372 271 KDTEEEELEIAALELEALEEAALELKLLALLLNLA 305
|
|
| EF-hand_6 |
pfam13405 |
EF-hand domain; |
237-262 |
3.16e-04 |
|
EF-hand domain;
Pssm-ID: 463869 [Multi-domain] Cd Length: 30 Bit Score: 39.08 E-value: 3.16e-04
10 20
....*....|....*....|....*.
gi 55749678 237 ELEDLFNKLDQDGDGKVSLEEFQLGL 262
Cdd:pfam13405 1 ELREAFKLFDKDGDGKISLEELRKAL 26
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
383-575 |
3.42e-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: 45.44 E-value: 3.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 383 HQELSYQQGQVEQLARERDKARQDLERAE------KRNLEFVK-EMDDCHSTLEQLTEKKIKhleqgYRERLSLLRSEVE 455
Cdd:TIGR02169 715 SRKIGEIEKEIEQLEQEEEKLKERLEELEedlsslEQEIENVKsELKELEARIEELEEDLHK-----LEEALNDLEARLS 789
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 456 AERelfWEQAHRQRAALEWDVGRLQAEEAGLREKLTLALKENSRLQKEIVEVVEklsdsERLALKLQKDLEFVLKDKLEP 535
Cdd:TIGR02169 790 HSR---IPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQE-----QRIDLKEQIKSIEKEIENLNG 861
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 55749678 536 QSAELLAQEERFAAVLKEYELKCRDLQDRNDELQAELEGL 575
Cdd:TIGR02169 862 KKEELEEELEELEAALRDLESRLGDLKKERDELEAQLREL 901
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
963-1365 |
4.37e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 44.89 E-value: 4.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 963 RPAASCRGQAERL--QAIQEERARSWSRGTQEQASEQQARAEGALEPGCHKHSVEVARRGSLPS--HLQLADPQGSwQEQ 1038
Cdd:PLN02939 30 RLAVSCRARRRGFssQQKKKRGKNIAPKQRSSNSKLQSNTDENGQLENTSLRTVMELPQKSTSSddDHNRASMQRD-EAI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1039 LAAPEEgetkiALEREKDDMETKLLHLEDVVRALekhvdlrendrlefhRLSEENTLLKNDlGRVR--QELEAAESTHDA 1116
Cdd:PLN02939 109 AAIDNE-----QQTNSKDGEQLSDFQLEDLVGMI---------------QNAEKNILLLNQ-ARLQalEDLEKILTEKEA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1117 QRKEIEVLKKDKEKACSEM----------EVLNRQNQNYKDQLSQLNVR----VLQLGQEASTHQAQNEEHRVTIQMLTQ 1182
Cdd:PLN02939 168 LQGKINILEMRLSETDARIklaaqekihvEILEEQLEKLRNELLIRGATeglcVHSLSKELDVLKEENMLLKDDIQFLKA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1183 SLEEVVRSGQQqsdqiqklrveLECLNQEHQSLQLPWSELTQTLEESQDQVqgahLRLRQAQAQHLQEvrlvpqdRVAEL 1262
Cdd:PLN02939 248 ELIEVAETEER-----------VFKLEKERSLLDASLRELESKFIVAQEDV----SKLSPLQYDCWWE-------KVENL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1263 HRLLSL---QGEQARRRLDaQREEHEKQLKATEERVEEAEMILKNMEM--LLQEKVDKLKEQFEKNTKSDLLLKELYven 1337
Cdd:PLN02939 306 QDLLDRatnQVEKAALVLD-QNQDLRDKVDKLEASLKEANVSKFSSYKveLLQQKLKLLEERLQASDHEIHSYIQLY--- 381
|
410 420
....*....|....*....|....*...
gi 55749678 1338 AHLVRALQATEEKQRgAEKQSRLLEEKV 1365
Cdd:PLN02939 382 QESIKEFQDTLSKLK-EESKKRSLEHPA 408
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1050-1235 |
5.26e-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: 44.67 E-value: 5.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1050 ALEREKDDMETKLLHLE-DVVRALEKHVDLR---ENDRLEFHRLSEENTLLKNDLGRVRQELEAAESTHDAQRKEIEVLK 1125
Cdd:TIGR02169 312 EKERELEDAEERLAKLEaEIDKLLAEIEELEreiEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYR 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1126 KDKEKACSEMEVLNRQNQNYKDQLSQLNVRVLQLGQEASTHQAQ-------NEEHRVTIQMLTQSLEEVVRSGQQQSDQI 1198
Cdd:TIGR02169 392 EKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKineleeeKEDKALEIKKQEWKLEQLAADLSKYEQEL 471
|
170 180 190
....*....|....*....|....*....|....*..
