|
Name |
Accession |
Description |
Interval |
E-value |
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
122-584 |
1.75e-176 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 513.29 E-value: 1.75e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 122 RPMDELVTLEEA----DGGSDILLVVPKATVLQNQLDESQQERNDLMQL------------------KLQLEDQVTELRS 179
Cdd:pfam07888 1 KPLDELVTLEEEshgeEGGTDMLLVVPRAELLQNRLEECLQERAELLQAqeaanrqrekekerykrdREQWERQRRELES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 180 RVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILSQQQGEHVARILELEDDIQTMSDKVLMKEVELDRVRDmvk 259
Cdd:pfam07888 81 RVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKE--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 260 altrEQEKLLGQLKEFQADKEQSEAELQTVREENCHLNTELQEAKGRQEEQGAQVQRLKDKVAHMKDTLGQTQQKVAELE 339
Cdd:pfam07888 158 ----RAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 340 PLKEQLRGVQELAASSQQKAALLGEELASAAGARDRTIAELHRSRLEVAEVNGRLAELSLHMKEEKCQWSKERTGLLQSM 419
Cdd:pfam07888 234 ALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 420 EAEKDKILKLSAEILRLEKTVQEERSQSHMFKTELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQTEKQELLEY 499
Cdd:pfam07888 314 EADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEY 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 500 MRKLEARLEKVADEKWNEDAATEDEEAtaglscPAALTDSEDESPEDMRLPS----YGLCERGNT-----SSSPPGPRES 570
Cdd:pfam07888 394 IRQLEQRLETVADAKWSEAALTSTERP------DSPLSDSEDENPEALQPPRplghYSLCEQGQPdslllATPPPSPRDP 467
|
490
....*....|....
gi 1958787708 571 SSLVVINQPAPIAP 584
Cdd:pfam07888 468 ESTVVISQPAPLSS 481
|
|
| SKICH |
pfam17751 |
SKICH domain; The SKICH domains of SKIP and PIPP mediate plasma membrane localization. The ... |
15-118 |
6.15e-40 |
|
SKICH domain; The SKICH domains of SKIP and PIPP mediate plasma membrane localization. The functions of the SKICH domains of NDP52 and CALCOCO1 are not known.
Pssm-ID: 465482 Cd Length: 102 Bit Score: 142.00 E-value: 6.15e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 15 VSFLNVARTYVPNTKVECHYTLPPGTTPSASDWIGIFKVEAACVRDYHTFVWssVPETTTDGSPTHASVQFQASYLPKPG 94
Cdd:pfam17751 1 VVFQNVGEWYPPDEDIECSYTLTPDFTPSSWDWIGLFKVGWKSVNDYVTYVW--AKDDEVEGSNSVRQVLFKASYLPKEP 78
|
90 100
....*....|....*....|....
gi 1958787708 95 AQLYQFRYVNRQGRVCGQSPPFQF 118
Cdd:pfam17751 79 EGFYQFCYVSNLGSVVGISTPFQF 102
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
170-536 |
1.79e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 86.91 E-value: 1.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 170 LEDQVTELRSRVQELEaalataRQehSELTEQYKGLS-----RSHGELSEERDILSQQQGEHVARILELEDDIQTMSDKV 244
Cdd:COG1196 191 LEDILGELERQLEPLE------RQ--AEKAERYRELKeelkeLEAELLLLKLRELEAELEELEAELEELEAELEELEAEL 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 245 LMKEVELDRVRDMVKALTREQEKLLGQLKEFQADKEQSEAELQtvreencHLNTELQEAKGRQEEQGAQVQRLKDKVAHM 324
Cdd:COG1196 263 AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA-------RLEERRRELEERLEELEEELAELEEELEEL 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 325 KDTLGQTQQKVAELEplkEQLRGVQELAASSQQKAALLGEELASAAGARDRTIAELHRSRLEVAEVNGRLAELSLHMKEE 404
Cdd:COG1196 336 EEELEELEEELEEAE---EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 405 KcqwsKERTGLLQSMEAEKDKILKLSAEILRLEKTVQEERSQSHMFKTELAREKDSSLVQLSESKRELTELRSALRVLQK 484
Cdd:COG1196 413 L----ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE 488
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1958787708 485 EKEQLQTEKQELLEYMRKLEARLEKVADEKWNEDAATEDEEATAGLSCPAAL 536
Cdd:COG1196 489 AAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAAL 540
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
167-502 |
1.41e-16 |
|
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: 84.35 E-value: 1.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 167 KLQLEDQVTELRSRVQELEAALATARQEHS-------ELTEQYKGLSRSHGELSEERDILSQQQGEHVARILELEDDIQT 239
Cdd:TIGR02169 669 SRSEPAELQRLRERLEGLKRELSSLQSELRrienrldELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSS 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 240 MSDKVLMKEVELDRVRDMVKALTREQEKLLGQLKEFQADK-----EQSEAELQTVREENCHLNTELQEAKGRQEEQGAQV 314
Cdd:TIGR02169 749 LEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLshsriPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEK 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 315 QRLKDKVAHMKDTLGQTQQKV----AELEPLKEQLRGVQELAASSQQKAALLGEELASAAGARDRTIAELHRSRLEVAEV 390
Cdd:TIGR02169 829 EYLEKEIQELQEQRIDLKEQIksieKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEEL 908
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 391 NGRLAELSLHMKEEKCQWSkERTGLLQSMEAEKDKILKLSAEILRLEKTVQE-ERSQSHMFKTE----LAREkdsslvQL 465
Cdd:TIGR02169 909 EAQIEKKRKRLSELKAKLE-ALEEELSEIEDPKGEDEEIPEEELSLEDVQAElQRVEEEIRALEpvnmLAIQ------EY 981
|
330 340 350
....*....|....*....|....*....|....*..
gi 1958787708 466 SESKRELTELRSALRVLQKEKEQLQtEKQELLEYMRK 502
Cdd:TIGR02169 982 EEVLKRLDELKEKRAKLEEERKAIL-ERIEEYEKKKR 1017
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
145-386 |
8.42e-16 |
|
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: 8.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 145 KATVLQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILSQQQG 224
Cdd:COG1196 254 ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELE 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 225 EHVARILELEDDIQTMSDKVLMKEVELDRVRDMVKALTREQEKLLGQLKEFQADKEQSEAELQTVREENCHLNTELQEAK 304
Cdd:COG1196 334 ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 305 GRQEEQGAQVQRLKDKVAHMKDTLGQTQQKVAELEplkEQLRGVQELAASSQQKAALLGEELASAAGARDRTIAELHRSR 384
Cdd:COG1196 414 ERLERLEEELEELEEALAELEEEEEEEEEALEEAA---EEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490
|
..
gi 1958787708 385 LE 386
Cdd:COG1196 491 AR 492
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
145-437 |
1.60e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 80.75 E-value: 1.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 145 KATVLQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILSQQQG 224
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 225 EHVARILELEDDIQTMsdkvlmkEVELDRVRDMVKALTREQEKLLGQLKEFQADKEQSEAELQTVREEnchlntELQEAK 304
Cdd:COG1196 306 RLEERRRELEERLEEL-------EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA------LLEAEA 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 305 GRQEEQGAQVQRLKDKVAHMKdtlgQTQQKVAELEPLKEQLRGVQELAASSQQKAALLGEELASAAGARDRTIAELHRSR 384
Cdd:COG1196 373 ELAEAEEELEELAEELLEALR----AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1958787708 385 LEVAEVNGRLAELSLHMKEEKcqwsKERTGLLQSMEAEKDKILKLSAEILRLE 437
Cdd:COG1196 449 EEEAELEEEEEALLELLAELL----EEAALLEAALAELLEELAEAAARLLLLL 497
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
149-434 |
1.61e-15 |
|
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: 80.87 E-value: 1.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 149 LQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILSQQQGEHVA 228
Cdd:TIGR02168 244 LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEA 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 229 RILELEDDIQTMSDKVLMKEVELDRvrdmvkaLTREQEKLLGQLKEFQADKEQSEAELQTVREENCHLNTELQEAKGRQE 308
Cdd:TIGR02168 324 QLEELESKLDELAEELAELEEKLEE-------LKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 309 EQGAQVQRLKDKVAHMKDTLGQTQQKVAELEPLKEQLRgvqelAASSQQKAALLGEELASAAGARDRTIAELHRSRLEVA 388
Cdd:TIGR02168 397 SLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE-----LKELQAELEELEEELEELQEELERLEEALEELREELE 471
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1958787708 389 EVNGRLAELslhmkEEKCQWSKERTGLLQSMEAEKDKILKLSAEIL 434
Cdd:TIGR02168 472 EAEQALDAA-----ERELAQLQARLDSLERLQENLEGFSEGVKALL 512
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
149-513 |
1.14e-14 |
|
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: 78.19 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 149 LQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILSQQQGEHVA 228
Cdd:TIGR02169 341 LEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSE 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 229 RILELEDDIQTMSDKVLMKEVELDRVRDMVKALTREQEKLLGQLKEFQADKEQSEAELQTVREENCHLNTELQEAKGRQE 308
Cdd:TIGR02169 421 ELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQAR 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 309 EQGAQVQRLKDKVAHMKDTLGQTQQKVAELEPLKEQLRGVQELAASSQQKAALLGEELASAagardRTIAELHRSRLeva 388
Cdd:TIGR02169 501 ASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAGNRLNNVVVEDDAVAK-----EAIELLKRRKA--- 572
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 389 evnGRLAELSLH-MKEEKCQWSKER----------------------------TGLLQSMEAEKD-----KILKLSAEIL 434
Cdd:TIGR02169 573 ---GRATFLPLNkMRDERRDLSILSedgvigfavdlvefdpkyepafkyvfgdTLVVEDIEAARRlmgkyRMVTLEGELF 649
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 435 ----------------RLEKTVQEERSQSHMFKTE-LAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQTEKQELL 497
Cdd:TIGR02169 650 eksgamtggsraprggILFSRSEPAELQRLRERLEgLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLE 729
|
410
....*....|....*.
gi 1958787708 498 EYMRKLEARLEKVADE 513
Cdd:TIGR02169 730 QEEEKLKERLEELEED 745
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
144-506 |
2.00e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 77.40 E-value: 2.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 144 PKATVLQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILSQQQ 223
Cdd:TIGR02168 691 EKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERL 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 224 GEHVARILELEDDIQTMSDKVLMKEVELDRVRDMVKALTREqeklLGQLKEFQADKEQSEAELQTVREENCHLNTELQEA 303
Cdd:TIGR02168 771 EEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAE----LTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 304 KGRQEEqgaQVQRLKDKVAHMKDTLGQTQqkvAELEPLKEQLRGVQELAASSQQKAALLGEELASAAGARDRTIAELHRS 383
Cdd:TIGR02168 847 IEELSE---DIESLAAEIEELEELIEELE---SELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEEL 920
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 384 RLEVAEVNGRLAELslhmkEEKCQWSKERTGLLQSMEAEkdkilklsaEILRLEKTVQEERSQSHMFKTELAREKDS-SL 462
Cdd:TIGR02168 921 REKLAQLELRLEGL-----EVRIDNLQERLSEEYSLTLE---------EAEALENKIEDDEEEARRRLKRLENKIKElGP 986
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1958787708 463 VQLsESKRELTELRSALRVLQKEKEQLQTEKQELLEYMRKLEAR 506
Cdd:TIGR02168 987 VNL-AAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDRE 1029
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
149-546 |
2.77e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 76.90 E-value: 2.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 149 LQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILSQQQGEHVA 228
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 229 RILELEDDIQTMSDKVLMKEVELDRVRDMVKALTREQEKLLGQLKEFQADKEQSEAELQTVREENCHLNTELQEAKGRQE 308
Cdd:COG1196 394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 309 EQGAQVQRLKDKVAHMKDTLGQTQQKVAELEPLKEQ---LRGVQELAASSQQKAALLGEELASAAGARDRTIAELHRSRL 385
Cdd:COG1196 474 LLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGvkaALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVV 553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 386 EVAEVNGRLAEL--------------------SLHMKEEKCQWSKERTGLLQSMEAEKDKILKLSAEIL----------- 434
Cdd:COG1196 554 EDDEVAAAAIEYlkaakagratflpldkirarAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLlgrtlvaarle 633
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 435 -------RLEKTVQEERSQSHMFKTELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQTEKQELLEYMRKLEARL 507
Cdd:COG1196 634 aalrravTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAE 713
|
410 420 430
....*....|....*....|....*....|....*....
gi 1958787708 508 EKVADEKWNEDAATEDEEATAGLSCPAALTDSEDESPED 546
Cdd:COG1196 714 EERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEA 752
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
149-485 |
3.63e-14 |
|
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: 76.65 E-value: 3.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 149 LQNQLDESQQERNDLMQ-LKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDilsqqqgehv 227
Cdd:TIGR02169 196 KRQQLERLRREREKAERyQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEK---------- 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 228 aRILELEDDIQTMSDKVL-MKEVELDRVRDMVKALTREQEKLLGQLKEFQADKEQSEAELQTVREENCHLNTELQEAKGR 306
Cdd:TIGR02169 266 -RLEEIEQLLEELNKKIKdLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELERE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 307 QEEQGAQVQRLKDKVAHMKDTLGQTQQKVAELEplKEQLRGVQELAaSSQQKAALLGEELASAAGARDRTIAELHRSRLE 386
Cdd:TIGR02169 345 IEEERKRRDKLTEEYAELKEELEDLRAELEEVD--KEFAETRDELK-DYREKLEKLKREINELKRELDRLQEELQRLSEE 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 387 VAEVNGRLAELslhmkEEKCQWSKERtgllqsMEAEKDKILKLSAEILRLEKTVQEERSQSHMFKTELAREKDsslvQLS 466
Cdd:TIGR02169 422 LADLNAAIAGI-----EAKINELEEE------KEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEK----ELS 486
|
330
....*....|....*....
gi 1958787708 467 ESKRELTELRSALRVLQKE 485
Cdd:TIGR02169 487 KLQRELAEAEAQARASEER 505
|
|
| Zn-C2H2_CALCOCO1 |
cd21967 |
C2H2-type zinc binding domain found in calcium-binding and coiled-coil domain-containing ... |
678-706 |
5.03e-14 |
|
C2H2-type zinc binding domain found in calcium-binding and coiled-coil domain-containing protein 1 (CALCOCO1) and similar proteins; CALCOCO1, also called calphoglin, or coiled-coil coactivator protein, or Sarcoma antigen NY-SAR-3, functions as a coactivator for aryl hydrocarbon and nuclear receptors (NR). It is recruited to promoters through its contact with the N-terminal basic helix-loop-helix-Per-Arnt-Sim (PAS) domain of transcription factors or coactivators, such as NCOA2. During ER-activation CALCOCO1 acts synergistically in combination with other NCOA2-binding proteins, such as EP300, CREBBP and CARM1. It is involved in the transcriptional activation of target genes in the Wnt/CTNNB1 pathway. It functions as a secondary coactivator in LEF1-mediated transcriptional activation via its interaction with CTNNB1. In association with CCAR1, CALCOCO1 enhances GATA1- and MED1-mediated transcriptional activation from the gamma-globin promoter during erythroid differentiation of K562 erythroleukemia cells. CALCOCO1 contains a C2H2-type zinc binding domain.
Pssm-ID: 412013 Cd Length: 29 Bit Score: 66.37 E-value: 5.03e-14
10 20
....*....|....*....|....*....
gi 1958787708 678 KECPICKERFPAESDKDALEDHMDGHFFF 706
Cdd:cd21967 1 KECPICKERFPLECDKDALEDHIDSHFFF 29
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
150-513 |
1.01e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 75.09 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 150 QNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILSQQQGEHVAR 229
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 230 ILELEDDIQTMSDkvlmkevELDRVRDMVKALTREQEKLLGQLKEFQADKEQSEAELQTVREENCHLNTELQEAKGRQEE 309
Cdd:TIGR02168 756 LTELEAEIEELEE-------RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLES 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 310 qgaQVQRLKDKVAHMKDTLGQTQQKVAELEPLKEQLRGVQELAASSQQKAALLGEElasaagaRDRTIAELHRSRLEVAE 389
Cdd:TIGR02168 829 ---LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNE-------RASLEEALALLRSELEE 898
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 390 VNGRLAELSLHMKEEKcqwsKERTGLLQSMEAEKDKILKLSAEILRLEKTVQEERSQSHMFKTELAREKDSSlvqLSESK 469
Cdd:TIGR02168 899 LSEELRELESKRSELR----RELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDD---EEEAR 971
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958787708 470 RELTELRSAL--------------RVLQKEKEQLQTEKQELLEYMRKLEARLEKVADE 513
Cdd:TIGR02168 972 RRLKRLENKIkelgpvnlaaieeyEELKERYDFLTAQKEDLTEAKETLEEAIEEIDRE 1029
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
225-542 |
1.46e-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: 74.71 E-value: 1.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 225 EHVARILELEDDIQTMSDKVLMKEVELDRVRDMVKALTREQEKLLGQLKEFQADKEQSEAELQTVREENCHLNTELQEAK 304
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 305 GRQEEQGAQvqrlkdkvahmkdtLGQTQQKVAELEPLKEQLrgvQELAASSQQKAALLGEELASAAgardrtiAELHRSR 384
Cdd:TIGR02168 761 AEIEELEER--------------LEEAEEELAEAEAEIEEL---EAQIEQLKEELKALREALDELR-------AELTLLN 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 385 LEVAEVNGRLAELslhmKEEKCQWSKERTGLLQSMEAEKDKILKLSAEILRLEKTVQEERSQShmfkTELAREKDSSLVQ 464
Cdd:TIGR02168 817 EEAANLRERLESL----ERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL----EALLNERASLEEA 888
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 465 LSESKRELTELRSALRVLQKEKEQLQTEKQELLEYMRKLEARLEKV-ADEKWNEDAATEDEEATAG--LSCPAALTDSED 541
Cdd:TIGR02168 889 LALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLeVRIDNLQERLSEEYSLTLEeaEALENKIEDDEE 968
|
.
