|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1119-1430 |
3.16e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 81.52 E-value: 3.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1119 EREKDDMETKLLHLEDVVRALEKHVDLRENDR---LEFHRLSEE-----NTLLKNDLGRVRQELEAAESTHDAQRKEIEV 1190
Cdd:COG1196 178 ERKLEATEENLERLEDILGELERQLEPLERQAekaERYRELKEElkeleAELLLLKLRELEAELEELEAELEELEAELEE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1191 LKKDKEKACSEMEVLNRQNQNYKDQLSQLNVRVLQLGQEASTHQAQNEEHRVTIQMLTQSLEEVVRSGQQQSDQIQKLRV 1270
Cdd:COG1196 258 LEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1271 ELECLNQEHQSLQLPWSELTQTLEESQDQVQGAHLRLRQAQAQHLQEVR--LVPQDRVAELHRLLsLQGEQARRRLDAQR 1348
Cdd:COG1196 338 ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEelLEALRAAAELAAQL-EELEEAEEALLERL 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1349 EEHEKQLKATEERVEEAEMILKNMEMLLQEKVDKLKEQFEKNTKSDLLLKELYVENAHLVRALQATEEKQRGAEKQSRLL 1428
Cdd:COG1196 417 ERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLL 496
|
..
gi 2217334791 1429 EE 1430
Cdd:COG1196 497 LE 498
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1119-1443 |
7.16e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 73.94 E-value: 7.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1119 EREKDDMETKLLHLEDVVRALEKHVD-LRENDRL--EFHRLSEE-----NTLLKNDLGRVRQELEAAESTHDAQRKEIEV 1190
Cdd:TIGR02168 178 ERKLERTRENLDRLEDILNELERQLKsLERQAEKaeRYKELKAElreleLALLVLRLEELREELEELQEELKEAEEELEE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1191 LKKDKEKACSEMEVLNRQNQNYKDQLSQLNVRVLQLGQEASTHQAQNEEHRVTIQMLTQSLEEVVRSGQQQSDQIQKLRV 1270
Cdd:TIGR02168 258 LTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1271 ELECLNQEHQSLQLPWSELTQTLEESQDQVQGAHLRLRQAQAQHLQEVRlvpqdRVAELhrllslqgEQARRRLDAQREE 1350
Cdd:TIGR02168 338 ELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS-----KVAQL--------ELQIASLNNEIER 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1351 HEKQLKATEERVEEAEMILKNMEMLLQEKvdKLKEQFEKNTKSDLLLKELYVENAHLVRALQatEEKQRGAEKQSRLLEE 1430
Cdd:TIGR02168 405 LEARLERLEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLEEALE--ELREELEEAEQALDAA 480
|
330
....*....|...
gi 2217334791 1431 KvRALNKLVSRIA 1443
Cdd:TIGR02168 481 E-RELAQLQARLD 492
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1118-1444 |
1.19e-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: 73.17 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1118 LEREKDDMETKLLHLEDVVRALEKHVdlrENDRLEFHRLSEENTLLKNDLGRVRQELEAAESTHDAQRKEIEVLKKDKEK 1197
Cdd:TIGR02168 717 LRKELEELSRQISALRKDLARLEAEV---EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ 793
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1198 ACSEMEVLNRQNQNYKDQLSQLNVRVLQLGQEASTHQAQNEEHRVTIQMLTQSLEevvrsgqQQSDQIQKLRVELEclnq 1277
Cdd:TIGR02168 794 LKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIE-------ELSEDIESLAAEIE---- 862
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1278 ehqslqlpwsELTQTLEESQDQVQgAHLRLRQAQAQHLQEVRLVPQDRVAELHRLlslqgEQARRRLDAQREEHEKQLKA 1357
Cdd:TIGR02168 863 ----------ELEELIEELESELE-ALLNERASLEEALALLRSELEELSEELREL-----ESKRSELRRELEELREKLAQ 926
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1358 TEERVEEAEMilknmemllqeKVDKLKEQFekntksdlllkelyveNAHLVRALQATEEKQRGAEKQSRLLEEKVRALNK 1437
Cdd:TIGR02168 927 LELRLEGLEV-----------RIDNLQERL----------------SEEYSLTLEEAEALENKIEDDEEEARRRLKRLEN 979
|
....*..
gi 2217334791 1438 LVSRIAP 1444
Cdd:TIGR02168 980 KIKELGP 986
|
|
| EF-hand_7 |
pfam13499 |
EF-hand domain pair; |
198-259 |
2.30e-11 |
|
EF-hand domain pair;
Pssm-ID: 463900 [Multi-domain] Cd Length: 67 Bit Score: 60.73 E-value: 2.30e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217334791 198 ESQIRGVWEELGVGSSGHLSEQELAVVCQSVGLQG-LEKEELEDLFNKLDQDGDGKVSLEEFQ 259
Cdd:pfam13499 1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEpLSDEEVEELFKEFDLDKDGRISFEEFL 63
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1051-1443 |
9.35e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 63.82 E-value: 9.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1051 RSWSRGTQEQASEQQARAEGALEPGCHkhsveVARRGSLPSHLQLADP-QGSWQEQLAAPEegetkiALEREKDDMETKL 1129
Cdd:PRK04863 293 RELYTSRRQLAAEQYRLVEMARELAEL-----NEAESDLEQDYQAASDhLNLVQTALRQQE------KIERYQADLEELE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1130 LHLEDVVRALEKHVDLRENDRLEFHRLSEENTLLKNDLGRVRQELEAAESTHDAQRKEIEVLkkDKEKACSEMEVLNRQN 1209
Cdd:PRK04863 362 ERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQAL--ERAKQLCGLPDLTADN 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1210 -----QNYKDQLSQLNVRVLQLGQEASTHQAQNEEHRVTIQMLTQSLEEVVRSGQQQSdQIQKLR--VELECLNQEHQSL 1282
Cdd:PRK04863 440 aedwlEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRSEAWDV-ARELLRrlREQRHLAEQLQQL 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1283 QLPWSELTQTLEESQDQVQgahlRLRQAQAQHLQEVrlvpqDRVAELHRLLSLQGEQ------ARRRLDAQREEHEKQLK 1356
Cdd:PRK04863 519 RMRLSELEQRLRQQQRAER----LLAEFCKRLGKNL-----DDEDELEQLQEELEARleslseSVSEARERRMALRQQLE 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1357 ATEERVEEAEmILKNMEMLLQEKVDKLKEQFEKNtksdlllkelyVENAHLVRAL-QATEEKQRGAEKQSRLLEEKVRAL 1435
Cdd:PRK04863 590 QLQARIQRLA-ARAPAWLAAQDALARLREQSGEE-----------FEDSQDVTEYmQQLLERERELTVERDELAARKQAL 657
|
....*...
gi 2217334791 1436 NKLVSRIA 1443
Cdd:PRK04863 658 DEEIERLS 665
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1152-1435 |
1.30e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 63.16 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1152 EFHRLSEENTLLKNDLGRVRQELEAAESTHDAQRKEIEVLKKDKEKACSEMEVLNRQNQ-------NYKDQLSQLNVRVL 1224
Cdd:TIGR02169 689 ELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSsleqeieNVKSELKELEARIE 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1225 QLgqEASTHQAQNEEHRVTIQMLTQSLEEVVRSGQQQSDQIQKLRVELECLNQEHQSLQLPWSELTQTLEESQDQVQGAH 1304
Cdd:TIGR02169 769 EL--EEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLK 846
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1305 LRLRQ-AQAQHLQEVRLVPQDRVAELHRLLSLQGEQARRRLDAQREEHEKQLKATEERVEEAEMILKNMEMLLQEKVDKL 1383
Cdd:TIGR02169 847 EQIKSiEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKL 926
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2217334791 1384 KEQFEKNTKSDLLLKELYVENAHLVRALQATEEKQRgaekqsrlLEEKVRAL 1435
Cdd:TIGR02169 927 EALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQR--------VEEEIRAL 970
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
393-701 |
2.64e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 62.01 E-value: 2.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 393 VEQLARERDKARQDLERAEKRNLEFVKEMDDCHSTLEQLTEKKIKHLEqgYRERLSLLRSEVEAERELFWEQAHRQRAAL 472
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAER--YQALLKEKREYEGYELLKEKEALERQKEAI 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 473 EWDVGRLQAEEAGLREKLtlalkenSRLQKEIVEVVEKLSDSERLALKLQKDLEFVLKDKLEpqsaELLAQEERFAAVLK 552
Cdd:TIGR02169 243 ERQLASLEEELEKLTEEI-------SELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIG----ELEAEIASLERSIA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 553 EYELKCRDLQDRNDELQAELEGLWARLPKNRHSPSwSPDGRRRQLpglgpagISFLGNSAPVSIETELMMEQVKEHYQDL 632
Cdd:TIGR02169 312 EKERELEDAEERLAKLEAEIDKLLAEIEELEREIE-EERKRRDKL-------TEEYAELKEELEDLRAELEEVDKEFAET 383
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217334791 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 |
4.07e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 61.61 E-value: 4.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 362 ALDNELMTVDSAVQQAALACYHQELSYQQGQVEQLARERDKARQDLERAEKRNLEFVKEMDDCHSTLEQLTEK--KIKHL 439
Cdd:TIGR02168 224 ELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEisRLEQQ 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 440 EQGYRERL-SLLRSEVEAERELfwEQAHRQRAALEWDVGRLQAEEAGLREKLTLALKENSRLQKEIVEVVEKLSDSERLA 518
Cdd:TIGR02168 304 KQILRERLaNLERQLEELEAQL--EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 519 LKLQKDLefvlkdklepqsAELLAQEERFAAVLKEYELKCRDLQDRNDELQAELEGLWARLPKNRHSPSwspdgrRRQLP 598
Cdd:TIGR02168 382 ETLRSKV------------AQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKEL------QAELE 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 599 glgpagisflgnsapvsiETELMMEQVKEHYQDLRTQLETKvnyyEREIAALKRNFEKERKDMEQARRRevsvLEGQKAD 678
Cdd:TIGR02168 444 ------------------ELEEELEELQEELERLEEALEEL----REELEEAEQALDAAERELAQLQAR----LDSLERL 497
|
330 340
....*....|....*....|
gi 2217334791 679 LEELHEKSQEVIWGLQEQLQ 698
Cdd:TIGR02168 498 QENLEGFSEGVKALLKNQSG 517
|
|
| EFh |
cd00051 |
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ... |
212-259 |
4.67e-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: 53.71 E-value: 4.67e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2217334791 212 SSGHLSEQELAVVCQSVGLqGLEKEELEDLFNKLDQDGDGKVSLEEFQ 259
Cdd:cd00051 13 GDGTISADELKAALKSLGE-GLSEEEIDEMIREVDKDGDGKIDFEEFL 59
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1100-1386 |
5.74e-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: 60.85 E-value: 5.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1100 GSWQEQLAAPEEGETKIA-LEREKDDMETKLLHLEDVVRALEKhvdLRENDRLEFHRLSEENTL-LKNDLGRVRQELEAA 1177
Cdd:TIGR02169 230 KEKEALERQKEAIERQLAsLEEELEKLTEEISELEKRLEEIEQ---LLEELNKKIKDLGEEEQLrVKEKIGELEAEIASL 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1178 ESTHDAQRKEIEVLKKDKEKACSEMEVLNRQNQNYKDQLSQLNVRVLQLGQEASTHQAQNEEhrvtiqmLTQSLEEVVRS 1257
Cdd:TIGR02169 307 ERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELED-------LRAELEEVDKE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1258 GQQQSDQIQKLRVELECLNQEHQSLQLPWSELTQTLEESQDQVQGAHLRLRQAQAQH--LQEVRLVPQDRVAELhrllsl 1335
Cdd:TIGR02169 380 FAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKIneLEEEKEDKALEIKKQ------ 453
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2217334791 1336 qgEQARRRLDAQREEHEKQLKATEERVEEAEMILKNmemlLQEKVDKLKEQ 1386
Cdd:TIGR02169 454 --EWKLEQLAADLSKYEQELYDLKEEYDRVEKELSK----LQRELAEAEAQ 498
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1128-1433 |
1.42e-08 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 59.37 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1128 KLLHLEDVVRALEKHVDLRENDRLEFHRLSEENTLLKNDLGRvRQELEAAESTHDAQRKEIEVLKKDKEKACSEmevlnR 1207
Cdd:pfam17380 273 QLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVER-RRKLEEAEKARQAEMDRQAAIYAEQERMAME-----R 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1208 QNQNYKDQLSQLNVRVLQLGQEASTHQAQNEEHRVTIQMLTQSLEEVVRsgqQQSDQIQKLRVELEclnQEHQSLQLPWS 1287
Cdd:pfam17380 347 ERELERIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVR---QELEAARKVKILEE---ERQRKIQQQKV 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1288 ELTQTLEESQDQVQGAHLRLRQAQAQHLQEVRLVPQDRVAELHRLLSLQGEQARRRLDAQREEHEKQLKATEER-VEEAE 1366
Cdd:pfam17380 421 EMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRkILEKE 500
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217334791 1367 MILKNMEMLLQEKVDKLKEQFEKNTKSDLLLKELYVENAHLVRALQATEEKQRGAEKQSRLLEEKVR 1433
Cdd:pfam17380 501 LEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSR 567
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1099-1350 |
3.04e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.41 E-value: 3.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1099 QGSWQEQLAAPEEGETKIA-LEREKDDMETKLLHLEDVVRALEKHVDLRENDRLEFH-----------RLSEENTLLKND 1166
Cdd:COG1196 238 EAELEELEAELEELEAELEeLEAELAELEAELEELRLELEELELELEEAQAEEYELLaelarleqdiaRLEERRRELEER 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1167 LGRVRQELEAAESTHDAQRKEIEVLKKDKEKACSEMEVLNRQNQNYKDQLSQLNVRVLQLGQEASTHQAQNEEHRVTIQM 1246
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1247 LTQSLEEVVRSGQQQSDQIQKLRVELECLNQEHQSLQLPWSELTQTLEESQDQVQGAHLRLRQAQAQHLQEVRLVPQDRV 1326
Cdd:COG1196 398 LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA 477
|
250 260
....*....|....*....|....