gi 55749678 1199 QKLRVELECLNQEHQSLQLPWSELTQTLEESQDQVQG 1235
Cdd:TIGR02169 472 YDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRG 508
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1115-1298 |
5.73e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 5.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1115 DAQRKeIEVLKKDKEKACSEMEVLNRQNQNYKDQLSQLNVR--VLQLGQEASTHQAQNEEHRVTIQMLTQSLEEVVRSgq 1192
Cdd:COG4913 607 DNRAK-LAALEAELAELEEELAEAEERLEALEAELDALQERreALQRLAEYSWDEIDVASAEREIAELEAELERLDAS-- 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1193 qqSDQIQKLRVELECLNQEHQSLQLPWSELTQTLEESQDQVQGAHLRLRQAQAQHLQEVRLVPQDRVAEL-HRLLSLQGE 1271
Cdd:COG4913 684 --SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLeERFAAALGD 761
|
170 180 190
....*....|....*....|....*....|.
gi 55749678 1272 ----QARRRLDAQREEHEKQLKATEERVEEA 1298
Cdd:COG4913 762 averELRENLEERIDALRARLNRAEEELERA 792
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1078-1311 |
8.59e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.85 E-value: 8.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1078 LRENDRLEFHRLSEENTLLKNDLGRVRQELEAAEsthdaqrKEIEVLKKDkekacSEMEVLNRQNQNYKDQLSQLNVRVL 1157
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAE-------AALEEFRQK-----NGLVDLSEEAKLLLQQLSELESQLA 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1158 QLGQEASTHQAQNEEHRVTIQMLTQSLEEVvrsgqQQSDQIQKLRVELECLNQEhqslqlpWSELTQTLEESQDQVQGAH 1237
Cdd:COG3206 230 EARAELAEAEARLAALRAQLGSGPDALPEL-----LQSPVIQQLRAQLAELEAE-------LAELSARYTPNHPDVIALR 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1238 LRLRQAQAQHLQEVRLVPQDRVAELhRLLSLQGEQARRRLDAQRE------EHEKQLKATEERVEEAEMILKNMEMLLQE 1311
Cdd:COG3206 298 AQIAALRAQLQQEAQRILASLEAEL-EALQAREASLQAQLAQLEArlaelpELEAELRRLEREVEVARELYESLLQRLEE 376
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1105-1376 |
9.52e-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: 43.80 E-value: 9.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1105 QELEAAESTHDAQRKEIEVLKKDKEKACSEMEVLNRQNQNYK---DQLSQLNVRVLQLGQEasthqaqNEEHRVTIQMLT 1181
Cdd:TIGR00618 542 TSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKediPNLQNITVRLQDLTEK-------LSEAEDMLACEQ 614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1182 QSLEEvvrsgqQQSDQIQKLRVELEcLNQEHQSLQLPWSELTQTLEE-SQDQVQGAHLRLRQAQAQHLQEVRLVPQdrvA 1260
Cdd:TIGR00618 615 HALLR------KLQPEQDLQDVRLH-LQQCSQELALKLTALHALQLTlTQERVREHALSIRVLPKELLASRQLALQ---K 684
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1261 ELHRLLSLQG--EQARRRLDAQREEHEKQLKATEERVEEAEMI------LKNMEMLLQEKVDKLKEQFekntksDLLLKE 1332
Cdd:TIGR00618 685 MQSEKEQLTYwkEMLAQCQTLLRELETHIEEYDREFNEIENASsslgsdLAAREDALNQSLKELMHQA------RTVLKA 758
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 55749678 1333 LyvENAHLVRALQATEEKQRGAEKQ--SRLLEEKVRALNKLVSRIA 1376
Cdd:TIGR00618 759 R--TEAHFNNNEEVTAALQTGAELShlAAEIQFFNRLREEDTHLLK 802
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1047-1375 |
1.17e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.47 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1047 TKIALErEKDDMETKLLhLEDVVRALEKhvDLRENDRLEFHRLSEentllkndLGRVRQELEAAESTHDAQRKEIEVLKK 1126