gi 1958787708 542 E 542
Cdd:TIGR02168 969 E 969
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
145-375 |
1.72e-13 |
|
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: 72.87 E-value: 1.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 145 KATVLQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILSQQQG 224
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 225 EHVARILELEDDIQTMSDKVLMKEV-------ELDRVRDMVKALTREQEKLLGQLKEFQADKEQSEAELQTVREEnchLN 297
Cdd:COG4942 101 AQKEELAELLRALYRLGRQPPLALLlspedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE---LE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958787708 298 TELQEAKGRQEEQGAQVQRLKDKVAHMKDTLGQTQQKVAELEPLKEQLrgvQELAASSQQKAALLGEELASAAGARDR 375
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL---EALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
149-526 |
2.21e-12 |
|
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: 70.43 E-value: 2.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 149 LQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELteQY-----KGLSRSHGELSEERDILSQQQ 223
Cdd:TIGR04523 150 KEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKL--ELllsnlKKKIQKNKSLESQISELKKQN 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 224 GEhvarileLEDDIQTMSDKVLMKEVELDRVRDMVKALTREQEKLLGQLKEFQADKEQSEAELQTVREENCHLNTELQEA 303
Cdd:TIGR04523 228 NQ-------LKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDL 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 304 KgRQEEQG------AQVQRLKDKVAHMKDTLGQTQQKVAELEPLKEQLRGVQELAASSQQKaalLGEELASAAGARDRTI 377
Cdd:TIGR04523 301 N-NQKEQDwnkelkSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSE---KQRELEEKQNEIEKLK 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 378 AELHRSRLEVAEVNGRLAELSLHMKEEKcQWSKERTGLLQSMEAEKDKILK----LSAEILRLEKTVQEERSQSHMFKT- 452
Cdd:TIGR04523 377 KENQSYKQEIKNLESQINDLESKIQNQE-KLNQQKDEQIKKLQQEKELLEKeierLKETIIKNNSEIKDLTNQDSVKELi 455
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958787708 453 --ELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQTEKQELLEYMRKLEarlEKVADEKWNEDAATEDEEA 526
Cdd:TIGR04523 456 ikNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELE---EKVKDLTKKISSLKEKIEK 528
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
149-526 |
2.21e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 70.45 E-value: 2.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 149 LQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALAT---ARQEHSELTEQYKGLSRSHGELSEERDILSQQQGE 225
Cdd:PRK02224 204 LHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEheeRREELETLEAEIEDLRETIAETEREREELAEEVRD 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 226 HVARILELEDDIQTMSDKVLMKEVELDRVRDMVKALTREQEKLLGQLKEFQADKEQSEAELQTVREENCHLNTELQEAKG 305
Cdd:PRK02224 284 LRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELRE 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 306 RQEEqgaqvqrLKDKVAHMKDTLGQTQQKVAELEPLKEQLRGVQELAASSQQKAALLGEELASaagARDRTIAELHRSRL 385
Cdd:PRK02224 364 EAAE-------LESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELRE---ERDELREREAELEA 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 386 EVAEVNGRLAELSLHMKEEK---CQWSKERTGLLQSMEAEKDKILKLSAEILRLEKTvQEERSQSHmfktelarEKDSSL 462
Cdd:PRK02224 434 TLRTARERVEEAEALLEAGKcpeCGQPVEGSPHVETIEEDRERVEELEAELEDLEEE-VEEVEERL--------ERAEDL 504
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958787708 463 VQLSESKRELTELRSALRVLQKEKEQLQTEKQELLEYMRKLEARLEKVADEKwnEDAATEDEEA 526
Cdd:PRK02224 505 VEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEK--REAAAEAEEE 566
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
176-498 |
1.09e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 68.54 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 176 ELRSRVQELEAALATARQEhsELTEQYKGLSRSHGELSEERDILSQQQGEHVARILELEDDIQTMSDKVLMKEVELDRVR 255
Cdd:TIGR02168 217 ELKAELRELELALLVLRLE--ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALA 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 256 DMVKALTREQEKLLGQLKEFQADKEQSEAELQTVREENCHLNTELQEAKGRQEEQGAQVQRLKDKVAHMKdtlgqtqqkv 335
Cdd:TIGR02168 295 NEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELE---------- 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 336 AELEPLKEQLRGVQELAASSQQKAALLGEELASAAGARDRTIAELHRSrlevaevngrlaelslhmKEEKCQWSKERTGL 415
Cdd:TIGR02168 365 AELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERL------------------EDRRERLQQEIEEL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 416 LQSM-EAEKDKILKLSAEILRLEKTVQEERSQSHMFKTELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQTEKQ 494
Cdd:TIGR02168 427 LKKLeEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSE 506
|
....
gi 1958787708 495 ELLE 498
Cdd:TIGR02168 507 GVKA 510
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
276-513 |
1.94e-11 |
|
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: 66.33 E-value: 1.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 276 QADKEQSEAELQTVREENCHLNTELQEAKGRQEEQGAQVQRLKDKVAHMKDTLGQTQQKVAELEplkEQLRGVQELAASS 355
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE---AELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 356 QQKAALLGEELASaagardrtiaelhrsRLEVAEVNGRLAELSLHMKEEKCQWSKERTGLLQS-MEAEKDKILKLSA--- 431
Cdd:COG4942 96 RAELEAQKEELAE---------------LLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYlAPARREQAEELRAdla 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 432 EILRLEKTVQEERSQSHMFKTELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQTEKQELLEYMRKLEARLEKVA 511
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
..
gi 1958787708 512 DE 513
Cdd:COG4942 241 ER 242
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
145-528 |
2.01e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 67.10 E-value: 2.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 145 KATVLQNQLDESQQERNDLMQLK---LQLEDQVTELRSRVQELEAALATARQEHSELtEQYKGLSRSHGELSEERDILSQ 221
Cdd:COG4717 65 KPELNLKELKELEEELKEAEEKEeeyAELQEELEELEEELEELEAELEELREELEKL-EKLLQLLPLYQELEALEAELAE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 222 QQG------EHVARILELEDDIQTMSDKVLMKEVELDRVRDMVKALTREQ-EKLLGQLKEFQADKEQSEAELQTVREENC 294
Cdd:COG4717 144 LPErleeleERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 295 HLNTELQEAKGRQEEQgAQVQRLKDK------------VAHMKDTLGQTQQKVAEL-------------------EPLKE 343
Cdd:COG4717 224 ELEEELEQLENELEAA-ALEERLKEArlllliaaallaLLGLGGSLLSLILTIAGVlflvlgllallflllarekASLGK 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 344 QLRGVQELAASSQQKAALLGEELASAAGARDRTIAELHRSRLEVAEVNGRLAELSLHMKEEKCQWS-KERTGLLQSMEAE 422
Cdd:COG4717 303 EAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELeQEIAALLAEAGVE 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 423 KDKILKLSAEILRLEKTVQEERSQshmFKTELAREKDSSLVQLSESKREltELRSALRVLQKEKEQLQTEKQELLEYMRK 502
Cdd:COG4717 383 DEEELRAALEQAEEYQELKEELEE---LEEQLEELLGELEELLEALDEE--ELEEELEELEEELEELEEELEELREELAE 457
|
410 420
....*....|....*....|....*.
gi 1958787708 503 LEARLEKVADEKWNEDAATEDEEATA 528
Cdd:COG4717 458 LEAELEQLEEDGELAELLQELEELKA 483
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
149-518 |
2.56e-11 |
|
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: 67.45 E-value: 2.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 149 LQNQLDESQQERNDLMQLKLQ-----LEDQVTELRSRVQELEAALATARQEHSELTEQYKGL---SRSHG-----ELSEE 215
Cdd:pfam15921 243 VEDQLEALKSESQNKIELLLQqhqdrIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIqeqARNQNsmymrQLSDL 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 216 RDILSQQQGEHVARILELEDDIQTMSDKVLMKEVELDRVRDMVKALTREQEKLLGQLKEFQADKEQSEAELQTVREENCH 295
Cdd:pfam15921 323 ESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKR 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 296 L-------NTELQEAKGRQEEQGAQVQRLKDKVAHMK-DTLGQTQQKV-----------------AELEPLKEQLRG-VQ 349
Cdd:pfam15921 403 LwdrdtgnSITIDHLRRELDDRNMEVQRLEALLKAMKsECQGQMERQMaaiqgkneslekvssltAQLESTKEMLRKvVE 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 350 ELAA------SSQQKAALLGEELASAAGARDRTIAELHRSRlevAEVNGRLAELS-LHMKEEKCQWSKERTGLLQSMEAE 422
Cdd:pfam15921 483 ELTAkkmtleSSERTVSDLTASLQEKERAIEATNAEITKLR---SRVDLKLQELQhLKNEGDHLRNVQTECEALKLQMAE 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 423 KDKILK-LSAEILRLEKTV-QEERSQSHMF--KTELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQTEKQELLE 498
Cdd:pfam15921 560 KDKVIEiLRQQIENMTQLVgQHGRTAGAMQveKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVN 639
|
410 420
....*....|....*....|
gi 1958787708 499 YMRKleaRLEKVADEKWNED 518
Cdd:pfam15921 640 AGSE---RLRAVKDIKQERD 656
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
152-513 |
1.46e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 64.70 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 152 QLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAalatARQEHSELTEQYKGLSRSHGELSEERDILSQQQGEHVARIL 231
Cdd:PRK03918 201 ELEEVLREINEISSELPELREELEKLEKEVKELEE----LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 232 ELEDDIQTMSD--KVLMKEVELDRVRDMVKALTREQEKLLGQLkefqadkEQSEAELQTVREENCHLNTELQEAKGRQEE 309
Cdd:PRK03918 277 ELEEKVKELKElkEKAEEYIKLSEFYEEYLDELREIEKRLSRL-------EEEINGIEERIKELEEKEERLEELKKKLKE 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 310 QGAQVQRLKDKVahmkDTLGQTQQKVAELEPLKEQLRG--VQELAassqqkaallgEELASAAGARDRTIAELHRSRLEV 387
Cdd:PRK03918 350 LEKRLEELEERH----ELYEEAKAKKEELERLKKRLTGltPEKLE-----------KELEELEKAKEEIEEEISKITARI 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 388 AEVNGRLAELSLHMKE-EKCQWSKERTGLLQSMEAEKDKILKLSAEILRLEKTVQEERSQSHMFKTEL-----AREKDSS 461
Cdd:PRK03918 415 GELKKEIKELKKAIEElKKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELrelekVLKKESE 494
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1958787708 462 LVQLSESKRELTELRSALRVLQKEK-EQLQTEKQELLEYMRKLEARLEKVADE 513
Cdd:PRK03918 495 LIKLKELAEQLKELEEKLKKYNLEElEKKAEEYEKLKEKLIKLKGEIKSLKKE 547
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
155-440 |
1.62e-10 |
|
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: 64.70 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 155 ESQQERNDLMQLKLQLED-QVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILSQQQGEHVARILEL 233
Cdd:TIGR02169 766 RIEELEEDLHKLEEALNDlEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDL 845
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 234 EDDIqtmsdKVLMKEVELDRVRdmvkaltreQEKLLGQLKEFQADKEQSEAELQTVREENCHLNTELQEAKGRQEEQGAQ 313
Cdd:TIGR02169 846 KEQI-----KSIEKEIENLNGK---------KEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQ 911
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 314 VQRLKDKVAHMKDTLGQTQQKVAELEPLKEQLRGVQELAASS---QQKAALLGEELASAAGARDRTIAELhrsrlevAEV 390
Cdd:TIGR02169 912 IEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLedvQAELQRVEEEIRALEPVNMLAIQEY-------EEV 984
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1958787708 391 NGRLAELslhmkEEKcqwskertglLQSMEAEKDKILKLSAEILRLEKTV 440
Cdd:TIGR02169 985 LKRLDEL-----KEK----------RAKLEEERKAILERIEEYEKKKREV 1019
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
159-495 |
2.97e-10 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 63.59 E-value: 2.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 159 ERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEE-RDILSQQQGEHVARI-LELEDD 236
Cdd:pfam05483 416 EDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEvEDLKTELEKEKLKNIeLTAHCD 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 237 IQTMSDKVLMKE-----VELDRVRDMVKALTREQEKLLGQLKEFQADKEQSEAELQTVREE--------NCHLNTELQEA 303
Cdd:pfam05483 496 KLLLENKELTQEasdmtLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEfiqkgdevKCKLDKSEENA 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 304 KGRQEEQGAQVQRLKDKVAHMKDTLGQTQQKVAELEPLKEQLRGVQELA-ASSQQ------KAALLGEELASAAGA---- 372
Cdd:pfam05483 576 RSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGsAENKQlnayeiKVNKLELELASAKQKfeei 655
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 373 --------RDRTIAElhRSRLEVAEVNGRLAELSLHMKEE---KCQWS-KERTGLLQSMEAEKDKILKLSAEILRLEKTV 440
Cdd:pfam05483 656 idnyqkeiEDKKISE--EKLLEEVEKAKAIADEAVKLQKEidkRCQHKiAEMVALMEKHKHQYDKIIEERDSELGLYKNK 733
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1958787708 441 QEERSQShmfktelareKDSSLVQLSESKRELTELRSALRVLQKEKEQLQTEKQE 495
Cdd:pfam05483 734 EQEQSSA----------KAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| Zn-C2H2_12 |
pfam18112 |
Autophagy receptor zinc finger-C2H2 domain; This domain is found in calcium-binding and ... |
678-704 |
3.60e-10 |
|
Autophagy receptor zinc finger-C2H2 domain; This domain is found in calcium-binding and coiled-coil domain 2/NDP25 (CALCOCO2/NDP25) found in Homo sapiens. CALCOCO2/NDP25 is an ubiquitin-binding autophagy receptor involved in the selective autophagic degradation of invading pathogens. This domain is a typical C2H2-type zinc finger which specifically recognizes mono-ubiquitin or poly-ubiquitin chain. The overall ubiquitin-binding mode utilizes the C-terminal alpha-helix to interact with the solvent-exposed surface of the central beta-sheet of ubiquitin, similar to that observed in the RABGEF1/Rabex-5 or POLN/Pol-eta zinc finger.
Pssm-ID: 407946 Cd Length: 27 Bit Score: 55.34 E-value: 3.60e-10
10 20
....*....|....*....|....*..
gi 1958787708 678 KECPICKERFPAESDKDALEDHMDGHF 704
Cdd:pfam18112 1 KECPLCGEMFSPNIDQSEFEEHVESHF 27
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
250-548 |
1.03e-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: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 250 ELDRVRDMVKALTREQEKLLGQLKEFQADKEQSE------------------AELQTVREENCHLNTELQEAKGRQEEQG 311
Cdd:TIGR02169 178 ELEEVEENIERLDLIIDEKRQQLERLRREREKAEryqallkekreyegyellKEKEALERQKEAIERQLASLEEELEKLT 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 312 AQVQRLKDKVAHMKDTLGQTQQKVAELEP-----LKEQLRGVQELAASSQQKAALLGEELASAAGARDRTIAELHRSRLE 386
Cdd:TIGR02169 258 EEISELEKRLEEIEQLLEELNKKIKDLGEeeqlrVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 387 VAEVNGRLAElslhmkeekcqWSKERTGLLQSMEAEKDKILKLSAEILRLEKTVQEERsqshmfktelaREKDSSLVQLS 466
Cdd:TIGR02169 338 IEELEREIEE-----------ERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETR-----------DELKDYREKLE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 467 ESKRELTELRSALRVLQKEKEQLQTEKQELLEYMRKLEARLEKVADEKwnEDAATEDEEATAGLSCPAALTDSEDESPED 546
Cdd:TIGR02169 396 KLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEK--EDKALEIKKQEWKLEQLAADLSKYEQELYD 473
|
..
gi 1958787708 547 MR 548
Cdd:TIGR02169 474 LK 475
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
124-529 |
1.34e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.62 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 124 MDELVTLEEADGGSDILLVVPKATVLQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYK 203
Cdd:PRK03918 371 KEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHR 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 204 G--LSRSHGELSEERdilsqqqgEHVARILELEDDIQ---TMSDKVLMKEVELDRVRDMVKALTREQEKLlgqlKEFQAD 278
Cdd:PRK03918 451 KelLEEYTAELKRIE--------KELKEIEEKERKLRkelRELEKVLKKESELIKLKELAEQLKELEEKL----KKYNLE 518
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 279 K-EQSEAELQTVREENCHLNTELQEAKGRQEEqgaqVQRLKDKVAHMKDTLGQTQQKVAEL---------EPLKEQLRGV 348
Cdd:PRK03918 519 ElEKKAEEYEKLKEKLIKLKGEIKSLKKELEK----LEELKKKLAELEKKLDELEEELAELlkeleelgfESVEELEERL 594
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 349 QELAASSQQKAALLG--EELASAAGARDRTIAELHRSRLEVAEVNGRLAELSLHMKEEKCQWSKERtgllqsMEAEKDKI 426
Cdd:PRK03918 595 KELEPFYNEYLELKDaeKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEE------YEELREEY 668
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 427 LKLSAEILRLEKTVQEERSQshmfKTELARekdsSLVQLSESKRELTELRSALRVLQKEKEQLqtekQELLEYMRKLEAR 506
Cdd:PRK03918 669 LELSRELAGLRAELEELEKR----REEIKK----TLEKLKEELEEREKAKKELEKLEKALERV----EELREKVKKYKAL 736
|
410 420
....*....|....*....|...
gi 1958787708 507 LEKVADEKWNEDAATEDEEATAG 529
Cdd:PRK03918 737 LKERALSKVGEIASEIFEELTEG 759
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
158-514 |
1.57e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 61.21 E-value: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 158 QERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILSQQQGEHVARILELEDDI 237
Cdd:PRK02224 314 ARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEI 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 238 QTMSDKVLMKEVELDRVRDMVKALTREQEKLLGQLKEFQAD--------------------------------------- 278
Cdd:PRK02224 394 EELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATlrtarerveeaealleagkcpecgqpvegsphvetieed 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 279 ---KEQSEAELQTVREENCHLN------TELQEAKGRQEEQGAQVQRLKDKVAHMKDTLGQTQQKVAElepLKEQlrgVQ 349
Cdd:PRK02224 474 rerVEELEAELEDLEEEVEEVEerleraEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEE---LRER---AA 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 350 ELAASSQQKAallgeelASAAGARDRtiAELHRSrlEVAEVNGRLAELslhmkeekcqwsKERTGLLQSMEAEKDKILKL 429
Cdd:PRK02224 548 ELEAEAEEKR-------EAAAEAEEE--AEEARE--EVAELNSKLAEL------------KERIESLERIRTLLAAIADA 604
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 430 SAEILRLektvQEERSQshmfKTELAREKDSSLVQLSESKRELTELRSALRVlqkekEQLQTEKQELLEYMRKLEARLEK 509
Cdd:PRK02224 605 EDEIERL----REKREA----LAELNDERRERLAEKRERKRELEAEFDEARI-----EEAREDKERAEEYLEQVEEKLDE 671
|
....*
gi 1958787708 510 VADEK 514
Cdd:PRK02224 672 LREER 676
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
145-372 |
2.16e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 59.84 E-value: 2.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 145 KATVLQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRShgelseerdilSQQQG 224
Cdd:COG3883 31 ELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA-----------LYRSG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 225 EHVARILEL--EDDIQTMSDKVLMkeveLDRVRDMVKALTREQEKLLGQLKEFQADKEQSEAELQTVREENCHLNTELQE 302
Cdd:COG3883 100 GSVSYLDVLlgSESFSDFLDRLSA----LSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEA 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 303 AKgrqEEQGAQVQRLKDKVAHMKDTLGQTQQKVAELEPLKEQLRGVQELAASSQQKAALLGEELASAAGA 372
Cdd:COG3883 176 QQ---AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 242
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
150-524 |
2.30e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 60.82 E-value: 2.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 150 QNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELteqykglsRSHGELSE-ERDILSQQQGEHVA 228
Cdd:PRK02224 250 REELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDL--------LAEAGLDDaDAEAVEARREELED 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 229 RILELEDDIQTMSDKVLMKEVELDRVRDMVKALTREQEKLLGQLKEFQADKEQSEAELQTVREENCHLNTELQEAKGRQE 308
Cdd:PRK02224 322 RDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFG 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 309 EQGAQVQRLKDKVAHMKDTLGQTQQKVAELEPLKEQLRGVQELAASSQQKAA-------LLGEELASAAGARDRTIAELH 381
Cdd:PRK02224 402 DAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKcpecgqpVEGSPHVETIEEDRERVEELE 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 382 RS----RLEVAEVNGRLAEL-SLHMKEEKCQWSKERTGLLQSMEAEKDKIL---KLSAEILRLEK--------------T 439
Cdd:PRK02224 482 AEledlEEEVEEVEERLERAeDLVEAEDRIERLEERREDLEELIAERRETIeekRERAEELRERAaeleaeaeekreaaA 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 440 VQEERSQSHM-----FKTELAREKDS--SLVQLSESKRELTELRSALRVLQKEKEQLQ---TEKQELL----EYMRKLEA 505
Cdd:PRK02224 562 EAEEEAEEAReevaeLNSKLAELKERieSLERIRTLLAAIADAEDEIERLREKREALAelnDERRERLaekrERKRELEA 641
|
410
....*....|....*....