gi 2217334791 1327 AELHRLLSLQGEQARRRLDAQREE 1350
Cdd:COG1196 478 ALAELLEELAEAAARLLLLLEAEA 501
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1125-1442 |
4.66e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 57.72 E-value: 4.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1125 METKLLHLEDVVRALEKHVDLrENDRL------------EFHRLSEENTLLKNDLGRVRQELEAAESTHDAQRK------ 1186
Cdd:TIGR04523 216 LESQISELKKQNNQLKDNIEK-KQQEInektteisntqtQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKqlnqlk 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1187 -EIEVLKKDKEKACS------------EMEVLNRQNQNYKDQLSQLNVRVLQLGQEASTHQAQNEEHRVTIQMLTQSLEE 1253
Cdd:TIGR04523 295 sEISDLNNQKEQDWNkelkselknqekKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEK 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1254 VVRSGQQQSDQIQKLRVELECLNQEHQSLQlpwsELTQTLEESQDQVQGAHLRLRQaQAQHLQEVRLVPQDRVAELHRLL 1333
Cdd:TIGR04523 375 LKKENQSYKQEIKNLESQINDLESKIQNQE----KLNQQKDEQIKKLQQEKELLEK-EIERLKETIIKNNSEIKDLTNQD 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1334 SlQGEQARRRLDAQREEHEKQLKATEERVEEAEMILKNMEMLLQEKVDKLKEQFEKNTKSDLLLKELyvenahlvralqa 1413
Cdd:TIGR04523 450 S-VKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDL------------- 515
|
330 340
....*....|....*....|....*....
gi 2217334791 1414 teekqrgaEKQSRLLEEKVRALNKLVSRI 1442
Cdd:TIGR04523 516 --------TKKISSLKEKIEKLESEKKEK 536
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
363-575 |
6.40e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.64 E-value: 6.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 363 LDNELMTVDSAVQQAALACYHQELSYQQGQVEQLARERDKARQDLERAEKRNLEFVKEMDDCHSTLEQLTEKKIKHLEQg 442
Cdd:COG1196 225 LEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD- 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 443 yRERLSLLRSEVEAERelfwEQAHRQRAALEWDVGRLQAEEAGLREKLTLALKENSRLQKEIVEVVEKLSDSERLALKLQ 522
Cdd:COG1196 304 -IARLEERRRELEERL----EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2217334791 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 |
6.98e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.37 E-value: 6.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 341 EILQSLDFSVDEKVNLLELTW-ALDNELMTVDS--AVQQAALACYHQELSYQQGQVEQLARERDKARQDLERAEKRNLEF 417
Cdd:TIGR02168 270 EELRLEVSELEEEIEELQKELyALANEISRLEQqkQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEEL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 418 VKEMDDChstLEQLTEKKIKhleqgyRERLSLLRSEVEAErelfWEQAHRQRAALEWDVGRLQAEEAGLREKLTLALKEN 497
Cdd:TIGR02168 350 KEELESL---EAELEELEAE------LEELESRLEELEEQ----LETLRSKVAQLELQIASLNNEIERLEARLERLEDRR 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217334791 498 SRLQKEIVEVVEKLSDSERLALKLQKDLEFVLKDKLEPQSAELLAQEERFAAVLKEYELKCRDLQDRNDELQAELEGL 575
Cdd:TIGR02168 417 ERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSL 494
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1163-1442 |
1.47e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 56.18 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1163 LKNDLGRVRQELEAAESTHDAQRKEIEvlkkdkEKAcSEMEVLNRQNQNYKDQLSQLNVRVLQLGQEASTHQAQNEEHRV 1242
Cdd:TIGR04523 340 LNEQISQLKKELTNSESENSEKQRELE------EKQ-NEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDE 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1243 TIQMLTQSLEEVVRSGQQQSDQIQKLRVELECLNQEHQSLQLPWSELTQTLEESQDQVQGAHLRLRQAQaQHLQEVRLVP 1322
Cdd:TIGR04523 413 QIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIK-QNLEQKQKEL 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1323 QDRVAELHRLLS-----------LQGEQAR-----RRLDAQREEHEKQLKATEERVEEAEMILKNMEML-----LQEKVD 1381
Cdd:TIGR04523 492 KSKEKELKKLNEekkeleekvkdLTKKISSlkekiEKLESEKKEKESKISDLEDELNKDDFELKKENLEkeideKNKEIE 571
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217334791 1382 KLKEQFE----KNTKSDLLLKELYVENAHLVRALQATEEKQRGAEKQSRLLEEKVRALNKLVSRI 1442
Cdd:TIGR04523 572 ELKQTQKslkkKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNI 636
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
384-597 |
2.50e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.71 E-value: 2.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 384 QELSYQQGQVEQLARERDKARQDLERAEKRNLEFVKEMDDCHSTLEQLTEK---KIKHLEQGYRERLSLLRSEVEAEREl 460
Cdd:COG1196 302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEleeAEAELAEAEEALLEAEAELAEAEEE- 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 461 fWEQAHRQRAALEWDVGRLQAEEAGLREKLTLALKENSRLQKEIVEVVEKLSDSERLALKLQKDLEFVLKDKLEpQSAEL 540
Cdd:COG1196 381 -LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE-LEEEE 458
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2217334791 541 LAQEERFAAVLKEYELKCRDLQDRNDELQAELEGLWARLPKNRHSPSWSPDGRRRQL 597
Cdd:COG1196 459 EALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALL 515
|
|
| EF-hand_8 |
pfam13833 |
EF-hand domain pair; |
212-258 |
4.08e-07 |
|
EF-hand domain pair;
Pssm-ID: 404678 [Multi-domain] Cd Length: 54 Bit Score: 48.08 E-value: 4.08e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2217334791 212 SSGHLSEQELAVVCQSVGLQGLEKEELEDLFNKLDQDGDGKVSLEEF 258
Cdd:pfam13833 1 EKGVITREELKRALALLGLKDLSEDEVDILFREFDTDGDGYISFDEF 47
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1150-1413 |
4.96e-07 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 54.36 E-value: 4.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1150 RLEFHRLSEENTLLKNDLG--RVRQELEAAESTHDAQ-----------RKEIEVLKK---DKEKACSEMEVLNRQNQNYK 1213
Cdd:pfam05557 6 ESKARLSQLQNEKKQMELEhkRARIELEKKASALKRQldresdrnqelQKRIRLLEKreaEAEEALREQAELNRLKKKYL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1214 DQLSQLnvrvlqlgqeASTHQAQNEEHRVTIQMLTQSLEEVVRSGQQQSDQIQKLRVELECLNQEHQSLQLPWSELTQ-- 1291
Cdd:pfam05557 86 EALNKK----------LNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQlr 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1292 -TLEESQDQVQGAHLRLR------QAQAQHLQEVRlvpqDRVAELHRLLSLQGEQARRRldaqreEHEKQLKATEERVEe 1364
Cdd:pfam05557 156 qNLEKQQSSLAEAEQRIKelefeiQSQEQDSEIVK----NSKSELARIPELEKELERLR------EHNKHLNENIENKL- 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2217334791 1365 aemilknmemLLQEKVDKLKEQFEKNTKSDLLLKELYVENAHLVRALQA 1413
Cdd:pfam05557 225 ----------LLKEEVEDLKRKLEREEKYREEAATLELEKEKLEQELQS 263
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1163-1392 |
5.82e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 53.61 E-value: 5.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1163 LKNDLGRVRQELEAAESTHDAQRKEIEVLKKDKEKACSEMEVLNRQNQNYKDQLSQLNVRVLQLGQEASTHQAQNEEHR- 1241
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKe 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1242 ------VTIQMLTQSLEEVVRSGQQQSDQIQKLRVELECLNQEHQslqlpwsELTQTLEESQDQVQgahlRLRQAQAQHL 1315
Cdd:COG4942 105 elaellRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARR-------EQAEELRADLAELA----ALRAELEAER 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217334791 1316 QEVRLVPQDRVAELHRLLSLQGEQAR--RRLDAQREEHEKQLKATEERVEEaemilknmemlLQEKVDKLKEQFEKNTK 1392
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKllARLEKELAELAAELAELQQEAEE-----------LEALIARLEAEAAAAAE 241
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
366-690 |
6.78e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.29 E-value: 6.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 366 ELMTVDSAVQQAALACYHQELSYQQGQVEQLARERDKARQ-------DLERAEKRNLEFVKEMDDCHSTLEQLTEKKIKH 438
Cdd:TIGR02168 687 EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRqisalrkDLARLEAEVEQLEERIAQLSKELTELEAEIEEL 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 439 LEQGYRERLSLLRSEVE-AERELFWEQAHRQRAALEWDVGRLQAEEAGLREK---------------------LTLALKE 496
Cdd:TIGR02168 767 EERLEEAEEELAEAEAEiEELEAQIEQLKEELKALREALDELRAELTLLNEEaanlrerleslerriaaterrLEDLEEQ 846
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 497 NSRLQKEIVEVVEKLSDSERLALKLQKDLEFVL--KDKLEPQSAELLAQEERFAAVLKEYELKCRDLQDRNDELQAELEG 574
Cdd:TIGR02168 847 IEELSEDIESLAAEIEELEELIEELESELEALLneRASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQ 926
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 575 LWARLPKNRhspswspdGRRRQLpglgpagisflgnSAPVSIETELMMEQVKEHYQDL---RTQLETKVNYYEREIAALK 651
Cdd:TIGR02168 927 LELRLEGLE--------VRIDNL-------------QERLSEEYSLTLEEAEALENKIeddEEEARRRLKRLENKIKELG 985
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2217334791 652 R-NFEKERKDMEQARRREvsVLEGQKADLEELHEKSQEVI 690
Cdd:TIGR02168 986 PvNLAAIEEYEELKERYD--FLTAQKEDLTEAKETLEEAI 1023
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
392-713 |
1.41e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.15 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 392 QVEQLARERDKA-RQDLERAEKRNLEF---VKEMDDCHSTLEQlTEKKIKHLEQ---GYRERLSLLRSEVEAERELFWEQ 464
Cdd:TIGR02169 199 QLERLRREREKAeRYQALLKEKREYEGyelLKEKEALERQKEA-IERQLASLEEeleKLTEEISELEKRLEEIEQLLEEL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 465 AHRQRA-------ALEWDVGRLQAEEAGLREKLTLALKENSRLQKEIVEVVEKLSDSERLALKLQKDLE--FVLKDKLEP 535
Cdd:TIGR02169 278 NKKIKDlgeeeqlRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEeeRKRRDKLTE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 536 QSAELLAQEERFAAVLKEYELKCRDLQDRNDELQAELEGLwarlpKNRHSPSWSPDGRRRQLPGLGPAGISFLGNSAPVS 615
Cdd:TIGR02169 358 EYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKL-----KREINELKRELDRLQEELQRLSEELADLNAAIAGI 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 616 IETELMMEQVKEHYQDlrtqletkvnyyerEIAALKRNFEKERKDMEQARRREVSVLEGQKADLEELHEKSQEViwglqE 695
Cdd:TIGR02169 433 EAKINELEEEKEDKAL--------------EIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQREL-----A 493
|
330
....*....|....*...
gi 2217334791 696 QLQDTARGPEPEQMGLAP 713
Cdd:TIGR02169 494 EAEAQARASEERVRGGRA 511
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1171-1365 |
1.80e-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: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1171 RQELEAAESTHDAQRKEIEVLKKDKEKACSEME-------VLNRQNQNYKDQLSQLNVRVLQLGQEASTHQAQNEEHR-- 1241
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAalerriaALARRIRALEQELAALEAELAELEKEIAELRAELEAQKee 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1242 -----VTIQML-----------TQSLEEVVRSG-------QQQSDQIQKLRVELECLNQEHQSLQlpwsELTQTLEESQD 1298
Cdd:COG4942 106 laellRALYRLgrqpplalllsPEDFLDAVRRLqylkylaPARREQAEELRADLAELAALRAELE----AERAELEALLA 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217334791 1299 QVQGAHLRLRQAQAQHLQEVRLVPQDRVAELHRLLSLQgeQARRRLDAQREEHEKQLKATEERVEEA 1365
Cdd:COG4942 182 ELEEERAALEALKAERQKLLARLEKELAELAAELAELQ--QEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1149-1401 |
2.13e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 52.32 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1149 DRLEFHRLSEENTLLKNDLGRVRQELeaaeSTHDAQRKEIEvlkkdkEKACSEMEVLNRQNQNYKDQLSQLNVRVLQLGQ 1228
Cdd:PHA02562 158 DLLDISVLSEMDKLNKDKIRELNQQI----QTLDMKIDHIQ------QQIKTYNKNIEEQRKKNGENIARKQNKYDELVE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1229 EASTHQAQNEEhrvtiqmLTQSLEEVVRSGQQQSDQIQKLRVELECLNQEHQSLQlpwSEL------------TQTLEES 1296
Cdd:PHA02562 228 EAKTIKAEIEE-------LTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQ---KVIkmyekggvcptcTQQISEG 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1297 QDQVQGAHLRLRQAQAQHLQEvrlvpQDRVAELHRLLSLQGEQARRRLDAQRE-EHEKQLKATEerVEEAEMILKNMEML 1375
Cdd:PHA02562 298 PDRITKIKDKLKELQHSLEKL-----DTAIDELEEIMDEFNEQSKKLLELKNKiSTNKQSLITL--VDKAKKVKAAIEEL 370
|
250 260 270
....*....|....*....|....*....|....
