|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
106-440 |
2.24e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 73.94 E-value: 2.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 106 ESSLKDASYEKESTEAQ--SLEAFYEKLTESKSELEDEILILEKELKEEKSKHSKQDELMSEISKRIQSLEDESKSLKSQ 183
Cdd:TIGR02168 676 RREIEELEEKIEELEEKiaELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 184 VAEAKTTFKIFQMNEERLKIAIKDALSENSQLQESQKQLLQEAEEWREQVNELNKQRMTFEDSKVHVEQVLCDKENQIKS 263
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAA 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 264 LTERLRKMKDWTAVLGEEIAdddNLEWEMKSDSENDAHLDNQPKGALKKLihaAKLRASLKTLEGERNQIYTQLSEVDKT 343
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIE---SLAAEIEELEELIEELESELEALLNER---ASLEEALALLRSELEELSEELRELESK 909
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 344 KEELTECIKNLQTEQASLQSENTQFENETQKLQQKLkvmTELYQENEMILHRKLTMEENYRLEKEEKLSKADEKINH--- 420
Cdd:TIGR02168 910 RSELRRELEELREKLAQLELRLEGLEVRIDNLQERL---SEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKElgp 986
|
330 340
....*....|....*....|....
gi 1387233842 421 ----AAEELETYRKRAKDLEEELE 440
Cdd:TIGR02168 987 vnlaAIEEYEELKERYDFLTAQKE 1010
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
80-377 |
2.63e-12 |
|
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: 70.48 E-value: 2.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 80 ELSTLIEEKCKLlEKFSIVQKEYESLE-----SSLKDASYEKESTEAQ--SLEAFYEKLTESKSELEDEIlilekelkee 152
Cdd:TIGR02169 199 QLERLRREREKA-ERYQALLKEKREYEgyellKEKEALERQKEAIERQlaSLEEELEKLTEEISELEKRL---------- 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 153 kskHSKQDELmSEISKRIQSL-EDESKSLKSQVAEakttfkiFQMNEERLKIAIKDALSENSQLQESQKQ-------LLQ 224
Cdd:TIGR02169 268 ---EEIEQLL-EELNKKIKDLgEEEQLRVKEKIGE-------LEAEIASLERSIAEKERELEDAEERLAKleaeidkLLA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 225 EAEEWREQVNELNKQRMTFEDSKVHVEQVLCDKENQIKSLTERLRKMKDWTAVLGEEIAD-----------DDNLEWEMK 293
Cdd:TIGR02169 337 EIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKlkreinelkreLDRLQEELQ 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 294 SDSENDAHLDNQPKGA---LKKLIHAAK-LRASLKTLEGERNQIYTQLSEVDKTKEELTECIKNLQTEQASLQSENTQFE 369
Cdd:TIGR02169 417 RLSEELADLNAAIAGIeakINELEEEKEdKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAE 496
|
....*...
gi 1387233842 370 NETQKLQQ 377
Cdd:TIGR02169 497 AQARASEE 504
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
85-390 |
6.30e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 69.32 E-value: 6.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 85 IEEKCKLLEKFSIVQKEYESLESSLKDASYEKESTEAQSLEAFYEKLTESKSELEDEILILEKELKEEKSKHSKQDELMS 164
Cdd:TIGR02168 198 LERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVS 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 165 EISKRIQSLEDESKSLKSQVAEAKTTFKIFQMNEERLKIAIKDALSENSQLQESQKQLLQEAEEWREQVNELNKQRMTFE 244
Cdd:TIGR02168 278 ELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 245 DSKVHVEQVLCDKENQIKSLTERLRKMKDWTAVLGEEIADDDN----LEWEMKSDSENDAHLDNQPKGALKKLihaakLR 320
Cdd:TIGR02168 358 AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNeierLEARLERLEDRRERLQQEIEELLKKL-----EE 432
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 321 ASLKTLEGERNQIYTQLSEVDKTKEELTECIKNLQTEQASLQSENTQFENETQKLQQKLKVMTELYQENE 390
Cdd:TIGR02168 433 AELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLE 502
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
75-508 |
6.10e-11 |
|
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: 65.90 E-value: 6.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 75 KKLAIELSTLIEEKCKLLEKFSiVQKEYESLESSLK-DASYEKesteAQSLEAFYEKltesksELEDEILILEKELKEEK 153
Cdd:pfam05483 182 RQVYMDLNNNIEKMILAFEELR-VQAENARLEMHFKlKEDHEK----IQHLEEEYKK------EINDKEKQVSLLLIQIT 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 154 SKHSKQDEL---MSEISKRIQSLEDESKSLKSQVAEAKTTFKIFQMNEERLKIAIKDALSENSQLQE----SQKQLLQEA 226
Cdd:pfam05483 251 EKENKMKDLtflLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEdlqiATKTICQLT 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 227 EEWREQVNELNKQRMTFEDSKVHVEQVLCDKENQIKSLTERLRKMKDWTAVLGEEIADDDN-LEWEMKSDSENDAHLDNQ 305
Cdd:pfam05483 331 EEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSeLEEMTKFKNNKEVELEEL 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 306 PK--GALKKLIHAAK---------------LRASLKTLEGERNQIYTQLSEVDKTKEELTECIKNLQTEQASLQSENTQF 368
Cdd:pfam05483 411 KKilAEDEKLLDEKKqfekiaeelkgkeqeLIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIEL 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 369 ENETQKLQQKLKVMTElyQENEMILHRKLTMEENYRLEKEE-----KLSKADEKINHAAEELETYRKRAKDLEEELERTI 443
Cdd:pfam05483 491 TAHCDKLLLENKELTQ--EASDMTLELKKHQEDIINCKKQEermlkQIENLEEKEMNLRDELESVREEFIQKGDEVKCKL 568
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1387233842 444 HSYQGQIISHEKKAHDNWLAARTAERNLNDLRKEnAHNRQKltetefKIELLEKDPYALDVPNTA 508
Cdd:pfam05483 569 DKSEENARSIEYEVLKKEKQMKILENKCNNLKKQ-IENKNK------NIEELHQENKALKKKGSA 626
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
160-469 |
3.21e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.80 E-value: 3.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 160 DELMSEISKRIQSLEDES------KSLKSQVAEAKTTFKIFQMNEERLKIAIKDAlsensQLQESQKQLLQEAEEWREQV 233
Cdd:COG1196 192 EDILGELERQLEPLERQAekaeryRELKEELKELEAELLLLKLRELEAELEELEA-----ELEELEAELEELEAELAELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 234 NELNKQRMTFEDSKVHVEQVLcDKENQIKSLTERLRKMKDWTAVLGEEIADD-DNLEWEMKSDSENDAHLDNQPKGALKK 312
Cdd:COG1196 267 AELEELRLELEELELELEEAQ-AEEYELLAELARLEQDIARLEERRRELEERlEELEEELAELEEELEELEEELEELEEE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 313 LIHA-AKLRASLKTLEGERNQIYTQLSEVDKTKEELTECIKNLQTEQASLQSENTQFENETQKLQQKLKVMTELYQENEM 391
Cdd:COG1196 346 LEEAeEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387233842 392 ILHRKLTMEENyRLEKEEKLSKADEKINHAAEELETYRKRAKDLEEELERTIHSYQGQIISHEKKAHDNWLAARTAER 469
Cdd:COG1196 426 LEEALAELEEE-EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
76-498 |
5.35e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.16 E-value: 5.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 76 KLAIELSTLIEEKCKLLEKFSIVQKEYESLESSLKD-ASYEKESTEAQSLEAFYEKLTESKSELEDEILILEKELKEEKS 154
Cdd:PRK03918 242 ELEKELESLEGSKRKLEEKIRELEERIEELKKEIEElEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEE 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 155 KHSKQDELMSEISK---RIQSLEDESKSLKSQVAEAKTTFKIFQMNEERLKIA--IKDALSENSQlqESQKQLLQEAEEW 229
Cdd:PRK03918 322 EINGIEERIKELEEkeeRLEELKKKLKELEKRLEELEERHELYEEAKAKKEELerLKKRLTGLTP--EKLEKELEELEKA 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 230 REqvnELNKQRMTFEDSKVHVEQvlcdKENQIKSLTERLRKMKDWTAVLGEEIADDDNLEW------EMKSDSENDAHLD 303
Cdd:PRK03918 400 KE---EIEEEISKITARIGELKK----EIKELKKAIEELKKAKGKCPVCGRELTEEHRKELleeytaELKRIEKELKEIE 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 304 NQPKgalkklihaaKLRASLKTLEGERNQIYTQLSEvdktkEELTECIKNLQTEQASLQSEntqfenetqKLQQKLKVMT 383
Cdd:PRK03918 473 EKER----------KLRKELRELEKVLKKESELIKL-----KELAEQLKELEEKLKKYNLE---------ELEKKAEEYE 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 384 ELYQENEMILHRKLTMEEnyRLEKEEKLSKADEKINHAAEELEtyrKRAKDLEEELERTIHSYQGQI---ISHEKKAHDN 460
Cdd:PRK03918 529 KLKEKLIKLKGEIKSLKK--ELEKLEELKKKLAELEKKLDELE---EELAELLKELEELGFESVEELeerLKELEPFYNE 603
|
410 420 430
....*....|....*....|....*....|....*...