Cdd:TIGR04523 106 SKINSE-IKNDKEQKNK-LEVELNKLEK--QKKENKKNIDKFLTE--------IKKKEKELEKLNNKYNDLKKQKEELEN 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1127 DKEKACSEMEVLNRQNQNYKDQLSQLNVRVLQLgqeasthQAQNEEHRvtiqMLTQSLEEVVRSGQQQSDQIQKLRVELE 1206
Cdd:TIGR04523 174 ELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNL-------KKKIQKNK----SLESQISELKKQNNQLKDNIEKKQQEIN 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1207 CLNQEHQSLQLPWSELTQTLEESQDQVQGAHLRLRQAQAQHLQEvrlvpQDRVAELHRLLSLQGEQARRRLDaqrEEHEK 1286
Cdd:TIGR04523 243 EKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKEL-----EKQLNQLKSEISDLNNQKEQDWN---KELKS 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1287 QLKATEERVEEAEMILKNMEmllqEKVDKLKEQFEKNTKSdllLKELYVENAHLVRALqatEEKQRGAEKQSRLLEEKVR 1366
Cdd:TIGR04523 315 ELKNQEKKLEEIQNQISQNN----KIISQLNEQISQLKKE---LTNSESENSEKQREL---EEKQNEIEKLKKENQSYKQ 384
|
....*....
gi 55749678 1367 ALNKLVSRI 1375
Cdd:TIGR04523 385 EIKNLESQI 393
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1077-1376 |
1.19e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 43.67 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1077 DLRENDRLEFHRLSEEntlLKNDLGRVRQELEAAESTHDAQRKEIEVLKKDKEKACSEMEVLNRQNQNYKDQLSQLNVRV 1156
Cdd:pfam12128 586 DLKRIDVPEWAASEEE---LRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEK 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1157 ----LQLGQEASTHQAQNEEHRVTIQ-MLTQSLEEVVRSGQQQSDQIQKLRVELeclnqehqslQLPWSELTQTLEESQD 1231
Cdd:pfam12128 663 qsekDKKNKALAERKDSANERLNSLEaQLKQLDKKHQAWLEEQKEQKREARTEK----------QAYWQVVEGALDAQLA 732
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1232 QVQGAHLRLRQAQAQHLQEVRlvpqdrvAELHRLLSLQG--EQARRRLDAQREEHEKQLKATEERVEEAEMILKNMEMLL 1309
Cdd:pfam12128 733 LLKAAIAARRSGAKAELKALE-------TWYKRDLASLGvdPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETW 805
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 55749678 1310 QEKVDKLKEQFEKNTKSDLLLKELYVENAHLVRALQATEEKQRGA-EKQSRLLEEKVRALNKLVSRIA 1376
Cdd:pfam12128 806 LQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKAsEKQQVRLSENLRGLRCEMSKLA 873
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1036-1370 |
1.30e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1036 QEQLAAPEEGETKIA-LEREKDDMETKLLHLEDVVRALEKHVDLRENDRLEfhrLSEENTLLKNDLGRVRQELEAAESTH 1114
Cdd:PRK02224 240 DEVLEEHEERREELEtLEAEIEDLRETIAETEREREELAEEVRDLRERLEE---LEEERDDLLAEAGLDDADAEAVEARR 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1115 DAQRKEIEVLKKDKEKACSEMEVLNRQNQNYKDQLSQLNVRVLQLGQEASTHQAQNEEHRVTIQMLTQSLEEVVRSGQQQ 1194
Cdd:PRK02224 317 EELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEEL 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1195 SDQIQKLRVELECLNQEHQSLQLPWSELTQTLEESQDQVQGAHLRLRQAQA-----------QHLQEVRLVP-----QDR 1258
Cdd:PRK02224 397 RERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEAlleagkcpecgQPVEGSPHVEtieedRER 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1259 VAELHRLLslqgEQARRRLDAQREEHE--KQLKATEERVEEAEMILKNMEMLLQEKVDKLKEQFEKntksdllLKELYVE 1336
Cdd:PRK02224 477 VEELEAEL----EDLEEEVEEVEERLEraEDLVEAEDRIERLEERREDLEELIAERRETIEEKRER-------AEELRER 545
|
330 340 350
....*....|....*....|....*....|....