gi 2217334791 1376 LQEKVD------KLKEQFEK--NTKSDlLLKELY 1401
Cdd:PHA02562 371 QAEFVDnaeelaKLQDELDKivKTKSE-LVKEKY 403
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1183-1442 |
3.35e-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: 3.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1183 AQRKEIEVLKKDKEKACSEMEVLNRQNQNYKDQLSQLNvrvlqlgQEASTHQAQNEEHRVTIQMLTQSLEEVVRSGQQQS 1262
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELE-------EELEQLRKELEELSRQISALRKDLARLEAEVEQLE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1263 DQIQKLRVELECLNQEHQslqlpwsELTQTLEESQD--QVQGAHLRLRQAQAQHLQEVRLVPQDRVAELHRLLSLQGEQA 1340
Cdd:TIGR02168 747 ERIAQLSKELTELEAEIE-------ELEERLEEAEEelAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1341 rRRLDAQREEHEKQLKATEERVEEAEMILKNME---MLLQEKVDKLKEQFEK-NTKSDLLLKELYVENAHLVRA---LQA 1413
Cdd:TIGR02168 820 -ANLRERLESLERRIAATERRLEDLEEQIEELSediESLAAEIEELEELIEElESELEALLNERASLEEALALLrseLEE 898
|
250 260
....*....|....*....|....*....
gi 2217334791 1414 TEEKQRGAEKQSRLLEEKVRALNKLVSRI 1442
Cdd:TIGR02168 899 LSEELRELESKRSELRRELEELREKLAQL 927
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
392-579 |
3.85e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 3.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 392 QVEQLARERDKARQDLERAEKRnlefVKEMDDCHSTLEQLtekkikhleqgyreRLSLLRSEVEAERELFWEQAHRQRAA 471
Cdd:COG4913 611 KLAALEAELAELEEELAEAEER----LEALEAELDALQER--------------REALQRLAEYSWDEIDVASAEREIAE 672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 472 LE----------WDVGRLQAEEAGLREKLTLALKENSRLQKEIVEVVEKLSDSERLALKLQKDLEFVLKDKLEPQSAELl 541
Cdd:COG4913 673 LEaelerldassDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALL- 751
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2217334791 542 aqEERFAAVLKE--YELKCRDLQDRNDELQAELEGLWARL 579
Cdd:COG4913 752 --EERFAAALGDavERELRENLEERIDALRARLNRAEEEL 789
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1104-1433 |
5.99e-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: 5.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1104 EQLAAPEEGETKIALEREK-DDMETKLLHLEDVVRALEKHVDLRENDR---LEFHRLSE-----ENTLLKNDLGRVRQEL 1174
Cdd:TIGR02169 160 DEIAGVAEFDRKKEKALEElEEVEENIERLDLIIDEKRQQLERLRRERekaERYQALLKekreyEGYELLKEKEALERQK 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1175 EAAESTHDAQRKEIEVLKKDKEKACSEMEVLNRqnqnykdQLSQLNVRVLQLGQ-EASTHQAQNEEHRVTIQMLTQSLEE 1253
Cdd:TIGR02169 240 EAIERQLASLEEELEKLTEEISELEKRLEEIEQ-------LLEELNKKIKDLGEeEQLRVKEKIGELEAEIASLERSIAE 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1254 VVRSGQQQSDQIQKLRVELECLNQEHQ--------------SLQLPWSELTQTLEESQDQVQ---GAHLRLRQAQAQHLQ 1316
Cdd:TIGR02169 313 KERELEDAEERLAKLEAEIDKLLAEIEelereieeerkrrdKLTEEYAELKEELEDLRAELEevdKEFAETRDELKDYRE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1317 EVRLVpQDRVAELHRLLSLQGEQArRRLDAQREEHEKQLKATEERVEEAEMILKNMEMLLQEKVDKLKEQFEKNTKSDLL 1396
Cdd:TIGR02169 393 KLEKL-KREINELKRELDRLQEEL-QRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQE 470
|
330 340 350
....*....|....*....|....*....|....*..
gi 2217334791 1397 LKELYVENAHLVRALQATEEKQRGAEKQSRLLEEKVR 1433
Cdd:TIGR02169 471 LYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVR 507
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
392-573 |
6.52e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.09 E-value: 6.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 392 QVEQLARERDKAR--QDL--ERAEKRNLEFVKEMDDCHSTLEQLTEKKIKHLEQgyRERLSLLRSEVEAERElfweQAHR 467
Cdd:COG1196 201 QLEPLERQAEKAEryRELkeELKELEAELLLLKLRELEAELEELEAELEELEAE--LEELEAELAELEAELE----ELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 468 QRAALEWDVGRLQAEEAGLREKLtlalkenSRLQKEIVEVVEKLSDSERLALKLQKDLEfVLKDKLEPQSAELLAQEERF 547
Cdd:COG1196 275 ELEELELELEEAQAEEYELLAEL-------ARLEQDIARLEERRRELEERLEELEEELA-ELEEELEELEEELEELEEEL 346
|
170 180
....*....|....*....|....*.
gi 2217334791 548 AAVLKEYELKCRDLQDRNDELQAELE 573
Cdd:COG1196 347 EEAEEELEEAEAELAEAEEALLEAEA 372
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1214-1448 |
7.25e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.15 E-value: 7.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1214 DQLSQLNVRVLQLGQEASTHQAQNEEHRVTIQMLTQSLEEVVRSGQQQSDQIQKLRVELECLNQEHQSLQLPWSELTQTL 1293
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1294 EESQDQVqGAHLRLRQAQAQHLQEVRLVPQDRVAELHRLLSLQGEQARRRLDaQREEHEKQLKATEERVEEAEMILKNME 1373
Cdd:COG4942 100 EAQKEEL-AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARRE-QAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217334791 1374 MLLQEKVDKLKEQFEKNTKSDLLLKELYVENAHLVRALQATEEKQRGAEKQSRLLEEKVRALNKLVSRIAPAALS 1448
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| FRQ1 |
COG5126 |
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
212-258 |
7.88e-06 |
|
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 47.09 E-value: 7.88e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2217334791 212 SSGHLSEQELAVVCQSVGLqglEKEELEDLFNKLDQDGDGKVSLEEF 258
Cdd:COG5126 82 GDGKISADEFRRLLTALGV---SEEEADELFARLDTDGDGKISFEEF 125
|
|
| FRQ1 |
COG5126 |
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
202-262 |
1.09e-05 |
|
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 46.71 E-value: 1.09e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217334791 202 RGVWEELGVGSSGHLSEQELAVVCQSVGLQGLEkEELEDLFNKLDQDGDGKVSLEEFQLGL 262
Cdd:COG5126 36 ATLFSEADTDGDGRISREEFVAGMESLFEATVE-PFARAAFDLLDTDGDGKISADEFRRLL 95
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1164-1438 |
1.36e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.07 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1164 KNDLGRVRQELEAAESTHDAQRKEIEVLKKDKEKAcsemevlnrqnQNYKDQLSQL-NVRVLQLGQEASTHQAQNEEHRV 1242
Cdd:TIGR02169 176 LEELEEVEENIERLDLIIDEKRQQLERLRREREKA-----------ERYQALLKEKrEYEGYELLKEKEALERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1243 TIQMLTQSLEEVVRSGQQQSDQIQKLRVELECLN--------QEHQSLQLPWSELTQTLEESQDQVQGAHLRLRQAQAQH 1314
Cdd:TIGR02169 245 QLASLEEELEKLTEEISELEKRLEEIEQLLEELNkkikdlgeEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERL 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1315 lqevrlvpQDRVAELHRLLSlQGEQARRRLDAQReeheKQLKATEERVEEAEMILKNMEMLLQEKVDKLKEQFEK----N 1390
Cdd:TIGR02169 325 --------AKLEAEIDKLLA-EIEELEREIEEER----KRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDElkdyR 391
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2217334791 1391 TKSDLLLKELYVENAHLVRALqatEEKQRGAEKQSRLLEEKVRALNKL 1438
Cdd:TIGR02169 392 EKLEKLKREINELKRELDRLQ---EELQRLSEELADLNAAIAGIEAKI 436
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1029-1403 |
1.67e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.75 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1029 LRPAASCRGQAERLQAIQEE--RARSWSRGTQE--QASEQQARAEGALEPGCHKHSVEVARRGSLPShlQLADPQGSWQE 1104
Cdd:PTZ00121 1410 LKKAAAAKKKADEAKKKAEEkkKADEAKKKAEEakKADEAKKKAEEAKKAEEAKKKAEEAKKADEAK--KKAEEAKKADE 1487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1105 QLAAPEEGETKIALEREKDDMETKLLHLE--------DVVRALEKHVDLRENDRLEFHRLSEE----NTLLKNDLGRVRQ 1172
Cdd:PTZ00121 1488 AKKKAEEAKKKADEAKKAAEAKKKADEAKkaeeakkaDEAKKAEEAKKADEAKKAEEKKKADElkkaEELKKAEEKKKAE 1567
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1173 ELEAAESTHDAQRKEIEVLKKDKEKACSEMEVLNRQNQNYKDQlsqlNVRVLQLGQEASTHQAQNEEHRVTIQMLTQSLE 1252
Cdd:PTZ00121 1568 EAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE----EAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEA 1643
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1253 EVVRSGQQQSDQIQKLRVELECLNQEHQSLQLPWSELTQtlEESQDQVQGAHLRLRQAQAQHLQEVRLVPQDRVAELHRL 1332
Cdd:PTZ00121 1644 EEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKK--AEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEEL 1721
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217334791 1333 LSLQGEQARRRLDAQREEHEKQLKATEERVEEAEmilknmemllQEKVDKLKEQFEKNTKSDLLLKELYVE 1403
Cdd:PTZ00121 1722 KKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE----------KKKIAHLKKEEEKKAEEIRKEKEAVIE 1782
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1166-1438 |
1.81e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 49.67 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1166 DLGRVRQELEAAESTHDAQRKEI-EVLK----------------KDKEKACSEMEVLNRQNQNYKDQLSQ---------- 1218
Cdd:PRK10929 24 DEKQITQELEQAKAAKTPAQAEIvEALQsalnwleerkgsleraKQYQQVIDNFPKLSAELRQQLNNERDeprsvppnms 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1219 ---LNVRVLQLGQE--ASTHQAQNEEHRvtIQMLTQSLEEVvrsGQQQSDqIQKLrvelecLNQEHQSLQLPWSELTqTL 1293
Cdd:PRK10929 104 tdaLEQEILQVSSQllEKSRQAQQEQDR--AREISDSLSQL---PQQQTE-ARRQ------LNEIERRLQTLGTPNT-PL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1294 EESQDQVQGAHLRLRQAQAQHLQEVRLVPQDRvAELHRLLSLQGEQARRRLDAQREEHEKQLKAteERVEEAEMILKNME 1373
Cdd:PRK10929 171 AQAQLTALQAESAALKALVDELELAQLSANNR-QELARLRSELAKKRSQQLDAYLQALRNQLNS--QRQREAERALESTE 247
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217334791 1374 MLLQEKVD---KLKEQFEKNtksdlllKELYVENAHLVRALQATEEKQRGAEKQSrlleEKVR-ALNKL 1438
Cdd:PRK10929 248 LLAEQSGDlpkSIVAQFKIN-------RELSQALNQQAQRMDLIASQQRQAASQT----LQVRqALNTL 305
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
340-579 |
1.82e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.55 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 340 REILQSLDFSVDEKVNLLEltwALDNELMTVDSAVQQAALACYHQELSYQ--QGQVEQLARERDKARQDLERAEKRNLEF 417
Cdd:COG1196 238 EAELEELEAELEELEAELE---ELEAELAELEAELEELRLELEELELELEeaQAEEYELLAELARLEQDIARLEERRREL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 418 VKEMDDCHSTLEQLTEKKIKHLEQ--GYRERLSLLRSEVEAERELFWEQAHRQRAALEwDVGRLQAEEAGLREKLTLALK 495
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEEleELEEELEEAEEELEEAEAELAEAEEALLEAEA-ELAEAEEELEELAEELLEALR 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 496 ENSRLQKEIVEVVEKLSDSERLALKLQKDLEFVLKD--KLEPQSAELLAQEERFAAVLKEYELKCRDLQDRNDELQAELE 573
Cdd:COG1196 394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEAlaELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
....*.