gi 1958787708 506 RLEKVADEKWNEDAATEDE 524
Cdd:PRK02224 642 EFDEARIEEAREDKERAEE 660
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
146-548 |
8.66e-09 |
|
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: 59.08 E-value: 8.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 146 ATVLQNQLDESQ-QERNDLMQLKLQLEDQ-VTELRSRVQELEAAL-ATARQEHSELTEQYKGLSRSHG-----------E 211
Cdd:pfam12128 485 AEVERLQSELRQaRKRRDQASEALRQASRrLEERQSALDELELQLfPQAGTLLHFLRKEAPDWEQSIGkvispellhrtD 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 212 LSEERDILSQQQGE-------HVARI-----LELEDDIQTMSDKVlmkEVELDRVRDMVKALTREQEKLLGQLKEFQADK 279
Cdd:pfam12128 565 LDPEVWDGSVGGELnlygvklDLKRIdvpewAASEEELRERLDKA---EEALQSAREKQAAAEEQLVQANGELEKASREE 641
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 280 EQSEAELQTVREENCHLNTELQEAKGRQEEQGAQVQRLKD----KVAHMKDTLGQTQQkvAELEPLKEQLRgvqELAASS 355
Cdd:pfam12128 642 TFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANerlnSLEAQLKQLDKKHQ--AWLEEQKEQKR---EARTEK 716
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 356 QQKAALLGEELASAAGARDRTIAelhrsrlevAEVNGRLAELSlhmkeekcQWSKERTGLLQSMEAEKDKILKLSAEILR 435
Cdd:pfam12128 717 QAYWQVVEGALDAQLALLKAAIA---------ARRSGAKAELK--------ALETWYKRDLASLGVDPDVIAKLKREIRT 779
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 436 LEKTV-------QEERSQSHMFKTELAREKDSSLVQLSESKRELTELRSALRVLQK---------EKEQLQTEKQ--ELL 497
Cdd:pfam12128 780 LERKIeriavrrQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQQLARLIAdtklrraklEMERKASEKQqvRLS 859
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1958787708 498 EYMRKLEARLEKVADEKWNEDAATEDEEATAGLSCPAALTDSEDESPEDMR 548
Cdd:pfam12128 860 ENLRGLRCEMSKLATLKEDANSEQAQGSIGERLAQLEDLKLKRDYLSESVK 910
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
158-546 |
8.75e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.90 E-value: 8.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 158 QERNDLMQLKLQLEDQV-TELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEerdILSQQQgEHVARILELEDD 236
Cdd:PRK02224 184 DQRGSLDQLKAQIEEKEeKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADE---VLEEHE-ERREELETLEAE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 237 IQTMSDKVLMKEVELDRVRDMVKALTREQEKLLGQLKEFQADKEQSEAELQTVREENCHLNTELQEAKGRQEEQGAQVQR 316
Cdd:PRK02224 260 IEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQA 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 317 LKDkvahmkdtlgqtqqkvaELEPLKEQLRGVQELAASSQQKAALLGEELASAAGARDRTIAELHRSRLEVAEVNGRLAE 396
Cdd:PRK02224 340 HNE-----------------EAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGD 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 397 LSLHMKEEkcqwSKERTGLLQSMEAEKDKILKLSAEILRLEKTVQEERSQSHMFKT-ELARE-KDSSLVQLSESKRE-LT 473
Cdd:PRK02224 403 APVDLGNA----EDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCpECGQPvEGSPHVETIEEDRErVE 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 474 ELRSALRVLQKEKEQLQtEKQELLEYMRKLEARLEKVADEKWN--------EDAATEDEEATAGLSCPAALTDSEDESPE 545
Cdd:PRK02224 479 ELEAELEDLEEEVEEVE-ERLERAEDLVEAEDRIERLEERREDleeliaerRETIEEKRERAEELRERAAELEAEAEEKR 557
|
.
gi 1958787708 546 D 546
Cdd:PRK02224 558 E 558
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
232-495 |
1.08e-08 |
|
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: 58.90 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 232 ELEDDIQTMSDKVLMKEVELDRVRDMVKALTREQEKLLGQLKEFQADKEQSEAELQTVREENCHLNTELQEAKGRQEEQG 311
Cdd:TIGR00606 692 ELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQE 771
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 312 AQVQRLKDKVAHMKDtlgqTQQKVAELEPLKEQLRGVQELAAssQQKAALLGEELasaagarDRTIAELhrsRLEVAEVN 391
Cdd:TIGR00606 772 TLLGTIMPEEESAKV----CLTDVTIMERFQMELKDVERKIA--QQAAKLQGSDL-------DRTVQQV---NQEKQEKQ 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 392 GRLAELSLHMkEEKCQWSKERTGLLQSMeaeKDKILKLSAEILRLEKTVQeERSQSHMFKTELAREKDSSLVQLSESKRE 471
Cdd:TIGR00606 836 HELDTVVSKI-ELNRKLIQDQQEQIQHL---KSKTNELKSEKLQIGTNLQ-RRQQFEEQLVELSTEVQSLIREIKDAKEQ 910
|
250 260
....*....|....*....|....
gi 1958787708 472 LTELRSALRVLQKEKEQLQTEKQE 495
Cdd:TIGR00606 911 DSPLETFLEKDQQEKEELISSKET 934
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
149-524 |
1.15e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.54 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 149 LQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEA------ALATARQEHSELTEQYKGLSRSHGELSEERDILSQQ 222
Cdd:PRK03918 243 LEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEkvkelkELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 223 QGEHVARILELEDdiqtmsdkvlmKEVELDRVRDMVKALTREQEKLLGQLKEFQaDKEQSEAELQTVREENC-----HLN 297
Cdd:PRK03918 323 INGIEERIKELEE-----------KEERLEELKKKLKELEKRLEELEERHELYE-EAKAKKEELERLKKRLTgltpeKLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 298 TELQEAKGRQEEqgaqvqrLKDKVAHMKDTLGQTQQKVAELEPLKEQLRGvqelaasSQQKAALLGEELasaagardrti 377
Cdd:PRK03918 391 KELEELEKAKEE-------IEEEISKITARIGELKKEIKELKKAIEELKK-------AKGKCPVCGREL----------- 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 378 AELHRSRLevaevngrLAELSLHMK--EEKCQWSKERTGLLQSMEAEKDKILKLSAEILRLEKTVQEERSQSHMFKTELA 455
Cdd:PRK03918 446 TEEHRKEL--------LEEYTAELKriEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNL 517
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958787708 456 REKDSSLVQLSESKRELTELRSALRVLQKE---KEQLQTEKQELLEYMRKLEARLEKVADEKWNEDAATEDE 524
Cdd:PRK03918 518 EELEKKAEEYEKLKEKLIKLKGEIKSLKKElekLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEE 589
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
130-514 |
1.31e-08 |
|
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: 58.70 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 130 LEEADGGSDILLVVPKATVLQNQ-----------------------LDESQQER-----NDLMQLKLQLEDQVTE----L 177
Cdd:pfam12128 227 IRDIQAIAGIMKIRPEFTKLQQEfntlesaelrlshlhfgyksdetLIASRQEErqetsAELNQLLRTLDDQWKEkrdeL 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 178 RSRVQELEAALATARQEHSELTEQYK-----GLSRSHGELSEERDIlsQQQGEHVARILE-LEDDIQTMSDK-----VLM 246
Cdd:pfam12128 307 NGELSAADAAVAKDRSELEALEDQHGafldaDIETAAADQEQLPSW--QSELENLEERLKaLTGKHQDVTAKynrrrSKI 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 247 KEVELDRVRDMVKALTREQEKLLGQLKEFQADKEQSEAELqtvREENCHLNTELQEAKGRQEEQGAQVQRLKDKVAHMKD 326
Cdd:pfam12128 385 KEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESEL---REQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPE 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 327 TLGQTQQKVAELEPLKEQlrgvQELAASSQQKAALlgeELASAAGARDRTIAELHRSRLEVAEVNGRLAEL--------- 397
Cdd:pfam12128 462 LLLQLENFDERIERAREE----QEAANAEVERLQS---ELRQARKRRDQASEALRQASRRLEERQSALDELelqlfpqag 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 398 SLH--MKEEKCQWSKE-----------RTGLLQSMEAEKDK-ILKLSAEILRLEK--------TVQEERSQSHMFKT--- 452
Cdd:pfam12128 535 TLLhfLRKEAPDWEQSigkvispellhRTDLDPEVWDGSVGgELNLYGVKLDLKRidvpewaaSEEELRERLDKAEEalq 614
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958787708 453 ---ELAREKDSSLVQLS----ESKRELTELRSA-------LRVLQKEKEQLQTEKQELL-EYMRKLEARLEKVADEK 514
Cdd:pfam12128 615 sarEKQAAAEEQLVQANgeleKASREETFARTAlknarldLRRLFDEKQSEKDKKNKALaERKDSANERLNSLEAQL 691
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
147-361 |
1.90e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 57.72 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 147 TVLQNQLDESQQERNDLMQLKLQ-LEDQVTELRSRVQELEAALATARQEHS--ELTEQYKGLSRSHGELSEERDILSQQQ 223
Cdd:COG3206 156 ALAEAYLEQNLELRREEARKALEfLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAEL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 224 GEHVARILELEDDIQTMSDKV--LMKEVELDRVRDMVKALTREQEKLLGQL-----------KEFQADKEQSEAELQTVR 290
Cdd:COG3206 236 AEAEARLAALRAQLGSGPDALpeLLQSPVIQQLRAQLAELEAELAELSARYtpnhpdvialrAQIAALRAQLQQEAQRIL 315
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958787708 291 EEnchLNTELQEAKGRQEEQGAQVQRLKDKVAhmkdTLGQTQQKVAELEPLKEQLRGVQELAASSQQKAAL 361
Cdd:COG3206 316 AS---LEAELEALQAREASLQAQLAQLEARLA----ELPELEAELRRLEREVEVARELYESLLQRLEEARL 379
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
145-492 |
2.44e-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: 57.34 E-value: 2.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 145 KATVLQNQLDESQQERNdlmqlklQLEDQVTELRSRVQELEAalatarqEHSELTEQYKglsrshGELSEERDILSQQQg 224
Cdd:TIGR04523 322 KLEEIQNQISQNNKIIS-------QLNEQISQLKKELTNSES-------ENSEKQRELE------EKQNEIEKLKKENQ- 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 225 EHVARILELEDDIQTMSDKVLMKEVELDRVRDMVKALTREQEKLLGQLKEFQADKEQSEAELQTVREENCHLNTELQEAK 304
Cdd:TIGR04523 381 SYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLD 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 305 GRQEEQGAQVQRLKDKVAHMKDTLGQTQQ----KVAELEPLKEQLRGV-QELAASSQQKAALLG--EELASAAGARDRTI 377
Cdd:TIGR04523 461 NTRESLETQLKVLSRSINKIKQNLEQKQKelksKEKELKKLNEEKKELeEKVKDLTKKISSLKEkiEKLESEKKEKESKI 540
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 378 AELHRSRLEVAEVNGR--LAELSLHMKEEKCQWSKERTGLLQSMEAEKDKILKLSAEILRLEKTVQEersqshmfKTELA 455
Cdd:TIGR04523 541 SDLEDELNKDDFELKKenLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEE--------KEKKI 612
|
330 340 350
....*....|....*....|....*....|....*..
gi 1958787708 456 REKDSslvQLSESKRELTELRSALRVLQKEKEQLQTE 492
Cdd:TIGR04523 613 SSLEK---ELEKAKKENEKLSSIIKNIKSKKNKLKQE 646
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
170-380 |
3.04e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.23 E-value: 3.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 170 LEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILSQQqgehvARILELEDDIQtmsdkvlmkev 249
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAE-----REIAELEAELE----------- 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 250 ELDRVRDMVKALTREQEKLlgqlkefqadkeqsEAELQTVREENCHLNTELQEAKGRQEEQGAQVQRLKDKVAHMKDtlG 329
Cdd:COG4913 679 RLDASSDDLAALEEQLEEL--------------EAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAED--L 742
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1958787708 330 QTQQKVAELEPLKEQLRGvqelAASSQQKAALLGEELASAAGARDRTIAEL 380
Cdd:COG4913 743 ARLELRALLEERFAAALG----DAVERELRENLEERIDALRARLNRAEEEL 789
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
232-490 |
5.97e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.46 E-value: 5.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 232 ELEDDIQTMSDkvLMKEveLDRVRD-MVKAltREQEKLLGQLKEFQADKEQSEAELQTVREEnchlntelqEAKGRQEEQ 310
Cdd:COG4913 222 DTFEAADALVE--HFDD--LERAHEaLEDA--REQIELLEPIRELAERYAAARERLAELEYL---------RAALRLWFA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 311 GAQVQRLKDKVAHMKDTLGQTQQKVAELEPLKEQLRgvQELAASSQQKAALLGEELASAAgardrtiAELHRSRLEVAEV 390
Cdd:COG4913 287 QRRLELLEAELEELRAELARLEAELERLEARLDALR--EELDELEAQIRGNGGDRLEQLE-------REIERLERELEER 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 391 NGRLAELslhmkeekcqwskertgllqsmeaeKDKILKLSAEILRLEKTVQEERSQSHMFKTELAREKDSSLVQLSESKR 470
Cdd:COG4913 358 ERRRARL-------------------------EALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEA 412
|
250 260
....*....|....*....|
gi 1958787708 471 ELTELRSALRVLQKEKEQLQ 490
Cdd:COG4913 413 ALRDLRRELRELEAEIASLE 432
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
158-509 |
6.17e-08 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 56.07 E-value: 6.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 158 QERNDLMQLKLQLEDQVTELRSR-----------VQELEAA-------LATARQEHSELTEQYKGLSRSHGELSEERDIL 219
Cdd:pfam15964 307 KERDDLMSALVSVRSSLAEAQQRessayeqvkqaVQMTEEAnfektkaLIQCEQLKSELERQKERLEKELASQQEKRAQE 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 220 SQQQGEHVARILE-LEDDIQTMSDKVLMKEVELDRVrdmvkalTREQEKLLGQLKEFQADKEQSEAELQTVREEnchLNT 298
Cdd:pfam15964 387 KEALRKEMKKEREeLGATMLALSQNVAQLEAQVEKV-------TREKNSLVSQLEEAQKQLASQEMDVTKVCGE---MRY 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 299 ELQEAKGRQEEQGAQVQRLKDKvahmkdTLGQTQQKVAELEPLKEQLRGVQELAASSQQKAALLGEELASAAGARDRTIA 378
Cdd:pfam15964 457 QLNQTKMKKDEAEKEHREYRTK------TGRQLEIKDQEIEKLGLELSESKQRLEQAQQDAARAREECLKLTELLGESEH 530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 379 ELHRSRLEVAEVNGRLAELSLHMKEEKCQWSKERTGLLQSMEAEKDKILKLSAEILRLEKT-VQEERSQSHMFKT---EL 454
Cdd:pfam15964 531 QLHLTRLEKESIQQSFSNEAKAQALQAQQREQELTQKMQQMEAQHDKTVNEQYSLLTSQNTfIAKLKEECCTLAKkleEI 610
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1958787708 455 AREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQTEKQELLEYMRKLEARLEK 509
Cdd:pfam15964 611 TQKSRSEVEQLSQEKEYLQDRLEKLQKRNEELEEQCVQHGRMHERMKQRLRQLDK 665
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
254-513 |
7.55e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.84 E-value: 7.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 254 VRDMVKALTREQEKLLGQLK---EFQADKEQSEAELQTVREenchlntELQEAKGRQEEQGAQVQRLKDKvahmKDTLGQ 330
Cdd:TIGR02169 144 VTDFISMSPVERRKIIDEIAgvaEFDRKKEKALEELEEVEE-------NIERLDLIIDEKRQQLERLRRE----REKAER 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 331 TQQKVAELEPLKEQLRgVQELAASSQQKAALLGeELASAAGARDRTIAELHRSRLEVAEVNGRLAELSLHMKEEkcqwSK 410
Cdd:TIGR02169 213 YQALLKEKREYEGYEL-LKEKEALERQKEAIER-QLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDL----GE 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 411 ERtgllqsMEAEKDKILKLSAEILRLEKTVQEERSQSHmfktELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQ 490
Cdd:TIGR02169 287 EE------QLRVKEKIGELEAEIASLERSIAEKERELE----DAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLT 356
|
250 260
....*....|....*....|...
gi 1958787708 491 TEKQELLEYMRKLEARLEKVADE 513
Cdd:TIGR02169 357 EEYAELKEELEDLRAELEEVDKE 379
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
149-506 |
8.38e-08 |
|
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: 55.89 E-value: 8.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 149 LQNQLDESQQERNDLMQLKLQ----LEDQVTELRSRVQELEAALATAR---QEHSELTEQYKGLSRSH-GELSEERDILS 220
Cdd:pfam15921 115 LQTKLQEMQMERDAMADIRRResqsQEDLRNQLQNTVHELEAAKCLKEdmlEDSNTQIEQLRKMMLSHeGVLQEIRSILV 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 221 QQQGEHVARILElEDDIQTMSDKVLMKEV-----ELDR-----------VRDMVKALTRE-QEKLLGQLKEFQADKEQ-- 281
Cdd:pfam15921 195 DFEEASGKKIYE-HDSMSTMHFRSLGSAIskilrELDTeisylkgrifpVEDQLEALKSEsQNKIELLLQQHQDRIEQli 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 282 SEAELQ---------TVREENCHLNTELQEAKGRQEEQGA----QVQRLKDKVAHMKDTLGQTQQKVAE-LEPLKEQLrg 347
Cdd:pfam15921 274 SEHEVEitgltekasSARSQANSIQSQLEIIQEQARNQNSmymrQLSDLESTVSQLRSELREAKRMYEDkIEELEKQL-- 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 348 vqELAASSQQKAALLGEELASAAGARDRTIAELhrsrleVAEVNGRLAELSLHMKEEKCQWSKErTGLLQSMEAEKDKIL 427
Cdd:pfam15921 352 --VLANSELTEARTERDQFSQESGNLDDQLQKL------LADLHKREKELSLEKEQNKRLWDRD-TGNSITIDHLRRELD 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 428 KLSAEILRLEKTV---------QEERSQSHMFKTELAREKDSSLVQLSESKRELteLRSALRVLQKEKEQLQTEKQELLE 498
Cdd:pfam15921 423 DRNMEVQRLEALLkamksecqgQMERQMAAIQGKNESLEKVSSLTAQLESTKEM--LRKVVEELTAKKMTLESSERTVSD 500
|
....*...
gi 1958787708 499 YMRKLEAR 506
Cdd:pfam15921 501 LTASLQEK 508
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
149-507 |
8.63e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 8.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 149 LQNQLDESQQERNDLMQLKLQ-LEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDIlsqQQGEHV 227
Cdd:COG4717 175 LQEELEELLEQLSLATEEELQdLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERL---KEARLL 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 228 ARILELEDDIQTMSDKVLMKEVELDRVRDMVKALtreqekLLGQLKEFQADKEQSEAELQTVREENCHLNTELQEAKGRQ 307
Cdd:COG4717 252 LLIAAALLALLGLGGSLLSLILTIAGVLFLVLGL------LALLFLLLAREKASLGKEAEELQALPALEELEEEELEELL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 308 EEQGAQVQRLKDKVAHMKDTLGQTQQKVAELEPLKEQLRgVQELAASSQQKAALLGEELASAAGARDRTIAELHRSRLEV 387
Cdd:COG4717 326 AALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ-LEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEEL 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 388 AEVNGRLAEL-----SLHMKEEKCQWSKERTGLLQSMEAEKDKILKLSAEILRLEKTVQE-ERSQSHMfktELAREKDSS 461
Cdd:COG4717 405 EELEEQLEELlgeleELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQlEEDGELA---ELLQELEEL 481
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1958787708 462 LVQLSESKRELTELRSALRVLQKEKEQLQTEKQ-ELLEYMRKLEARL 507
Cdd:COG4717 482 KAELRELAEEWAALKLALELLEEAREEYREERLpPVLERASEYFSRL 528
|
|
| Zn-C2H2_CALCOCO1_TAX1BP1_like |
cd21965 |
autophagy receptor zinc finger-C2H2 domain found in calcium-binding and coiled-coil ... |
680-703 |
2.05e-07 |
|
autophagy receptor zinc finger-C2H2 domain found in calcium-binding and coiled-coil domain-containing proteins, TAX1BP1 and similar proteins; The family includes calcium-binding and coiled-coil domain-containing proteins (CALCOCO1 and CALCOCO2), TAX1BP1 and similar proteins. CALCOCO1, also called calphoglin, or coiled-coil coactivator protein, or Sarcoma antigen NY-SAR-3, functions as a coactivator for aryl hydrocarbon and nuclear receptors (NR). CALCOCO2, also called antigen nuclear dot 52 kDa protein, or nuclear domain 10 protein NDP52, or nuclear domain 10 protein 52, or nuclear dot protein 52, is an ubiquitin-binding autophagy receptor involved in the selective autophagic degradation of invading pathogens. TAX1BP1, also called TRAF6-binding protein (T6BP), is a novel ubiquitin-binding adaptor protein involved in the negative regulation of the NF-kappaB transcription factor, a key player in inflammatory responses, immunity and tumorigenesis. The family also includes Drosophila melanogaster Spindle-F (Spn-F) that is the central mediator of IK2 kinase-dependent dendrite pruning in drosophila sensory neurons. This model corresponds to the C2H2-type zinc binding domain found in family members. It is a typical C2H2-type zinc finger which specifically recognizes mono-ubiquitin or poly-ubiquitin chain. The overall ubiquitin-binding mode utilizes the C-terminal alpha-helix to interact with the solvent-exposed surface of the central beta-sheet of ubiquitin, similar to that observed in the RABGEF1/Rabex-5 or POLN/Pol-eta zinc finger.