gi 1387233842 461 WLAARTAERNLNDLRKENAHNRQKLTETEFKIELLEKD 498
Cdd:PRK03918 604 YLELKDAEKELEREEKELKKLEEELDKAFEELAETEKR 641
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
91-441 |
5.43e-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: 63.16 E-value: 5.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 91 LLEKFSIVQKEYESLESSLKDASYEKEstEAQSLEAFYEKLTESKSELEDEILILEKELKEEKSKHSKQDELMSEISKRI 170
Cdd:TIGR02169 648 LFEKSGAMTGGSRAPRGGILFSRSEPA--ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEI 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 171 QSLEDESKSLKSQVAEAKTTFKIFQMNEERLKIAIKDALSENSQLQEsqkqllqEAEEWREQVNEL----NKQRM-TFED 245
Cdd:TIGR02169 726 EQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEE-------DLHKLEEALNDLearlSHSRIpEIQA 798
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 246 SKVHVEQVLCDKENQIKSLTERLRKMKDWTAVLGEEIAD--DDNLEWEMKSDSENDA-HLDNQPKGALKKLIhaAKLRAS 322
Cdd:TIGR02169 799 ELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQElqEQRIDLKEQIKSIEKEiENLNGKKEELEEEL--EELEAA 876
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 323 LKTLEGERNQIYtqlSEVDKTKEELTECIKNLQTEQASLQSENTQFENETQKLQQKLKVMTEL---------YQENEMIL 393
Cdd:TIGR02169 877 LRDLESRLGDLK---KERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIedpkgedeeIPEEELSL 953
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1387233842 394 hRKLTMEenyRLEKEEKLSKADEKINHAAEELETYRKRAKDLEEELER 441
Cdd:TIGR02169 954 -EDVQAE---LQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAK 997
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
147-441 |
7.86e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.77 E-value: 7.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 147 KELKEEKSK-HSKQDELmSEISKRIQSLEDESKSLKSQVAEAKTTFKIFQMNEERLKIAIKDALSENSQLQESQKQLLQE 225
Cdd:TIGR02168 684 EKIEELEEKiAELEKAL-AELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 226 AEEWREQVNELNKQRMTFEDSKVHVEQVLCDKENQIKSLTERLRKMKDWTAVLGEEIADDDnlewEMKSDSENDAHLDNQ 305
Cdd:TIGR02168 763 IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLR----ERLESLERRIAATER 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 306 PKGALKKLI-----HAAKLRASLKTLEGERNQIYTQLSEVDKTKEELTECIK-------NLQTEQASLQSENTQFENETQ 373
Cdd:TIGR02168 839 RLEDLEEQIeelseDIESLAAEIEELEELIEELESELEALLNERASLEEALAllrseleELSEELRELESKRSELRRELE 918
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1387233842 374 KLQQKLKVMTELYQENEM-ILHRKLTMEENYRLEKEEklskADEKINHAAEELETYRKRAKDLEEELER 441
Cdd:TIGR02168 919 ELREKLAQLELRLEGLEVrIDNLQERLSEEYSLTLEE----AEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
164-497 |
1.12e-09 |
|
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: 61.96 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 164 SEISKRIQSLEDESKSLKSQVAEAKTtfKIFQMNEERLKIAIKdaLSENSQLQESQKQLLQEAEEWREQVNELNKQRMTF 243
Cdd:TIGR04523 162 NDLKKQKEELENELNLLEKEKLNIQK--NIDKIKNKLLKLELL--LSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 244 EDSKVHVEQVLCDKENQIKSLTERLRKMKDWTAVLGEEIADD----DNLEWEMKSDSENDAHLDNQPKGALKKlihaaKL 319
Cdd:TIGR04523 238 QQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNnkkiKELEKQLNQLKSEISDLNNQKEQDWNK-----EL 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 320 RASLKTLEGERNQIYTQLSEVDKTKEELTECIKNLQTEQASLQSENTQFENETQKLQQKLKVmteLYQENEmilhrkltm 399
Cdd:TIGR04523 313 KSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEK---LKKENQ--------- 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 400 eenyrlEKEEKLSKADEKINhaaeELETYRKRAKDLEEELERTIHSYQGQIISHEKKaHDNWLAARTAERN-LNDLRKEN 478
Cdd:TIGR04523 381 ------SYKQEIKNLESQIN----DLESKIQNQEKLNQQKDEQIKKLQQEKELLEKE-IERLKETIIKNNSeIKDLTNQD 449
|
330
....*....|....*....
gi 1387233842 479 AHNRQKLTETEFKIELLEK 497
Cdd:TIGR04523 450 SVKELIIKNLDNTRESLET 468
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
73-498 |
1.35e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.62 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 73 REKKLAIELSTLIEEKCKLLEK-FSIVQKEYESLESSLKDASYEKE--STEAQSLEAFYEKLTESKSELEdeililekel 149
Cdd:PRK03918 179 ERLEKFIKRTENIEELIKEKEKeLEEVLREINEISSELPELREELEklEKEVKELEELKEEIEELEKELE---------- 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 150 kEEKSKHSKQDELMSEISKRIQSLEDESKSLKSQVAEAKttfKIFQMNEE--RLKIAIKDALSENSQLQESQKQLLQEAE 227
Cdd:PRK03918 249 -SLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK---ELKEKAEEyiKLSEFYEEYLDELREIEKRLSRLEEEIN 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 228 EWREQVNELNKqrmtfedskvhveqvlcdKENQIKSLTERLRKMKDWTAVLGEeiaddDNLEWEMksdsendahldnqpk 307
Cdd:PRK03918 325 GIEERIKELEE------------------KEERLEELKKKLKELEKRLEELEE-----RHELYEE--------------- 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 308 gALKKLIHAAKLRASLKTLEGERnqIYTQLSEVDKTKEELTECIKNLQTEQASLQSENTQFE---NETQKLQQKLKVMTE 384
Cdd:PRK03918 367 -AKAKKEELERLKKRLTGLTPEK--LEKELEELEKAKEEIEEEISKITARIGELKKEIKELKkaiEELKKAKGKCPVCGR 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 385 LYQENemilHRKLTMEEnYRLEkeekLSKADEKINHAAEELETYRKRAKDLEEELER-----TIHSYQGQIISHEKKahd 459
Cdd:PRK03918 444 ELTEE----HRKELLEE-YTAE----LKRIEKELKEIEEKERKLRKELRELEKVLKKeseliKLKELAEQLKELEEK--- 511
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1387233842 460 nwlaarTAERNLNDLRKENAHNR---QKLTETEFKIELLEKD 498
Cdd:PRK03918 512 ------LKKYNLEELEKKAEEYEklkEKLIKLKGEIKSLKKE 547
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
112-440 |
1.00e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.90 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 112 ASYEKESTEAQSLEAFYEKLTESKSELE----DEILILEKELKEEKSKHSKQDELMSE----------ISKRIQSLEDES 177
Cdd:PRK02224 244 EEHEERREELETLEAEIEDLRETIAETErereELAEEVRDLRERLEELEEERDDLLAEaglddadaeaVEARREELEDRD 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 178 KSLKSQVAEAKTTFKIFQMNEERLKIAIKDALSENSQLQESQKQLLQEAEEWREQVNELNKQRMTFEDSKVHVEQVLCDK 257
Cdd:PRK02224 324 EELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDA 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 258 ENQIKSLTERLRKMKDWTAVLGEEIAD-DDNLEWEMKSDSENDAHLD-------NQPkgaLKKLIHAAKL---RASLKTL 326
Cdd:PRK02224 404 PVDLGNAEDFLEELREERDELREREAElEATLRTARERVEEAEALLEagkcpecGQP---VEGSPHVETIeedRERVEEL 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 327 EGERNQIYTQLSEVDKTKEELTECIKNlqteqaslqsentqfENETQKLQQKLKVMTELYQENEMILHRKLTMEENYRLE 406
Cdd:PRK02224 481 EAELEDLEEEVEEVEERLERAEDLVEA---------------EDRIERLEERREDLEELIAERRETIEEKRERAEELRER 545
|
330 340 350
....*....|....*....|....*....|....*..
gi 1387233842 407 KEEKLSKADEK---INHAAEELETYRKRAKDLEEELE 440
Cdd:PRK02224 546 AAELEAEAEEKreaAAEAEEEAEEAREEVAELNSKLA 582
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
316-498 |
1.65e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.14 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 316 AAKLRASLKTLEGERNQIYTQLSEVDKTKEELTECIKNLQTEQASLQSENtqfENETQKLQQKLKVMTELyQENEMILHR 395
Cdd:TIGR02168 693 IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEV---EQLEERIAQLSKELTEL-EAEIEELEE 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 396 KLTMEENYRLEKEEKLSKADEKINHAAEELETYRKRAKDLEEELERT---IHSYQGQIISHEKKAHDNWLAARTAERNLN 472
Cdd:TIGR02168 769 RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLneeAANLRERLESLERRIAATERRLEDLEEQIE 848
|
170 180
....*....|....*....|....*.
gi 1387233842 473 DLRKENAHNRQKLTETEFKIELLEKD 498
Cdd:TIGR02168 849 ELSEDIESLAAEIEELEELIEELESE 874
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
73-443 |
2.46e-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: 2.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 73 REKKLAIElsTLIEEKCKLLEKFSIVQKEYESLESSLKDasYEKESteaQSLEAFYEKLTESKSELEDEILILEKELKEE 152
Cdd:TIGR04523 366 EEKQNEIE--KLKKENQSYKQEIKNLESQINDLESKIQN--QEKLN---QQKDEQIKKLQQEKELLEKEIERLKETIIKN 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 153 KSKHSKQDELMSEISKRIQSLEDESKSLKSQVAEAKTTFKIFQMNEERLKIAIKDALSENSQLQESQKQLLQEAEEWREQ 232
Cdd:TIGR04523 439 NSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKK 518
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 233 VNELNKQRMTFEDSKVHVEQVLCDKENQIKSLTERLRKMKDWTAVLG--EEIA----DDDNLEwemKSDSENDAHLDNQ- 305
Cdd:TIGR04523 519 ISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEknKEIEelkqTQKSLK---KKQEEKQELIDQKe 595
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 306 ------PKGALKKLIHAAKLRASLKTLEGERNQIYTQLSEVDKTKEELTECIKNLQTEQASLQSENTQFENETQKLQQKL 379
Cdd:TIGR04523 596 kekkdlIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKI 675
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1387233842 380 KVMTELYQ--ENEMILHRKLTMEENYRLEKEEKLSKADEKINHAAEELETYRKRAKDLEEELERTI 443
Cdd:TIGR04523 676 DDIIELMKdwLKELSLHYKKYITRMIRIKDLPKLEEKYKEIEKELKKLDEFSKELENIIKNFNKKF 741
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
90-498 |
5.01e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.31 E-value: 5.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 90 KLLEKFSIVQKEYESLESSLKDASYEKESTE-AQSLEAFYEKLTESKSELEDEILilekelkeekskhsKQDELMSEIsK 168
Cdd:COG4717 92 ELQEELEELEEELEELEAELEELREELEKLEkLLQLLPLYQELEALEAELAELPE--------------RLEELEERL-E 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 169 RIQSLEDESKSLKSQVAEAKTTF-KIFQMNEERLKIAIKDALSENSQLQESQKQLLQEAEEWREQVNELNKQRMTFEDSK 247
Cdd:COG4717 157 ELRELEEELEELEAELAELQEELeELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 248 VHVEQVlcdkenqiksltERLRKMKDWTAVLGEEIAdddnLEWEMKSDSENDAHLDNQPKGALKKLIHAAKLRASLKTLE 327
Cdd:COG4717 237 EAAALE------------ERLKEARLLLLIAAALLA----LLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 328 GERNQIYTQLSEVDK-TKEELTECIKNLQTEQASLQSENTQFENETQKLQQKLKVMTELYQENEmilhrkltmEENYRLE 406
Cdd:COG4717 301 GKEAEELQALPALEElEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ---------LEELEQE 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 407 KEEKLSKADekinhaAEELETYRKRAKDLEE--ELERTIHSYQGQIISHEKKAHDNWLAA---------RTAERNLNDLR 475
Cdd:COG4717 372 IAALLAEAG------VEDEEELRAALEQAEEyqELKEELEELEEQLEELLGELEELLEALdeeeleeelEELEEELEELE 445
|
410 420
....*....|....*....|...