gi 2217334791 574 GLWARL 579
Cdd:COG1196 474 LLEAAL 479
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1032-1440 |
2.46e-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: 48.96 E-value: 2.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1032 AASCRGQAERLQaiqeerarswsrgTQEQASEQQARAEGALEPgCHKHSVEvARRGSLPSHLQLA-----DPQGSWQEQL 1106
Cdd:pfam15921 287 ASSARSQANSIQ-------------SQLEIIQEQARNQNSMYM-RQLSDLE-STVSQLRSELREAkrmyeDKIEELEKQL 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1107 AAPEEGETKIALEREKDDMETKllHLEDVVRALEKHVDLREND----RLEFHRLSEENTLLKNDLGRVRQELEaaESTHD 1182
Cdd:pfam15921 352 VLANSELTEARTERDQFSQESG--NLDDQLQKLLADLHKREKElsleKEQNKRLWDRDTGNSITIDHLRRELD--DRNME 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1183 AQRKEiEVLKKDKEKACSEMEVLNRQNQNYKDQLSQLNVRVLQLG----------QEASTHQAQNEEHRVTIQMLTQSLE 1252
Cdd:pfam15921 428 VQRLE-ALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLEstkemlrkvvEELTAKKMTLESSERTVSDLTASLQ 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1253 EVVRSGQQQSDQIQKLRVELECLNQEHQSLqlpwseltqtleesqdQVQGAHLRLRQAQAQHLQeVRLVPQDRVAELHR- 1331
Cdd:pfam15921 507 EKERAIEATNAEITKLRSRVDLKLQELQHL----------------KNEGDHLRNVQTECEALK-LQMAEKDKVIEILRq 569
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1332 ----LLSLQGEQARRRLDAQREEHEKQLKATEERVEeaemiLKNMEMLLQEKVDKLKEQFEKntKSDLLLKELYVENAHL 1407
Cdd:pfam15921 570 qienMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLE-----LQEFKILKDKKDAKIRELEAR--VSDLELEKVKLVNAGS 642
|
410 420 430
....*....|....*....|....*....|...
gi 2217334791 1408 VRALQATEEKQrgaeKQSRLLEEKVRALNKLVS 1440
Cdd:pfam15921 643 ERLRAVKDIKQ----ERDQLLNEVKTSRNELNS 671
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1038-1440 |
2.64e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 49.07 E-value: 2.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1038 QAERLQAIQEERARSWSRGTQEQASEQQARAEGALEPGchKHSVEVARRGSLPSHL---QLADPQGSWQEQLAAPEEGET 1114
Cdd:pfam12128 600 EELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKA--SREETFARTALKNARLdlrRLFDEKQSEKDKKNKALAERK 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1115 KIALEREKD-DMETKLLHLEDVVRALEKHVDLRENDRLEFHRLSEENTLLKNDLGRVRQELEAAESTHDAQRKEIEvlkk 1193
Cdd:pfam12128 678 DSANERLNSlEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALE---- 753
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1194 dkekacsemevlnrqnQNYKDQLSQLNV---RVLQLGQEasthqaqneehrvtIQMLTQSLEEVVRSGQQQSDQIQKLRv 1270
Cdd:pfam12128 754 ----------------TWYKRDLASLGVdpdVIAKLKRE--------------IRTLERKIERIAVRRQEVLRYFDWYQ- 802
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1271 elECLNQEHQSLQLPWSELTQTLEESQDQV--QGAHLRLRQAQAQHLQEVRLVPQDRVAELHRLL-SLQGEQARRRLDAQ 1347
Cdd:pfam12128 803 --ETWLQRRPRLATQLSNIERAISELQQQLarLIADTKLRRAKLEMERKASEKQQVRLSENLRGLrCEMSKLATLKEDAN 880
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1348 REEHEKQLKATEERVEEAEMILKNMEMLLQEKVDKLKEQFEKNTKSDL------LLKELYVENAHLVRALQATEEKQRGA 1421
Cdd:pfam12128 881 SEQAQGSIGERLAQLEDLKLKRDYLSESVKKYVEHFKNVIADHSGSGLaetwesLREEDHYQNDKGIRLLDYRKLVPYLE 960
|
410
....*....|....*....
gi 2217334791 1422 EKQSRLLEEKVRALNKLVS 1440
Cdd:pfam12128 961 QWFDVRVPQSIMVLREQVS 979
|
|
| EFh_parvalbumin_like |
cd16251 |
EF-hand, calcium binding motif, found in parvalbumin-like EF-hand family; The family includes ... |
198-259 |
3.47e-05 |
|
EF-hand, calcium binding motif, found in parvalbumin-like EF-hand family; The family includes alpha- and beta-parvalbumins, and a group of uncharacterized calglandulin-like proteins. Parvalbumins are small, acidic, cytosolic EF-hand-containing Ca2+-buffer and Ca2+ transporter/shuttle proteins belonging to EF-hand superfamily. They are expressed by vertebrates in fast-twitch muscle cells, specific neurons of the central and peripheral nervous system, sensory cells of the mammalian auditory organ (Corti's cell), and some other cells, and characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix) called AB, CD, and EF, but only CD and EF can chelate metal ions, such as Ca2+ and Mg2+. Thus, they may play an additional role in Mg2+ handling. Moreover, parvalbumins represent one of the major animal allergens. In metal-bound states, parvalbumins possess a rigid and stable tertiary structure and display strong allergenicity. In contrast, the metal-free parvalbumins are intrinsically disordered, and the loss of metal ions results in a conformational change that decreases their IgE binding capacity. Furthermore, parvalbumins have been widely used as a neuronal marker for a variety of functional brain systems. They also function as a Ca2+ shuttle transporting Ca2+ from troponin-C (TnC) to the sarcoplasmic reticulum (SR) Ca2+ pump during muscle relaxation. Thus they may facilitate myocardial relaxation and play important roles in cardiac diastolic dysfunction. Parvalbumins consists of alpha- and beta- sublineages, which can be distinguished on the basis of isoelectric point (pI > 5 for alpha; pI
Pssm-ID: 319994 [Multi-domain] Cd Length: 101 Bit Score: 44.06 E-value: 3.47e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217334791 198 ESQIRGVWEELGVGSSGHLSEQELAVVCQSVGLQG--LEKEELEDLFNKLDQDGDGKVSLEEFQ 259
Cdd:cd16251 33 EDQIKKVFQILDKDKSGFIEEEELKYILKGFSIAGrdLTDEETKALLAAGDTDGDGKIGVEEFA 96
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1038-1435 |
4.57e-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: 4.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1038 QAERLQAIQEERARSWSRGTQEQASEQQARAEGALEpgchKHSVEVARRGSLPSHLQLADPQGSWQEQLAApEEGETKIA 1117
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ----LEELEEAEEALLERLERLEEELEELEEALAE-LEEEEEEE 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1118 LEREKDDMETKLLHLEDVVRALEKHVDLRENDRLEFHRLSEENTLLKNDLGRVRQELEAAESTHDAQRKEIEVLKKDKEK 1197
Cdd:COG1196 441 EEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLR 520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1198 ACSEMEVLNRQNQNYKDQ---------LSQLNVRVLQLGQEASTHQAQNEEHRVTIQMLTQSLEEVVRSGQQQSDQIQKL 1268
Cdd:COG1196 521 GLAGAVAVLIGVEAAYEAaleaalaaaLQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAA 600
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1269 RVELECLNQEHQSLQLP-----------------WSELTQTLEESQDQVQGAHLRLRQAQAQHLQEVRlvpqdRVAELHR 1331
Cdd:COG1196 601 VDLVASDLREADARYYVlgdtllgrtlvaarleaALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRR-----ELLAALL 675
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1332 LLSLQGEQARRRLDAQREEHEKQLKATEERVEEAEMILKNMEMLLQEKVDKLKEQFEKNTKSDLLLKELYVENAHLVRAL 1411
Cdd:COG1196 676 EAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEE 755
|
410 420
....*....|....*....|....
gi 2217334791 1412 QATEEKQRGAEKQSRLLEEKVRAL 1435
Cdd:COG1196 756 LPEPPDLEELERELERLEREIEAL 779
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1172-1446 |
5.15e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.20 E-value: 5.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1172 QELEAAESTHDAQRKEIEVLKKDKEKACSEMEVLNRQNQNYKDQLSQLNVRVLQLGQEASTHQAQNEEHRVTIQMLTQSL 1251
Cdd:COG4372 31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1252 EEVVRSGQQQSDQIQKLRVELECLNQEHQSLQLPWSELTQTLEESQDQVQGAHLRLRQAQAQHLQEVRLVPQDRVAELHR 1331
Cdd:COG4372 111 EELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1332 LLSLQGEQARRRLDAQREEHEKQLKATEERVEEAEMILKNMEMLLQEKVDKLKEQFEKNTKSDLLLKELYVENAHLVRAL 1411
Cdd:COG4372 191 EANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVE 270
|
250 260 270
....*....|....*....|....*....|....*
gi 2217334791 1412 QATEEKQRGAEKQSRLLEEKVRALNKLVSRIAPAA 1446
Cdd:COG4372 271 KDTEEEELEIAALELEALEEAALELKLLALLLNLA 305
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1181-1446 |
5.17e-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: 5.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1181 HDAQRKEIEVLKKDKEKACS---EMEVLNRQNQNYKDQLSQLNVRVLQLGQEASTHQAQNEEHRVTIQMLTQSLEEVVRS 1257
Cdd:TIGR02169 659 SRAPRGGILFSRSEPAELQRlreRLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKER 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1258 GQQQSDQIQKLRVELECLNQEHQSLQLPWSELTQTLEESQDQVQGAHLRLRQAQAQHLQ-EVRLVPQDRVAELHRLLSLQ 1336
Cdd:TIGR02169 739 LEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQaELSKLEEEVSRIEARLREIE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1337 GEQARRRLDAQREEHEKQ-LKATEERVEEAEMILKNMEMLLQEKVDKLKEQFEKNTKSdllLKELYVENAHLVRALQATE 1415
Cdd:TIGR02169 819 QKLNRLTLEKEYLEKEIQeLQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAA---LRDLESRLGDLKKERDELE 895
|
250 260 270
....*....|....*....|....*....|.
gi 2217334791 1416 EKQRGAEKQSRLLEEKVRALNKLVSRIAPAA 1446
Cdd:TIGR02169 896 AQLRELERKIEELEAQIEKKRKRLSELKAKL 926
|
|
| EF-hand_5 |
pfam13202 |
EF hand; |
238-259 |
6.55e-05 |
|
EF hand;
Pssm-ID: 433035 [Multi-domain] Cd Length: 25 Bit Score: 41.15 E-value: 6.55e-05
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1249-1449 |
6.78e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.74 E-value: 6.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1249 QSLEEVVRSGQQQSDQIQKLRVELECLNQEHQSLQLPWSELTQTLEESQDQVQGAHLRLRQAQAQHLQEvrlvpQDRVAE 1328
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL-----EERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1329 LHRLLSLQGEQaRRRLDAQREEHEKQLKATEERVEEaemilknmemlLQEKVDKLKEQFEKNTKS-DLLLKELYVENAHL 1407
Cdd:TIGR02168 752 LSKELTELEAE-IEELEERLEEAEEELAEAEAEIEE-----------LEAQIEQLKEELKALREAlDELRAELTLLNEEA 819
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2217334791 1408 VRALQATEEKQRGAEKQSRLLEEKVRALNKLVSRIAPAALSV 1449
Cdd:TIGR02168 820 ANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEI 861
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1043-1446 |
7.01e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 47.64 E-value: 7.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1043 QAIQEERARswsRGTQEQ-ASEQQARAEGALEPGCHKhsvevARRGSLPSHLQLA-DPQGSWQEQLAAPEegetkiALER 1120
Cdd:COG3096 286 RALELRREL---FGARRQlAEEQYRLVEMARELEELS-----ARESDLEQDYQAAsDHLNLVQTALRQQE------KIER 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1121 EKDDMETKLLHLEDVVRALEKHVDLRENDRLEFHRLSEENTLLKNDLGRVRQELEAAESTHDAQRKEIEVLkkDKEKACS 1200
Cdd:COG3096 352 YQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQAVQAL--EKARALC 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1201 EMEVLNRQN-----QNYKDQLSQLNVRVLQLGQEASTHQAQNEEHRVTIQMLTQSLEEVVRS--GQQQSDQIQKLRvELE 1273
Cdd:COG3096 430 GLPDLTPENaedylAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIAGEVERSqaWQTARELLRRYR-SQQ 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1274 CLNQEHQSLQLPWSELTQtLEESQDQVQgahlRLRQAQAQHLQEVRlvpqDRVAELHRLLSlqgeqarrRLDAQREEHEK 1353
Cdd:COG3096 509 ALAQRLQQLRAQLAELEQ-RLRQQQNAE----RLLEEFCQRIGQQL----DAAEELEELLA--------ELEAQLEELEE 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1354 QLkateERVEEAEMILKNMEMLLQEKVDKLKEQFEKNTKSDLLLKEL------YVENAHLV-RALQATEEKQRGAEKQSR 1426
Cdd:COG3096 572 QA----AEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERLreqsgeALADSQEVtAAMQQLLEREREATVERD 647
|
410 420
....*....|....*....|
gi 2217334791 1427 LLEEKVRALNKLVSRIAPAA 1446
Cdd:COG3096 648 ELAARKQALESQIERLSQPG 667
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1036-1431 |
9.08e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.44 E-value: 9.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1036 RGQAERLQAIQEERARSwsRGTQEQASEQQARAEGALEPGCHKHSVEVARRGSlpSHLQLADPQGSWQEQLAAPEEGETK 1115
Cdd:PTZ00121 1377 KKKADAAKKKAEEKKKA--DEAKKKAEEDKKKADELKKAAAAKKKADEAKKKA--EEKKKADEAKKKAEEAKKADEAKKK 1452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1116 IALEREKDDMETKLLHLEDVVRALEKHVDLRENDrlEFHRLSEENTLLKNDLGRVRQELEAAESTHDAQ-RKEIEVLKKD 1194
Cdd:PTZ00121 1453 AEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKAD--EAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEeAKKADEAKKA 1530
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1195 KEKACSEmEVLNRQNQNYKDQLSQLNvRVLQLGQEASTHQAQNEEHRVtiQMLTQSLEEVVRSGQQQSDQIQKLRVELEC 1274
Cdd:PTZ00121 1531 EEAKKAD-EAKKAEEKKKADELKKAE-ELKKAEEKKKAEEAKKAEEDK--NMALRKAEEAKKAEEARIEEVMKLYEEEKK 1606
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1275 LNQEhqslQLPWSELTQTLEESQDQVQGAHLRLRQAQAQHLQEVRLVPQDRVAElhRLLSLQGEQARRRLDAQREEHEKQ 1354
Cdd:PTZ00121 1607 MKAE----EAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAE--EENKIKAAEEAKKAEEDKKKAEEA 1680
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217334791 1355 LKATEERVEEAEMILKNMEMllQEKVDKLKEQF-EKNTKSDLLLKELYVENAHLVRALQATEEKQRGAEKQSRLLEEK 1431
Cdd:PTZ00121 1681 KKAEEDEKKAAEALKKEAEE--AKKAEELKKKEaEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEK 1756
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1036-1391 |
1.11e-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: 46.66 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1036 RGQAERLQAIQEERARSWSRGTQEQASEQQARAegalepgchkhsvEVARRGSLPSHlqladpqgswQEQLAAPEEGE-T 1114
Cdd:pfam17380 295 KMEQERLRQEKEEKAREVERRRKLEEAEKARQA-------------EMDRQAAIYAE----------QERMAMERERElE 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1115 KIALEREKDDMETklLHLEDVVRALEKhvdLRENDRLEFHRLSeentllKNDlgRVRQELEAAesthdaqrKEIEVLKKD 1194
Cdd:pfam17380 352 RIRQEERKRELER--IRQEEIAMEISR---MRELERLQMERQQ------KNE--RVRQELEAA--------RKVKILEEE 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1195 KEKACSEMEVLNRQNQNYKDQLSQLNVRVLQLGQEASTHQAQNEEHRVTIQM-LTQSLEEVVRSGQQQSDQIQKLRVELE 1273
Cdd:pfam17380 411 RQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVeRLRQQEEERKRKKLELEKEKRDRKRAE 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1274 CLNQEHQSLQLPWSELTQTLEESQDQVQGAHLRLRQAQAQHLQEVRLVPQDRvaelhrllslqgeQARRRLDAQREEHEK 1353
Cdd:pfam17380 491 EQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEER-------------RKQQEMEERRRIQEQ 557
|
330 340 350
....*....|....*....|....*....|....*....