Pssm-ID: 412012 Cd Length: 24 Bit Score: 47.18 E-value: 2.05e-07
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
202-519 |
2.11e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.30 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 202 YKGLSRSHGELSEERDILSqqqgEHVARILELEDDIQTMSDKVLMKEVELDRVRDMVKALTREQEKLLGQLKEFQADKE- 280
Cdd:PRK03918 164 YKNLGEVIKEIKRRIERLE----KFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEe 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 281 --QSEAELQTVREENCHLNTELQEAKGRQEEQGAQVQRLKDKVAHMKDT-------------LGQTQQKVAELEP----L 341
Cdd:PRK03918 240 ieELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELkekaeeyiklsefYEEYLDELREIEKrlsrL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 342 KEQLRGVQELAASSQQKAALLGEELASAAGARDRtIAELHRSRLEVAEVNGRLAELSLHMKEEKCQWSKERTGLLQSMEA 421
Cdd:PRK03918 320 EEEINGIEERIKELEEKEERLEELKKKLKELEKR-LEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEK 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 422 EK----DKILKLSAEILRLEKTVQEERSQSHMFKT----------ELAREKDSSLV-----QLSESKRELTELRSALRVL 482
Cdd:PRK03918 399 AKeeieEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcgrELTEEHRKELLeeytaELKRIEKELKEIEEKERKL 478
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1958787708 483 QKEKEQLQTE---------KQELLEYMRKLEARLEKVADEKWNEDA 519
Cdd:PRK03918 479 RKELRELEKVlkkeselikLKELAEQLKELEEKLKKYNLEELEKKA 524
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
147-510 |
2.54e-07 |
|
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: 54.41 E-value: 2.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 147 TVLQNQLD-------ESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRshgELSEERDIL 219
Cdd:pfam01576 43 NALQEQLQaetelcaEAEEMRARLAARKQELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEE---QLDEEEAAR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 220 SQQQGEHV---ARILELEDDIQTMSDK--VLMKEVEL--DRVRDMVKALTREQEKL--LGQLKEFQaDKEQSEAELQTVR 290
Cdd:pfam01576 120 QKLQLEKVtteAKIKKLEEDILLLEDQnsKLSKERKLleERISEFTSNLAEEEEKAksLSKLKNKH-EAMISDLEERLKK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 291 EENCHLntELQEAKGRQEEQGAQVQ-RLKDKVAHMKDTLGQTQQKVAELEPLkeQLRGVQELAASSQQKAAL-------- 361
Cdd:pfam01576 199 EEKGRQ--ELEKAKRKLEGESTDLQeQIAELQAQIAELRAQLAKKEEELQAA--LARLEEETAQKNNALKKIreleaqis 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 362 -LGEELASAAGARDRtiAELHRSRLEvaevngrlaelslhmkEEKCQWSKERTGLLQSMEAEKDKILKLSAEILRLEKTV 440
Cdd:pfam01576 275 eLQEDLESERAARNK--AEKQRRDLG----------------EELEALKTELEDTLDTTAAQQELRSKREQEVTELKKAL 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 441 QEErSQSHMFKTELAREKDSSLV-----QLSESKRELTELRSALRVLQKEKEQLQTE-------KQELLEYMRKLEARLE 508
Cdd:pfam01576 337 EEE-TRSHEAQLQEMRQKHTQALeelteQLEQAKRNKANLEKAKQALESENAELQAElrtlqqaKQDSEHKRKKLEGQLQ 415
|
..
gi 1958787708 509 KV 510
Cdd:pfam01576 416 EL 417
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
149-514 |
6.35e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.02 E-value: 6.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 149 LQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELS-EERDILSQQQGEHV 227
Cdd:COG1196 440 EEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEgFLEGVKAALLLAGL 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 228 ARILELEDDIQTMSDKV----------LMKEVELDRVRDMVKALTREQEKLLGQLKEFQADKEQSEAELQTVREENCHLN 297
Cdd:COG1196 520 RGLAGAVAVLIGVEAAYeaaleaalaaALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGA 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 298 ------TELQEAKGRQEEQGAQVQRLKDKVAHMKDTLGQTQQKVAELEPLKEQLRGVQELAASSQQKAALLGEELASAAG 371
Cdd:COG1196 600 avdlvaSDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEA 679
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 372 ARDRTIAELHRSRLEVAEVNGRLAELSLHMKEEKcqwskertgllQSMEAEKDKILKLSAEILRLEKTVQEERSQSHMFK 451
Cdd:COG1196 680 ELEELAERLAEEELELEEALLAEEEEERELAEAE-----------EERLEEELEEEALEEQLEAEREELLEELLEEEELL 748
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958787708 452 TELAREKDSSLVQLSESKRELTELRSALRVL--------------QKEKEQLQTEKQELLEYMRKLEARLEKVADEK 514
Cdd:COG1196 749 EEEALEELPEPPDLEELERELERLEREIEALgpvnllaieeyeelEERYDFLSEQREDLEEARETLEEAIEEIDRET 825
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
149-510 |
8.27e-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: 52.33 E-value: 8.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 149 LQNQLDESQQERNDLMQL-------KLQLEDQVTELRSRVQELEAALATARQEHSELTeqyKGLSRSHGELSEERDILSQ 221
Cdd:TIGR04523 45 IKNELKNKEKELKNLDKNlnkdeekINNSNNKIKILEQQIKDLNDKLKKNKDKINKLN---SDLSKINSEIKNDKEQKNK 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 222 QQGEHVA---RILELEDDIQTMSDKVLMKEVELDRVRDMVKALTREQEKLLGQLKEFQADKEQSEAELQTVREENCHLNT 298
Cdd:TIGR04523 122 LEVELNKlekQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 299 EL---QEAKGRQEEQGAQVQRLKDKVAHMKDTLGQTQQkvaELEPLKEQLRGVQE--LAASSQQkaallgeelasaagar 373
Cdd:TIGR04523 202 LLsnlKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQ---EINEKTTEISNTQTqlNQLKDEQ---------------- 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 374 DRTIAELHRSRLEVAEVNGRLAELS----------LHMKEEKCQ-WSKERTGLLQSmeaEKDKILKLSAEILRLEKTVQE 442
Cdd:TIGR04523 263 NKIKKQLSEKQKELEQNNKKIKELEkqlnqlkseiSDLNNQKEQdWNKELKSELKN---QEKKLEEIQNQISQNNKIISQ 339
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958787708 443 ERSQShmfkTELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQTEKQELLEYMRKLEARLEKV 510
Cdd:TIGR04523 340 LNEQI----SQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQ 403
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
151-405 |
8.30e-07 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 51.45 E-value: 8.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 151 NQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILSQQQGEHVARI 230
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 231 LELEDDIQTMSDKVLM----------KEVELDRVRDMVKALTREQE----------KLLGQLKEFQADKEQSEAELQtVR 290
Cdd:COG1340 81 DELNEKLNELREELDElrkelaelnkAGGSIDKLRKEIERLEWRQQtevlspeeekELVEKIKELEKELEKAKKALE-KN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 291 EENCHLNTELQEAKGRQEEQGAQVQRLKDKVAHMKDTLGQTQQKVAElepLKEQLRGVQELAASSQQKAALLGEELasaa 370
Cdd:COG1340 160 EKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADE---LRKEADELHKEIVEAQEKADELHEEI---- 232
|
250 260 270
....*....|....*....|....*....|....*
gi 1958787708 371 garDRTIAELHRSRLEVAEVNGRLAELSLHMKEEK 405
Cdd:COG1340 233 ---IELQKELRELRKELKKLRKKQRALKREKEKEE 264
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
149-292 |
9.05e-07 |
|
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: 50.69 E-value: 9.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 149 LQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDI--LSQQQGEH 226
Cdd:COG1579 22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYeaLQKEIESL 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958787708 227 VARILELEDDIQTMSDKVLMKEVELDRVRDMVKALTREQEKLLGQLKEFQADKEQSEAELQTVREE 292
Cdd:COG1579 102 KRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREE 167
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
168-514 |
1.91e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.22 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 168 LQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEerdiLSQQQGEHVARILELEDDIQTMsDKVLMK 247
Cdd:PRK03918 296 IKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEE----LKKKLKELEKRLEELEERHELY-EEAKAK 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 248 EVELDRVRDMVKALTreQEKLLGQLKEFQADKEQSEAELQTVREENCHLNT----------ELQEAKGR---------QE 308
Cdd:PRK03918 371 KEELERLKKRLTGLT--PEKLEKELEELEKAKEEIEEEISKITARIGELKKeikelkkaieELKKAKGKcpvcgreltEE 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 309 EQGAQVQRLKDKVAHMKDTLGQTQQKVAELEPLKEQLRGV--QELAASSQQKAALLGEELASAAGARDrtIAELHRSRLE 386
Cdd:PRK03918 449 HRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVlkKESELIKLKELAEQLKELEEKLKKYN--LEELEKKAEE 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 387 VAEVNGRLAELSlhmkeekcqwsKERTGLLQSMEAEKDKILKLsAEILRLEKTVQEERSQSHmfkTELAREKDSSLVQLS 466
Cdd:PRK03918 527 YEKLKEKLIKLK-----------GEIKSLKKELEKLEELKKKL-AELEKKLDELEEELAELL---KELEELGFESVEELE 591
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1958787708 467 ESKRELTELRSALRVLQKEKEQLQTEKQELLEYMRKLEARLEKVADEK 514
Cdd:PRK03918 592 ERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETE 639
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
258-543 |
2.67e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.81 E-value: 2.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 258 VKALTREQEKLLGQLKEFQADKEQSE--AELQTVREENCHLNTELQeakgRQEEQGAQVQRLKDKVAhmkDTLGQTQQKV 335
Cdd:PRK02224 178 VERVLSDQRGSLDQLKAQIEEKEEKDlhERLNGLESELAELDEEIE----RYEEQREQARETRDEAD---EVLEEHEERR 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 336 AELEPLKEQLRGVQELAASSQQKAALLGEELASA-------AGARDRTIAELHRSRLEVAEVNGRLAELSLHMKEEKCQW 408
Cdd:PRK02224 251 EELETLEAEIEDLRETIAETEREREELAEEVRDLrerleelEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRL 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 409 SKERTgllqSMEAEKDKILKLSAEILRLEKTVQEERSQShmfkTELAREKDSSLVQLSESKRELTELRSALRVLQKE--- 485
Cdd:PRK02224 331 EECRV----AAQAHNEEAESLREDADDLEERAEELREEA----AELESELEEAREAVEDRREEIEELEEEIEELRERfgd 402
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958787708 486 -----------KEQLQTEKQELLEYMRKLEARLEKVadekwnEDAATEDEEATAGLSCPAALTDSEDES 543
Cdd:PRK02224 403 apvdlgnaedfLEELREERDELREREAELEATLRTA------RERVEEAEALLEAGKCPECGQPVEGSP 465
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
171-372 |
2.93e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.21 E-value: 2.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 171 EDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILSQQQGEHVARILELEDDIQTMSDKV------ 244
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELgerara 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 245 ------LMKEVE-----------LDRVrDMVKALTREQEKLLGQLKEFQADKEQSEAELQTVREEnchLNTELQEAKGRQ 307
Cdd:COG3883 95 lyrsggSVSYLDvllgsesfsdfLDRL-SALSKIADADADLLEELKADKAELEAKKAELEAKLAE---LEALKAELEAAK 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958787708 308 EEQGAQVQRLKDKVAHMKDTLGQTQQKVAELEPLKEQLRGVQELAASSQQKAALLGEELASAAGA 372
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
251-526 |
4.48e-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: 50.44 E-value: 4.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 251 LDRVRDMVKALTREQEKLLGQ------LKEFQADKEQSEAELQTVReenchlnteLQEAKGRQEEQGAQVQRLKDKVAHM 324
Cdd:TIGR02168 188 LDRLEDILNELERQLKSLERQaekaerYKELKAELRELELALLVLR---------LEELREELEELQEELKEAEEELEEL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 325 KDTLGQTQQKVAELE----PLKEQLRGVQELAASSQQKAALLGEELASAAgardrtiAELHRSRLEVAEVNGRLAelslh 400
Cdd:TIGR02168 259 TAELQELEEKLEELRlevsELEEEIEELQKELYALANEISRLEQQKQILR-------ERLANLERQLEELEAQLE----- 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 401 mkeekcQWSKERTGLLQSMEAEKDKILKLSAEILRLEKTVQEERSQSHMFKTelarekdsslvQLSESKRELTELRSALR 480
Cdd:TIGR02168 327 ------ELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELES-----------RLEELEEQLETLRSKVA 389
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1958787708 481 VLQKEKEQLQTEKQELLEYMRKLEARLEKVADEkwNEDAATEDEEA 526
Cdd:TIGR02168 390 QLELQIASLNNEIERLEARLERLEDRRERLQQE--IEELLKKLEEA 433
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
252-494 |
4.85e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.02 E-value: 4.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 252 DRVRDMVKALTREQEKLLGQLKEFQADKEQSEAELQTVREENCHLNTElqeakgrqEEQGAQVQRLKDkvahMKDTLGQT 331
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLS--------EEAKLLLQQLSE----LESQLAEA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 332 QQKVAELEPLKEQLRgvQELAASSQQKAALLGEELASAAgardrtIAELHRSRLEVAEVNGRLAELSLHMKEEKcqwsKE 411
Cdd:COG3206 232 RAELAEAEARLAALR--AQLGSGPDALPELLQSPVIQQL------RAQLAELEAELAELSARYTPNHPDVIALR----AQ 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 412 RTGLLQSMEAEKDKIL-KLSAEILRLEKTVQEERSQSHMFKTELAREKDSSlVQLSESKRELTELRSALRVLQKEKEQLQ 490
Cdd:COG3206 300 IAALRAQLQQEAQRILaSLEAELEALQAREASLQAQLAQLEARLAELPELE-AELRRLEREVEVARELYESLLQRLEEAR 378
|
....
gi 1958787708 491 TEKQ 494
Cdd:COG3206 379 LAEA 382
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
145-323 |
6.38e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 6.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 145 KATVLQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATA-RQEHSELTEQYKGLSRSHGELSEERDILSQQq 223
Cdd:COG4913 289 RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEAL- 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 224 gehvARILELEDDiqtmsdkvlmkeVELDRVRDMVKALTREQEKLLGQLKEFQADKEQSEAELQTVREENCHLNTELQEA 303
Cdd:COG4913 368 ----LAALGLPLP------------ASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASL 431
|
170 180
....*....|....*....|
gi 1958787708 304 KGRQEEQGAQVQRLKDKVAH 323
Cdd:COG4913 432 ERRKSNIPARLLALRDALAE 451
|
|
| COG4192 |
COG4192 |
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ... |
149-513 |
7.80e-06 |
|
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal transduction mechanisms];
Pssm-ID: 443346 [Multi-domain] Cd Length: 640 Bit Score: 49.30 E-value: 7.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 149 LQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELeaALATARQEHSELTEQYKGLSRSHGELSEERDILSQQQGEHVA 228
Cdd:COG4192 39 LSNQIRYILDDSLPKLQASLKLEENSNELVAALPEF--AAATNTTERSQLRNQLNTQLADIEELLAELEQLTQDAGDLRA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 229 RILELEDDIQtmsdkvlmkevELDRVRDMVKALTREQEKLLGQLKEFQAD-KEQSEAELQTVREENCHLNTELQEAKGRQ 307
Cdd:COG4192 117 AVADLRNLLQ-----------QLDSLLTQRIALRRRLQELLEQINWLHQDfNSELTPLLQEASWQQTRLLDSVETTESLR 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 308 EEQGA--QVQRLKDKVAHMKDTLGQ--TQQKVAELEPLKEQLrgvQELAASSQQKAALLGEelASAAGARDRTIAELhrs 383
Cdd:COG4192 186 NLQNElqLLLRLLAIENQIVSLLREvaAARDQADVDNLFDRL---QYLKDELDRNLQALKN--YPSTITLRQLIDEL--- 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 384 rLEVAEVNGRLAELslhMKEEkcqwsKERTGLLQSMEAEKDKILKLSAEilRLEKTVQEERSQSHMFKTELAREKDSS-- 461
Cdd:COG4192 258 -LAIGSGEGGLPSL---RRDE-----LAAQATLEALAEENNSILEQLRT--QISGLVGNSREQLVALNQETAQLVQQSgi 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 462 ----------------------------LVQLSES-----------------KRELTELRSALRV-LQKEKEQLQTEKQE 495
Cdd:COG4192 327 lllaiallslllavlinyfyvrrrlvkrLNALSDAmaaiaagdldvpipvdgNDEIGRIARLLRVfRDQAIEKTQELETE 406
|
410
....*....|....*...