gi 1387233842 476 KENAHNRQKLTETEFKIELLEKD 498
Cdd:COG4717 446 EELEELREELAELEAELEQLEED 468
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
77-371 |
6.15e-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: 56.61 E-value: 6.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 77 LAIELSTLIEEKCKLLEKFSIVQKEYESLESSLKDasYEKEsteaqsLEAFYEKLTESKSELEDEILILEKELKEEKSKH 156
Cdd:TIGR02169 728 LEQEEEKLKERLEELEEDLSSLEQEIENVKSELKE--LEAR------IEELEEDLHKLEEALNDLEARLSHSRIPEIQAE 799
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 157 -SKQDELMSEISKRIQS--------------LEDESKSLKSQVAEAKTTFKIFQMNEERLKIAIKDALSENSQLQESQKQ 221
Cdd:TIGR02169 800 lSKLEEEVSRIEARLREieqklnrltlekeyLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRD 879
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 222 LLQEAEEWREQVNELNKQRMTFEDSKVHVEQVLCDKENQIKSLTERLrkmkdwtAVLGEEIADDDNLEWEMKSDSENDAH 301
Cdd:TIGR02169 880 LESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKL-------EALEEELSEIEDPKGEDEEIPEEELS 952
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 302 LDNqpkgaLKKLIHaaKLRASLKTLEGERNQIYTQLSEVDKTKEELTECIKNLQTEQASLQSENTQFENE 371
Cdd:TIGR02169 953 LED-----VQAELQ--RVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKK 1015
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
74-441 |
1.18e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.53 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 74 EKKLAIELSTLIEEKCKLLEKFSIVQKEYESLESSLKDASYEKESTEAQSLEAFYEKLTESKSELEDEILILEKELKEEK 153
Cdd:PTZ00121 1389 EKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEE 1468
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 154 SKHSKQDELMSEISKRIQSLEDESKSLKSQVAEAKTTFKIFQMNEERLKIAIKDALSENSQLQESQK-QLLQEAEEWR-- 230
Cdd:PTZ00121 1469 AKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKaDEAKKAEEKKka 1548
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 231 EQVNELNKQRMTFEDSKVHVEQVLCDKENQIKSLTERLRKMKDWTAvlgEEIADDDNLEWEMKSDSENDAHLDNQPKGAL 310
Cdd:PTZ00121 1549 DELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARI---EEVMKLYEEEKKMKAEEAKKAEEAKIKAEEL 1625
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 311 KKLIHAAKLRASLKTLEGERNQIYTQLSEVDKTKEELTECIKNLQTEQASLQSENTQFENETQKLQQKLKVMTELYQENE 390
Cdd:PTZ00121 1626 KKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAE 1705
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1387233842 391 MIlhRKLTMEEnyrLEKEEKLSKADEKINHAAEELETYRKRAKDLEEELER 441
Cdd:PTZ00121 1706 EL--KKKEAEE---KKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKK 1751
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
208-443 |
2.54e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 53.61 E-value: 2.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 208 ALSENSQLQESQKQLlqeaEEWREQVNELNKQRMTFEDSKVHVEQVLCDKENQIKSLTERLRKMKDWTAVLGEEIADddn 287
Cdd:COG4942 15 AAAQADAAAEAEAEL----EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 288 LEwemKSDSENDAHLDNQpKGALKKLIHAAKLRASLKTLE-----GERNQIYTQLSEVDKTKEELTECIKNLQTEQASLQ 362
Cdd:COG4942 88 LE---KEIAELRAELEAQ-KEELAELLRALYRLGRQPPLAlllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 363 SENTQFENETQKLQQKLKVMTElyqenemiLHRKLTMEENyrlEKEEKLSKADEKINHAAEELETYRKRAKDLEEELERT 442
Cdd:COG4942 164 ALRAELEAERAELEALLAELEE--------ERAALEALKA---ERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
.
gi 1387233842 443 I 443
Cdd:COG4942 233 E 233
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
93-390 |
4.90e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.40 E-value: 4.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 93 EKFSIVQKEYESLESSLKDASYEKESTEAQSLEAFYEKLTESKSELEDEILILEKELKEEKSKHSKQDELMSEISKRIQS 172
Cdd:COG1196 213 ERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 173 LEDESKSLKSQVAEAKTTFKIFQMNEERLKIAIKDALSENSQLQESQKQLLQEAEEWREQVNELNKQRMTFEDSKVHVEQ 252
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 253 VLCDKENQIKSLTERLRKMKdwtAVLGEEIADDDNLEWEMKSDSENDAHLDNQPKGALKKLIHAAKLRASLKTLEGERNQ 332
Cdd:COG1196 373 ELAEAEEELEELAEELLEAL---RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1387233842 333 iytQLSEVDKTKEELTECIKNLQTEQASLQSENTQFENETQKLQQKLKVMTELYQENE 390
Cdd:COG1196 450 ---EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
85-439 |
6.09e-07 |
|
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: 53.20 E-value: 6.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 85 IEEKCKLLEKFSIVQKEYESLESSLKDAsYEKESTEAQSLEAFYEKLTESKSELEDEILILEKELKEEKSKHSKQDELMS 164
Cdd:pfam15921 453 IQGKNESLEKVSSLTAQLESTKEMLRKV-VEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQ 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 165 EIS------KRIQSLEDESKSLKSQVAEAKTTFKIFQMNEERLKIAIKDALSENSQLQESQKQLLQEAEEWREQVNEL-- 236
Cdd:pfam15921 532 ELQhlknegDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFki 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 237 --NKQRMTFEDSKVHVEQVLCDKENQIKSLTERLRKMKDWTAvlgeeiaDDDNLEWEMKSdSENDAHLDNQPKGALKKli 314
Cdd:pfam15921 612 lkDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQ-------ERDQLLNEVKT-SRNELNSLSEDYEVLKR-- 681
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 315 haaKLRASLKTLEGERNQIYTQLSEVDKTKEELTECIKNLQTEQA-------SLQSENTQFENETQKLQQKLKVMTELYQ 387
Cdd:pfam15921 682 ---NFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGhamkvamGMQKQITAKRGQIDALQSKIQFLEEAMT 758
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1387233842 388 ENEMILHrkLTMEENYRLEKEekLSKADEKINHAAEELETYRKRAKDLEEEL 439
Cdd:pfam15921 759 NANKEKH--FLKEEKNKLSQE--LSTVATEKNKMAGELEVLRSQERRLKEKV 806
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
74-493 |
7.99e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.84 E-value: 7.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 74 EKKLAIELSTLIEEKCKLLEKFSIVQKEYESL---ESSLKDASYEKESTEAQSLEAFYEKLTESKSELEDEILILEKELK 150
Cdd:PTZ00121 1340 EAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKkkeEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKK 1419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 151 EEKSKHSKQDELMSEISKRIQSLEDESKSLKSQVAEAKTTFKIFQMNEERLKiaiKDALSENSQLQESQKQLLQEAEEWR 230
Cdd:PTZ00121 1420 ADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK---ADEAKKKAEEAKKADEAKKKAEEAK 1496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 231 EQVNELNKQrmtfEDSKVHVEQVlcdKENQIKSLTERLRKMKdwtavlgEEIADDDNLEWEMKSDSENDAHLDNQPKGAL 310
Cdd:PTZ00121 1497 KKADEAKKA----AEAKKKADEA---KKAEEAKKADEAKKAE-------EAKKADEAKKAEEKKKADELKKAEELKKAEE 1562
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 311 KKLIHAAklraslKTLEGERNQIYTQLSEVDKTKEELTECIKNLQTEQASLQSENTQFENETQKLQQKLKVMTELYQENE 390
Cdd:PTZ00121 1563 KKKAEEA------KKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVE 1636
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 391 milhrKLTMEENYRLEKEEKLSKADEKINHAAEEL----ETYRKRAKDL--EEELERTIHSYQGQIISHEKKAHDNWLAA 464
Cdd:PTZ00121 1637 -----QLKKKEAEEKKKAEELKKAEEENKIKAAEEakkaEEDKKKAEEAkkAEEDEKKAAEALKKEAEEAKKAEELKKKE 1711
|
410 420
....*....|....*....|....*....