gi 55749678 1337 NAHLVRALQATEEKQRGAEKQSRLLEEKVRALNK 1370
Cdd:PRK02224 546 AAELEAEAEEKREAAAEAEEEAEEAREEVAELNS 579
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1089-1375 |
1.38e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.36 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1089 LSEENTLLKNDLgrvRQELEAAESThDAQRKEIEVLKKDKEKACSEMEVLNRQNQNYKDQ-------------LSQLNVR 1155
Cdd:PRK11281 54 LEAEDKLVQQDL---EQTLALLDKI-DRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDndeetretlstlsLRQLESR 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1156 VLQLGQEASTHQ-------------------AQNE--EHRVTIQMLTQSLEEVVRSGQQQS-DQIQKLRVELECLNQ--E 1211
Cdd:PRK11281 130 LAQTLDQLQNAQndlaeynsqlvslqtqperAQAAlyANSQRLQQIRNLLKGGKVGGKALRpSQRVLLQAEQALLNAqnD 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1212 HQSLQLPWSELTQTLEESQDQVQGAHLRLRQAQAQHLQEVRlvpqdrvaelhrllslqgeqarrrldaqreeHEKQLKAT 1291
Cdd:PRK11281 210 LQRKSLEGNTQLQDLLQKQRDYLTARIQRLEHQLQLLQEAI-------------------------------NSKRLTLS 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1292 EERVEEAEmilkNMEMLLQEKVDKL-KEQFEKNTK-SDLLLK-----------ELYVENAhLVRALQATeekqrgaekqs 1358
Cdd:PRK11281 259 EKTVQEAQ----SQDEAARIQANPLvAQELEINLQlSQRLLKateklntltqqNLRVKNW-LDRLTQSE----------- 322
|
330
....*....|....*....
gi 55749678 1359 RLLEEKVRALNK--LVSRI 1375
Cdd:PRK11281 323 RNIKEQISVLKGslLLSRI 341
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1046-1369 |
1.43e-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: 43.11 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1046 ETKIALEREKDDMETKLLHLEDVVRALEKHVDLRENDRLEFHRLSEentLLKNDLGRVRQELEAAESTHDAQRKEIEVLK 1125
Cdd:TIGR00606 688 QTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAP---GRQSIIDLKEKEIPELRNKLQKVNRDIQRLK 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1126 KDKEKACSEMEVLNRQNQNYKDQLSQLNVrvlqlgqeasthqaqneehrvtIQMLTQSLEEVVRSGQQQSDQIQKLRVEL 1205
Cdd:TIGR00606 765 NDIEEQETLLGTIMPEEESAKVCLTDVTI----------------------MERFQMELKDVERKIAQQAAKLQGSDLDR 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1206 EC--LNQEHQSLQLPWSELTQTLEESQDQVQGahlrlRQAQAQHLQEvrlvpqdRVAEL--HRLLSLQGEQARRRLDAQR 1281
Cdd:TIGR00606 823 TVqqVNQEKQEKQHELDTVVSKIELNRKLIQD-----QQEQIQHLKS-------KTNELksEKLQIGTNLQRRQQFEEQL 890
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1282 EEHEKQLK----ATEERVEEAEMILKNMEMLLQEKVDKLKEQFEKNTKSDLLLKELYVENAHLVRALQATEEK-QRGAEK 1356
Cdd:TIGR00606 891 VELSTEVQslirEIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKiQDGKDD 970
|
330
....*....|...