gi 1958787708 496 LLEYMRkLEARLEKVADE 513
Cdd:COG4192 407 IEERKR-IEKNLRQTQDE 423
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
176-513 |
1.39e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 48.80 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 176 ELRSRVQELEAALATARQEHSEltEQYKglsrsHGELSEERDILSQQQGEhvarileLEDDIQTMSDkvlmkevELDRVR 255
Cdd:COG3096 282 ELSERALELRRELFGARRQLAE--EQYR-----LVEMARELEELSARESD-------LEQDYQAASD-------HLNLVQ 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 256 DMVkaltREQEKLlgqlKEFQADkeqseaelqtvreenchlnteLQEAKGRQEEQGAQVQRLKDKVAHMKDTLGQTQQKV 335
Cdd:COG3096 341 TAL----RQQEKI----ERYQED---------------------LEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEV 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 336 AELeplKEQLRGVQElAASSQQKAALlgeELASAAGARDRTIAELHRSRLEVAEVNGRLAELslhmKEEKCQWSKERTGL 415
Cdd:COG3096 392 DSL---KSQLADYQQ-ALDVQQTRAI---QYQQAVQALEKARALCGLPDLTPENAEDYLAAF----RAKEQQATEEVLEL 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 416 LQSME------AEKDKILKLsaeilrLEKTVQE-ERSQSHMFKTEL---AREKDSSLVQLSESKRELTELRSALRVLQKE 485
Cdd:COG3096 461 EQKLSvadaarRQFEKAYEL------VCKIAGEvERSQAWQTARELlrrYRSQQALAQRLQQLRAQLAELEQRLRQQQNA 534
|
330 340 350
....*....|....*....|....*....|....*...
gi 1958787708 486 KEQLQ----------TEKQELLEYMRKLEARLEKVADE 513
Cdd:COG3096 535 ERLLEefcqrigqqlDAAEELEELLAELEAQLEELEEQ 572
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
232-528 |
1.73e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.21 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 232 ELEDDIQTMSDKVLMKEVELDRVRDMVKALTREQEKLLGQLKEFQAdkeqseaELQTVREENCHLNTELQEAKGRQEEQG 311
Cdd:COG1340 12 ELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELRE-------EAQELREKRDELNEKVKELKEERDELN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 312 AQVQRLKDKVAHMKDTLGQTQQKVAELEPLKEQLRGVQElaasSQQKAALLGEElasaagarDRTIAElhrsrlevaevn 391
Cdd:COG1340 85 EKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEW----RQQTEVLSPEE--------EKELVE------------ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 392 gRLAELslhmkeekcqwsKERTGLLQSMEAEKDKILKLSAEIlrleKTVQEERSQSHMFKTELAREKDSSLVQLSESKRE 471
Cdd:COG1340 141 -KIKEL------------EKELEKAKKALEKNEKLKELRAEL----KELRKEAEEIHKKIKELAEEAQELHEEMIELYKE 203
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958787708 472 LTELRSALRVLQKEKEQLQTE-----------KQELLEYMRKLEARLEKVADEKWNEDAATEDEEATA 528
Cdd:COG1340 204 ADELRKEADELHKEIVEAQEKadelheeiielQKELRELRKELKKLRKKQRALKREKEKEELEEKAEE 271
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
179-389 |
1.77e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.45 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 179 SRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILSQQQGEHVARILELEDDIQTMSDKVlmkeveldrvrdmv 258
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL-------------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 259 KALTREQEKLLGQLKEFQA-------------------------DKEQSEAELQTVREENCHLNTELQEAKGRQEEQGAQ 313
Cdd:COG4942 86 AELEKEIAELRAELEAQKEelaellralyrlgrqpplalllspeDFLDAVRRLQYLKYLAPARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958787708 314 VQRLKDKVAHMKDTLGQTQQKVAELEPLKEQLRGVQELAASSQQKAALLGEELASAAGARDRTIAELHRSRLEVAE 389
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
157-509 |
1.99e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 48.18 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 157 QQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQE-HSELTEQYKGLSRSHGELSEERDILSQQQGEHVARILELED 235
Cdd:pfam05483 175 EYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEmHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKEN 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 236 DIQTMS-------DKVLMKEVELDRVRDMVKALTREQEKLLGQLKEFQADKEQS-------EAELQTVREENCHLNtelq 301
Cdd:pfam05483 255 KMKDLTflleesrDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSmstqkalEEDLQIATKTICQLT---- 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 302 eakgrqEEQGAQVQRLKDKVAHMKDTLGQTQQKVAELEplkEQLRGVQELAASSQQKAALLGEELASAAGARDRTIAELH 381
Cdd:pfam05483 331 ------EEKEAQMEELNKAKAAHSFVVTEFEATTCSLE---ELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKN 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 382 RSRLEVAEVNGRLAELSLHMKEEKcQWSK----------ERTGLLQSMEAEkdkILKLSAEILRLEKTVQEERSQSHMFK 451
Cdd:pfam05483 402 NKEVELEELKKILAEDEKLLDEKK-QFEKiaeelkgkeqELIFLLQAREKE---IHDLEIQLTAIKTSEEHYLKEVEDLK 477
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958787708 452 TELAREK------DSSLVQLSESKRELTELRSALRV-LQKEKEQLQTEKQELLEYMRKLEARLEK 509
Cdd:pfam05483 478 TELEKEKlknielTAHCDKLLLENKELTQEASDMTLeLKKHQEDIINCKKQEERMLKQIENLEEK 542
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
147-289 |
2.17e-05 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 47.06 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 147 TVLQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALA----TARQEHSELTEQYKGLSRSHGELSEE------- 215
Cdd:pfam09787 43 TALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQeeaeSSREQLQELEEQLATERSARREAEAElerlqee 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 216 ----RDILSQQQGEHVARILELEDDIQTMSDKVLMK------EVELD-RVRD----------MVKALTREQEKLLGQLK- 273
Cdd:pfam09787 123 lrylEEELRRSKATLQSRIKDREAEIEKLRNQLTSKsqssssQSELEnRLHQltetliqkqtMLEALSTEKNSLVLQLEr 202
|
170
....*....|....*..
gi 1958787708 274 -EFQADKEQSEAELQTV 289
Cdd:pfam09787 203 mEQQIKELQGEGSNGTS 219
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
245-558 |
2.65e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.83 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 245 LMKEVELDRVRDMVKALTREQEKLLGQLKEFQADKEQSEaELQTVREENchlntELQEAKGRQEEQGAQVQRLKDKVAHM 324
Cdd:PTZ00121 1475 AKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKAD-EAKKAEEAK-----KADEAKKAEEAKKADEAKKAEEKKKA 1548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 325 KDTLGQTQQKVAELEPLKEQLRGVQELAASSQQKAallgEELASAAGARDRTIAELHRSRLEVAEVNGRLAELSLHMKEE 404
Cdd:PTZ00121 1549 DELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKA----EEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEE 1624
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 405 KCQWSKERTGLLQSMEAEKDKILKlsAEILR------------LEKTVQEERSQSHMFKT--ELAREKDSSLVQLSESKR 470
Cdd:PTZ00121 1625 LKKAEEEKKKVEQLKKKEAEEKKK--AEELKkaeeenkikaaeEAKKAEEDKKKAEEAKKaeEDEKKAAEALKKEAEEAK 1702
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 471 ELTELRSALRVLQKEKEQLQTEKQEllEYMRKLEARLEKVADEKWNEDAATEDEEATAglscPAALTDSEDESPEDMRLP 550
Cdd:PTZ00121 1703 KAEELKKKEAEEKKKAEELKKAEEE--NKIKAEEAKKEAEEDKKKAEEAKKDEEEKKK----IAHLKKEEEKKAEEIRKE 1776
|
....*...
gi 1958787708 551 SYGLCERG 558
Cdd:PTZ00121 1777 KEAVIEEE 1784
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
220-456 |
3.37e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.68 E-value: 3.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 220 SQQQGEHVARILELEDDIQTMSDKVLMKEVELDRVRDMVKALTREQEKLLGQLKEFQADKEQSEAELQTVREENCHLNTE 299
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 300 LQEAKGRQEEQGAQVQRLkdkvahmkdtlgqtqQKVAELEPLkeqlrgvqeLAASSQQKAALLGEELASAAGARDRTIAE 379
Cdd:COG4942 99 LEAQKEELAELLRALYRL---------------GRQPPLALL---------LSPEDFLDAVRRLQYLKYLAPARREQAEE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958787708 380 LHRSRLEVAEVNGRLAELSLHMKEEKCQWSKERTGLLQSMEAEKDKILKLSAEILRLEKTVQEERSQSHMFKTELAR 456
Cdd:COG4942 155 LRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
151-350 |
4.03e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.96 E-value: 4.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 151 NQLDESQQERNDLMQLKLQ-LEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILsqqqgehvAR 229
Cdd:PRK02224 522 EELIAERRETIEEKRERAEeLRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL--------ER 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 230 ILELEDDIQTMSDkvlmkevELDRVRDMVKALTREQEKLLGQLKEFQADKEQSEAELQTVREEnchlntELQEAKGRQEE 309
Cdd:PRK02224 594 IRTLLAAIADAED-------EIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARIE------EAREDKERAEE 660
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1958787708 310 QGAQV----QRLKDKVAHMKDTLGQTQQKVAELEPLKEQLRGVQE 350
Cdd:PRK02224 661 YLEQVeeklDELREERDDLQAEIGAVENELEELEELRERREALEN 705
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
169-321 |
4.44e-05 |
|
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: 45.30 E-value: 4.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 169 QLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDilsqqqgEHVARILELEDDIQTMSD----KV 244
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIE-------EVEARIKKYEEQLGNVRNnkeyEA 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958787708 245 LMKEVEldrvrdmvkALTREQEKLLGQLKEFQADKEQSEAELQTVREENCHLNTELQEAKGRQEEQGAQVQRLKDKV 321
Cdd:COG1579 94 LQKEIE---------SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEEL 161
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
165-446 |
4.81e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.43 E-value: 4.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 165 QLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQykgLSRSHGELSEERDILSQQQgehvARILELEDDIQTMSDKV 244
Cdd:COG4372 24 ILIAALSEQLRKALFELDKLQEELEQLREELEQAREE---LEQLEEELEQARSELEQLE----EELEELNEQLQAAQAEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 245 LMKEVELDRVRDMVKALTREQEKLLGQLKEFQADKEQSEAELQTVREENCHLNTELQEAKGRQEEQGAQVQRLKDKVAHM 324
Cdd:COG4372 97 AQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 325 KDTlgQTQQKVAELEPLKEQLRGVQELAASSQQKAALLGEELASAAGARDRTIAElhrsRLEVAEVNGRLAELSLHMKEE 404
Cdd:COG4372 177 SEA--EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEA----KLGLALSALLDALELEEDKEE 250
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1958787708 405 KCQWSKERTGLLQSMEAEKDKILKLSAEILRLEKTVQEERSQ 446
Cdd:COG4372 251 LLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAA 292
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
151-292 |
4.98e-05 |
|
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: 4.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 151 NQLDESQQERNDLMQLK---LQLEDQVTELR---SRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILSQQQG 224
Cdd:COG4913 651 QRLAEYSWDEIDVASAEreiAELEAELERLDassDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELD 730
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958787708 225 EHVARILELEDDIQ----TMSDKVLMKEVELDRVRDMVKALTREQEKLlgqlkefQADKEQSEAELQTVREE 292
Cdd:COG4913 731 ELQDRLEAAEDLARlelrALLEERFAAALGDAVERELRENLEERIDAL-------RARLNRAEEELERAMRA 795
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
155-508 |
6.83e-05 |
|
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: 46.27 E-value: 6.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 155 ESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATarqehselteqykglsrshgelseerdiLSQQQGEHVARILELE 234
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHKRARIELEKKASA----------------------------LKRQLDRESDRNQELQ 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 235 DDIQTMSDKVLMKEVELDRVRDMVKALTREQEKLLGQLKEfqadKEQSEAELqtvREENCHLNTELQEAKGRQEEQGAQV 314
Cdd:pfam05557 55 KRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNE----KESQLADA---REVISCLKNELSELRRQIQRAELEL 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 315 QRLKDKVAHMKDTLGQTQQKVAELEPLKEQLRGVQELAASSQQKAALLGEELAS---------AAGARDRTIAELHRSRL 385
Cdd:pfam05557 128 QSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSqeqdseivkNSKSELARIPELEKELE 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 386 EVAEVNGRLAELS---LHMKEEKCQWSKErtglLQSMEAEKDKILKLSAEILRLEKTVQEERS--QSH---MFKTELARE 457
Cdd:pfam05557 208 RLREHNKHLNENIenkLLLKEEVEDLKRK----LEREEKYREEAATLELEKEKLEQELQSWVKlaQDTglnLRSPEDLSR 283
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1958787708 458 KdssLVQLSES----KRELTELRSALRVLQKEKEQLQTEKQELLEYMRKLEARLE 508
Cdd:pfam05557 284 R---IEQLQQReivlKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLK 335
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
185-504 |
7.10e-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: 46.48 E-value: 7.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 185 EAALATARQEHSELTEQYKGLSRSHGELSEERDILSQQQGEHVAriLELEDDiqtmsdkvlmKEVELDRVRDMVKALTRE 264
Cdd:COG3096 784 EKRLEELRAERDELAEQYAKASFDVQKLQRLHQAFSQFVGGHLA--VAFAPD----------PEAELAALRQRRSELERE 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 265 QEKLLGQLKEFQADKEQSEAELQTVREENCHLN------------------TELQEAKGRQEEQGAQVQRLKDKVAHMKD 326
Cdd:COG3096 852 LAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANlladetladrleelreelDAAQEAQAFIQQHGKALAQLEPLVAVLQS 931
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 327 TLGQTQQKVAELEPLKEQLRGV-QELAASSQ--QKAALLGEELASAAGARDRTIAELHRSRLEVAEVNGRLAELSLHMKE 403
Cdd:COG3096 932 DPEQFEQLQADYLQAKEQQRRLkQQIFALSEvvQRRPHFSYEDAVGLLGENSDLNEKLRARLEQAEEARREAREQLRQAQ 1011
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 404 EKC-QWSKERTGLLQSMEAEKDKILKLSAEILRLEKTVQ---EERSQSHMfktelarekdsslvqlSESKRELTELRSAL 479
Cdd:COG3096 1012 AQYsQYNQVLASLKSSRDAKQQTLQELEQELEELGVQADaeaEERARIRR----------------DELHEELSQNRSRR 1075
|
330 340
....*....|....*....|....*
gi 1958787708 480 RVLQKEKEQLQTEKQELLEYMRKLE 504
Cdd:COG3096 1076 SQLEKQLTRCEAEMDSLQKRLRKAE 1100
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
160-309 |
9.12e-05 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 45.01 E-value: 9.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 160 RNDLMQ-LKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELseerdilsqqqgehvariLELEDDIQ 238
Cdd:smart00787 138 RMKLLEgLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQL------------------KQLEDELE 199
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958787708 239 TMsdkvlmKEVELDRVRDMVKALTREQEKLLGQLKEFQADKEQSEAELQTVREENCHLNTELQEAKGRQEE 309
Cdd:smart00787 200 DC------DPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQ 264
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
149-321 |
9.27e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.78 E-value: 9.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 149 LQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHgELSEERDI---LSQQQGE 225
Cdd:PHA02562 218 KQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVI-KMYEKGGVcptCTQQISE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 226 HVARILELED---DIQTMSDKVLMKEVELDRVRDMVKALTREqekllgqLKEFQADKEQSEAELQTVREENCHLNTELQE 302
Cdd:PHA02562 297 GPDRITKIKDklkELQHSLEKLDTAIDELEEIMDEFNEQSKK-------LLELKNKISTNKQSLITLVDKAKKVKAAIEE 369
|
170 180
....*....|....*....|...
gi 1958787708 303 AKG----RQEEQGAQVQRLKDKV 321
Cdd:PHA02562 370 LQAefvdNAEELAKLQDELDKIV 392
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
151-444 |
1.08e-04 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 44.80 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 151 NQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILSQQQGEhvari 230
Cdd:pfam15905 73 KDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLELTRVNELLKAKFSE----- 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 231 lelEDDIQTMSDKVLmkevELDRVRDMVKALTRE----QEKLLGQLKEFQADKEQSEAELQTVREENCHLNTELQEAKGR 306
Cdd:pfam15905 148 ---DGTQKKMSSLSM----ELMKLRNKLEAKMKEvmakQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 307 QEEQGAQVQRLkdkvahmkdtlgqtQQKVAELEPLKEQLRGVQELAAssqqkaallgeelasaagARDRTIAELhRSRLE 386
Cdd:pfam15905 221 TEKLLEYITEL--------------SCVSEQVEKYKLDIAQLEELLK------------------EKNDEIESL-KQSLE 267
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 387 VAEVngrlaELSLHMKE--EKCQWSKERTGLLQSMEAEKDkiLKLSAEILRLEKTVQEER 444
Cdd:pfam15905 268 EKEQ-----ELSKQIKDlnEKCKLLESEKEELLREYEEKE--QTLNAELEELKEKLTLEE 320
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
153-506 |
1.31e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.72 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 153 LDESQQERNDLMQLKLQLEDQ---VTELRSRVQELEAALATARQEHSELTE----------QYKGLSRSHGELSEERDIL 219
Cdd:PRK04863 285 LEEALELRRELYTSRRQLAAEqyrLVEMARELAELNEAESDLEQDYQAASDhlnlvqtalrQQEKIERYQADLEELEERL 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 220 SQQQgehvaRILELEDDIQTMSD-KVLMKEVELDRVR----DMVKAL----TR-----------EQEKLLGQLKEFQADK 279
Cdd:PRK04863 365 EEQN-----EVVEEADEQQEENEaRAEAAEEEVDELKsqlaDYQQALdvqqTRaiqyqqavqalERAKQLCGLPDLTADN 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 280 -----EQSEAELQTVREENCHLNTELQ--EAKGRQEEQGAQ-VQRLKDKVA-------------------HMKDTLGQTQ 332
Cdd:PRK04863 440 aedwlEEFQAKEQEATEELLSLEQKLSvaQAAHSQFEQAYQlVRKIAGEVSrseawdvarellrrlreqrHLAEQLQQLR 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 333 QKVAELEPLKEQLRGVQELAASSQQKaalLGEELASAAgardrtiaelhrsrlEVAEVNGRLAELSLHMKEEKCQWSKER 412
Cdd:PRK04863 520 MRLSELEQRLRQQQRAERLLAEFCKR---LGKNLDDED---------------ELEQLQEELEARLESLSESVSEARERR 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 413 TGLLQSMEaekdkilKLSAEILRLEKTVQEersqshmfktelAREKDSSLVQLSE-------SKRELTELRSAL----RV 481
Cdd:PRK04863 582 MALRQQLE-------QLQARIQRLAARAPA------------WLAAQDALARLREqsgeefeDSQDVTEYMQQLlereRE 642
|
410 420
....*....|....*....|....*
gi 1958787708 482 LQKEKEQLQTEKQELLEYMRKLEAR 506
Cdd:PRK04863 643 LTVERDELAARKQALDEEIERLSQP 667
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
152-540 |
1.41e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 152 QLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLS-RSHGELSEERDILSQQQGEHVARI 230
Cdd:COG4913 282 RLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRR 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 231 LELEDDIQTMSDKVLMKEVELDRVRDMVKALTREQEKLLGQLKEFQADKEQSEAELQTVREEnchLNTELQEAKGRQEEQ 310
Cdd:COG4913 362 ARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRE---LEAEIASLERRKSNI 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 311 GAQVQRLKDKVAhmkDTLGQTQQK---VAEL---EPLKEQLRGVQELAASSQ----------QKAAL-------LGEEL- 366
Cdd:COG4913 439 PARLLALRDALA---EALGLDEAElpfVGELievRPEEERWRGAIERVLGGFaltllvppehYAAALrwvnrlhLRGRLv 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 367 ---ASAAGARDRTIAELHRS---RLEVAE------VNGRLAELSLHMK----EE--KCQWSKERTGLLQSMEA--EKD-- 424
Cdd:COG4913 516 yerVRTGLPDPERPRLDPDSlagKLDFKPhpfrawLEAELGRRFDYVCvdspEElrRHPRAITRAGQVKGNGTrhEKDdr 595
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 425 ---------------KILKLSAEILRLEKTVQEERSQSHMFKTELA-----------------------------REKDS 460
Cdd:COG4913 596 rrirsryvlgfdnraKLAALEAELAELEEELAEAEERLEALEAELDalqerrealqrlaeyswdeidvasaereiAELEA 675
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 461 SLVQLSESKRELTELRSALRVLQKEKEQLQTEKQELLEYMRKLEARLEKVADEkwnEDAATEDEEATAGLSCPAALTDSE 540
Cdd:COG4913 676 ELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEE---LDELQDRLEAAEDLARLELRALLE 752
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
332-507 |
1.94e-04 |
|
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: 43.37 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 332 QQKVAELEPLKEQLRGVQELAASSQQKAALLGEELASAAGARDRTIAELHRSRLEVAEVNGRLAELSLHMKEEKCQwsKE 411
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN--KE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 412 RTGLLQSMEAEKDKILKLSAEILRLEKTVQEERSQSHMFKTELAREKDsslvqlsESKRELTELRSALRVLQKEKEQLQT 491
Cdd:COG1579 91 YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEA-------ELEEKKAELDEELAELEAELEELEA 163
|
170
....*....|....*.