gi 2217334791 1354 QLKATEERvEEAEMILKNMEMLLQ-EKVDKLKEQFEKNT 1391
Cdd:pfam17380 558 MRKATEER-SRLEAMEREREMMRQiVESEKARAEYEATT 595
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
376-516 |
1.13e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 376 QAALACYHQELSYQQGQVEQLARERDKARQDLERAEKRNLEF-VKEMDDCHSTLEQLTEKK--IKHLEQGYRERLSLLRS 452
Cdd:COG4913 294 EAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELeeRERRRARLEALLAALGL 373
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217334791 453 EVEAERELFWEQAHRQRAALEwdvgRLQAEEAGLREKLTLALKENSRLQKEIVEVVEKLSDSER 516
Cdd:COG4913 374 PLPASAEEFAALRAEAAALLE----ALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1117-1283 |
1.19e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1117 ALEREKDDMETKLLHLEDVVRALEKHVDLREN---------------DRLEFHRLSEENTLLKNDLGRVRQELEAAESTH 1181
Cdd:COG4913 239 RAHEALEDAREQIELLEPIRELAERYAAARERlaeleylraalrlwfAQRRLELLEAELEELRAELARLEAELERLEARL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1182 DAQRKEIEVLK--------KDKEKACSEMEVLNRQNQNYKDQLSQLNVRVLQLGQEASTHQAQNEEHRVTIQMLTQSLEE 1253
Cdd:COG4913 319 DALREELDELEaqirgnggDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEE 398
|
170 180 190
....*....|....*....|....*....|....
gi 2217334791 1254 VVRSGQQQ----SDQIQKLRVELECLNQEHQSLQ 1283
Cdd:COG4913 399 ELEALEEAlaeaEAALRDLRRELRELEAEIASLE 432
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
383-575 |
1.35e-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: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 383 HQELSYQQGQVEQLARERDKARQDLERAE------KRNLEFVK-EMDDCHSTLEQLTEKKIKhleqgYRERLSLLRSEve 455
Cdd:TIGR02169 715 SRKIGEIEKEIEQLEQEEEKLKERLEELEedlsslEQEIENVKsELKELEARIEELEEDLHK-----LEEALNDLEAR-- 787
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 456 aERELFWEQAHRQRAALEWDVGRLQAEEAGLREKLTLALKENSRLQKEIVEVVEklsdsERLALKLQKDLEFVLKDKLEP 535
Cdd:TIGR02169 788 -LSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQE-----QRIDLKEQIKSIEKEIENLNG 861
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2217334791 536 QSAELLAQEERFAAVLKEYELKCRDLQDRNDELQAELEGL 575
Cdd:TIGR02169 862 KKEELEEELEELEAALRDLESRLGDLKKERDELEAQLREL 901
|
|
| EF-hand_1 |
pfam00036 |
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ... |
237-262 |
1.46e-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: 1.46e-04
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1114-1442 |
1.49e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.55 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1114 TKIALErEKDDMETKLLhLEDVVRALEKhvDLRENDRLEFHRLSEentlLKNDlgrvRQELEAAESTHDAQRKEIEVLKK 1193
Cdd:TIGR04523 106 SKINSE-IKNDKEQKNK-LEVELNKLEK--QKKENKKNIDKFLTE----IKKK----EKELEKLNNKYNDLKKQKEELEN 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1194 DKEKACSEMEVLNRQNQNYKDQLSQLNVRVLQLgqeasthQAQNEEHRvtiqMLTQSLEEVVRSGQQQSDQIQKLRVELE 1273
Cdd:TIGR04523 174 ELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNL-------KKKIQKNK----SLESQISELKKQNNQLKDNIEKKQQEIN 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1274 CLNQEHQSLQLPWSELTQTLEESQDQVQGAHLRLRQAQAQHLQEvrlvpQDRVAELHRLLSLQGEQARRRLDaqrEEHEK 1353
Cdd:TIGR04523 243 EKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKEL-----EKQLNQLKSEISDLNNQKEQDWN---KELKS 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1354 QLKATEERVEEAEMILKNMEmllqEKVDKLKEQFEKNTKSdllLKELYVENAHLVRALqatEEKQRGAEKQSRLLEEKVR 1433
Cdd:TIGR04523 315 ELKNQEKKLEEIQNQISQNN----KIISQLNEQISQLKKE---LTNSESENSEKQREL---EEKQNEIEKLKKENQSYKQ 384
|
....*....
gi 2217334791 1434 ALNKLVSRI 1442
Cdd:TIGR04523 385 EIKNLESQI 393
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1172-1443 |
1.60e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 46.50 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1172 QELEAAESTHDAQRKEIEVLKKDKEKACSEMEVLNRQNQNYK---DQLSQLNVRVLQLGQEasthqaqNEEHRVTIQMLT 1248
Cdd:TIGR00618 542 TSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKediPNLQNITVRLQDLTEK-------LSEAEDMLACEQ 614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1249 QSLEEvvrsgqQQSDQIQKLRVELEcLNQEHQSLQLPWSELTQTLEE-SQDQVQGAHLRLRQAQAQHLQEVRLVPQdrvA 1327
Cdd:TIGR00618 615 HALLR------KLQPEQDLQDVRLH-LQQCSQELALKLTALHALQLTlTQERVREHALSIRVLPKELLASRQLALQ---K 684
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1328 ELHRLLSLQG--EQARRRLDAQREEHEKQLKATEERVEEAEMI------LKNMEMLLQEKVDKLKEQFekntksDLLLKE 1399
Cdd:TIGR00618 685 MQSEKEQLTYwkEMLAQCQTLLRELETHIEEYDREFNEIENASsslgsdLAAREDALNQSLKELMHQA------RTVLKA 758
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2217334791 1400 LyvENAHLVRALQATEEKQRGAEKQ--SRLLEEKVRALNKLVSRIA 1443
Cdd:TIGR00618 759 R--TEAHFNNNEEVTAALQTGAELShlAAEIQFFNRLREEDTHLLK 802
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1173-1438 |
1.97e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 45.29 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1173 ELEAAESTHDAQRKEIEVLKKDKEKacsemevLNRQNQNYKDQLSQLNVRVLQLGQEASTHQAQNEEHRVTIQMLTQSLE 1252
Cdd:COG1340 9 SLEELEEKIEELREEIEELKEKRDE-------LNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1253 EVVRSGQQQSDQIQKLRVELECLNQEHQSL--------QLPWSELTQTL---EESQ--DQVQGAHLRLRQAQAQHLQEVR 1319
Cdd:COG1340 82 ELNEKLNELREELDELRKELAELNKAGGSIdklrkeieRLEWRQQTEVLspeEEKElvEKIKELEKELEKAKKALEKNEK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1320 LvpQDRVAELhRLLSLQGEQARRRLDAQREEHEKQLKATEERVEEAEMILKNMEML------LQEKVDKLKEQFEKntks 1393
Cdd:COG1340 162 L--KELRAEL-KELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELhkeiveAQEKADELHEEIIE---- 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2217334791 1394 dllLKELYVENAHLVRALQATEEKQRGAEKQSRLLEEKVRALNKL 1438
Cdd:COG1340 235 ---LQKELRELRKELKKLRKKQRALKREKEKEELEEKAEEIFEKL 276
|
|
| EFh |
smart00054 |
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ... |
237-258 |
2.35e-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: 2.35e-04
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1030-1432 |
2.38e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 45.66 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1030 RPAASCRGQAERL--QAIQEERARSWSRGTQEQASEQQARAEGALEPGCHKHSVEVARRGSLPS--HLQLADPQGSwQEQ 1105
Cdd:PLN02939 30 RLAVSCRARRRGFssQQKKKRGKNIAPKQRSSNSKLQSNTDENGQLENTSLRTVMELPQKSTSSddDHNRASMQRD-EAI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1106 LAAPEEgetkiALEREKDDMETKLLHLEDVVRALekhvdlrendrlefhRLSEENTLLKNDlGRVR--QELEAAESTHDA 1183
Cdd:PLN02939 109 AAIDNE-----QQTNSKDGEQLSDFQLEDLVGMI---------------QNAEKNILLLNQ-ARLQalEDLEKILTEKEA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1184 QRKEIEVLKKDKEKACSEM----------EVLNRQNQNYKDQLSQLNVR----VLQLGQEASTHQAQNEEHRVTIQMLTQ 1249
Cdd:PLN02939 168 LQGKINILEMRLSETDARIklaaqekihvEILEEQLEKLRNELLIRGATeglcVHSLSKELDVLKEENMLLKDDIQFLKA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1250 SLEEVVRSGQQqsdqiqklrveLECLNQEHQSLQLPWSELTQTLEESQDQVqgahLRLRQAQAQHLQEvrlvpqdRVAEL 1329
Cdd:PLN02939 248 ELIEVAETEER-----------VFKLEKERSLLDASLRELESKFIVAQEDV----SKLSPLQYDCWWE-------KVENL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1330 HRLLSL---QGEQARRRLDaQREEHEKQLKATEERVEEAEMILKNMEM--LLQEKVDKLKEQFEKNTKSDLLLKELYven 1404
Cdd:PLN02939 306 QDLLDRatnQVEKAALVLD-QNQDLRDKVDKLEASLKEANVSKFSSYKveLLQQKLKLLEERLQASDHEIHSYIQLY--- 381
|
410 420
....*....|....*....|....*...
gi 2217334791 1405 AHLVRALQATEEKQRgAEKQSRLLEEKV 1432
Cdd:PLN02939 382 QESIKEFQDTLSKLK-EESKKRSLEHPA 408
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1117-1302 |
2.38e-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: 45.83 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1117 ALEREKDDMETKLLHLE-DVVRALEKHVDLR---ENDRLEFHRLSEENTLLKNDLGRVRQELEAAESTHDAQRKEIEVLK 1192
Cdd:TIGR02169 312 EKERELEDAEERLAKLEaEIDKLLAEIEELEreiEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYR 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1193 KDKEKACSEMEVLNRQNQNYKDQLSQLNVRVLQLGQEASTHQAQ-------NEEHRVTIQMLTQSLEEVVRSGQQQSDQI 1265
Cdd:TIGR02169 392 EKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKineleeeKEDKALEIKKQEWKLEQLAADLSKYEQEL 471
|
170 180 190
....*....|....*....|....*....|....*..
gi 2217334791 1266 QKLRVELECLNQEHQSLQLPWSELTQTLEESQDQVQG 1302
Cdd:TIGR02169 472 YDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRG 508
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1182-1365 |
2.95e-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: 2.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1182 DAQRKeIEVLKKDKEKACSEMEVLNRQNQNYKDQLSQLNVR--VLQLGQEASTHQAQNEEHRVTIQMLTQSLEEVVRSgq 1259
Cdd:COG4913 607 DNRAK-LAALEAELAELEEELAEAEERLEALEAELDALQERreALQRLAEYSWDEIDVASAEREIAELEAELERLDAS-- 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1260 qqSDQIQKLRVELECLNQEHQSLQLPWSELTQTLEESQDQVQGAHLRLRQAQAQHLQEVRLVPQDRVAEL-HRLLSLQGE 1338
Cdd:COG4913 684 --SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLeERFAAALGD 761
|
170 180 190
....*....|....*....|....*....|.