gi 55749678 1357 QSRLLEEKVRALN 1369
Cdd:TIGR00606 971 YLKQKETELNTVN 983
|
|
| XopAW |
NF041410 |
XopAW family type III secretion system calcium-binding effector; |
212-264 |
1.49e-03 |
|
XopAW family type III secretion system calcium-binding effector;
Pssm-ID: 469301 [Multi-domain] Cd Length: 227 Bit Score: 41.59 E-value: 1.49e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 55749678 212 SSGHLSEQELAVVCQS---VGLQGLEKEELEDLFNKLDQDGDGKVSLEEFQLGLFS 264
Cdd:NF041410 76 GDGSLSSDELAAAAPPpppPPDQAPSTELADDLLSALDTDGDGSISSDELSAGLTS 131
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1106-1371 |
1.57e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.21 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1106 ELEAAESTHDAQRKEIEVLKKDKEKacsemevLNRQNQNYKDQLSQLNVRVLQLGQEASTHQAQNEEHRVTIQMLTQSLE 1185
Cdd:COG1340 9 SLEELEEKIEELREEIEELKEKRDE-------LNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1186 EVVRSGQQQSDQIQKLRVELECLNQEHQSL--------QLPWSELTQTL---EESQ--DQVQGAHLRLRQAQAQHLQEVR 1252
Cdd:COG1340 82 ELNEKLNELREELDELRKELAELNKAGGSIdklrkeieRLEWRQQTEVLspeEEKElvEKIKELEKELEKAKKALEKNEK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1253 LvpQDRVAELhRLLSLQGEQARRRLDAQREEHEKQLKATEERVEEAEMILKNMEML------LQEKVDKLKEQFEKntks 1326
Cdd:COG1340 162 L--KELRAEL-KELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELhkeiveAQEKADELHEEIIE---- 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 55749678 1327 dllLKELYVENAHLVRALQATEEKQRGAEKQSRLLEEKVRALNKL 1371
Cdd:COG1340 235 ---LQKELRELRKELKKLRKKQRALKREKEKEELEEKAEEIFEKL 276
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1053-1368 |
2.59e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.47 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1053 REKDDMETKLLHLEDVV-RALEKHVDLRENDRlEFHRLSEENTLLKNDLgRVRQELEA-AESTH---DAQRKEIEVLKKD 1127
Cdd:pfam01576 2 RQEEEMQAKEEELQKVKeRQQKAESELKELEK-KHQQLCEEKNALQEQL-QAETELCAeAEEMRarlAARKQELEEILHE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1128 KEKACSEMEVLNRQNQNYKDQLSQlNVRVL--QLGQEASTHQAQNEEhRVTIQMLTQSLEEVVRSGQQQSDQIQKlrvel 1205
Cdd:pfam01576 80 LESRLEEEEERSQQLQNEKKKMQQ-HIQDLeeQLDEEEAARQKLQLE-KVTTEAKIKKLEEDILLLEDQNSKLSK----- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1206 eclnqEHQSLQLPWSELTQTLEESQDQVQG-AHLRLRQAQAQHLQEVRLVPQDRvaelhrlLSLQGEQARRRLDAQREEH 1284
Cdd:pfam01576 153 -----ERKLLEERISEFTSNLAEEEEKAKSlSKLKNKHEAMISDLEERLKKEEK-------GRQELEKAKRKLEGESTDL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1285 EKQLKATEERVEEAEMILKNMEMLLQEKVDKLKEQFEKNTKSDLLLKELYVENAHLVRALQATEEKQRGAEKQSRLLEEK 1364
Cdd:pfam01576 221 QEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEE 300
|
....
gi 55749678 1365 VRAL 1368
Cdd:pfam01576 301 LEAL 304
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1043-1370 |
2.73e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1043 EEGETKIALEREKDDMETKLLHLEDVVRALEKHVDLRENDRLEFHRLSEENTLLKNDLGRVRQELEAAESTHDAQRKEIE 1122
Cdd:PRK03918 197 EKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1123 VLK------KDKEKACSEMEVLNRQNQNYKDQLSQLNVRVLQLGQEASTHQAQ---NEEHRVTIQMLTQSLEEVVR---- 1189
Cdd:PRK03918 277 ELEekvkelKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERikeLEEKEERLEELKKKLKELEKrlee 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1190 ---------SGQQQSDQIQKLRVELECLNQEH------------QSLQLPWSELTQ---TLEESQDQVQGAHLRLRQAQA 1245
Cdd:PRK03918 357 leerhelyeEAKAKKEELERLKKRLTGLTPEKlekeleelekakEEIEEEISKITArigELKKEIKELKKAIEELKKAKG 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1246 QHLQEVRLVPQDRVAELHRLLSLQGEQARRRLdAQREEHEKQLKATEERVE----EAEMILKNMEML-----LQEKVDKL 1316
Cdd:PRK03918 437 KCPVCGRELTEEHRKELLEEYTAELKRIEKEL-KEIEEKERKLRKELRELEkvlkKESELIKLKELAeqlkeLEEKLKKY 515
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 55749678 1317 -KEQFEKNTKSDLLLKELYVENAHLVRALQATEEKQRGAEKQSRLLEEKVRALNK 1370
Cdd:PRK03918 516 nLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEE 570
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1050-1206 |
2.98e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1050 ALEREKDDMETKLLHLEDVVRALEKHVDLRENDRLEFHRLSEENTL------LKNDLGRVRQELEAAESTHD-------- 1115
Cdd:COG4913 614 ALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDeidvasAEREIAELEAELERLDASSDdlaaleeq 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1116 --AQRKEIEVLKKDKEKACSEMEVLNRQNQNYKDQLSQLNVRVLQLGQEASTHQAQNEEHRVTIQMLTQSLEEVVRSGQQ 1193
Cdd:COG4913 694 leELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEE 773
|
170
....*....|...