gi 1958787708 492 EKQELLEymrKLEARL 507
Cdd:COG1579 164 EREELAA---KIPPEL 176
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
145-495 |
2.06e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 44.81 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 145 KATVLQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKglsrshgelseerdilSQQQG 224
Cdd:pfam10174 483 KVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLK----------------KAHNA 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 225 EHVARILEleddiqTMSDKVLMKEVELDRVRDMVKALTREQEKLLGQLKEFQADKEQSEAELqtvreenchlnTELQEAK 304
Cdd:pfam10174 547 EEAVRTNP------EINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKI-----------AELESLT 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 305 GRQ-EEQGAQVQRLKDkvahmkdtlGQTQQKVAELEPLKEQLRGVQELAASSQQKAAllgEELasaagardrtIAELHRS 383
Cdd:pfam10174 610 LRQmKEQNKKVANIKH---------GQQEMKKKGAQLLEEARRREDNLADNSQQLQL---EEL----------MGALEKT 667
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 384 RLEVAEVNGRLA--ELSLHmkeekcqwskERTGLLQSMEAEKDKILKlsaEILrlektvqeERSQSHMFKTelAREKDS- 460
Cdd:pfam10174 668 RQELDATKARLSstQQSLA----------EKDGHLTNLRAERRKQLE---EIL--------EMKQEALLAA--ISEKDAn 724
|
330 340 350
....*....|....*....|....*....|....*..
gi 1958787708 461 -SLVQLSESKRELTELRSALrvLQKEKEQL-QTEKQE 495
Cdd:pfam10174 725 iALLELSSSKKKKTQEEVMA--LKREKDRLvHQLKQQ 759
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
149-491 |
2.57e-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: 44.40 E-value: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 149 LQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILSQQQGEHVA 228
Cdd:pfam01576 108 LEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEA 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 229 RILELEDDiqtmsdkvLMKEvelDRVRDMVKALTREQEKLLGQLKEFQADKEQSEAELqtvREENCHLNTELQEAKGRQE 308
Cdd:pfam01576 188 MISDLEER--------LKKE---EKGRQELEKAKRKLEGESTDLQEQIAELQAQIAEL---RAQLAKKEEELQAALARLE 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 309 EQGAQVQRLKDKVAHMKDTLGQTQQKVA------------------ELEPLKEQLRGV-------QELAASSQQKAALLG 363
Cdd:pfam01576 254 EETAQKNNALKKIRELEAQISELQEDLEseraarnkaekqrrdlgeELEALKTELEDTldttaaqQELRSKREQEVTELK 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 364 EELASAAGARDRTIAELHRSRLEVAEvngRLAELSLHMKEEKCQWSKERtgllQSMEAEKdkiLKLSAEIlrleKTVQEE 443
Cdd:pfam01576 334 KALEEETRSHEAQLQEMRQKHTQALE---ELTEQLEQAKRNKANLEKAK----QALESEN---AELQAEL----RTLQQA 399
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1958787708 444 RSQSHMFKTELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQT 491
Cdd:pfam01576 400 KQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSS 447
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
162-513 |
2.69e-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: 44.57 E-value: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 162 DLMQLKLQLEDQVTElrSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILSQQQ------GEHVARILELED 235
Cdd:TIGR00618 197 ELLTLRSQLLTLCTP--CMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLkkqqllKQLRARIEELRA 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 236 DIQTMSDkvLMKEVELDR----VRDMVKALTREQEKLLGQLKEFQADKEQSEAELQtvrEENCHLNTELQEAKGRQEEQG 311
Cdd:TIGR00618 275 QEAVLEE--TQERINRARkaapLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLM---KRAAHVKQQSSIEEQRRLLQT 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 312 AQVQRLKDKVAHMKDTL--GQTQQKVAELEPLK---EQLRGVQELAASSQQKAALLGEELASAAG------------ARD 374
Cdd:TIGR00618 350 LHSQEIHIRDAHEVATSirEISCQQHTLTQHIHtlqQQKTTLTQKLQSLCKELDILQREQATIDTrtsafrdlqgqlAHA 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 375 RTIAELHRSRLEVAEVNGRLAELSLHMKEEKCQWSKERTGLLQSMEAEKDKILKLSAEILRLEKTVQEERSQSHMFKTEL 454
Cdd:TIGR00618 430 KKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGS 509
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958787708 455 AREKDSSLVQLSES---KRELTELRSALRVLQKEKEQLQTEKQELLEYMRKLEARLEKVADE 513
Cdd:TIGR00618 510 CIHPNPARQDIDNPgplTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQS 571
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
145-366 |
3.22e-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: 44.24 E-value: 3.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 145 KATVLQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILSQQQG 224
Cdd:TIGR04523 448 QDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIE 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 225 EHVARILELEDDIQTMSDKVLMKEVELDrvRDMVKALTREQEKLLGQLKEFQADKEQSEAELQTVREEnchLNTELQEAK 304
Cdd:TIGR04523 528 KLESEKKEKESKISDLEDELNKDDFELK--KENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQ---KEKEKKDLI 602
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958787708 305 GRQEEQGAQVQRLKDKVAHMKdtlgqtqqkvAELEPLKEQLRGVQELAASSQQKAALLGEEL 366
Cdd:TIGR04523 603 KEIEEKEKKISSLEKELEKAK----------KENEKLSSIIKNIKSKKNKLKQEVKQIKETI 654
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
154-509 |
3.37e-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: 44.01 E-value: 3.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 154 DESQQERNDLMQL----KLQLEDQVTELRSRVQELEAalatarqEHSELTEQYKGLSRSHGELSEERDILsqqqgehVAR 229
Cdd:pfam01576 4 EEEMQAKEEELQKvkerQQKAESELKELEKKHQQLCE-------EKNALQEQLQAETELCAEAEEMRARL-------AAR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 230 ILELEDDIQTMsdkvlmkEVELDRVRDMVKALTREQEKLLGQLKEFQADKEQSEAELQTVREENCHLNTELQEAKGR--- 306
Cdd:pfam01576 70 KQELEEILHEL-------ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDill 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 307 QEEQGAQVQR----LKDKVAHMKDTLGQTQQKVAELEPLKEQLRGVQELAASSQQKAALLGEELASAAGARDRTIAELHR 382
Cdd:pfam01576 143 LEDQNSKLSKerklLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 383 srlEVAEVNGRLAEL--SLHMKEEKCQWSKERTG--LLQSMEAEKdKILKLSAEILRLEKTVQEERSQS----------- 447
Cdd:pfam01576 223 ---QIAELQAQIAELraQLAKKEEELQAALARLEeeTAQKNNALK-KIRELEAQISELQEDLESERAARnkaekqrrdlg 298
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958787708 448 ---HMFKTELAREKDSSLVQL---SESKRELTELRSALRVLQKEKE-QLQ----------TEKQELLEYMRKLEARLEK 509
Cdd:pfam01576 299 eelEALKTELEDTLDTTAAQQelrSKREQEVTELKKALEEETRSHEaQLQemrqkhtqalEELTEQLEQAKRNKANLEK 377
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
215-389 |
3.57e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.60 E-value: 3.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 215 ERDILSQQQGEHVARILELEDDIQTMSDkvlmkevELDRVRDMVKALTREQEKLLGQLKEFQADKEQSEAELQTVREenc 294
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEA-------RLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRN--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 295 hlNTELQEAKGRQEEQGAQVQRLKDKVAHMKDtlgqtqqkvaELEPLKEQLRGVQELAASSQQKAALLGEELASAAGARD 374
Cdd:COG1579 88 --NKEYEALQKEIESLKRRISDLEDEILELME----------RIEELEEELAELEAELAELEAELEEKKAELDEELAELE 155
|
170
....*....|....*
gi 1958787708 375 RTIAELHRSRLEVAE 389
Cdd:COG1579 156 AELEELEAEREELAA 170
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
245-414 |
3.82e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 43.69 E-value: 3.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 245 LMKEVELDRVRDMVKALTReQEKLLGQLKEFQADKEQSEaELQTVREENCHLNTELQEAKGRQEEQGAQVQRLKDKVAHM 324
Cdd:COG2433 355 VEKKVPPDVDRDEVKARVI-RGLSIEEALEELIEKELPE-EEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEEL 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 325 KDTLgqtQQKVAELEPLKEQLRgvqeLAASSQQKAALLGEELAsaagARDRTIAELHRsrlEVAEVNGRLAELSLHMKEE 404
Cdd:COG2433 433 EAEL---EEKDERIERLERELS----EARSEERREIRKDREIS----RLDREIERLER---ELEEERERIEELKRKLERL 498
|
170
....*....|
gi 1958787708 405 KCQWSKERTG 414
Cdd:COG2433 499 KELWKLEHSG 508
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
149-511 |
5.34e-04 |
|
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: 43.19 E-value: 5.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 149 LQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILSQQQ---GE 225
Cdd:pfam05557 88 LNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQsslAE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 226 HVARILELEDDIQTM-SDKVLMK------------EVELDRVRDMVKALtREQEKLLGQLKEFQAD-------KEQSEAE 285
Cdd:pfam05557 168 AEQRIKELEFEIQSQeQDSEIVKnskselaripelEKELERLREHNKHL-NENIENKLLLKEEVEDlkrklerEEKYREE 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 286 LQTVREENCHLNTELQ----------------EAKGRQEEQ--------GAQVQRLKDKVAHMKDTLGQTQQKVA----E 337
Cdd:pfam05557 247 AATLELEKEKLEQELQswvklaqdtglnlrspEDLSRRIEQlqqreivlKEENSSLTSSARQLEKARRELEQELAqylkK 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 338 LEPLKEQLRGVQELAASSQQKAALLGEElasaagaRD--RTIAELHRSRLEVAEVNGRLA-----------ELSLHMKEE 404
Cdd:pfam05557 327 IEDLNKKLKRHKALVRRLQRRVLLLTKE-------RDgyRAILESYDKELTMSNYSPQLLerieeaedmtqKMQAHNEEM 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 405 KCQWSKertgLLQSMEAEKDKILKLSAEI-LRLEKTVQEERSQSHMFKTELAREKDSSLVQLSESKRELTELRSAL---- 479
Cdd:pfam05557 400 EAQLSV----AEEELGGYKQQAQTLERELqALRQQESLADPSYSKEEVDSLRRKLETLELERQRLREQKNELEMELerrc 475
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958787708 480 ----------RVLQ--------------KEKEQLQTEKQELLEYMRKLEARLEKVA 511
Cdd:pfam05557 476 lqgdydpkktKVLHlsmnpaaeayqqrkNQLEKLQAEIERLKRLLKKLEDDLEQVL 531
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
149-397 |
6.36e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 6.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 149 LQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILSQQQGEHVA 228
Cdd:COG4372 57 AREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 229 RILELEDDIQTMSDKVLMKEVELDRVRDMVKALTREQEKLLGQLKEFQADKEQSEAELQTVREENCHLNTELQEAKGRQE 308
Cdd:COG4372 137 QIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPREL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 309 EQGAQVQRLKDKVAHMKDTLGQTQQKVAELEPLKEQLRGVQELAASSQQKAALLGEELASAAGARDRTIAELHRSRLEVA 388
Cdd:COG4372 217 AEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELK 296
|
....*....
gi 1958787708 389 EVNGRLAEL 397
Cdd:COG4372 297 LLALLLNLA 305
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
248-614 |
7.48e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 7.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 248 EVELDRVRDMVKALTREQEKLLGQLKEFQADKEQSEAELQTVREENCHLNTELQEAKGRQEEQGAQVQRLKDKvahmkdt 327
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREE------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 328 lgqtqqkvaelepLKEQLRGVQELAASSQQKAALLGEElasaagardrtiaelhrsrlEVAEVNGRLAELSlhmkeekcq 407
Cdd:COG3883 88 -------------LGERARALYRSGGSVSYLDVLLGSE--------------------SFSDFLDRLSALS--------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 408 wskertgllQSMEAEKDKILKLSAEILRLEKTvqeersqshmfKTELAREKDSSLVQLSESKRELTELRSALRVLQKEKE 487
Cdd:COG3883 126 ---------KIADADADLLEELKADKAELEAK-----------KAELEAKLAELEALKAELEAAKAELEAQQAEQEALLA 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 488 QLQTEKQELLEYMRKLEARLEKVADEKWNEDAATEDEEATAGLSCPAALTDSEDESPEDMRLPSYGLCERGNTSSSPPGP 567
Cdd:COG3883 186 QLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAA 265
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1958787708 568 RESSSLVVINQPAPIAPQLSGPGEASSSDSEAEDEKSVLMAAVQSGG 614
Cdd:COG3883 266 GAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGG 312
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
141-498 |
8.09e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.80 E-value: 8.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 141 LVVPKATvLQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELE--------------AALATARQEHSELTEQYKGLS 206
Cdd:pfam15921 588 MQVEKAQ-LEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLElekvklvnagserlRAVKDIKQERDQLLNEVKTSR 666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 207 RSHGELSEERDILSQQqgehvarILELEDDIQTMSDKVLMK----EVELDRVRDMVKALT----REQEKLLGQLKEFQAD 278
Cdd:pfam15921 667 NELNSLSEDYEVLKRN-------FRNKSEEMETTTNKLKMQlksaQSELEQTRNTLKSMEgsdgHAMKVAMGMQKQITAK 739
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 279 KEQSEA-----------------ELQTVREENCHLNTEL-------QEAKGRQEEQGAQVQRLKDKVAHMKDTLGQTQQK 334
Cdd:pfam15921 740 RGQIDAlqskiqfleeamtnankEKHFLKEEKNKLSQELstvatekNKMAGELEVLRSQERRLKEKVANMEVALDKASLQ 819
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 335 VAELEPL--KEQLRGVQELAASSQQKAALLGEELASAAGARDRTI--AELHRSRLEVAEVNGRLAELSLHmkeekcqwSK 410
Cdd:pfam15921 820 FAECQDIiqRQEQESVRLKLQHTLDVKELQGPGYTSNSSMKPRLLqpASFTRTHSNVPSSQSTASFLSHH--------SR 891
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 411 ERTGLLQSMEAEKDKILKLSAEILRLEKTVQEERSQSHMFKTELAREKDSSLVQLSESkreltELRSalRVLQKEKEQLQ 490
Cdd:pfam15921 892 KTNALKEDPTRDLKQLLQELRSVINEEPTVQLSKAEDKGRAPSLGALDDRVRDCIIES-----SLRS--DICHSSSNSLQ 964
|
....*...
gi 1958787708 491 TEKQELLE 498
Cdd:pfam15921 965 TEGSKSSE 972
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
162-525 |
8.90e-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: 42.85 E-value: 8.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 162 DLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHgelseERDILSQ-QQGEHVARIL--------- 231
Cdd:pfam01576 682 ELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQF-----ERDLQARdEQGEEKRRQLvkqvrelea 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 232 ELEDDIQTMSDKVLMK---EVELDRVRDMVKALTREQEKLLGQLKEFQADKEQseaelqtvreenchLNTELQEAKGRQE 308
Cdd:pfam01576 757 ELEDERKQRAQAVAAKkklELDLKELEAQIDAANKGREEAVKQLKKLQAQMKD--------------LQRELEEARASRD 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 309 EQGAQVQRLKDKVAHMKDTLGQTQQKVAELEPLKEQlrgvqelaasSQQKAALLGEELASaaGARDRTIAELHRSRLEva 388
Cdd:pfam01576 823 EILAQSKESEKKLKNLEAELLQLQEDLAASERARRQ----------AQQERDELADEIAS--GASGKSALQDEKRRLE-- 888
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 389 evnGRLAELSLHMKEEKCqwskertgllqSMEAEKDKILKLSAEILRLEKTVQEERSQSHmfKTELAREKDSSlvQLSES 468
Cdd:pfam01576 889 ---ARIAQLEEELEEEQS-----------NTELLNDRLRKSTLQVEQLTTELAAERSTSQ--KSESARQQLER--QNKEL 950
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958787708 469 KRELTELRSALRVLQKE------------KEQLQTEKQElleymRKLEARLEKVADEKWNEDAATEDEE 525
Cdd:pfam01576 951 KAKLQEMEGTVKSKFKSsiaaleakiaqlEEQLEQESRE-----RQAANKLVRRTEKKLKEVLLQVEDE 1014
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
287-499 |
1.12e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 42.37 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 287 QTVREENCHLNTELQEAKGRQEEQGAQVQRLKDKVahmkdTLGQTQQKVAELEplkEQLRGVQElAASSQQKAALLGEEL 366
Cdd:COG5022 834 ETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKET-----IYLQSAQRVELAE---RQLQELKI-DVKSISSLKLVNLEL 904
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 367 ASAAGARDRTIAELHRSRLEVaevngrlaeLSLHMKEEKCQWSKERTGLLQSMEAEKDKIL-KLSAEILRLeKTVQEERS 445
Cdd:COG5022 905 ESEIIELKKSLSSDLIENLEF---------KTELIARLKKLLNNIDLEEGPSIEYVKLPELnKLHEVESKL-KETSEEYE 974
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1958787708 446 QSHMFKTELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQTEKQELLEY 499
Cdd:COG5022 975 DLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPVEVAEL 1028
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
318-524 |
1.15e-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: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 318 KDKVAHMKDTLGQTQQKVAELEPLKEQLRgvQELAASSQQKAALlgeelasaagardRTIAELHRSRLEVAEVNGRLAEL 397
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALE--AELDALQERREAL-------------QRLAEYSWDEIDVASAEREIAEL 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 398 slhmkeekcqwskertgllqsmEAEKDKILKLSAEILRLEKtvqeersqshmfktelarekdsslvQLSESKRELTELRS 477
Cdd:COG4913 674 ----------------------EAELERLDASSDDLAALEE-------------------------QLEELEAELEELEE 706
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1958787708 478 ALRVLQKEKEQLQTEKQELLEYMRKLEARLEKVADEKWNEDAATEDE 524
Cdd:COG4913 707 ELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEE 753
|
|
| zf-C4H2 |
pfam10146 |
Zinc finger-containing protein; This is a family of proteins which appears to have a highly ... |
173-303 |
1.28e-03 |
|
Zinc finger-containing protein; This is a family of proteins which appears to have a highly conserved zinc finger domain at the C terminal end, described as -C-X2-CH-X3-H-X5-C-X2-C-. The structure is predicted to contain a coiled coil. Members are annotated as being tumour-associated antigen HCA127 in humans but this could not confirmed.