gi 2217334791 1339 ----QARRRLDAQREEHEKQLKATEERVEEA 1365
Cdd:COG4913 762 averELRENLEERIDALRARLNRAEEELERA 792
|
|
| EF-hand_6 |
pfam13405 |
EF-hand domain; |
237-262 |
3.31e-04 |
|
EF-hand domain;
Pssm-ID: 463869 [Multi-domain] Cd Length: 30 Bit Score: 39.08 E-value: 3.31e-04
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1145-1378 |
3.32e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 3.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1145 LRENDRLEFHRLSEENTLLKNDLGRVRQELEAAEsthdaqrKEIEVLKKDkekacSEMEVLNRQNQNYKDQLSQLNVRVL 1224
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAE-------AALEEFRQK-----NGLVDLSEEAKLLLQQLSELESQLA 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1225 QLGQEASTHQAQNEEHRVTIQMLTQSLEEVVRSGQQQS--DQIQKLRVELeclnqehqslqlpwSELTQTLEESQDQVQG 1302
Cdd:COG3206 230 EARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQlrAQLAELEAEL--------------AELSARYTPNHPDVIA 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1303 AHLRLRQAQAQHLQEVRLVPQDRVAELhRLLSLQGEQARRRLDAQRE------EHEKQLKATEERVEEAEMILKNMEMLL 1376
Cdd:COG3206 296 LRAQIAALRAQLQQEAQRILASLEAEL-EALQAREASLQAQLAQLEArlaelpELEAELRRLEREVEVARELYESLLQRL 374
|
..
gi 2217334791 1377 QE 1378
Cdd:COG3206 375 EE 376
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1113-1436 |
4.47e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 45.04 E-value: 4.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1113 ETKIALEREKDDMETKLLHLEDVVRALEKHVDLRENDRLEFHRLSEentLLKNDLGRVRQELEAAESTHDAQRKEIEVLK 1192
Cdd:TIGR00606 688 QTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAP---GRQSIIDLKEKEIPELRNKLQKVNRDIQRLK 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1193 KDKEKACSEMEVLNRQNQNYKDQLSQLNVrvlqlgqeasthqaqneehrvtIQMLTQSLEEVVRSGQQQSDQIQKLRVEL 1272
Cdd:TIGR00606 765 NDIEEQETLLGTIMPEEESAKVCLTDVTI----------------------MERFQMELKDVERKIAQQAAKLQGSDLDR 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1273 EC--LNQEHQSLQLPWSELTQTLEESQDQVQGahlrlRQAQAQHLQEvrlvpqdRVAEL--HRLLSLQGEQARRRLDAQR 1348
Cdd:TIGR00606 823 TVqqVNQEKQEKQHELDTVVSKIELNRKLIQD-----QQEQIQHLKS-------KTNELksEKLQIGTNLQRRQQFEEQL 890
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1349 EEHEKQLK----ATEERVEEAEMILKNMEMLLQEKVDKLKEQFEKNTKSDLLLKELYVENAHLVRALQATEEK-QRGAEK 1423
Cdd:TIGR00606 891 VELSTEVQslirEIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKiQDGKDD 970
|
330
....*....|...
gi 2217334791 1424 QSRLLEEKVRALN 1436
Cdd:TIGR00606 971 YLKQKETELNTVN 983
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1120-1435 |
5.30e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.78 E-value: 5.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1120 REKDDMETKLLHLEDVV-RALEKHVDLRENDRlEFHRLSEENTLLKNDLgRVRQELEA-AESTH---DAQRKEIEVLKKD 1194
Cdd:pfam01576 2 RQEEEMQAKEEELQKVKeRQQKAESELKELEK-KHQQLCEEKNALQEQL-QAETELCAeAEEMRarlAARKQELEEILHE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1195 KEKACSEMEVLNRQNQNYKDQLSQlNVRVL--QLGQEASTHQAQNEEhRVTIQMLTQSLEEVVRSGQQQSDQIQKlrvel 1272
Cdd:pfam01576 80 LESRLEEEEERSQQLQNEKKKMQQ-HIQDLeeQLDEEEAARQKLQLE-KVTTEAKIKKLEEDILLLEDQNSKLSK----- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1273 eclnqEHQSLQLPWSELTQTLEESQDQVQG-AHLRLRQAQAQHLQEVRLVPQDRvaelhrlLSLQGEQARRRLDAQREEH 1351
Cdd:pfam01576 153 -----ERKLLEERISEFTSNLAEEEEKAKSlSKLKNKHEAMISDLEERLKKEEK-------GRQELEKAKRKLEGESTDL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1352 EKQLKATEERVEEAEMILKNMEMLLQEKVDKLKEQFEKNTKSDLLLKELYVENAHLVRALQATEEKQRGAEKQSRLLEEK 1431
Cdd:pfam01576 221 QEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEE 300
|
....
gi 2217334791 1432 VRAL 1435
Cdd:pfam01576 301 LEAL 304
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1144-1443 |
5.35e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 44.83 E-value: 5.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1144 DLRENDRLEFHRLSEEntlLKNDLGRVRQELEAAESTHDAQRKEIEVLKKDKEKACSEMEVLNRQNQNYKDQLSQLNVRV 1223
Cdd:pfam12128 586 DLKRIDVPEWAASEEE---LRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEK 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1224 ----LQLGQEASTHQAQNEEHRVTIQ-MLTQSLEEVVRSGQQQSDQIQKLRVELeclnqehqslQLPWSELTQTLEESQD 1298
Cdd:pfam12128 663 qsekDKKNKALAERKDSANERLNSLEaQLKQLDKKHQAWLEEQKEQKREARTEK----------QAYWQVVEGALDAQLA 732
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1299 QVQGAHLRLRQAQAQHLQEVRlvpqdrvAELHRLLSLQG--EQARRRLDAQREEHEKQLKATEERVEEAEMILKNMEMLL 1376
Cdd:pfam12128 733 LLKAAIAARRSGAKAELKALE-------TWYKRDLASLGvdPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETW 805
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217334791 1377 QEKVDKLKEQFEKNTKSDLLLKELYVENAHLVRALQATEEKQRGA-EKQSRLLEEKVRALNKLVSRIA 1443
Cdd:pfam12128 806 LQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKAsEKQQVRLSENLRGLRCEMSKLA 873
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1110-1437 |
5.39e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 5.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1110 EEGETKIALEREKDDMETKLLHLEDVVRALEKHVDLRENDRLEFHRLSEENTLLKNDLGRVRQELEAAESTHDAQRKEIE 1189
Cdd:PRK03918 197 EKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1190 VLKKD-------KEKAcSEMEVLNRQNQNYKDQLSQLNVRVLQLGQEASTHQAQ---NEEHRVTIQMLTQSLEEVVR--- 1256
Cdd:PRK03918 277 ELEEKvkelkelKEKA-EEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERikeLEEKEERLEELKKKLKELEKrle 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1257 ----------SGQQQSDQIQKLRVELECLNQEH------------QSLQLPWSELTQ---TLEESQDQVQGAHLRLRQAQ 1311
Cdd:PRK03918 356 eleerhelyeEAKAKKEELERLKKRLTGLTPEKlekeleelekakEEIEEEISKITArigELKKEIKELKKAIEELKKAK 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1312 AQHLQEVRLVPQDRVAELHRLLSLQGEQARRRLdAQREEHEKQLKATEERVE----EAEMILKNMEML-----LQEKVDK 1382
Cdd:PRK03918 436 GKCPVCGRELTEEHRKELLEEYTAELKRIEKEL-KEIEEKERKLRKELRELEkvlkKESELIKLKELAeqlkeLEEKLKK 514
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2217334791 1383 L-KEQFEKNTKSDLLLKELYVENAHLVRALQATEEKQRGAEKQSRLLEEKVRALNK 1437
Cdd:PRK03918 515 YnLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEE 570
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1103-1437 |
5.67e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 5.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1103 QEQLAAPEEGETKIA-LEREKDDMETKLLHLEDVVRALEKHVDLRENDRLEfhrLSEENTLLKNDLGRVRQELEAAESTH 1181
Cdd:PRK02224 240 DEVLEEHEERREELEtLEAEIEDLRETIAETEREREELAEEVRDLRERLEE---LEEERDDLLAEAGLDDADAEAVEARR 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1182 DAQRKEIEVLKKDKEKACSEMEVLNRQNQNYKDQLSQLNVRVLQLGQEASTHQAQNEEHRVTIQMLTQSLEEVVRSGQQQ 1261
Cdd:PRK02224 317 EELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEEL 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1262 SDQIQKLRVELECLNQEHQSLQLPWSELTQTLEESQDQVQGAHLRLRQAQA-----------QHLQEVRLVP-----QDR 1325
Cdd:PRK02224 397 RERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEAlleagkcpecgQPVEGSPHVEtieedRER 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1326 VAELHRLLslqgEQARRRLDAQREEHE--KQLKATEERVEEAEMILKNMEMLLQEKVDKLKEQFEKntksdllLKELYVE 1403
Cdd:PRK02224 477 VEELEAEL----EDLEEEVEEVEERLEraEDLVEAEDRIERLEERREDLEELIAERRETIEEKRER-------AEELRER 545
|
330 340 350
....*....|....*....|....*....|....
gi 2217334791 1404 NAHLVRALQATEEKQRGAEKQSRLLEEKVRALNK 1437
Cdd:PRK02224 546 AAELEAEAEEKREAAAEAEEEAEEAREEVAELNS 579
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1156-1442 |
7.08e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.13 E-value: 7.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1156 LSEENTLLKNDLgrvRQELEAAESThDAQRKEIEVLKKDKEKACSEMEVLNRQNQNYKDQ-------------LSQLNVR 1222
Cdd:PRK11281 54 LEAEDKLVQQDL---EQTLALLDKI-DRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDndeetretlstlsLRQLESR 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1223 VLQLGQEASTHQ-------------------AQNE--EHRVTIQMLTQSLEEVVRSGQQQS-DQIQKLRVELECLNQ--E 1278
Cdd:PRK11281 130 LAQTLDQLQNAQndlaeynsqlvslqtqperAQAAlyANSQRLQQIRNLLKGGKVGGKALRpSQRVLLQAEQALLNAqnD 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1279 HQSLQLPWSELTQTLEESQDQVQGAHLRLRQAQAQHLQEVRlvpqdrvaelhrllslqgeqarrrldaqreeHEKQLKAT 1358
Cdd:PRK11281 210 LQRKSLEGNTQLQDLLQKQRDYLTARIQRLEHQLQLLQEAI-------------------------------NSKRLTLS 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1359 EERVEEAEmilkNMEMLLQEKVDKL-KEQFEKNTK-SDLLLK-----------ELYVENAhLVRALQATeekqrgaekqs 1425
Cdd:PRK11281 259 EKTVQEAQ----SQDEAARIQANPLvAQELEINLQlSQRLLKateklntltqqNLRVKNW-LDRLTQSE----------- 322
|
330
....*....|....*....
gi 2217334791 1426 RLLEEKVRALNK--LVSRI 1442
Cdd:PRK11281 323 RNIKEQISVLKGslLLSRI 341
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
388-708 |
9.39e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 43.81 E-value: 9.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 388 YQQGQVEQLARERDKARQDLERAEKRNLEFVKEMDdchstleqlTEKKIKHLEQGYRERLSLLRSEVEAERELFWEQAHR 467
Cdd:pfam02463 139 VQGGKIEIIAMMKPERRLEIEEEAAGSRLKRKKKE---------ALKKLIEETENLAELIIDLEELKLQELKLKEQAKKA 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 468 QRAALEWDVGRLQAEEAGLREKLTLALKENSRLQKEIVEVVEKLSDSERLALKLQKDLEFVLKD------KLEPQSAELL 541
Cdd:pfam02463 210 LEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKEnkeeekEKKLQEEELK 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 542 AQEERFAAVLKEYELKCRDLQDRNDELQAELEGLwARLPKNRHSPSWSPDGRRRQLpglgpagISFLGNSAPVSIETELM 621
Cdd:pfam02463 290 LLAKEEEELKSELLKLERRKVDDEEKLKESEKEK-KKAEKELKKEKEEIEELEKEL-------KELEIKREAEEEEEEEL 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 622 MEQVKEHYQDLRTQLETKVNYYEREIAALKRNFE-KERKDMEQARRREVSVLEGQKADLEELHEKSQEVIWGLQEQLQDT 700
Cdd:pfam02463 362 EKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEeLELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIEL 441
|
....*...