gi 1387233842 465 RTAERNLNDLRKENAHNRQKLTETEFKIE 493
Cdd:PTZ00121 1712 AEEKKKAEELKKAEEENKIKAEEAKKEAE 1740
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
106-487 |
8.03e-07 |
|
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: 52.80 E-value: 8.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 106 ESSLKDASYEKesteAQSLEAFYEKLTESKSELEDEILILEKELKEEKSKHSKQDELMSEISKRIQSL--EDESKSLKSQ 183
Cdd:pfam05483 62 QEGLKDSDFEN----SEGLSRLYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELqfENEKVSLKLE 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 184 VAEAKTTFKIFQMNEER-LKIAIKDALSENSqlqESQKQLLQEAEEWREQVNELN----KQRMTFEDSKV---------- 248
Cdd:pfam05483 138 EEIQENKDLIKENNATRhLCNLLKETCARSA---EKTKKYEYEREETRQVYMDLNnnieKMILAFEELRVqaenarlemh 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 249 -----------HVEQ----VLCDKENQIKSL----TERLRKMKDWTAVLGEEIADDDNLEWEMKSDSENDAHLdNQPKGA 309
Cdd:pfam05483 215 fklkedhekiqHLEEeykkEINDKEKQVSLLliqiTEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKEL-IEKKDH 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 310 LKKLIHAAKLR-----ASLKTLEgERNQIYT------------QLSEVDKTKEELTECIKNLQTEQASLQSENTQFENET 372
Cdd:pfam05483 294 LTKELEDIKMSlqrsmSTQKALE-EDLQIATkticqlteekeaQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRL 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 373 QKLQQKLKVMTELYQENEMILHRKLTMEENYRLEKEEKLSKADEKinhaaEELETYRKRAKDLEEELERTIHSYQGQIIS 452
Cdd:pfam05483 373 EKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAED-----EKLLDEKKQFEKIAEELKGKEQELIFLLQA 447
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1387233842 453 HEKKAHD---NWLAARTAE----RNLNDLRKENAHNRQKLTE 487
Cdd:pfam05483 448 REKEIHDleiQLTAIKTSEehylKEVEDLKTELEKEKLKNIE 489
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
168-498 |
9.17e-07 |
|
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: 52.67 E-value: 9.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 168 KRIQSLEDESKSLKSQVAEAKTTFKIFQMNEERLKIAIKDaLSENSQLQESQKQLLQEAEEWREQVNELN-KQRMTFEDS 246
Cdd:pfam02463 153 ERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDL-EELKLQELKLKEQAKKALEYYQLKEKLELeEEYLLYLDY 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 247 KVHVEQVLCDKENQIKSLTERLRKMKdwtavlGEEIADDDNLEWEMKSDSENDAHLDNQPKGALKKLIHAAKLRASLKTL 326
Cdd:pfam02463 232 LKLNEERIDLLQELLRDEQEEIESSK------QEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKL 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 327 EGERNQIYTQLSEVDKTKEELTECIKNLQTEQASLQSENTQFENETQKLQQKLKVMTELYQENEMILHRKLT-------- 398
Cdd:pfam02463 306 ERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAkkkleser 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 399 ------MEENYRLEKEEKLSKADEKINHAAEELETYRKRAKDL---EEELERTIHSYQGQIIshEKKAHDNWLAARTAER 469
Cdd:pfam02463 386 lssaakLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEEleiLEEEEESIELKQGKLT--EEKEELEKQELKLLKD 463
|
330 340
....*....|....*....|....*....
gi 1387233842 470 NLNDLRKENAHNRQKLTETEFKIELLEKD 498
Cdd:pfam02463 464 ELELKKSEDLLKETQLVKLQEQLELLLSR 492
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
80-498 |
1.22e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 52.38 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 80 ELSTLIEEKCKLLEKFSIVQKEYESLESSLKDASYEKESTEAQsLEAFYEKLTESKSELEDEILILEKELKEEKS---KH 156
Cdd:TIGR02169 386 ELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAA-IAGIEAKINELEEEKEDKALEIKKQEWKLEQlaaDL 464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 157 SKQDELMSEISKRIQSLEDESKSLKSQVAEAKTTFKIFQmNEERLKIAIKDALSENSQ-LQESQKQLLQEAEEWREQVNE 235
Cdd:TIGR02169 465 SKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASE-ERVRGGRAVEEVLKASIQgVHGTVAQLGSVGERYATAIEV 543
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 236 LNKQRMTF---EDSKVHVEQVLCDKENQIKSLT-ERLRKMKDwTAVLGEEIADDDNLEWEMksdseNDAHLDNQPKGALK 311
Cdd:TIGR02169 544 AAGNRLNNvvvEDDAVAKEAIELLKRRKAGRATfLPLNKMRD-ERRDLSILSEDGVIGFAV-----DLVEFDPKYEPAFK 617
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 312 KL---------IHAAK---LRASLKTLEGE---------------RNQIYTQLSEVDKTkEELTECIKNLQTEQASLQSE 364
Cdd:TIGR02169 618 YVfgdtlvvedIEAARrlmGKYRMVTLEGElfeksgamtggsrapRGGILFSRSEPAEL-QRLRERLEGLKRELSSLQSE 696
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 365 NTQFENETQKLQQKLKVMT----ELYQENEMILHRKLTMEEnyRLE-KEEKLSKADEKINHAAEELETYRKRAkdleEEL 439
Cdd:TIGR02169 697 LRRIENRLDELSQELSDASrkigEIEKEIEQLEQEEEKLKE--RLEeLEEDLSSLEQEIENVKSELKELEARI----EEL 770
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1387233842 440 ERTIHSYQGQIisHEKKAHDNWLAARTAERNLNDLRKENAHNRQKLTETEFKIELLEKD 498
Cdd:TIGR02169 771 EEDLHKLEEAL--NDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLE 827
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
160-485 |
2.70e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.21 E-value: 2.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 160 DELMSEISKRIQSLEDESKS------LKSQVAEAKTTFKIFQMNEERLKI-AIKDALSENSQLQESQKQLLQEAEEwreQ 232
Cdd:TIGR02168 192 EDILNELERQLKSLERQAEKaerykeLKAELRELELALLVLRLEELREELeELQEELKEAEEELEELTAELQELEE---K 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 233 VNELNKQRMTFEDSKVHVEQVL-------CDKENQIKSLTERLRKMKDWTAVLGEEIADDDNleweMKSDSENDAHLDNQ 305
Cdd:TIGR02168 269 LEELRLEVSELEEEIEELQKELyalaneiSRLEQQKQILRERLANLERQLEELEAQLEELES----KLDELAEELAELEE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 306 PKGALKKLIhaAKLRASLKTLEGERNQIYTQLSEVDKTKEELTECIKNLQTEQASLQSENTQFENETQKLQQKLKvmtEL 385
Cdd:TIGR02168 345 KLEELKEEL--ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRE---RL 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 386 YQENEMILHRkltMEENYRLEKEEKLSKADEKINHAAEELETYR---KRAKDLEEELERTIHSYQGQIisHEKKAHDNWL 462
Cdd:TIGR02168 420 QQEIEELLKK---LEEAELKELQAELEELEEELEELQEELERLEealEELREELEEAEQALDAAEREL--AQLQARLDSL 494
|
330 340
....*....|....*....|....
gi 1387233842 463 AA-RTAERNLNDLRKENAHNRQKL 485
Cdd:TIGR02168 495 ERlQENLEGFSEGVKALLKNQSGL 518
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
317-498 |
3.23e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.15 E-value: 3.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 317 AKLRASLKTLEGERNQIYTQLSEVDKTKEELTECIKNLQTEQASLQSENTQFENETQKLQQKLKVMTELYQEN------- 389
Cdd:COG4942 37 AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELlralyrl 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 390 ------EMILH--------RKLTMEE---NYRLEKEEKLSKADEKINHAAEELETYRKRAKDLEEELERTIHSYQGQIIS 452
Cdd:COG4942 117 grqpplALLLSpedfldavRRLQYLKylaPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAE 196
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1387233842 453 HEKkahdnwlAARTAERNLNDLRKENAHNRQKLTETEFKIELLEKD 498
Cdd:COG4942 197 RQK-------LLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
72-440 |
3.23e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.83 E-value: 3.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 72 GREKKLAIELSTLiEEKCKLLEKFSIVQKEYESLESSLKDASYEKESTEAQSLEAFYEKLTESKSELEDEILILEKELKE 151
Cdd:PRK03918 345 KKLKELEKRLEEL-EERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKE 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 152 EKS-----KHSK--------------QDELMSEISKRIQSLEDESKSLKSQVAEAKttfkifqmneeRLKIAIKDALSEN 212
Cdd:PRK03918 424 LKKaieelKKAKgkcpvcgrelteehRKELLEEYTAELKRIEKELKEIEEKERKLR-----------KELRELEKVLKKE 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 213 SQLQeSQKQLLQEAEEWREQVNELNKQRMTFEDSKVH-VEQVLCDKENQIKSLTERLRKMKDWTAVLGEeiadddnLEWE 291
Cdd:PRK03918 493 SELI-KLKELAEQLKELEEKLKKYNLEELEKKAEEYEkLKEKLIKLKGEIKSLKKELEKLEELKKKLAE-------LEKK 564
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 292 MKSDSENDAHLDNQPKGALKKLIHAAKLRasLKTLEGERNQiYTQLSEVDKTKEELTECIKNLQTEQASLQSENTQFENE 371
Cdd:PRK03918 565 LDELEEELAELLKELEELGFESVEELEER--LKELEPFYNE-YLELKDAEKELEREEKELKKLEEELDKAFEELAETEKR 641
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1387233842 372 TQKLQQKLKVMTELYQENEmilHRKLtmeENYRLEKEEKLSKADEKINHAAEELETYRKRAKDLEEELE 440
Cdd:PRK03918 642 LEELRKELEELEKKYSEEE---YEEL---REEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELE 704
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
199-380 |
3.74e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.76 E-value: 3.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 199 ERLKIAIKDALSENSQLQESQKQLLQEAEEWREQVNELNKQRMTFEDSKVHVEQVLCDKENQIKSLTERLRKMKDwtaVL 278
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE---EL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 279 GEEIA------DDDNLEWEMKSDSENDAHLDNQpkgALKKLIHAakLRASLKTLEGERNQIYTQLSEVDKTKEELTECIK 352
Cdd:COG4942 107 AELLRalyrlgRQPPLALLLSPEDFLDAVRRLQ---YLKYLAPA--RREQAEELRADLAELAALRAELEAERAELEALLA 181
|
170 180
....*....|....*....|....*...