Pssm-ID: 462963 [Multi-domain] Cd Length: 213 Bit Score: 40.82 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 173 QVTELRSRVQELEAALATARQEHSELTEQYKGLSrshgELSEERDILSQQQGEHVARILELEDDIQTMSDKVLMKEVELD 252
Cdd:pfam10146 1 ALKDIRHKTAQLEKLKERLLKELEAHENEEKCLK----EYKKEMELLLQEKMAHVEELRLIHADINKMEKVIKEAEEERN 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1958787708 253 RVRDMVKALTREQEKLLGQLKEFQADKEQSEAELQTVREENCHLNTELQEA 303
Cdd:pfam10146 77 RVLEGAVRLHEEYIPLKLEIDRMRRELLGLEELPLLHEEEEDLIQTTIFEK 127
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
149-278 |
1.32e-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: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 149 LQNQLDESQQERNDLMQLKLQLEdqvtELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILSQQQGEHVA 228
Cdd:COG4913 673 LEAELERLDASSDDLAALEEQLE----ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR 748
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1958787708 229 RILE--LEDDIQTMSDKVLMKEVElDRVRDMVKALTREQEKLLGQLKEFQAD 278
Cdd:COG4913 749 ALLEerFAAALGDAVERELRENLE-ERIDALRARLNRAEEELERAMRAFNRE 799
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
152-505 |
1.34e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 42.37 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 152 QLDESQQERNDLMQLKLQLEDQVTELRSRVQELEaalataRQEHSELTEQYKGLSR--SHGELSEERDILSQQQgEHVAR 229
Cdd:COG5022 886 ELKIDVKSISSLKLVNLELESEIIELKKSLSSDL------IENLEFKTELIARLKKllNNIDLEEGPSIEYVKL-PELNK 958
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 230 ILE----LEDDIQTMSDKVLMKEVELDRVRDM---VKALTREQEKLLGQLKEFQADKEQSeaelqtvrEENCHLNTELQE 302
Cdd:COG5022 959 LHEveskLKETSEEYEDLLKKSTILVREGNKAnseLKNFKKELAELSKQYGALQESTKQL--------KELPVEVAELQS 1030
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 303 AKGRQEEQGAQVQRLKDKVAHMKDTLGQTQQKVAELEPLK-EQLRGVQELAASSQQKAA-------------LLGEELAS 368
Cdd:COG5022 1031 ASKIISSESTELSILKPLQKLKGLLLLENNQLQARYKALKlRRENSLLDDKQLYQLESTenllktinvkdleVTNRNLVK 1110
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 369 AAGARDRTIAELHRSRLEVAEVngRLAELSLHMKEEKCQWSKERTGLLQSMEAEKDKILKLSaeILRLEKTVQEERSQSH 448
Cdd:COG5022 1111 PANVLQFIVAQMIKLNLLQEIS--KFLSQLVNTLEPVFQKLSVLQLELDGLFWEANLEALPS--PPPFAALSEKRLYQSA 1186
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958787708 449 MFKtELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQTEKQELLEYMRKLEA 505
Cdd:COG5022 1187 LYD-EKSKLSSSEVNDLKNELIALFSKIFSGWPRGDKLKKLISEGWVPTEYSTSLKG 1242
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
234-422 |
1.35e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 234 EDDIQTMSDKVLMKEVELDRVRDMVKALTREQEKLLGQLKEFQADKEQSEAELQTVREENCHLNTELQEAKGRQEEQGAQ 313
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 314 VQR--------------------------LKDKVAHMKDTLGQTQQKVAELEPLKEQLRGVQELAASSQQKAALLGEELA 367
Cdd:COG3883 95 LYRsggsvsyldvllgsesfsdfldrlsaLSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1958787708 368 SAAGARDRTIAELhrsRLEVAEVNGRLAELSLHMKEEKCQWSKERTGLLQSMEAE 422
Cdd:COG3883 175 AQQAEQEALLAQL---SAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
170-348 |
1.38e-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: 42.25 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 170 LEDQVTELRSRVQELEAALAtaRQEhsELTEQYKGLSRSHGELSEERDILSQQQGEHVARILELEDDIQTMSDKVLMKEV 249
Cdd:COG3096 510 LAQRLQQLRAQLAELEQRLR--QQQ--NAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQ 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 250 ELDRVRDMVKALTREQEKLLGQLKEFQADKEQSEAELQTVReenchlntELQEAKGRQEEQGAQVQRLKDKVAHMKDTLG 329
Cdd:COG3096 586 QLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQ--------EVTAAMQQLLEREREATVERDELAARKQALE 657
|
170 180
....*....|....*....|....*..
gi 1958787708 330 QTQQKVA--------ELEPLKEQLRGV 348
Cdd:COG3096 658 SQIERLSqpggaedpRLLALAERLGGV 684
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
248-357 |
1.41e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 41.28 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 248 EVELDRVRDMVKALTREQEKLLGQLK----EFQADKEQSEAELQTVREENCHLNTELQEAKGRQEEQGAQVQRLKDKVAH 323
Cdd:pfam09787 46 TLELEELRQERDLLREEIQKLRGQIQqlrtELQELEAQQQEEAESSREQLQELEEQLATERSARREAEAELERLQEELRY 125
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1958787708 324 MKDTL--------GQTQQKVAELEPLKEQLRgVQELAASSQQ 357
Cdd:pfam09787 126 LEEELrrskatlqSRIKDREAEIEKLRNQLT-SKSQSSSSQS 166
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
145-458 |
1.42e-03 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 41.59 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 145 KATVLQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKglsrshgELSEERDILSQQQG 224
Cdd:pfam19220 77 RLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEALERQLAAETEQNR-------ALEEENKALREEAQ 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 225 EHVARILELEDDIQTMSDKVLMKEVELDRVRDMVKALTREQEKLLGQLKEFQAdkeQSEAELQTVREENCHLnTELQEAK 304
Cdd:pfam19220 150 AAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAELET---QLDATRARLRALEGQL-AAEQAER 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 305 GRQEEQ-GAQVQRLKDKVAHMKDTLGQTQQKVAELEPLKEQLRGVQELAASSQQKAALLGEELASAAGARDRTIAELHRS 383
Cdd:pfam19220 226 ERAEAQlEEAVEAHRAERASLRMKLEALTARAAATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEAD 305
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958787708 384 RLEVAEVNGRLAELSLHMKEEKCQWSKERTGLLQSMEAEKDKILKLSAEILRLEKTVQEERS----QSHMFKTELAREK 458
Cdd:pfam19220 306 LERRTQQFQEMQRARAELEERAEMLTKALAAKDAALERAEERIASLSDRIAELTKRFEVERAaleqANRRLKEELQRER 384
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
325-508 |
1.54e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 41.60 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 325 KDTLGQTQQKVAELEplkeqlRGVQElaaSSQQKAALLGE----ELASAAGARdrtiaELHRSRLEVAEVNGRLAELSLH 400
Cdd:PRK11637 46 RDQLKSIQQDIAAKE------KSVRQ---QQQQRASLLAQlkkqEEAISQASR-----KLRETQNTLNQLNKQIDELNAS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 401 MKEEKCQWSKERTGLLQSMEAE----KDKILKLsaeILRLEKTVQEERSQSHMFKTELAREKdsSLVQLSESKRELTELR 476
Cdd:PRK11637 112 IAKLEQQQAAQERLLAAQLDAAfrqgEHTGLQL---ILSGEESQRGERILAYFGYLNQARQE--TIAELKQTREELAAQK 186
|
170 180 190
....*....|....*....|....*....|..
gi 1958787708 477 SALrvlqkekEQLQTEKQELLEYMRKLEARLE 508
Cdd:PRK11637 187 AEL-------EEKQSQQKTLLYEQQAQQQKLE 211
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
171-492 |
1.56e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.87 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 171 EDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRshgelseerdiLSQQQGEHVARILELEDDiqTMSDKVLMKEVE 250
Cdd:PRK04863 836 EAELRQLNRRRVELERALADHESQEQQQRSQLEQAKE-----------GLSALNRLLPRLNLLADE--TLADRVEEIREQ 902
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 251 LDRVRDmVKALTREQEKLLGQLkefqadkEQSEAELQTVREENCHLNTELQEAKGRQEEQGAQVQRLKD---KVAHMKDT 327
Cdd:PRK04863 903 LDEAEE-AKRFVQQHGNALAQL-------EPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEvvqRRAHFSYE 974
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 328 lgQTQQKVAELEPLKEQLRgvqelaassqqkaallgEELASAAGARDRTIAELHRSRLEVAEVNGRLAEL--SLHMKEEK 405
Cdd:PRK04863 975 --DAAEMLAKNSDLNEKLR-----------------QRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLksSYDAKRQM 1035
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 406 CQWSKER---TGLLQSMEAEKdkilKLSAEILRLEKTVQEERSQshmfktelareKDSSLVQLSESKRELTELRSALRVL 482
Cdd:PRK04863 1036 LQELKQElqdLGVPADSGAEE----RARARRDELHARLSANRSR-----------RNQLEKQLTFCEAEMDNLTKKLRKL 1100
|
330
....*....|
gi 1958787708 483 QKEKEQLQTE 492
Cdd:PRK04863 1101 ERDYHEMREQ 1110
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
138-450 |
1.81e-03 |
|
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: 41.88 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 138 DILLVVPKATVLQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQykglsrshgELSEERD 217
Cdd:TIGR00618 595 RLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQE---------RVREHAL 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 218 ILSQQQGEHVARILELEDDIQTMSDKVLMKEVELDRvrdmVKALTREQEKLLGQL-KEFQADKEQSEAELQTVREENCHL 296
Cdd:TIGR00618 666 SIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQ----CQTLLRELETHIEEYdREFNEIENASSSLGSDLAAREDAL 741
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 297 NTELQEAKGRQEEQgAQVQRLKDKVAHMKDTLG-QTQQKVAELE-PLKEQLRGVQELAASSQQKAALLGEELASAAGARD 374
Cdd:TIGR00618 742 NQSLKELMHQARTV-LKARTEAHFNNNEEVTAAlQTGAELSHLAaEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILN 820
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958787708 375 rtiAELHRSRLEVAEVNGRLAELSLHMKEEKCQWSKERTGLLQsmeaeKDKILKLSAEILRLEKTVQEERSQSHMF 450
Cdd:TIGR00618 821 ---LQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQ-----LAQLTQEQAKIIQLSDKLNGINQIKIQF 888
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
145-505 |
1.94e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.43 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 145 KATVLQ---NQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEaalatarQEHSELTEQYKGLSRSHGELSEERDILSQ 221
Cdd:PRK01156 330 KLSVLQkdyNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIE-------SLKKKIEEYSKNIERMSAFISEILKIQEI 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 222 QQGEHVARILELEDDIQTMSDKVLMKEVELDRVRDMVKALTREQEKLLGQ------------------LKEFQADKEQSE 283
Cdd:PRK01156 403 DPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQsvcpvcgttlgeeksnhiINHYNEKKSRLE 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 284 AELQTVREENCHLNTELQEAKGRQEE-QGAQVQRLKDKVAHMKDTLGQTQQKVAELEPLKEQLRGVQELaaSSQQKAALL 362
Cdd:PRK01156 483 EKIREIEIEVKDIDEKIVDLKKRKEYlESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEI--KNRYKSLKL 560
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 363 G------EELASAAGARDRTIAELHRSRLEvaEVNGRLAELSLHMKEEKCQWS----------KERTGLLQSMEAEKDKI 426
Cdd:PRK01156 561 EdldskrTSWLNALAVISLIDIETNRSRSN--EIKKQLNDLESRLQEIEIGFPddksyidksiREIENEANNLNNKYNEI 638
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 427 LKLSAEILRLEKTVQEERSQSHMFKTELAREKDSSlVQLSES--------------KRELTELRSALRVLQKEKEQLQ-- 490
Cdd:PRK01156 639 QENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEIT-SRINDIednlkksrkalddaKANRARLESTIEILRTRINELSdr 717
|
410
....*....|....*.
gi 1958787708 491 -TEKQELLEYMRKLEA 505
Cdd:PRK01156 718 iNDINETLESMKKIKK 733
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
145-525 |
2.09e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 145 KATVLQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGlsrshgELSEERDILSQQQG 224
Cdd:PTZ00121 1063 KAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKK------KAEDARKAEEARKA 1136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 225 EHVARILELEDDIQTMSDKVLMKEVELDRVRDMVKALTREQEKLLGQLKEFQADKEQSEAELQTVREENCHLNTELQEAK 304
Cdd:PTZ00121 1137 EDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEE 1216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 305 GRQEEQGAQVQRLKDKVAHMKDtlgQTQQKVAELEPLKEQLRGVQE--LAASSQQKAALLGEELASA---AGARDRTIAE 379
Cdd:PTZ00121 1217 ARKAEDAKKAEAVKKAEEAKKD---AEEAKKAEEERNNEEIRKFEEarMAHFARRQAAIKAEEARKAdelKKAEEKKKAD 1293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 380 LHRSRLEVAEVN--GRLAELSLHMKE--EKCQWSKERTGLLQSMEAEK---DKILKLSAEILRLEKTVQEERSQSHMFKT 452
Cdd:PTZ00121 1294 EAKKAEEKKKADeaKKKAEEAKKADEakKKAEEAKKKADAAKKKAEEAkkaAEAAKAEAEAAADEAEAAEEKAEAAEKKK 1373
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958787708 453 ELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQTEKQElleymRKLEARLEKVADEKWNEDAATEDEE 525
Cdd:PTZ00121 1374 EEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAA-----KKKADEAKKKAEEKKKADEAKKKAE 1441
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
149-289 |
2.18e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.54 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 149 LQNQLDESQQERNDLMQLKLQLEDQ----------------VTELRSRVQELEAALATARQ----EHS---ELTEQYKGL 205
Cdd:COG3206 224 LESQLAEARAELAEAEARLAALRAQlgsgpdalpellqspvIQQLRAQLAELEAELAELSArytpNHPdviALRAQIAAL 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 206 --------SRSHGELSEERDILSQQQGEHVARILELEDDIQTMSDKvlmkEVELDRVRDMVKALTREQEKLLGQLKEFQA 277
Cdd:COG3206 304 raqlqqeaQRILASLEAELEALQAREASLQAQLAQLEARLAELPEL----EAELRRLEREVEVARELYESLLQRLEEARL 379
|
170
....*....|..
gi 1958787708 278 DKEQSEAELQTV 289
Cdd:COG3206 380 AEALTVGNVRVI 391
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
146-526 |
2.93e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.04 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 146 ATVLQNQLDESQQERNDLMQLKLQLE---DQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILSQQ 222
Cdd:PRK01156 168 YDKLKDVIDMLRAEISNIDYLEEKLKssnLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 223 QGEhvarILELEDDIQTMSDK---VLMKEVELDRVRDMVKALT-----------REQEKLLGQLKEFQADKEQSEAELQT 288
Cdd:PRK01156 248 EDM----KNRYESEIKTAESDlsmELEKNNYYKELEERHMKIIndpvyknrnyiNDYFKYKNDIENKKQILSNIDAEINK 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 289 VrEENCHLNTELQEAKGRQEEQGAQVQRLKDKVAHMKDTLGQTQQKVAELEPLKEQLRgvqELAASSQQKAALLGEELAS 368
Cdd:PRK01156 324 Y-HAIIKKLSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIE---EYSKNIERMSAFISEILKI 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 369 AAGARDRTIAELHRSRLEVAEVNGRLAELslhmkeekcqwsKERTGLLQSMEAEkdkiLKLSAEILrlektvqEERSQSH 448
Cdd:PRK01156 400 QEIDPDAIKKELNEINVKLQDISSKVSSL------------NQRIRALRENLDE----LSRNMEML-------NGQSVCP 456
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958787708 449 MFKTELAREKDSSLVQlsESKRELTELRSALRVLQKEKEQLQTEKQELleymRKLEARLEKVADEKW-NEDAATEDEEA 526
Cdd:PRK01156 457 VCGTTLGEEKSNHIIN--HYNEKKSRLEEKIREIEIEVKDIDEKIVDL----KKRKEYLESEEINKSiNEYNKIESARA 529
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
165-544 |
3.05e-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: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 165 QLKLQLEDQVTELR----------SRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILSQQQGEHVARILELE 234
Cdd:pfam15921 594 QLEKEINDRRLELQefkilkdkkdAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLS 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 235 DDIQTMSDKVLMKEVELDRVRDmvkaltreqeKLLGQLKEFQADKEQSEAELQTVREENCHlntELQEAKGRQEEQGA-- 312
Cdd:pfam15921 674 EDYEVLKRNFRNKSEEMETTTN----------KLKMQLKSAQSELEQTRNTLKSMEGSDGH---AMKVAMGMQKQITAkr 740
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 313 -QVQRLKDKVAHMKDTLGQTQQKVAELEPLKEQLRgvQELAASSQQKAALLGEelASAAGARDRTIAE--------LHRS 383
Cdd:pfam15921 741 gQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLS--QELSTVATEKNKMAGE--LEVLRSQERRLKEkvanmevaLDKA 816
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 384 RLEVAEVNG---RLAELSLHMKEEKCQWSKERTGL-LQSMEAEKDKILKlSAEILRLEKTVQEERSQS-----HMFKTEL 454
Cdd:pfam15921 817 SLQFAECQDiiqRQEQESVRLKLQHTLDVKELQGPgYTSNSSMKPRLLQ-PASFTRTHSNVPSSQSTAsflshHSRKTNA 895
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 455 AREkdsslvqlsESKRELTELRSALRVLQKEKEQLQTEKQE----------LLEYMRKLEARLEKVADEKWNEDAATEDE 524
Cdd:pfam15921 896 LKE---------DPTRDLKQLLQELRSVINEEPTVQLSKAEdkgrapslgaLDDRVRDCIIESSLRSDICHSSSNSLQTE 966
|
410 420
....*....|....*....|...