gi 2217334791 701 ARGPEPEQ 708
Cdd:pfam02463 442 KQGKLTEE 449
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
377-579 |
1.58e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 377 AALACYHQELSYQQGQVEQLARERDKARQDLERAE---KRNLEFVKEMDDCHSTLEQLTEKKikhleqgyrerlsllrSE 453
Cdd:PRK02224 206 ERLNGLESELAELDEEIERYEEQREQARETRDEADevlEEHEERREELETLEAEIEDLRETI----------------AE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 454 VEAERELFWEQAHRQRAALEwdvgRLQAEEAGLREKLTL-------ALKENSRLQKEIVEVVEKLSDSERLALKLQKDLE 526
Cdd:PRK02224 270 TEREREELAEEVRDLRERLE----ELEEERDDLLAEAGLddadaeaVEARREELEDRDEELRDRLEECRVAAQAHNEEAE 345
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2217334791 527 FVLK--DKLEPQSAELLAQEERFAAVLKEYELKCRDLQDRNDELQAELEGLWARL 579
Cdd:PRK02224 346 SLREdaDDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERF 400
|
|
| XopAW |
NF041410 |
XopAW family type III secretion system calcium-binding effector; |
212-264 |
1.85e-03 |
|
XopAW family type III secretion system calcium-binding effector;
Pssm-ID: 469301 [Multi-domain] Cd Length: 227 Bit Score: 41.59 E-value: 1.85e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2217334791 212 SSGHLSEQELAVVCQS---VGLQGLEKEELEDLFNKLDQDGDGKVSLEEFQLGLFS 264
Cdd:NF041410 76 GDGSLSSDELAAAAPPpppPPDQAPSTELADDLLSALDTDGDGSISSDELSAGLTS 131
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1007-1432 |
1.93e-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: 42.80 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1007 ELPLLGTERDA-SQTQPRMWEPPLRPAASCRGQAERLQAIQEERARSWSRGTQEQASEQQARAEgalepgCHKHSVEVAR 1085
Cdd:pfam15921 357 ELTEARTERDQfSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRE------LDDRNMEVQR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1086 RGSLPSHLQlADPQGSWQEQLAA---------------PEEGETKIALEREKDDMETKLLHLEDVVRALEK-HVDLREND 1149
Cdd:pfam15921 431 LEALLKAMK-SECQGQMERQMAAiqgkneslekvssltAQLESTKEMLRKVVEELTAKKMTLESSERTVSDlTASLQEKE 509
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1150 RlEFHRLSEENTLLKNDLGRVRQELEAAESTHDAQRK---EIEVLKKDKEKACSEMEVLNRQNQNykdqLSQLnvrVLQL 1226
Cdd:pfam15921 510 R-AIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNvqtECEALKLQMAEKDKVIEILRQQIEN----MTQL---VGQH 581
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1227 GQEASTHQAQNEEHRVTIQMLTQSLEEVVRSGQQQSDQIQKLRVELECLNQEHQSLQLPWSELTQTLEEsqdqvqgahlr 1306
Cdd:pfam15921 582 GRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKD----------- 650
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1307 LRQAQAQHLQEVRLVPQD--RVAELHRLLSLQGEQARRRLDAQREEHEKQLKATEERVEEAEMILKNMEM---------- 1374
Cdd:pfam15921 651 IKQERDQLLNEVKTSRNElnSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGsdghamkvam 730
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217334791 1375 --------------LLQEKVDKLKEQFEKNTKSDLLLKElyvENAHLVRALQ--ATEEKQRGAE-----KQSRLLEEKV 1432
Cdd:pfam15921 731 gmqkqitakrgqidALQSKIQFLEEAMTNANKEKHFLKE---EKNKLSQELStvATEKNKMAGElevlrSQERRLKEKV 806
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1117-1273 |
1.96e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1117 ALEREKDDMETKLLHLEDVVRALEKHVDLRENDRLEFHRLSEENTL------LKNDLGRVRQELEAAESTHD-------- 1182
Cdd:COG4913 614 ALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDeidvasAEREIAELEAELERLDASSDdlaaleeq 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1183 --AQRKEIEVLKKDKEKACSEMEVLNRQNQNYKDQLSQLNVRVLQLGQEASTHQAQNEEHRVTIQMLTQSLEEVVRSGQQ 1260
Cdd:COG4913 694 leELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEE 773
|
170
....*....|...
gi 2217334791 1261 QSDQIQKLRVELE 1273
Cdd:COG4913 774 RIDALRARLNRAE 786
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
388-578 |
2.08e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 388 YQQGQVEQLARERDKARQDLERAEKRNLEFVKEMDDCHSTLEQLTEKkikhleqgyRERLSLLRSEVEAERElfweQAHR 467
Cdd:COG4913 264 YAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAE---------LERLEARLDALREELD----ELEA 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 468 QRAALEWD-VGRLQAEEAGLREKLTLALKENSRLQKEIVEVVEKLSDSERLALKLQKDLEfVLKDKLEPQSAELlaQEER 546
Cdd:COG4913 331 QIRGNGGDrLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAA-ALLEALEEELEAL--EEAL 407
|
170 180 190
....*....|....*....|....*....|..
gi 2217334791 547 FAAVLKEyelkcRDLQDRNDELQAELEGLWAR 578
Cdd:COG4913 408 AEAEAAL-----RDLRRELRELEAEIASLERR 434
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1039-1350 |
2.44e-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: 42.63 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1039 AERLQAIQEERArswsrGTQEQASEQQARAEGALEpgchkhsvEVARRGSlpshlQLADPQ----------GSWQEQLAA 1108
Cdd:COG3096 360 TERLEEQEEVVE-----EAAEQLAEAEARLEAAEE--------EVDSLKS-----QLADYQqaldvqqtraIQYQQAVQA 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1109 PEE-----GETKIALEREKDDMET---KLLHLEDVVRALEKHVDLRENDRLEFHRLSEentLLKNDLGRV---------R 1171
Cdd:COG3096 422 LEKaralcGLPDLTPENAEDYLAAfraKEQQATEEVLELEQKLSVADAARRQFEKAYE---LVCKIAGEVersqawqtaR 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1172 QELEAAEStHDAQRKEIEVLKKdkekACSEMEVLNRQNQNYKDQLSQLNVRVLQLGQEASTHQAQNEEHRVTIQMLTQSL 1251
Cdd:COG3096 499 ELLRRYRS-QQALAQRLQQLRA----QLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQA 573
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1252 EEvvrSGQQQSDqiqkLRVELECLNQEHQSL--QLP-WSELTQTLEESQDQVqGAHLRLRQAQAQHLQevRLVPQDRVAE 1328
Cdd:COG3096 574 AE---AVEQRSE----LRQQLEQLRARIKELaaRAPaWLAAQDALERLREQS-GEALADSQEVTAAMQ--QLLEREREAT 643
|
330 340
....*....|....*....|..
gi 2217334791 1329 LHRLLSlqgEQARRRLDAQREE 1350
Cdd:COG3096 644 VERDEL---AARKQALESQIER 662
|
|
| EFh |
cd00051 |
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ... |
237-272 |
2.46e-03 |
|
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.
Pssm-ID: 238008 [Multi-domain] Cd Length: 63 Bit Score: 37.53 E-value: 2.46e-03
10 20 30
....*....|....*....|....*....|....*.
gi 2217334791 237 ELEDLFNKLDQDGDGKVSLEEFQLGLFSHEPALLLE 272
Cdd:cd00051 1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEE 36
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1258-1437 |
2.84e-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: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1258 GQQQSDQIQKLRVELECLNQEHQSLQLPWSELTQTLEESQDQ----------------VQGAHLRLRQAQAQhLQEVRLV 1321
Cdd:COG4913 605 GFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERrealqrlaeyswdeidVASAEREIAELEAE-LERLDAS 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1322 P------QDRVAELHRLLSlQGEQARRRLDAQREEHEKQLKATEERVEEAEMILKNMEMLL-QEKVDKLKEQFEKNTKSD 1394
Cdd:COG4913 684 SddlaalEEQLEELEAELE-ELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLArLELRALLEERFAAALGDA 762
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2217334791 1395 LLLKELyvenAHLVRALQATEEKQRGAEKQsrlLEEKVRALNK 1437
Cdd:COG4913 763 VERELR----ENLEERIDALRARLNRAEEE---LERAMRAFNR 798
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1099-1441 |
3.09e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 42.34 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1099 QGSWQEQLAAPEEGETKIALEREK--DDMETKLLHLEDVVRALEKHVDLRENDRLEFHRLSEEntllknDLGRVRQELEA 1176
Cdd:TIGR00606 232 QLESSREIVKSYENELDPLKNRLKeiEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEK------VFQGTDEQLND 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1177 AESTHDAQRKEIEVLKKDKEKacsEMEVLNRQNQNYKDQLSQLNVRVLQLGQEASTHQAQNEEHRVTIQMLTQSLE---- 1252
Cdd:TIGR00606 306 LYHNHQRTVREKERELVDCQR---ELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLEldgf 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1253 --------------EVVRSGQQ-------------------QSDQIQKLRVELECLNQ----EHQSLQLPWSELTQTLEE 1295
Cdd:TIGR00606 383 ergpfserqiknfhTLVIERQEdeaktaaqlcadlqskerlKQEQADEIRDEKKGLGRtielKKEILEKKQEELKFVIKE 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1296 SQDQVQGAH--LRLRQAQAQHLQEVRLVPQDRVAE--LHRLLSLQGEQAR--RRLDAQREEHEKQLKATEERveeaemil 1369
Cdd:TIGR00606 463 LQQLEGSSDriLELDQELRKAERELSKAEKNSLTEtlKKEVKSLQNEKADldRKLRKLDQEMEQLNHHTTTR-------- 534
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217334791 1370 KNMEMLLQEKVDKLKEQFEKNTK-SDLLLKEL-YVENAhlvRALQATEEKQRGAEKQSRlleEKVRALNKLVSR 1441
Cdd:TIGR00606 535 TQMEMLTKDKMDKDEQIRKIKSRhSDELTSLLgYFPNK---KQLEDWLHSKSKEINQTR---DRLAKLNKELAS 602
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1109-1214 |
3.14e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.15 E-value: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1109 PEEGETKIALEREKDDMETKLLHLEDVVRALEKHV-DLREndrlEFHRLSEENTLLKNDLGRVRQELEA-AESTHDAQR- 1185
Cdd:COG2433 395 PEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVeELEA----ELEEKDERIERLERELSEARSEERReIRKDREISRl 470
|
90 100 110
....*....|....*....|....*....|
gi 2217334791 1186 -KEIEVLKKDKEKACSEMEVLNRQNQNYKD 1214
Cdd:COG2433 471 dREIERLERELEEERERIEELKRKLERLKE 500
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
479-578 |
4.71e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 39.89 E-value: 4.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 479 LQAEEAGLREKLTLALKENSRLQKEIVEVVEKLSDSERLALKLQKDLEFVLKDK--LEPQSAELLAQEERFAAVLKEYEL 556
Cdd:pfam13851 31 LKEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLENYEKDKqsLKNLKARLKVLEKELKDLKWEHEV 110
|
90 100
....*....|....*....|..
gi 2217334791 557 kcrdLQDRNDELQAELEGLWAR 578
Cdd:pfam13851 111 ----LEQRFEKVERERDELYDK 128
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1038-1438 |
4.87e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 4.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1038 QAERLQAIQEERARSWSRGTQE--QASEQQARAEGALEPGCHKHSVEVARRGSlpSHLQLADPQGSWQEQLAAPEEGETK 1115
Cdd:PTZ00121 1279 KADELKKAEEKKKADEAKKAEEkkKADEAKKKAEEAKKADEAKKKAEEAKKKA--DAAKKKAEEAKKAAEAAKAEAEAAA 1356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1116 IALEREKDDMETKLLHLEDVVRALE----KHVDLRENDrlEFHRLSEENtllKNDLGRVRQELEAAESTHDAQRKEIEVL 1191
Cdd:PTZ00121 1357 DEAEAAEEKAEAAEKKKEEAKKKADaakkKAEEKKKAD--EAKKKAEED---KKKADELKKAAAAKKKADEAKKKAEEKK 1431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1192 KKD--KEKACSEMEVLNRQNQNYKDQLSQLNVRVLQLGQEASTHQAQNEEHRvTIQMLTQSLEEVVRSGQQ--QSDQIQK 1267
Cdd:PTZ00121 1432 KADeaKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAK-KADEAKKKAEEAKKKADEakKAAEAKK 1510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1268 LRVELECLNQEHQSLQLPWSELTQTLEESQ--DQVQGAHLRLRQAQAQHLQEVRLVPQDRVAELHRLLSL-------QGE 1338
Cdd:PTZ00121 1511 KADEAKKAEEAKKADEAKKAEEAKKADEAKkaEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALrkaeeakKAE 1590
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1339 QARRRLDAQREEHEKQLKATEERVEEAEMIlKNMEMLLQEKVDKLKEQFEKNT-----KSDLLLKElyvENAHLVRA--- 1410
Cdd:PTZ00121 1591 EARIEEVMKLYEEEKKMKAEEAKKAEEAKI-KAEELKKAEEEKKKVEQLKKKEaeekkKAEELKKA---EEENKIKAaee 1666
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2217334791 1411 -------------LQATEEKQRGAEKQSRLLEEKVRALNKL 1438
Cdd:PTZ00121 1667 akkaeedkkkaeeAKKAEEDEKKAAEALKKEAEEAKKAEEL 1707
|
|
| EFh_PI-PLC |
cd15898 |
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ... |
200-265 |
5.20e-03 |
|
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) isozymes; PI-PLC isozymes are signaling enzymes that hydrolyze the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. This family corresponds to the four EF-hand motifs containing PI-PLC isozymes, including PI-PLC-beta (1-4), -gamma (1-2), -delta (1,3,4), -epsilon (1), -zeta (1), eta (1-2). Lower eukaryotes such as yeast and slime molds contain only delta-type isozymes. In contrast, other types of isoforms present in higher eukaryotes. This family also includes 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase 1 (PLC1) from fungi. Some homologs from plants contain only two atypical EF-hand motifs and they are not included. All PI-PLC isozymes except sperm-specific PI-PLC-zeta share a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C2 domain. PI-PLC-zeta lacks the PH domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. Most of EF-hand motifs found in PI-PLCs consist of a helix-loop-helix structure, but lack residues critical to metal binding. Moreover, the EF-hand region of most of PI-PLCs may have an important regulatory function, but it has yet to be identified. However, PI-PLC-zeta is a key exception. It is responsible for Ca2+ oscillations in fertilized oocytes and exhibits a high sensitivity to Ca2+ mediated through its EF-hand domain. In addition, PI-PLC-eta2 shows a canonical EF-loop directing Ca2+-sensitivity and thus can amplify transient Ca2+ signals. Also it appears that PI-PLC-delta1 can regulate the binding of PH domain to PIP2 in a Ca2+-dependent manner through its functionally important EF-hand domains. PI-PLCs can be activated by a variety of extracellular ligands, such as growth factors, hormones, cytokines and lipids. Their activation has been implicated in tumorigenesis and/or metastasis linked to migration, proliferation, growth, inflammation, angiogenesis and actin cytoskeleton reorganization. PI-PLC-beta isozymes are activated by G-protein coupled receptor (GPCR) through different mechanisms. However, PI-PLC-gamma isozymes are activated by receptor tyrosine kinase (RTK), such as Rho and Ras GTPases. In contrast, PI-PLC-epsilon are activated by both GPCR and RTK. PI-PLC-delta1 and PLC-eta 1 are activated by GPCR-mediated calcium mobilization. The activation mechanism for PI-PLC-zeta remains unclear.