gi 1387233842 353 NLQTEQASLQSENTQFENETQKLQQKLK 380
Cdd:COG4942 182 ELEEERAALEALKAERQKLLARLEKELA 209
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
99-441 |
3.89e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.42 E-value: 3.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 99 QKEYESLESSLKDaSYEKESTEAQSLEAFYEKLTESKSELEDEILILEKELKEEKSKHSKQDELMSEISKRIQSLEDESK 178
Cdd:PRK02224 316 REELEDRDEELRD-RLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIE 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 179 SLKSQVAEAKTTF-------KIFQMNEERLKIAIK----------DALSENSQLQESQK-----QLLQEA------EEWR 230
Cdd:PRK02224 395 ELRERFGDAPVDLgnaedflEELREERDELREREAeleatlrtarERVEEAEALLEAGKcpecgQPVEGSphvetiEEDR 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 231 EQVNELNKQRMTFEDSKVHVEQ------VLCDKENQIKSLTERLRKMKDWTAVLGEEIADD-DNLEWEMKSDSENDAHLD 303
Cdd:PRK02224 475 ERVEELEAELEDLEEEVEEVEErleraeDLVEAEDRIERLEERREDLEELIAERRETIEEKrERAEELRERAAELEAEAE 554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 304 NQPKGALKKLIHAAKLRASLKTLEGERNQIYTQLSEVDK------TKEELTECIKNLQTEQASLQSENTQFENETQKLQQ 377
Cdd:PRK02224 555 EKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERirtllaAIADAEDEIERLREKREALAELNDERRERLAEKRE 634
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1387233842 378 KLKVMTELYQENEM-ILHRKLTMEENYRLEKEEKLSKADEK----------INHAAEELETYRKRAKDLEEELER 441
Cdd:PRK02224 635 RKRELEAEFDEARIeEAREDKERAEEYLEQVEEKLDELREErddlqaeigaVENELEELEELRERREALENRVEA 709
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
321-497 |
5.15e-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: 50.06 E-value: 5.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 321 ASLKTLEGERNQIYTQLSEVDKTKEELTECIKNLQTEQASLQSENTQFENETQKLQQKLKVMTELYQE---NEMILHRKL 397
Cdd:TIGR02168 232 LRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRleqQKQILRERL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 398 TMEENYRLEKEEKLSKADEKINHAAEELETYRKRAKDLEEELErtihSYQGQIISHEKKAHDNWLAARTAERNLNDLRKE 477
Cdd:TIGR02168 312 ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELE----SLEAELEELEAELEELESRLEELEEQLETLRSK 387
|
170 180
....*....|....*....|
gi 1387233842 478 NAHNRQKLTETEFKIELLEK 497
Cdd:TIGR02168 388 VAQLELQIASLNNEIERLEA 407
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
73-503 |
6.01e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.94 E-value: 6.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 73 REKKLAI-ELSTLIEEkckLLEKFSIVQKEYESLESSLK---------DASYEKESTEAQSLEAFYEKLTESKSELEDEI 142
Cdd:COG1196 270 EELRLELeELELELEE---AQAEEYELLAELARLEQDIArleerrrelEERLEELEEELAELEEELEELEEELEELEEEL 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 143 LILEKELKEEKSKHSKQDELMSEISKRIQSLEDESKSLKSQVAEAKTTFKIFQMNEERLKIAIKDALSENSQLQESQKQL 222
Cdd:COG1196 347 EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEEL 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 223 LQEAEEWREQVNELNKQRMTFEDSKVHVEQVLCDKENQIKSLTERLRKMKDWTAVLGEEIADDDNLEWeMKSDSENDAHL 302
Cdd:COG1196 427 EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL-LLLEAEADYEG 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 303 DNQPKGALKKLIHAAKLRASLKTLEGERNQIYTQLSE---------VDKTKEELTECIKNLQTEQAS------------- 360
Cdd:COG1196 506 FLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAalaaalqniVVEDDEVAAAAIEYLKAAKAGratflpldkirar 585
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 361 ------------------LQSENTQFENETQKLQQKLKVMTELYQENEMILHRKLTMEENYRLEKEEK--LSKADEKINH 420
Cdd:COG1196 586 aalaaalargaigaavdlVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGegGSAGGSLTGG 665
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 421 AAEELETYRKRAKDLEEELERTIHSYQGQIISHEKKAHDNWLAARTAERNLNDLRKENAHNRQKLTETEFKIELLEKDPY 500
Cdd:COG1196 666 SRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEE 745
|
...
gi 1387233842 501 ALD 503
Cdd:COG1196 746 ELL 748
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
310-456 |
6.27e-06 |
|
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: 48.00 E-value: 6.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 310 LKKLIHAAKLRASLKTLEGERNQIYTQLSEVDKTKEELTECIKNLQTEQASLQSENTQFENETQKLQQKLKVMTEL---- 385
Cdd:COG1579 6 LRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnv 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1387233842 386 -----YQ--ENEM-ILHRKLTMEENYRLEKEEKLSKADEKINHAAEELETYRKRAKDLEEELERTIHSYQGQIISHEKK 456
Cdd:COG1579 86 rnnkeYEalQKEIeSLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
80-499 |
7.16e-06 |
|
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: 49.58 E-value: 7.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 80 ELSTLIEEKCKLLE-KFSIVQKEYEsLESSLKDASYEKESTEAQSLEAFYEKLTESKSELEDEILILEKELKEEKSKHSK 158
Cdd:TIGR00618 180 QLALMEFAKKKSLHgKAELLTLRSQ-LLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKK 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 159 QDELmSEISKRIQSLEDESKSLKSQVAEAKTTFKIFQMNEERLKIAI--KDALSENSQLQESQKQLLQEaeewREQVNEL 236
Cdd:TIGR00618 259 QQLL-KQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQieQQAQRIHTELQSKMRSRAKL----LMKRAAH 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 237 NKQRMTFEDSKvHVEQVLCDKENQIKSLTErlrKMKDWTAVLGEEIADDDNLewemKSDSENDAHLDNQPKGALKKLIHA 316
Cdd:TIGR00618 334 VKQQSSIEEQR-RLLQTLHSQEIHIRDAHE---VATSIREISCQQHTLTQHI----HTLQQQKTTLTQKLQSLCKELDIL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 317 AKLRASLKTLEGERNQIYTQLSEVDKTKEELTECIKNLQTEQASLQSENTQFENETQKLQQKLKVMTELYQENEMIL--- 393
Cdd:TIGR00618 406 QREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHlqe 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 394 --------HRKLTMEENYRLEKE-----------------------------EKLSKADEKINHaaeELETYRKRAKDLE 436
Cdd:TIGR00618 486 trkkavvlARLLELQEEPCPLCGscihpnparqdidnpgpltrrmqrgeqtyAQLETSEEDVYH---QLTSERKQRASLK 562
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1387233842 437 EELERTIHSYQ--GQIISHEKKAHDNwlaARTAERNLNDLRKENAHNRQKLTEtEFKIELLEKDP 499
Cdd:TIGR00618 563 EQMQEIQQSFSilTQCDNRSKEDIPN---LQNITVRLQDLTEKLSEAEDMLAC-EQHALLRKLQP 623
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
101-498 |
7.48e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 49.63 E-value: 7.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 101 EYESLESSLKDASYEKESTEAQ--SLEAFYEKLTESKSELEDEILILEKELKEEKSKHSKQDELMSEISKRIQSLEDESK 178
Cdd:TIGR04523 34 EEKQLEKKLKTIKNELKNKEKElkNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 179 SLKSQVAEAKTTFKIFQMNEERLKIAIKDALSENSQLQesqkqllQEAEEWREQVNELNKQRMTFEDSKVHVEQVLCDKE 258
Cdd:TIGR04523 114 NDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKE-------KELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 259 NQIKSLTERLRKMKDWTAVLGEEIADDDNLEWEMksdsendAHLDNQPKgalkklihaaKLRASLKTLEGERNQIYTQLS 338
Cdd:TIGR04523 187 KNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQI-------SELKKQNN----------QLKDNIEKKQQEINEKTTEIS 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 339 EVDK----TKEELTECIKNLQTEQASLQSENTQFENETQKLQQKLKVMTELYQENEMILHRKLTME----ENYRLEKEEK 410
Cdd:TIGR04523 250 NTQTqlnqLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSElknqEKKLEEIQNQ 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 411 LSKADEKINHAAEELETYRKRAKDLE---EELERTIHSYQGQIISHEKKAHDNWLAARTAERNLNDLRKENAHNRQKLTE 487
Cdd:TIGR04523 330 ISQNNKIISQLNEQISQLKKELTNSEsenSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQ 409
|
410
....*....|.
gi 1387233842 488 TEFKIELLEKD 498
Cdd:TIGR04523 410 KDEQIKKLQQE 420
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
85-441 |
1.09e-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: 48.95 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 85 IEEKCKLL-EKFSIVQKEYESLESSLKD--ASYEKESTEAQSLEAFYEKLTESKSELEDEILILEKELKEEKSKHS---- 157
Cdd:pfam05483 273 LEEKTKLQdENLKELIEKKDHLTKELEDikMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSfvvt 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 158 -------KQDELMSEISKRIQSLEDESKSL------KSQVAEAKTTFKifqMNEERLKIAIKDALSENSQLQESQKQLLQ 224
Cdd:pfam05483 353 efeattcSLEELLRTEQQRLEKNEDQLKIItmelqkKSSELEEMTKFK---NNKEVELEELKKILAEDEKLLDEKKQFEK 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 225 EAEEWREQVNELNKQRMTFE----DSKVHVEQVLCDKE---NQIKSLTERLRKMK----------DWTAVLGEEIADD-D 286
Cdd:pfam05483 430 IAEELKGKEQELIFLLQAREkeihDLEIQLTAIKTSEEhylKEVEDLKTELEKEKlknieltahcDKLLLENKELTQEaS 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 287 NLEWEMKSDSENDAHLDNQPKGALKKLIHAAKLRASLKT-LEGERNQIYTQLSEV----DKTKEELTECIKNLQTEQASL 361
Cdd:pfam05483 510 DMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDeLESVREEFIQKGDEVkcklDKSEENARSIEYEVLKKEKQM 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 362 QSENTQFENETQKLQQKLKVMTELYQENEMiLHRKLTMEEN-----------YRLEKEEKLSKADEKINHAAEELETYRK 430
Cdd:pfam05483 590 KILENKCNNLKKQIENKNKNIEELHQENKA-LKKKGSAENKqlnayeikvnkLELELASAKQKFEEIIDNYQKEIEDKKI 668
|
410
....*....|.