gi 55749678 1194 QSDQIQKLRVELE 1206
Cdd:COG4913 774 RIDALRARLNRAE 786
|
|
| EFh |
cd00051 |
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ... |
237-272 |
3.32e-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: 37.14 E-value: 3.32e-03
10 20 30
....*....|....*....|....*....|....*.
gi 55749678 237 ELEDLFNKLDQDGDGKVSLEEFQLGLFSHEPALLLE 272
Cdd:cd00051 1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEE 36
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
388-1371 |
3.38e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.88 E-value: 3.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 388 YQQGQVEQLARERDKARQDLERAEKRNLEFVKEMDdchstleqlTEKKIKHLEQGYRERLSLLRSEVEAERELFWEQAHR 467
Cdd:pfam02463 139 VQGGKIEIIAMMKPERRLEIEEEAAGSRLKRKKKE---------ALKKLIEETENLAELIIDLEELKLQELKLKEQAKKA 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 468 QRAALEWDVGRLQAEEAGLREKLTLALKENSRLQKEIVEVVEKLSDSERLALKLQKDLEFVLKD------KLEPQSAELL 541
Cdd:pfam02463 210 LEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKEnkeeekEKKLQEEELK 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 542 AQEERFAAVLKEYELKCRDLQDRNDELQAELEGLwARLPKNRHSPSWSPDGRRRQLpglgpagISFLGNSAPVSIETELM 621
Cdd:pfam02463 290 LLAKEEEELKSELLKLERRKVDDEEKLKESEKEK-KKAEKELKKEKEEIEELEKEL-------KELEIKREAEEEEEEEL 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 622 MEQVKEHYQDLRTQLETKVNYYEREIAALKRNFE-KERKDMEQARRREVSVLEGQKADLEELHEKSQEVIWGLQEQLQDT 700
Cdd:pfam02463 362 EKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEeLELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIEL 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 701 ARGPEPEQmglapcctqalcglalrhhSHLQQIRREAEAELSGELSGLGALPARRDLTLEleeppqgplprgsQRSEQLE 780
Cdd:pfam02463 442 KQGKLTEE-------------------KEELEKQELKLLKDELELKKSEDLLKETQLVKL-------------QEQLELL 489
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 781 LERALKLQPCASEKRAQmcvslaleeeelelargkrvdgpSLEAEMQALPKDGLVAGSGQEGTRGLLPLRPGCGERPLAW 860
Cdd:pfam02463 490 LSRQKLEERSQKESKAR-----------------------SGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAIS 546
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 861 LAPGDGRESEEAAGAGPRRRQAQDTEATQSPAPAPAPASHGPSERWSRMQPCGVDGDIVPKepepFGASAAGLEQPGARE 940
Cdd:pfam02463 547 TAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQ----LDKATLEADEDDKRA 622
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 941 LPLLGTERDASQTQPRMWEPPLRPAASCRGQAERLQAIQEERARSWSRGTQEQASEQ--QARAEGALEPGCHKHSVEVAR 1018
Cdd:pfam02463 623 KVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQelQEKAESELAKEEILRRQLEIK 702
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1019 RGSLPSHLQLADPQGSWQEQLAAP-EEGETKIALEREKDDMETKLLHLEDVVRALEKhvdlRENDRLEFHRLSEENtllK 1097
Cdd:pfam02463 703 KKEQREKEELKKLKLEAEELLADRvQEAQDKINEELKLLKQKIDEEEEEEEKSRLKK----EEKEEEKSELSLKEK---E 775
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1098 NDLGRVRQELEAAESTHDAQRKEIEVLKKDKEKACSEMEVLNRQNQNYKDQLSQlnvrvlqlgqeasTHQAQNEEHRVTI 1177
Cdd:pfam02463 776 LAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEK-------------IKEEELEELALEL 842
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1178 QMLTQSLEEVVRSGQQQSDQIQKLRVELECLNQEHQSLQLPWSELTQTLEEsqdqvqgahlrlRQAQAQHLQEVRLVPQD 1257
Cdd:pfam02463 843 KEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEE------------KEKEEKKELEEESQKLN 910
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1258 RVAELHRLLSLQGEQARRRLDAQREEHEKQLKATEERVEEAEMILKNmemlLQEKVDKLKEQFEKNTKSDLLLKELYVEN 1337
Cdd:pfam02463 911 LLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEE----EEERNKRLLLAKEELGKVNLMAIEEFEEK 986
|
970 980 990
....*....|....*....|....*....|....