Pssm-ID: 320029 [Multi-domain] Cd Length: 137 Bit Score: 38.80 E-value: 5.20e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217334791 200 QIRGVWEELGVGSSGHLSEQELAVVCQSVGLQgLEKEELEDLFNKLDQDGDGKVSLEEFQLGLFSH 265
Cdd:cd15898 1 WLRRQWIKADKDGDGKLSLKEIKKLLKRLNIR-VSEKELKKLFKEVDTNGDGTLTFDEFEELYKSL 65
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
375-598 |
5.26e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.90 E-value: 5.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 375 QQAALACYHQELSYQQGQVEQLARERDKARQDLERAEKRNLEFVKEMDDCHSTLEQLtEKKIKHLEQgyreRLSLLRSEV 454
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAAL-EAELAELEK----EIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 455 EAERELFWE-----QAHRQRAALEWDVGRLQAEEAGLREKLTLALKENSRLQ-KEIVEVVEKLSDSERLALKLQKDLEfV 528
Cdd:COG4942 100 EAQKEELAEllralYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQaEELRADLAELAALRAELEAERAELE-A 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217334791 529 LKDKLEPQSAELLAQEERFAAVL-------KEYELKCRDLQDRNDELQAELEGLWARL-PKNRHSPSWSPDGRRRQLP 598
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLarlekelAELAAELAELQQEAEELEALIARLEAEAaAAAERTPAAGFAALKGKLP 256
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
385-575 |
6.18e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 6.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 385 ELSYQQGQVEQLARERDKARQDLERAEKRNLEFVKEMDDCHSTLEQL------TEKKIKHLEQgYRERLSLLRSEVEAER 458
Cdd:PRK03918 218 ELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELeerieeLKKEIEELEE-KVKELKELKEKAEEYI 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 459 EL--FWEQAHRQRAALEWDVGRLQAEEAGLREKLTLALKENSR---LQKEIVEVVEKLSDSERLALKLQKDLEfvLKDKL 533
Cdd:PRK03918 297 KLseFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERleeLKKKLKELEKRLEELEERHELYEEAKA--KKEEL 374
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2217334791 534 EPQSAELLAQE-ERFAAVLKEYELKCRDLQDRNDELQAELEGL 575
Cdd:PRK03918 375 ERLKKRLTGLTpEKLEKELEELEKAKEEIEEEISKITARIGEL 417
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1352-1437 |
7.28e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.97 E-value: 7.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1352 EKQLKATEERVEEAEMILKNMEML---LQEKVDKLKEQFEKnTKSDL------LLKELYVENAHLVRALQATEEKQRGAE 1422
Cdd:PRK00409 526 EELERELEQKAEEAEALLKEAEKLkeeLEEKKEKLQEEEDK-LLEEAekeaqqAIKEAKKEADEIIKELRQLQKGGYASV 604
|
90
....*....|....*
gi 2217334791 1423 KqSRLLEEKVRALNK 1437
Cdd:PRK00409 605 K-AHELIEARKRLNK 618
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1346-1435 |
7.37e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 40.25 E-value: 7.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1346 AQREEHEKQLKATEERVEEAEMILKNMEMLLQEKVDKLKEQFEKNTKSdlLLKELyvENAHLVRALQATEEKQRGAEKQS 1425
Cdd:cd16269 205 AKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKMEEEREN--LLKEQ--ERALESKLKEQEALLEEGFKEQA 280
|
90
....*....|
gi 2217334791 1426 RLLEEKVRAL 1435
Cdd:cd16269 281 ELLQEEIRSL 290
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1101-1373 |
7.62e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 40.71 E-value: 7.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1101 SWQEQLAAPEEGETKIALEREKDDMETKLLH-LEDVVRALEKhvdlrendRLEFHRLSEENTLLKNDLGRVRQELEAAES 1179
Cdd:COG5185 313 SLEEQLAAAEAEQELEESKRETETGIQNLTAeIEQGQESLTE--------NLEAIKEEIENIVGEVELSKSSEELDSFKD 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1180 THDAQRKEIEVLKKDKEKacsemevlnrQNQNYKDQLSQlnvrvlqlgqEASTHQAQNEEHRVTIQMLTQSLEEVVRSGQ 1259
Cdd:COG5185 385 TIESTKESLDEIPQNQRG----------YAQEILATLED----------TLKAADRQIEELQRQIEQATSSNEEVSKLLN 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1260 QQSDQIQKLRVELEclNQEHQSLQLPWSELTQTLEESQDQVQGAHLRLRQAQAQHLQEVRLVPQDRVAELHRLLSLQGEQ 1339
Cdd:COG5185 445 ELISELNKVMREAD--EESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQV 522
|
250 260 270
....*....|....*....|....*....|....
gi 2217334791 1340 ARRRLDAQREEHEKQLKATEERVEEAEMILKNME 1373
Cdd:COG5185 523 AESLKDFMRARGYAHILALENLIPASELIQASNA 556
|
|
| EFh_parvalbumins |
cd16253 |
EF-hand, calcium binding motif, found in parvalbumins; Parvalbumins are small, acidic, ... |
200-259 |
7.70e-03 |
|
EF-hand, calcium binding motif, found in parvalbumins; Parvalbumins are small, acidic, cytosolic EF-hand-containing Ca2+-buffer and Ca2+ transporter/shuttle proteins belonging to EF-hand superfamily. They are expressed by vertebrates in fast-twitch muscle cells, specific neurons of the central and peripheral nervous system, sensory cells of the mammalian auditory organ (Corti's cell), and some other cells, and characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix) called AB, CD, and EF, but only CD and EF can chelate metal ions, such as Ca2+ and Mg2+. Thus, they may play an additional role in Mg2+ handling. Moreover, parvalbumins represent one of the major animal allergens. In metal-bound states, parvalbumins possess a rigid and stable tertiary structure and display strong allergenicity. In contrast, the metal-free parvalbumins are intrinsically disordered, and the loss of metal ions results in a conformational change that decreases their IgE binding capacity. Furthermore, parvalbumins have been widely used as a neuronal marker for a variety of functional brain systems. They also function as a Ca2+ shuttle transporting Ca2+ from troponin-C (TnC) to the sarcoplasmic reticulum (SR) Ca2+ pump during muscle relaxation. Thus they may facilitate myocardial relaxation and play important roles in cardiac diastolic dysfunction. Parvalbumins consists of alpha- and beta- sublineages, which can be distinguished on the basis of isoelectric point (pI > 5 for alpha; pI
Pssm-ID: 319996 [Multi-domain] Cd Length: 101 Bit Score: 37.54 E-value: 7.70e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217334791 200 QIRGVWEELGVGSSGHLSEQELAVV--CQSVGLQGLEKEELEDLFNKLDQDGDGKVSLEEFQ 259
Cdd:cd16253 35 DIKKVFNILDQDKSGFIEEEELKLFlkNFSDGARVLSDKETKNFLAAGDSDGDGKIGVDEFK 96
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1103-1283 |
7.76e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 40.81 E-value: 7.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1103 QEQLAA--PEEGETKIALEREKDDMETKLLHLEDVVRALEKHVDLRENDRLEFHRLSEENTLLKNDLGRVRQELEAAEST 1180
Cdd:TIGR02168 336 AEELAEleEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDR 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1181 HDAQRKEIEVLKKDKEKAcsemevlnrqnqnykdQLSQLNVRVLQLGQEASTHQAQNEEHRVTIQMLTQSLEEVVRSGQQ 1260
Cdd:TIGR02168 416 RERLQQEIEELLKKLEEA----------------ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDA 479
|
170 180
....*....|....*....|...
gi 2217334791 1261 QSDQIQKLRVELECLNQEHQSLQ 1283
Cdd:TIGR02168 480 AERELAQLQARLDSLERLQENLE 502
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
390-697 |
7.77e-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: 40.87 E-value: 7.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 390 QGQVEQLARERDKARQDLERAEK--RNLEFVKEMddCHSTLEQLTEKKIKhLEQGYRERLSLLRSEVEAERelfweqahr 467
Cdd:pfam15921 443 QGQMERQMAAIQGKNESLEKVSSltAQLESTKEM--LRKVVEELTAKKMT-LESSERTVSDLTASLQEKER--------- 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 468 qraALEwdvgRLQAEEAGLREKLTLALKENSRLQKEIVEVVEKLSDSERLALKL-QKDLEF-VLKDKLEPQSaELLAQEE 545
Cdd:pfam15921 511 ---AIE----ATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMaEKDKVIeILRQQIENMT-QLVGQHG 582
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 546 RFA-AVLKEYELKCRDLQDRNDELQaELEGLwarlpKNRHspswspDGRRRQLPG-----------LGPAGISFLGNSAP 613
Cdd:pfam15921 583 RTAgAMQVEKAQLEKEINDRRLELQ-EFKIL-----KDKK------DAKIRELEArvsdlelekvkLVNAGSERLRAVKD 650
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 614 VSIETELMMEQVKEHYQDLrtqletkvNYYEREIAALKRNFEKERKDMEQARRREVSVLEGQKADLEELHE--KSQE--- 688
Cdd:pfam15921 651 IKQERDQLLNEVKTSRNEL--------NSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNtlKSMEgsd 722
|
330
....*....|....
gi 2217334791 689 -----VIWGLQEQL 697
Cdd:pfam15921 723 ghamkVAMGMQKQI 736
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
444-578 |
8.49e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.52 E-value: 8.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 444 RERLSLLRSEVEAERELFwEQAHRQRAALEWDVGRLQAEEAGLREKLTLA--LKENSRLQKEIvevveklsDSERLALKL 521
Cdd:COG1579 37 EDELAALEARLEAAKTEL-EDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnNKEYEALQKEI--------ESLKRRISD 107
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2217334791 522 QKDLEFVLKDKLEPQSAELLAQEERFAAVLKEYELKCRDLQDRNDELQAELEGLWAR 578
Cdd:COG1579 108 LEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
|
| PTZ00184 |
PTZ00184 |
calmodulin; Provisional |
214-258 |
9.45e-03 |
|
calmodulin; Provisional
Pssm-ID: 185504 [Multi-domain] Cd Length: 149 Bit Score: 38.20 E-value: 9.45e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2217334791 214 GHLSEQELAVVCQSVGlQGLEKEELEDLFNKLDQDGDGKVSLEEF 258
Cdd:PTZ00184 99 GFISAAELRHVMTNLG-EKLTDEEVDEMIREADVDGDGQINYEEF 142
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1039-1445 |
9.87e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 40.59 E-value: 9.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1039 AERLQAIQEERARSWSRGTQEQASEQQARAEGALEPGCHKHSVEVARrgslpSHLQLADPQgswqeQLAAPEEGETKIAL 1118
Cdd:pfam12128 275 ASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDR-----SELEALEDQ-----HGAFLDADIETAAA 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1119 EREK-DDMETKLLHLEDVVRALE-KHVDL-RENDRLEFHRLSEENTllknDLGRVRQELEAAESTHDAQRKEIEvlkKDK 1195
Cdd:pfam12128 345 DQEQlPSWQSELENLEERLKALTgKHQDVtAKYNRRRSKIKEQNNR----DIAGIKDKLAKIREARDRQLAVAE---DDL 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1196 EKACSEM-EVLNRQNQNYKDQLSQLNVRVlqlgqeasthqaqnEEHRVTIQMLTQSLEEVVRSGQQQsDQIQKLRVELEC 1274
Cdd:pfam12128 418 QALESELrEQLEAGKLEFNEEEYRLKSRL--------------GELKLRLNQATATPELLLQLENFD-ERIERAREEQEA 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1275 LNQEHQSLQLPWSELTQTLEESQDQVQGAHLRLRQaQAQHLQEVRLVPQDRVAELHRLLSLQG---EQARRRLDAQreeh 1351
Cdd:pfam12128 483 ANAEVERLQSELRQARKRRDQASEALRQASRRLEE-RQSALDELELQLFPQAGTLLHFLRKEApdwEQSIGKVISP---- 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217334791 1352 eKQLKATEERVEEAEMILKNMEMLLQEKVDKlkEQFEKNTKSDLLlKELYVENAHLVRALQATEEKQRGAEKQSRLLEEK 1431
Cdd:pfam12128 558 -ELLHRTDLDPEVWDGSVGGELNLYGVKLDL--KRIDVPEWAASE-EELRERLDKAEEALQSAREKQAAAEEQLVQANGE 633
|
410
....*....|....
gi 2217334791 1432 VRALNKLVSRIAPA 1445
Cdd:pfam12128 634 LEKASREETFARTA 647
|
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