gi 1387233842 431 RAKDLEEELER 441
Cdd:pfam05483 669 SEEKLLEEVEK 679
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
94-394 |
1.23e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 49.07 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 94 KFSIVQKEYESLES------SLKDASYEKESTEAQSLEAFYEKLTESKSELedeililekelkeekskhskqDELMSEIS 167
Cdd:pfam12128 242 EFTKLQQEFNTLESaelrlsHLHFGYKSDETLIASRQEERQETSAELNQLL---------------------RTLDDQWK 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 168 KRIQSLEDESKSLKSQVAEAKTTFKIFqmnEERLKIAIKDALsensqlqESQKQLLQEAEEWREQVNELNKQRMTFEDSK 247
Cdd:pfam12128 301 EKRDELNGELSAADAAVAKDRSELEAL---EDQHGAFLDADI-------ETAAADQEQLPSWQSELENLEERLKALTGKH 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 248 VHVEQ------VLCDKEN--QIKSLTERLRKMKDWTAVLGEEIADD-DNLEWEMKSDSENDAHLDNQPKGALKKLIHAAK 318
Cdd:pfam12128 371 QDVTAkynrrrSKIKEQNnrDIAGIKDKLAKIREARDRQLAVAEDDlQALESELREQLEAGKLEFNEEEYRLKSRLGELK 450
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387233842 319 LRASLKTLEGE-RNQIYTQLSEVDKTKEELTECIKNLQTEQASLQSENTQFENETQKLQQKLKVMTELYQENEMILH 394
Cdd:pfam12128 451 LRLNQATATPElLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELEL 527
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
79-497 |
1.46e-05 |
|
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: 48.89 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 79 IELSTLIEEKckLLEKFSIVQKEYESLESSLKDA-SYEKESTEAQSLEAFYEKLTESKSELEDEILILEKELKEEKSKhS 157
Cdd:TIGR00606 442 IELKKEILEK--KQEELKFVIKELQQLEGSSDRIlELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKL-R 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 158 KQDELMSEISKRIQSLEDESKSLKSQVAEAKTTFKIFQMNEERLkIAIKDALSENSQLQESQKQLLQEAEEWREQVNELN 237
Cdd:TIGR00606 519 KLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDEL-TSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLN 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 238 KQRMTFEDSKVHVEQVLCDKENQIKSLTErlrKMKDWTAVLGEEIaDDDNLEWEMKSDSENDAHLDNqpkgalkklihAA 317
Cdd:TIGR00606 598 KELASLEQNKNHINNELESKEEQLSSYED---KLFDVCGSQDEES-DLERLKEEIEKSSKQRAMLAG-----------AT 662
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 318 KLRASLKTLEGERNQIYTQLSEVD-KTKEELTECIKNLQTEQASLQSENTQFENETQKLQQKLKVMTELYQENEMILHRK 396
Cdd:TIGR00606 663 AVYSQFITQLTDENQSCCPVCQRVfQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLK 742
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 397 LTMEENYRlEKEEKLSKADEKINHAAEELETY-------RKRAKDLEEELErTIHSYQGQIISHEKKAHD--NWLAARTA 467
Cdd:TIGR00606 743 EKEIPELR-NKLQKVNRDIQRLKNDIEEQETLlgtimpeEESAKVCLTDVT-IMERFQMELKDVERKIAQqaAKLQGSDL 820
|
410 420 430
....*....|....*....|....*....|
gi 1387233842 468 ERNLNDLRKENAHNRQKLTETEFKIELLEK 497
Cdd:TIGR00606 821 DRTVQQVNQEKQEKQHELDTVVSKIELNRK 850
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
155-478 |
1.67e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 48.51 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 155 KHSKQDELMSEISKRIQSLEDESKSLKS-QVAEAKTTFKIFQMNEERLKIAIKdalsenSQLQESQKQLLQEAEEWREQV 233
Cdd:TIGR01612 487 ENSKQDNTVKLILMRMKDFKDIIDFMELyKPDEVPSKNIIGFDIDQNIKAKLY------KEIEAGLKESYELAKNWKKLI 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 234 NELNKQRMTFEDSKVHVEQvlcdkenQIKSLTERLRKMKDwtavlgeEIADDDNLEWEMKSDSENDAHLDNQPKGA--LK 311
Cdd:TIGR01612 561 HEIKKELEEENEDSIHLEK-------EIKDLFDKYLEIDD-------EIIYINKLKLELKEKIKNISDKNEYIKKAidLK 626
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 312 KLIhaaklraslktlegERNQIYtqLSEVDKTKE-ELTECIKNLQTEQASLQSENTQ-FENETQKLQQKLkvmTELYQEN 389
Cdd:TIGR01612 627 KII--------------ENNNAY--IDELAKISPyQVPEHLKNKDKIYSTIKSELSKiYEDDIDALYNEL---SSIVKEN 687
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 390 EMIlhrklTMEENYRLEK-EEKLSKADEKINHAAEE--------LETYRKRAKDLEEELERTIHSYqgqiISHE--KKAH 458
Cdd:TIGR01612 688 AID-----NTEDKAKLDDlKSKIDKEYDKIQNMETAtvelhlsnIENKKNELLDIIVEIKKHIHGE----INKDlnKILE 758
|
330 340
....*....|....*....|
gi 1387233842 459 DNWLAARTAERNLNDLRKEN 478
Cdd:TIGR01612 759 DFKNKEKELSNKINDYAKEK 778
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
58-414 |
1.77e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 48.51 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 58 LWRSFQSVRSRLYVGREKKLAIELSTLI--------EEKCKLLEKFSIVQKEYESLESslkdasyekesTEAQSLEAFYE 129
Cdd:TIGR01612 657 IYSTIKSELSKIYEDDIDALYNELSSIVkenaidntEDKAKLDDLKSKIDKEYDKIQN-----------METATVELHLS 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 130 KLTESKSELEDeililekelkeekskhskqdeLMSEISKRIQSleDESKSLKSQVAEakttfkiFQMNEERLKIAIKDAL 209
Cdd:TIGR01612 726 NIENKKNELLD---------------------IIVEIKKHIHG--EINKDLNKILED-------FKNKEKELSNKINDYA 775
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 210 SENSQLQESQKQLLQEAEEWREQVNELNKQ----RMTFEDSKVHVEQVLCdKENQIKSLTERLRKMKD-WTAVLGEEIAD 284
Cdd:TIGR01612 776 KEKDELNKYKSKISEIKNHYNDQINIDNIKdedaKQNYDKSKEYIKTISI-KEDEIFKIINEMKFMKDdFLNKVDKFINF 854
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 285 DDNLEWEMKSDSENDAHLDNQPKGALKKlihaaklrASLKTLEGERNQIYTQLSEVDKTKEELTECIKNLQTEQASLQ-S 363
Cdd:TIGR01612 855 ENNCKEKIDSEHEQFAELTNKIKAEISD--------DKLNDYEKKFNDSKSLINEINKSIEEEYQNINTLKKVDEYIKiC 926
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1387233842 364 ENT-----QFENETQKLQQKLKVMTELYQENEMILHRKLTMEENYRLEKEEKLSKA 414
Cdd:TIGR01612 927 ENTkesieKFHNKQNILKEILNKNIDTIKESNLIEKSYKDKFDNTLIDKINELDKA 982
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
160-497 |
1.91e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.14 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 160 DELMSEISKRIQSLEDESkslksqvaEAKTTFKIFQmnEERLKIAIKDALSENSQLQESQKQLLQEAEEWREQVNELNKQ 239
Cdd:TIGR02169 190 DLIIDEKRQQLERLRRER--------EKAERYQALL--KEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 240 RMTFEDSKVHVEQVLCDKENQIKSLTErlrkmkDWTAVLGEEIAdddnlewEMKSDSENdahldnqpkgaLKKLIHAAKL 319
Cdd:TIGR02169 260 ISELEKRLEEIEQLLEELNKKIKDLGE------EEQLRVKEKIG-------ELEAEIAS-----------LERSIAEKER 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 320 RasLKTLEGERNQIYTQLSEVDKTKEELTECIKNLQTEQASLQSENTQFENETQKLQQKLKVMTELYQEnemiLHRKLTm 399
Cdd:TIGR02169 316 E--LEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAE----TRDELK- 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 400 eenyrlEKEEKLSKADEKINHAAEELETYRKRAKDLEEELER---TIHSYQGQIISHEKKAHDNWLAARTAERNLNDLRK 476
Cdd:TIGR02169 389 ------DYREKLEKLKREINELKRELDRLQEELQRLSEELADlnaAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAA 462
|
330 340
....*....|....*....|.
gi 1387233842 477 ENAHNRQKLTETEFKIELLEK 497
Cdd:TIGR02169 463 DLSKYEQELYDLKEEYDRVEK 483
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
82-497 |
2.78e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 47.81 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 82 STLIEEKCKLLEKFSIVQKEYESLESSLKDASYEKESTEAQS------LEAFYEKLTESKSELEDEILILEKELKEEKSK 155
Cdd:pfam15921 331 SELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESgnlddqLQKLLADLHKREKELSLEKEQNKRLWDRDTGN 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 156 HSKQDELMSEISKR---IQSLEDESKSLKSQVaeakttfkifQMNEERLKIAIKDALSENSQLQESQKQLLQEAEEWREQ 232
Cdd:pfam15921 411 SITIDHLRRELDDRnmeVQRLEALLKAMKSEC----------QGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKV 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 233 VNELNKQRMTFEDSKVHVEQV---LCDKENQIKSLTERLRKMKDWTAVLGEEIADDDNLEWEMKS-DSENDA-------- 300
Cdd:pfam15921 481 VEELTAKKMTLESSERTVSDLtasLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNvQTECEAlklqmaek 560
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 301 ---------HLDNQPKGALKKLIHAAKLRASLKTLEGERNQIYTQLSEVDKTKEELTECIKNLQTEQASLQSENTQFENE 371
Cdd:pfam15921 561 dkvieilrqQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNA 640
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 372 TqklQQKLKVMTELYQENEMILHrkltmeenyrlekEEKLSKADekINHAAEELETYRKRAKDLEEELERTIHSYQGQII 451
Cdd:pfam15921 641 G---SERLRAVKDIKQERDQLLN-------------EVKTSRNE--LNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLK 702
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1387233842 452 SHEKKAHDNWLAARTAE-------RNLNDLRKENAHNRQKLTETEFKIELLEK 497
Cdd:pfam15921 703 SAQSELEQTRNTLKSMEgsdghamKVAMGMQKQITAKRGQIDALQSKIQFLEE 755
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
300-469 |
3.89e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 3.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 300 AHLDNQPKGALKKLihaAKLRASLKTLEGERNQIYTQLSEVDKTKEELTECIKNLQTEQASLQSENTQFENETQKLQQKL 379
Cdd:COG3883 12 AFADPQIQAKQKEL---SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 380 KVMTELYQEN-------EMILH--------RKLT-----MEENYRL-----EKEEKLSKADEKINHAAEELETYRKRAKD 434
Cdd:COG3883 89 GERARALYRSggsvsylDVLLGsesfsdflDRLSalskiADADADLleelkADKAELEAKKAELEAKLAELEALKAELEA 168
|
170 180 190
....*....|....*....|....*....|....*..