gi 55749678 1338 ahLVRALQATEEKQRGAEKQSRLLEEKVRALNKL 1371
Cdd:pfam02463 987 --EERYNKDELEKERLEEEKKKLIRAIIEETCQR 1018
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
377-579 |
3.87e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.56 E-value: 3.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 377 AALACYHQELSYQQGQVEQLARERDKARQDLERAE---KRNLEFVKEMDDCHSTLEQLTEKKikhleqgyrerlsllrSE 453
Cdd:PRK02224 206 ERLNGLESELAELDEEIERYEEQREQARETRDEADevlEEHEERREELETLEAEIEDLRETI----------------AE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 454 VEAERELFWEQAHRQRAALEwdvgRLQAEEAGLREKLTL-------ALKENSRLQKEIVEVVEKLSDSERLALKLQKDLE 526
Cdd:PRK02224 270 TEREREELAEEVRDLRERLE----ELEEERDDLLAEAGLddadaeaVEARREELEDRDEELRDRLEECRVAAQAHNEEAE 345
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 55749678 527 FVLK--DKLEPQSAELLAQEERFAAVLKEYELKCRDLQDRNDELQAELEGLWARL 579
Cdd:PRK02224 346 SLREdaDDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERF 400
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1042-1147 |
4.32e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.38 E-value: 4.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1042 PEEGETKIALEREKDDMETKLLHLEDVVRALEKHV-DLREndrlEFHRLSEENTLLKNDLGRVRQELEA-AESTHDAQR- 1118
Cdd:COG2433 395 PEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVeELEA----ELEEKDERIERLERELSEARSEERReIRKDREISRl 470
|
90 100 110
....*....|....*....|....*....|
gi 55749678 1119 -KEIEVLKKDKEKACSEMEVLNRQNQNYKD 1147
Cdd:COG2433 471 dREIERLERELEEERERIEELKRKLERLKE 500
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
940-1365 |
5.82e-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: 41.26 E-value: 5.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 940 ELPLLGTERDA-SQTQPRMWEPPLRPAASCRGQAERLQAIQEERARSWSRGTQEQASEQQARAEgalepgCHKHSVEVAR 1018
Cdd:pfam15921 357 ELTEARTERDQfSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRE------LDDRNMEVQR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1019 RGSLPSHLQlADPQGSWQEQLAA---------------PEEGETKIALEREKDDMETKLLHLEDVVRALEK-HVDLREND 1082
Cdd:pfam15921 431 LEALLKAMK-SECQGQMERQMAAiqgkneslekvssltAQLESTKEMLRKVVEELTAKKMTLESSERTVSDlTASLQEKE 509
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1083 RlEFHRLSEENTLLKNDLGRVRQELEAAESTHDAQRK---EIEVLKKDKEKACSEMEVLNRQNQNykdqLSQLnvrVLQL 1159
Cdd:pfam15921 510 R-AIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNvqtECEALKLQMAEKDKVIEILRQQIEN----MTQL---VGQH 581
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1160 GQEASTHQAQNEEHRVTIQMLTQSLEEVVRSGQQQSDQIQKLRVELECLNQEHQSLQLPWSELTQTLEEsqdqvqgahlr 1239
Cdd:pfam15921 582 GRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKD----------- 650
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1240 LRQAQAQHLQEVRLVPQD--RVAELHRLLSLQGEQARRRLDAQREEHEKQLKATEERVEEAEMILKNMEM---------- 1307
Cdd:pfam15921 651 IKQERDQLLNEVKTSRNElnSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGsdghamkvam 730
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 55749678 1308 --------------LLQEKVDKLKEQFEKNTKSDLLLKElyvENAHLVRALQ--ATEEKQRGAE-----KQSRLLEEKV 1365
Cdd:pfam15921 731 gmqkqitakrgqidALQSKIQFLEEAMTNANKEKHFLKE---EKNKLSQELStvATEKNKMAGElevlrSQERRLKEKV 806
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1191-1370 |
6.11e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 6.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1191 GQQQSDQIQKLRVELECLNQEHQSLQlpwsELTQTLEESQDQVQGAHLRLRQAQAQHLQEVRLVP-QDRVAELHRLLS-- 1267
Cdd:COG4913 605 GFDNRAKLAALEAELAELEEELAEAE----ERLEALEAELDALQERREALQRLAEYSWDEIDVASaEREIAELEAELErl 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1268 LQGEQARRRLDAQREEHEKQLKATEERVEEaemilknmemlLQEKVDKLKEQFEKNTKSDLLLKELYVENAHLVRALQAT 1347
Cdd:COG4913 681 DASSDDLAALEEQLEELEAELEELEEELDE-----------LKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA 749
|
170 180
....*....|....*....|....