gi 1958787708 525 EATAGLSC---PAALTDSEDESP 544
Cdd:pfam15921 967 GSKSSETCsrePVLLHAGELEDP 989
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
230-347 |
3.21e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 40.39 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 230 ILELEDDIQTMSDKVLMKEVE-LDRVRDMVKALTREQEKLLGQLKEFQADKEQ-SEAELQTVREENCHLNTELQEAKGRQ 307
Cdd:smart00787 148 GLDENLEGLKEDYKLLMKELElLNSIKPKLRDRKDALEEELRQLKQLEDELEDcDPTELDRAKEKLKKLLQEIMIKVKKL 227
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1958787708 308 EEQGAQVQRLKDKVAHMKDTLGQTQQKVAELEPLKEQLRG 347
Cdd:smart00787 228 EELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRG 267
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
375-526 |
3.99e-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: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 375 RTIAELHRSRLEVAEVNGRLAELSLHMKEEKcqwsKERTGLLQSMEAEKDKILKLSAEILRLEKTVQE-----ERSQSHM 449
Cdd:COG1579 7 RALLDLQELDSELDRLEHRLKELPAELAELE----DELAALEARLEAAKTELEDLEKEIKRLELEIEEveariKKYEEQL 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958787708 450 FKTELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQTEKQELLEYMRKLEARLEKVADEKWNEDAATEDEEA 526
Cdd:COG1579 83 GNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELE 159
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
117-505 |
4.08e-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: 40.71 E-value: 4.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 117 QFREPRPMDELVTLEEADGG--------SDILLVVPKATVLQNQLDESQQernDLMQLKLQLEDQ---VTELRSRVQELE 185
Cdd:COG3096 305 QYRLVEMARELEELSARESDleqdyqaaSDHLNLVQTALRQQEKIERYQE---DLEELTERLEEQeevVEEAAEQLAEAE 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 186 AALATARQEHSELTEQYKGLSRSHGELsEERDILSQQ---QGEHVARILELED-DIQTMSDkvlmkevELDRVRDMVKAL 261
Cdd:COG3096 382 ARLEAAEEEVDSLKSQLADYQQALDVQ-QTRAIQYQQavqALEKARALCGLPDlTPENAED-------YLAAFRAKEQQA 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 262 TREQEKLLGQLKEFQADKEQSEAELQTVREENCHlnTELQEAKGRQEEQGAQVQRLKdkvaHMKDTLGQTQQKVAELEPL 341
Cdd:COG3096 454 TEEVLELEQKLSVADAARRQFEKAYELVCKIAGE--VERSQAWQTARELLRRYRSQQ----ALAQRLQQLRAQLAELEQR 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 342 KEQLRGVQELAASSQQKAallGEELASAAGardrtiAELHRSRLEVaevngRLAELSLHMKEEkcqwSKERTGLLQSMEA 421
Cdd:COG3096 528 LRQQQNAERLLEEFCQRI---GQQLDAAEE------LEELLAELEA-----QLEELEEQAAEA----VEQRSELRQQLEQ 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 422 EKDKILKLSAeilrlektvqeersqshmfKTELAREKDSSLVQLSE-------SKRELTELRSAL----RVLQKEKEQLQ 490
Cdd:COG3096 590 LRARIKELAA-------------------RAPAWLAAQDALERLREqsgealaDSQEVTAAMQQLlereREATVERDELA 650
|
410
....*....|....*
gi 1958787708 491 TEKQELLEYMRKLEA 505
Cdd:COG3096 651 ARKQALESQIERLSQ 665
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
149-367 |
4.88e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 40.28 E-value: 4.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 149 LQNQLDESQQERNDLMQLKlQLEDQVTELRSRVQELEAALATArqeHSELTEQYKGLSRSHGELSEerdilSQQqgehva 228
Cdd:PRK11281 106 LKDDNDEETRETLSTLSLR-QLESRLAQTLDQLQNAQNDLAEY---NSQLVSLQTQPERAQAALYA-----NSQ------ 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 229 RILELEDdiqtmsdkvlmkevELDRVRDMVKALTREQ-EKLLGQLKEFQADKEQSEAELQTvreenchlNTELQE-AKGR 306
Cdd:PRK11281 171 RLQQIRN--------------LLKGGKVGGKALRPSQrVLLQAEQALLNAQNDLQRKSLEG--------NTQLQDlLQKQ 228
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958787708 307 QEEQGAQVQRLKDKVAHMKDT-----LGQTQQKVAELEplkeqlrgVQELAASSQQKaALLGEELA 367
Cdd:PRK11281 229 RDYLTARIQRLEHQLQLLQEAinskrLTLSEKTVQEAQ--------SQDEAARIQAN-PLVAQELE 285
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
460-514 |
5.98e-03 |
|
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];
Pssm-ID: 443204 [Multi-domain] Cd Length: 287 Bit Score: 39.33 E-value: 5.98e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1958787708 460 SSLVQLSESKRELTELRSALRVLQKEKEQLQTEKQELLEYMRKLEARLEKVADEK 514
Cdd:COG4026 125 QNIPEYNELREELLELKEKIDEIAKEKEKLTKENEELESELEELREEYKKLREEN 179
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
149-515 |
6.32e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 39.67 E-value: 6.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 149 LQNQLDESQQE-------RNDLMQLKLQLEDQVTELRSRVQELEAALATARQehselteqykglsrshgeLSEERDILSq 221
Cdd:pfam05622 64 LQKQLEQLQEEnfrletaRDDYRIKCEELEKEVLELQHRNEELTSLAEEAQA------------------LKDEMDILR- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 222 qqgEHVARILELEDDIQTMSDKV-----LMKEVELDRVRDMVKAL-TREQEKllgQLKEFQADKEQSEAELQTVREENCH 295
Cdd:pfam05622 125 ---ESSDKVKKLEATVETYKKKLedlgdLRRQVKLLEERNAEYMQrTLQLEE---ELKKANALRGQLETYKRQVQELHGK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 296 LNTELQEAK------GRQEEQGAQVQRLKDKVAHMKDTLGQTQqkvaeleplkEQLRGVQELAASSQQKAALLGEELASA 369
Cdd:pfam05622 199 LSEESKKADklefeyKKLEEKLEALQKEKERLIIERDTLRETN----------EELRCAQLQQAELSQADALLSPSSDPG 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 370 agarDRTIAELHRSrlEVAEVNGRLAELSLHMKEEKCQWSKERTGLLQSM--EAEK-------------DKILKLSAEIL 434
Cdd:pfam05622 269 ----DNLAAEIMPA--EIREKLIRLQHENKMLRLGQEGSYRERLTELQQLleDANRrkneletqnrlanQRILELQQQVE 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 435 RLEKTVQEERSQSHMFKTeLAREKDSSLVQLSESKRELTELRSALRVLQ-KEKEQLQTEKQELLEYMRKLEARLeKVADE 513
Cdd:pfam05622 343 ELQKALQEQGSKAEDSSL-LKQKLEEHLEKLHEAQSELQKKKEQIEELEpKQDSNLAQKIDELQEALRKKDEDM-KAMEE 420
|
..
gi 1958787708 514 KW 515
Cdd:pfam05622 421 RY 422
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
176-526 |
6.51e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.12 E-value: 6.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 176 ELRsRVQELEAALATARQEHSELTEQYKGLSRSHgELSEERDILSQQQGEHV------ARILELEDDIQTMSDKVLMKEV 249
Cdd:PTZ00121 1186 EVR-KAEELRKAEDARKAEAARKAEEERKAEEAR-KAEDAKKAEAVKKAEEAkkdaeeAKKAEEERNNEEIRKFEEARMA 1263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 250 ELDRVRDMVKALTREQEKLLGQLKEFQADKEQSEAELQTVREEnchLNTELQEAKgRQEEQGAQVQRLKDKVAHMKDTlG 329
Cdd:PTZ00121 1264 HFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADE---AKKKAEEAK-KADEAKKKAEEAKKKADAAKKK-A 1338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 330 QTQQKVAELEPLKEQLRGVQELAASSQQKAALLGEELASAAGARDRTIAELHRSRLEV---AEVNGRLAELSLHMKEEKc 406
Cdd:PTZ00121 1339 EEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAkkkAEEDKKKADELKKAAAAK- 1417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 407 qwSKERTGLLQSMEAEKDKILKLSAEILR----LEKTVQEERSQSHMFKTELAREKDSSLVQLSESKRELTELRSALRVL 482
Cdd:PTZ00121 1418 --KKADEAKKKAEEKKKADEAKKKAEEAKkadeAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEA 1495
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1958787708 483 QKEKEQLQTEKQElleymrKLEARLEKVADEKWNEDAATEDEEA 526
Cdd:PTZ00121 1496 KKKADEAKKAAEA------KKKADEAKKAEEAKKADEAKKAEEA 1533
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
146-510 |
6.69e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 39.77 E-value: 6.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 146 ATVLQNQLDESQQERNDL-MQL--------------------KLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKG 204
Cdd:pfam01576 217 STDLQEQIAELQAQIAELrAQLakkeeelqaalarleeetaqKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRD 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 205 LSRS----HGELSEERDILSQQQGEHVARILELEDDIQTMSDKVLMKEVEldrVRDMVKALTREQEKLLGQLKEFQADKE 280
Cdd:pfam01576 297 LGEElealKTELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQ---LQEMRQKHTQALEELTEQLEQAKRNKA 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 281 QSEAELQTVREENCHLNTELQEAKGRQEEQGAQVQRLKDKVAHMKDTLGQTQQKVAELeplkeqlrgvqelaassQQKAA 360
Cdd:pfam01576 374 NLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAEL-----------------AEKLS 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 361 LLGEELASAAGARDRTIAELHRSRLEVAEVNGRLAELSLHMKEEKCQWSKERTGLLQsMEAEKDkilklsaeilrlekTV 440
Cdd:pfam01576 437 KLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQ-LEDERN--------------SL 501
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 441 QEERSQSHMFKTELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQTEKQELLEYMRKLEARLEKV 510
Cdd:pfam01576 502 QEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKL 571
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
117-548 |
6.79e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.12 E-value: 6.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 117 QFREPRPMDELVTLEEADGGSDillVVPKATVLQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHS 196
Cdd:PTZ00121 1219 KAEDAKKAEAVKKAEEAKKDAE---EAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEA 1295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 197 ELTEQYKGLSRSHGELSEER--DILSQQQGEHVARILELEDDIQTMSDKVLMKEVELDRVRDMVKAltREQEKLLGQLKE 274
Cdd:PTZ00121 1296 KKAEEKKKADEAKKKAEEAKkaDEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEA--AEEKAEAAEKKK 1373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 275 FQADKEQSEAELQTvrEENchlnTELQEAKGRQEEQGAQVQRLKDKVAHMK--DTLGQTQQKVAELEPLK---EQLRGVQ 349
Cdd:PTZ00121 1374 EEAKKKADAAKKKA--EEK----KKADEAKKKAEEDKKKADELKKAAAAKKkaDEAKKKAEEKKKADEAKkkaEEAKKAD 1447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 350 ELA--ASSQQKAALLGEELASAAGARD-RTIAELHRSRLEV---AEVNGRLAELSLHMKEEKcqwsKERTGLLQSMEAEK 423
Cdd:PTZ00121 1448 EAKkkAEEAKKAEEAKKKAEEAKKADEaKKKAEEAKKADEAkkkAEEAKKKADEAKKAAEAK----KKADEAKKAEEAKK 1523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 424 DKILKLSAEILRLE--KTVQEERSQSHMFKTE---LAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQtEKQELLE 498
Cdd:PTZ00121 1524 ADEAKKAEEAKKADeaKKAEEKKKADELKKAEelkKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIE-EVMKLYE 1602
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1958787708 499 YMRKLEA-RLEKVADEKWNEDAATEDEEATAGLSCPAALTDSEDESPEDMR 548
Cdd:PTZ00121 1603 EEKKMKAeEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELK 1653
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
211-525 |
7.78e-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: 39.72 E-value: 7.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 211 ELSEERDILSQQQGEHVARILE-----LEDDIQTMSDKVLMKEVELDRVRDMVKAL-TREQEKLLGQ--LKEFQADKEQS 282
Cdd:pfam15921 60 ELDSPRKIIAYPGKEHIERVLEeyshqVKDLQRRLNESNELHEKQKFYLRQSVIDLqTKLQEMQMERdaMADIRRRESQS 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 283 EAELQTVREENCHlntELQEAKGRQEE----QGAQVQRLKDKVAHMKDTLGQTQQKVAELEplkeqlrgvQELAASSQQK 358
Cdd:pfam15921 140 QEDLRNQLQNTVH---ELEAAKCLKEDmledSNTQIEQLRKMMLSHEGVLQEIRSILVDFE---------EASGKKIYEH 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 359 AALLGEELASAAGARDRTIAELHRsrlEVAEVNGRLAELSLHMKEEKCQwSKERTGLLqsMEAEKDKILKL----SAEIL 434
Cdd:pfam15921 208 DSMSTMHFRSLGSAISKILRELDT---EISYLKGRIFPVEDQLEALKSE-SQNKIELL--LQQHQDRIEQLisehEVEIT 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 435 RLEKTVQEERSQSHMFKTEL------AREKDSS-LVQLSESKRELTELRSALRVLQK--EKEQLQTEKQELLEYMRKLEA 505
Cdd:pfam15921 282 GLTEKASSARSQANSIQSQLeiiqeqARNQNSMyMRQLSDLESTVSQLRSELREAKRmyEDKIEELEKQLVLANSELTEA 361
|
330 340
....*....|....*....|
gi 1958787708 506 RLEKvadEKWNEDAATEDEE 525
Cdd:pfam15921 362 RTER---DQFSQESGNLDDQ 378
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
332-525 |
8.67e-03 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 39.32 E-value: 8.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 332 QQKVAELEPLK-EQLRGVQELAASSQQKAALLGEELASAAGARDRTIAELHRSRLEVAEVNGRLAELSLHMK-------- 402
Cdd:pfam03528 7 QQRVAELEKENaEFYRLKQQLEAEFNQKRAKFKELYLAKEEDLKRQNAVLQEAQVELDALQNQLALARAEMEnikavatv 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 403 ----------EEKCQWSKERTGLLQSMeaeKDKILKLSAEI-LRLEktvqEERSQSHMFKTELAREKDSSLVQLSESKRE 471
Cdd:pfam03528 87 sentkqeaidEVKSQWQEEVASLQAIM---KETVREYEVQFhRRLE----QERAQWNQYRESAEREIADLRRRLSEGQEE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1958787708 472 lTELRSALRVLQKEKEQLQTEKQELLEYMRKLEARLEKvADEKWNEDAATEDEE 525
Cdd:pfam03528 160 -ENLEDEMKKAQEDAEKLRSVVMPMEKEIAALKAKLTE-AEDKIKELEASKMKE 211
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
158-513 |
9.19e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 39.32 E-value: 9.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 158 QERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLS-RSHGELSEERDILSQQQG-EHVARILEleD 235
Cdd:pfam05483 85 KEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSlKLEEEIQENKDLIKENNAtRHLCNLLK--E 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 236 DIQTMSDKVLMKEVELDRVRDMVKALTREQEKLLGQLKEFQADKEQSEAELQTVREENC----HLNTELQEAKGRQEEQG 311
Cdd:pfam05483 163 TCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHekiqHLEEEYKKEINDKEKQV 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 312 A----QVQRLKDKVAHMKDTLGQTQQKVAELEplkEQLRGVQELAASSQQKAALLGEELASAAGARDRTIAELHRSRLEV 387
Cdd:pfam05483 243 SllliQITEKENKMKDLTFLLEESRDKANQLE---EKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDL 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 388 AEVNGRLAELSLHMKEEKCQWSKERTGLLQSMEAEKDKILKLSaEILRLEKTVQEERSQSHMFKTELAREKDSSLvqlse 467
Cdd:pfam05483 320 QIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLE-ELLRTEQQRLEKNEDQLKIITMELQKKSSEL----- 393
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1958787708 468 skRELTELRSALRVLQKEKEQLQTEKQELLEYMRKlearLEKVADE 513
Cdd:pfam05483 394 --EEMTKFKNNKEVELEELKKILAEDEKLLDEKKQ----FEKIAEE 433
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
236-389 |
9.26e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 39.22 E-value: 9.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 236 DIQTMSDKVLM------KEVELDRVRDMVKALTREQE---KLLGQLKEfQADKEQSEAELQTVREENCHLNTELQEAKGR 306
Cdd:pfam05262 173 DTDSISDKKVVealredNEKGVNFRRDMTDLKERESQedaKRAQQLKE-ELDKKQIDADKAQQKADFAQDNADKQRDEVR 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 307 QEEQGAQVQRLKDKV--AHMKDTLGQTQQKVAElEPLKEQLRGVQELAASSQQKAALLGEELASAAGARDRTIAELHRSR 384
Cdd:pfam05262 252 QKQQEAKNLPKPADTssPKEDKQVAENQKREIE-KAQIEIKKNDEEALKAKDHKAFDLKQESKASEKEAEDKELEAQKKR 330
|
....*
gi 1958787708 385 LEVAE 389
Cdd:pfam05262 331 EPVAE 335
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
145-526 |
9.41e-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: 39.64 E-value: 9.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 145 KATVLQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELT---EQYKGLSRSHGELSEERDILSQ 221
Cdd:TIGR00606 218 KACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKalkSRKKQMEKDNSELELKMEKVFQ 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 222 QQGEhvarilELEDDIQTMSDKVLMKEVELDRVRDMVKALTREQEKLLGQLKEFQADKEQSEAELQTVREENCHLNTELQ 301
Cdd:TIGR00606 298 GTDE------QLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQ 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 302 EAKGRQE----EQGAQVQRLKDKVAHMKDTLGQTQQKVAE--LEPLKEQLRGVQELAASSQQKAALLGEELASAAGARDR 375
Cdd:TIGR00606 372 SLATRLEldgfERGPFSERQIKNFHTLVIERQEDEAKTAAqlCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEK 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 376 TIAELHRSRLEVAEVNG---RLAELSLHMKEEKCQWSK-ERTGLLQSMEAEKDKILKLSAEILRLEKTVQEERSQSHMFK 451
Cdd:TIGR00606 452 KQEELKFVIKELQQLEGssdRILELDQELRKAERELSKaEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHT 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 452 TE------LAREKDSSLVQLSESK----------------------------RELTELRSALRVLQKEKEQLQTEKQELL 497
Cdd:TIGR00606 532 TTrtqmemLTKDKMDKDEQIRKIKsrhsdeltsllgyfpnkkqledwlhsksKEINQTRDRLAKLNKELASLEQNKNHIN 611
|
410 420
....*....|....*....|....*....
gi 1958787708 498 EYMRKLEARLEKVADeKWNEDAATEDEEA 526
Cdd:TIGR00606 612 NELESKEEQLSSYED-KLFDVCGSQDEES 639
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
145-435 |
9.43e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 39.57 E-value: 9.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 145 KATVLQNQLDESQQERNDLMQLKLQLEDQVTELRSRVQELEAALATARQEHSELTEQYKGLSRSHGELSEERDILSQQQg 224
Cdd:pfam02463 723 LADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEE- 801
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 225 ehvarilELEDDIQTMSDKVLMKEVELDRVRDMVKALTREQEKLLGQLKEFQADKEQSEAELQTVREENC-HLNTELQEA 303
Cdd:pfam02463 802 -------ELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITkEELLQELLL 874
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170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787708 304 KGRQEEQGAQVQRLKDKVAHMKDTLGQTQQKVAELEPLKEQLRGVQELAASSQQKAALLGEELASAAGARDRTIAELHRS 383
Cdd:pfam02463 875 KEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENN 954
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250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958787708 384 RLEVAEVNGRLAELSLHM----------KEEKCQWSKERTGLLQSMEAEKDKILKLSAEILR 435
Cdd:pfam02463 955 KEEEEERNKRLLLAKEELgkvnlmaieeFEEKEERYNKDELEKERLEEEKKKLIRAIIEETC 1016
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