gi 1387233842 435 LEEELERTIHSYQGQI--ISHEKKAHDNWLAARTAER 469
Cdd:COG3883 169 AKAELEAQQAEQEALLaqLSAEEAAAEAQLAELEAEL 205
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
205-390 |
3.92e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 3.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 205 IKDALSENSQLQESQKQLLQEAEEWREQVNELNKQRMTFEDSKVHVEQVLCDKENQIKSLTERLRK----MKDWTAVLGE 280
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEErreeLGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 281 EIADDDNLEWEMKSDSENDAhLDNQpkGALKKLIHAAklRASLKTLEGERNQIYTQLSEVDKTKEELTECIKNLQTEQAS 360
Cdd:COG3883 98 SGGSVSYLDVLLGSESFSDF-LDRL--SALSKIADAD--ADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190
....*....|....*....|....*....|
gi 1387233842 361 LQSENTQFENETQKLQQKLKVMTELYQENE 390
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELE 202
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
317-441 |
4.44e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 46.77 E-value: 4.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 317 AKLRASLKTLEGERNQIYTQLSEVDKTKEEltECIKNLQTEQASLQSENtqfenetQKLQQKLKVMTELYQENEMILhRK 396
Cdd:COG2433 383 EELIEKELPEEEPEAEREKEHEERELTEEE--EEIRRLEEQVERLEAEV-------EELEAELEEKDERIERLEREL-SE 452
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1387233842 397 LTMEENYRLEKEEKLSKADEKINHAAEELETYRKRAKDLEEELER 441
Cdd:COG2433 453 ARSEERREIRKDREISRLDREIERLERELEEERERIEELKRKLER 497
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
113-498 |
7.29e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.43 E-value: 7.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 113 SYEKESTEAQSLEAFYEKLTESKSELEDEILILEKELKEekskHSKQDELMSEISKRIQSLEDESKSLKSQVAEAKTTFK 192
Cdd:PRK01156 323 KYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNQILELEGY----EMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILK 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 193 IFQMNEERLK-------IAIKDALSENSQLQESQKQLLQEAEEWREQVNELNKQRM------TFEDSKvhVEQVLCDKEN 259
Cdd:PRK01156 399 IQEIDPDAIKkelneinVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVcpvcgtTLGEEK--SNHIINHYNE 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 260 QIKSLTERLRKMKDWTAVLGEEIADDDNLEWEM-KSDSENDAHLDNQPKGALKKLIHAAKLRASLKTLEGERNQIYTQLS 338
Cdd:PRK01156 477 KKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLeSEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYK 556
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 339 EVD-KTKEELTECIKNLQTEQASLQSENTQFENETQKlqQKLKVMTELYQENEMILHRKLTMEENYRLEKEEKLSKADEK 417
Cdd:PRK01156 557 SLKlEDLDSKRTSWLNALAVISLIDIETNRSRSNEIK--KQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNK 634
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 418 INHAAE---ELETYRKRAKDLEEELER--TIHSYQGQIISHEKKAHDNW--LAARTAERNLNDLRKENAH--NRQKLTET 488
Cdd:PRK01156 635 YNEIQEnkiLIEKLRGKIDNYKKQIAEidSIIPDLKEITSRINDIEDNLkkSRKALDDAKANRARLESTIeiLRTRINEL 714
|
410
....*....|
gi 1387233842 489 EFKIELLEKD 498
Cdd:PRK01156 715 SDRINDINET 724
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
317-487 |
8.45e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.20 E-value: 8.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 317 AKLRASLKTLEGERNQIYTQLSEVDKTKEELTECIKNLQTEQASLqsentqfENETQKLQQKLKvmtELYQENEMiLHRK 396
Cdd:TIGR02168 256 EELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL-------EQQKQILRERLA---NLERQLEE-LEAQ 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 397 LTMEENYRLEKEEKLSKADEKINHAAEELETYR---KRAKDLEEELERTIHSYQGQIISHEKKAHD--NWLAARTAERNL 471
Cdd:TIGR02168 325 LEELESKLDELAEELAELEEKLEELKEELESLEaelEELEAELEELESRLEELEEQLETLRSKVAQleLQIASLNNEIER 404
|
170
....*....|....*..
gi 1387233842 472 NDLRKEN-AHNRQKLTE 487
Cdd:TIGR02168 405 LEARLERlEDRRERLQQ 421
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
80-499 |
9.82e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 45.98 E-value: 9.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 80 ELSTLIEEKCKLLEKFSIVQKEYESLESSLKDASYEKESTEAQSLEAFYEKLTESKSELEDEILILekelkeekskhskQ 159
Cdd:pfam12128 355 ELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQAL-------------E 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 160 DELMSEISKRIQSLEDESKSLKSQVAEAKttfkiFQMN------EERLKIAIKDALSENSQL--------QESQKQLLQE 225
Cdd:pfam12128 422 SELREQLEAGKLEFNEEEYRLKSRLGELK-----LRLNqatatpELLLQLENFDERIERAREeqeaanaeVERLQSELRQ 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 226 AEEWREQVNE-LNKQRMTFEDSKVHVEQVLCDKENQIKSLTERLRK-MKDWTAVLGEEIADDDNLEWEMksDSENDahlD 303
Cdd:pfam12128 497 ARKRRDQASEaLRQASRRLEERQSALDELELQLFPQAGTLLHFLRKeAPDWEQSIGKVISPELLHRTDL--DPEVW---D 571
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 304 NQPKGALKklIHAAKLRAslktlegERNQIYTQLSEVDKTKEELTECIKNLQTEQAS---LQSENTQFENETQKLQQKLK 380
Cdd:pfam12128 572 GSVGGELN--LYGVKLDL-------KRIDVPEWAASEEELRERLDKAEEALQSAREKqaaAEEQLVQANGELEKASREET 642
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 381 VMTELYQENEMILHRKLTMEENYRLEKEEKLSkadEKINHAAEELETYRKRAKDLEEELERTIHSYQGQIISHEKKAHDN 460
Cdd:pfam12128 643 FARTALKNARLDLRRLFDEKQSEKDKKNKALA---ERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAY 719
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1387233842 461 WLAARTAERNLNDL-------RKENAHNRQKLTETEFKIELLEKDP 499
Cdd:pfam12128 720 WQVVEGALDAQLALlkaaiaaRRSGAKAELKALETWYKRDLASLGV 765
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
323-497 |
1.04e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 323 LKTLEGERNQIYTQLSEVDKTKEELTEciknLQTEQASLQSENTQFENETQKLQQKLKVMtELYQENEMILHRKLTMEEN 402
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELEE----LEEELEELEAELEELREELEKLEKLLQLL-PLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 403 YR--LEKEEKLSKADEKINHAAEELETYRKrakDLEEELERTIHSYQGQIISHEKKAHDNWLAARTAERNLNDLRKENAH 480
Cdd:COG4717 148 LEelEERLEELRELEEELEELEAELAELQE---ELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEE 224
|
170
....*....|....*..
gi 1387233842 481 NRQKLTETEFKIELLEK 497
Cdd:COG4717 225 LEEELEQLENELEAAAL 241
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
195-489 |
1.22e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.90 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 195 QMNEERLKIAIKDALSENSQLQESQKQLLQEAEEWREQVNELNKqrmtfedskvhveqvlcdkenQIKSLTERLRKMKDw 274
Cdd:COG1340 7 SSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNA---------------------QVKELREEAQELRE- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 275 tavlgeeiadddnlewEMKSDSENDAHLDNQPKGALKKLihaAKLRASLKTLEGERNQIYTQLSEVDKTKEELTECIKNL 354
Cdd:COG1340 65 ----------------KRDELNEKVKELKEERDELNEKL---NELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQ 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 355 QTEQASLQSENtqfenetqKLQQKLKVMTELYQENEMIL--HRKLTMEENYRLEKEEKLSKADEKINHAAEELETYRKRA 432
Cdd:COG1340 126 QTEVLSPEEEK--------ELVEKIKELEKELEKAKKALekNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEM 197
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 433 KDLEEELERT---IHSYQGQIISHEKKAHDNWLAARTAERNLNDLRKENAHNRQKLTETE 489
Cdd:COG1340 198 IELYKEADELrkeADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALK 257
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
73-453 |
1.33e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 73 REKKLAIELSTLIEEKCKLLEKFSIVQKEYESLESSLKDasYEKESTEAQSLEAFYEKL-TESKSELEDEILILEKELKE 151
Cdd:COG4717 119 EKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEE--LRELEEELEELEAELAELqEELEELLEQLSLATEEELQD 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 152 EKSKHSKQDELMSEISKRIQSLEDESKSLKSQVAEAKTTFKIFQMNEERLK--------------IAIKDALSENSQ--- 214
Cdd:COG4717 197 LAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEarlllliaaallalLGLGGSLLSLILtia 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 215 -------------LQESQKQLLQEAEEWREQVNELNKQRMTFEDSKVHVEQVLCDKENQIKSLTERLRKMKDWTAVLGEE 281
Cdd:COG4717 277 gvlflvlgllallFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREA 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 282 IADDDNLEWEmKSDSENDAHLDNQPKGALKKLIHAAKLRASLKTLEGERNQIYTQLSEVDKTKEELTEciknlQTEQASL 361
Cdd:COG4717 357 EELEEELQLE-ELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLE-----ALDEEEL 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 362 QSENTQFENETQKLQQKLKVMTELYQENEMILHRkltMEENYRL-EKEEKLSKADEKINHAAEELETYRKRAKDLEEELE 440
Cdd:COG4717 431 EEELEELEEELEELEEELEELREELAELEAELEQ---LEEDGELaELLQELEELKAELRELAEEWAALKLALELLEEARE 507
|
410
....*....|...