gi 55749678 1348 E-EKQRGAEKQSRLLEEKVRALNK 1370
Cdd:COG4913 750 LlEERFAAALGDAVERELRENLEE 773
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
972-1283 |
7.55e-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: 41.09 E-value: 7.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 972 AERLQAIQEERArswsrGTQEQASEQQARAEGALEpgchkhsvEVARRGSlpshlQLADPQ----------GSWQEQLAA 1041
Cdd:COG3096 360 TERLEEQEEVVE-----EAAEQLAEAEARLEAAEE--------EVDSLKS-----QLADYQqaldvqqtraIQYQQAVQA 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1042 PEE-----GETKIALEREKDDMET---KLLHLEDVVRALEKHVDLRENDRLEFHRLSEentLLKNDLGRV---------R 1104
Cdd:COG3096 422 LEKaralcGLPDLTPENAEDYLAAfraKEQQATEEVLELEQKLSVADAARRQFEKAYE---LVCKIAGEVersqawqtaR 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1105 QELEAAEStHDAQRKEIEVLKKdkekACSEMEVLNRQNQNYKDQLSQLNVRVLQLGQEASTHQAQNEEHRVTIQMLTQSL 1184
Cdd:COG3096 499 ELLRRYRS-QQALAQRLQQLRA----QLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQA 573
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749678 1185 EEvvrsgqQQSDQIQkLRVELECLNQEHQSL--QLP-WSELTQTLEESQDQVqGAHLRLRQAQAQHLQevRLVPQDRVAE 1261
Cdd:COG3096 574 AE------AVEQRSE-LRQQLEQLRARIKELaaRAPaWLAAQDALERLREQS-GEALADSQEVTAAMQ--QLLEREREAT 643
|
330 340
....*....|....*....|..
gi 55749678 1262 LHRLLSlqgEQARRRLDAQREE 1283
Cdd:COG3096 644 VERDEL---AARKQALESQIER 662
|
|
| EFh_PI-PLC |
cd15898 |
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ... |
200-265 |
7.61e-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: 38.42 E-value: 7.61e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 55749678 200 QIRGVWEELGVGSSGHLSEQELAVVCQSVGLQgLEKEELEDLFNKLDQDGDGKVSLEEFQLGLFSH 265
Cdd:cd15898 1 WLRRQWIKADKDGDGKLSLKEIKKLLKRLNIR-VSEKELKKLFKEVDTNGDGTLTFDEFEELYKSL 65
|
|
| EFh_parvalbumins |
cd16253 |
EF-hand, calcium binding motif, found in parvalbumins; Parvalbumins are small, acidic, ... |
200-259 |
8.40e-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: 37.16 E-value: 8.40e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 55749678 200 QIRGVWEELGVGSSGHLSEQELAVV--CQSVGLQGLEKEELEDLFNKLDQDGDGKVSLEEFQ 259
Cdd:cd16253 35 DIKKVFNILDQDKSGFIEEEELKLFlkNFSDGARVLSDKETKNFLAAGDSDGDGKIGVDEFK 96
|
|
| |