gi 1387233842 441 RTIHSYQGQIISH 453
Cdd:COG4717 508 EYREERLPPVLER 520
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
185-381 |
1.33e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 185 AEAKTTFKIFQMNEERLKIAIKDALSENSQLQESQKQLLQEAEEWREQVNELNKQRMTFEDSKVHVEQVLCDKENQIKsl 264
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 265 tERLRKMK-------DWTAVLGEEIADD--DNLEWeMKSDSENDAHLDNQPKGALKKLIHA-AKLRASLKTLEGERNQIY 334
Cdd:COG3883 90 -ERARALYrsggsvsYLDVLLGSESFSDflDRLSA-LSKIADADADLLEELKADKAELEAKkAELEAKLAELEALKAELE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1387233842 335 TQLSEVDKTKEELTECIKNLQTEQASLQSENTQFENETQKLQQKLKV 381
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
91-436 |
1.35e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 45.42 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 91 LLEKFSIVQKEYESLESSLKdaSYEKESTEAQSLEafyekLTESKSELEDEILILEKELKEEKSKHSKQDELMSEISKRI 170
Cdd:TIGR00606 787 CLTDVTIMERFQMELKDVER--KIAQQAAKLQGSD-----LDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQI 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 171 QSLEDESKSLKSQVAEAKTTFKIFQMNEERLK----------IAIKDALSENSQLQESQKQLLQEAEEWREQVNELNKQ- 239
Cdd:TIGR00606 860 QHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVelstevqsliREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKa 939
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 240 RMTFEDSKVHVEQV---LCDKENQIKSLTERLRKMKdwtavlgeeiadDDNLEWEMKSDSENDAHLD--NQPKGALKKLI 314
Cdd:TIGR00606 940 QDKVNDIKEKVKNIhgyMKDIENKIQDGKDDYLKQK------------ETELNTVNAQLEECEKHQEkiNEDMRLMRQDI 1007
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 315 HAAKLRASLKTLEGERNQIYTQLSEVdktKEELTECIKNLQTEQAslqsenTQFENETQKLQQKLKVMTelyQENEMILH 394
Cdd:TIGR00606 1008 DTQKIQERWLQDNLTLRKRENELKEV---EEELKQHLKEMGQMQV------LQMKQEHQKLEENIDLIK---RNHVLALG 1075
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1387233842 395 RKLTMEENYRLEKEE----KLSKADEKINHAAEELETYRKRAKDLE 436
Cdd:TIGR00606 1076 RQKGYEKEIKHFKKElrepQFRDAEEKYREMMIVMRTTELVNKDLD 1121
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
74-460 |
2.26e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 74 EKKLAIELSTLIEEKCKLlEKFSIVQKEYESLESSLKDASYEKESTEAQSLEAFYEKLTESKSELEDEILILEKELKEEK 153
Cdd:PTZ00121 1429 EKKKADEAKKKAEEAKKA-DEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAE 1507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 154 SKHSKQDELMSEISKRIQSL---EDESKSLKSQVAEAKTTFKIFQMNEERLKIAIKDALSENSQLQESQKQLLQEAEEWR 230
Cdd:PTZ00121 1508 AKKKADEAKKAEEAKKADEAkkaEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAK 1587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 231 --EQVNELNKQRMTFEDSKVHVEQVLCDKENQIKSltERLRK----MKDWTAVLGEEIADDDNLEWEMKSDSENDAHLDN 304
Cdd:PTZ00121 1588 kaEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA--EELKKaeeeKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAE 1665
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 305 QPKGALKKLIHAAKLRaslKTLEGERNQiytqlSEVDKTKEELTECIKNLQTEQAslqsENTQFENETQKLQQKLKVMTE 384
Cdd:PTZ00121 1666 EAKKAEEDKKKAEEAK---KAEEDEKKA-----AEALKKEAEEAKKAEELKKKEA----EEKKKAEELKKAEEENKIKAE 1733
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1387233842 385 LYQENEMILHRKltmEENYRLEKEEKLSKADEKINHAAEELETYRKRAKDLEEELERTIHSYQGQIISHEKKAHDN 460
Cdd:PTZ00121 1734 EAKKEAEEDKKK---AEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDN 1806
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
101-487 |
2.93e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 44.58 E-value: 2.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 101 EYESLESSLKDASYEKESTEAQSLEafyeKLTESKSELEDEILILEKELKeekskhskqdelmseisKRIQSLEDESKSL 180
Cdd:pfam02463 159 EEEAAGSRLKRKKKEALKKLIEETE----NLAELIIDLEELKLQELKLKE-----------------QAKKALEYYQLKE 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 181 KSQVAEAKTTFKIFQmneerlkiaikdalsensQLQESQKQLLQEAEEWREQVNELNKQRMTFEDSKVHVEQVLCDKENQ 260
Cdd:pfam02463 218 KLELEEEYLLYLDYL------------------KLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEK 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 261 IKSLTERLRKMKDwtAVLGEEIADDDNLEWEMKSDSENDAHLDNQPKGALKKLIHAAKLRASLKTLEGERN-QIYTQLSE 339
Cdd:pfam02463 280 EKKLQEEELKLLA--KEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEiKREAEEEE 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 340 VDKTKEELTECIKNLQTEQASLQSENTQFENETQKLQQKLKVMTELYQENEMILHRKLTMEENYRLEKEEKLSKaDEKIN 419
Cdd:pfam02463 358 EEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEI-LEEEE 436
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387233842 420 HAAEELETYRKRAKDLEEELERTIHSYQGQIISHEKKAHDNWLAARTAERNLNDLRKENAHNRQKLTE 487
Cdd:pfam02463 437 ESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESK 504
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
259-442 |
3.02e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 3.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 259 NQIKSLTERLRKMKDWTAVLGEEIADDDNLEWEMKSDSENDAHLDNQpKGALKKLIHAAKLRASLKTLEGERNQIYTQLS 338
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREE-LEKLEKLLQLLPLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 339 EVDKTKEEltecIKNLQTEQASLQSENTQFENETQKLQQKLKVMTELYQEnemilhrkltmeenyrlEKEEKLSKADEKI 418
Cdd:COG4717 150 ELEERLEE----LRELEEELEELEAELAELQEELEELLEQLSLATEEELQ-----------------DLAEELEELQQRL 208
|
170 180
....*....|....*....|....
gi 1387233842 419 NHAAEELETYRKRAKDLEEELERT 442
Cdd:COG4717 209 AELEEELEEAQEELEELEEELEQL 232
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
230-447 |
3.05e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 3.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 230 REQVNELNKQRMTFEDSKVHVEQVLCDKENQIKSLTERLRKMKDWTAVLGEEIaddDNLEWEmksdsendAHLDnqpkgA 309
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEI---DVASAE--------REIA-----E 672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 310 LKKLIhaAKLRASLKTLEgernQIYTQLSEVDKTKEELTECIKNLQTEQASLQSENTQFENETQKLQQKLKVMTELYQEn 389
Cdd:COG4913 673 LEAEL--ERLDASSDDLA----ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL- 745
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1387233842 390 emilHRKLTMEENYRLEKEEKLskADEKINHAAEELETYRKRAKDLEEELERTIHSYQ 447
Cdd:COG4913 746 ----ELRALLEERFAAALGDAV--ERELRENLEERIDALRARLNRAEEELERAMRAFN 797
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
207-471 |
5.03e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.75 E-value: 5.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 207 DALSENSQLQESQKQLLQEAEEWREQVNELNKQRMTFEDskvhVEQVLCDKENQIKSLTERLRKMKDW-TAVLGEEIADD 285
Cdd:PRK11281 46 DALNKQKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQ----LKQQLAQAPAKLRQAQAELEALKDDnDEETRETLSTL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 286 DNLEWEMKSDSENDAHLDNQpkgalKKLIHAAKLRASLKTLEgERNQ------------IYTQLSEVDKTKEELTECIKN 353
Cdd:PRK11281 122 SLRQLESRLAQTLDQLQNAQ-----NDLAEYNSQLVSLQTQP-ERAQaalyansqrlqqIRNLLKGGKVGGKALRPSQRV 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 354 -LQTEQASLQSENTQfeneTQKLQQKLKVMTELYQenemiLHRKLTMEENYRLEKEEKLSKadEKINhaaeeletyRKRA 432
Cdd:PRK11281 196 lLQAEQALLNAQNDL----QRKSLEGNTQLQDLLQ-----KQRDYLTARIQRLEHQLQLLQ--EAIN---------SKRL 255
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1387233842 433 KDLEEELErtihsyqgQIISHEKKAH--DNWLAARTAERNL 471
Cdd:PRK11281 256 TLSEKTVQ--------EAQSQDEAARiqANPLVAQELEINL 288
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
59-490 |
5.32e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.50 E-value: 5.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 59 WRSFQSVRSRL-YVGREKKLAIELSTLIEEKCKLLEKFSIVQKEYESLESSLKDASYEKESTEAQSL------------E 125
Cdd:TIGR00606 556 SRHSDELTSLLgYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSsyedklfdvcgsQ 635
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 126 AFYEKLTESKSELEDEILILEKELKEEKSKHSKQDELMSEIS----------KRIQSLEDESKSLKSQV----AEAKTTF 191
Cdd:TIGR00606 636 DEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQsccpvcqrvfQTEAELQEFISDLQSKLrlapDKLKSTE 715
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 192 KIFQMNEERLKIAIKDALSENSQLQESQKQLLQEAEEWREQVNELNKQRMTFEDSKVHVEQVLCDKENQIKSLT-----E 266
Cdd:TIGR00606 716 SELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTdvtimE 795
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 267 RLR-KMKDWTAVLGEEIADDDNLEWEM------KSDSENDAHLDN--QPKGALKKLI-----HAAKLRASLKTLEGERNQ 332
Cdd:TIGR00606 796 RFQmELKDVERKIAQQAAKLQGSDLDRtvqqvnQEKQEKQHELDTvvSKIELNRKLIqdqqeQIQHLKSKTNELKSEKLQ 875
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 333 IYTQLSEVDKTKEELTECIKNLQteqaSLQSENTQFENETQKLQQKLKvmtELYQENEMILHRkltmeenyrleKEEKLS 412
Cdd:TIGR00606 876 IGTNLQRRQQFEEQLVELSTEVQ----SLIREIKDAKEQDSPLETFLE---KDQQEKEELISS-----------KETSNK 937
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387233842 413 KADEKINHAAEELETYRKRAKDLEEELERTIHSYqgqiisheKKAHDNWLAARTAERNLNDLRKENAHNRQKLTETEF 490
Cdd:TIGR00606 938 KAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDY--------LKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDI 1007
|
|
| prsA |
PRK00059 |
peptidylprolyl isomerase; Provisional |
158-357 |
5.94e-04 |
|
peptidylprolyl isomerase; Provisional
Pssm-ID: 234605 [Multi-domain] Cd Length: 336 Bit Score: 42.78 E-value: 5.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 158 KQDELMSEISKRIQSLEDESKSLKSQVaeaKTTFKIFQMNEERLKIAIKDALSENSQLQESQKQLLQEAEEWREQVNElN 237
Cdd:PRK00059 111 SEEELNKEVDKKINEIKKQFNNDEEQF---EEALKATGFTEETFKEYLKNQIIIEKVINEVVKDVKVTDKDAQKYYNE-N 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 238 KQRMTFEDSKVHVEQVLCDKENQIKSLTERLRKMKDWtAVLGEEIADD----DNLEwEMKSDSENDAHLDNQPKGALKKL 313
Cdd:PRK00059 187 KSKFTEKPNTMHLAHILVKTEDEAKKVKKRLDKGEDF-AKVAKEVSQDpgskDKGG-DLGDVPYSDSGYDKEFMDGAKAL 264
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387233842 314 --------IHA----------AKLRASLKTLEGERNQIYTQLSEvDKTKEELTECIKNLQTE 357
Cdd:PRK00059 265 kegeisapVKTqfgyhiikaiKKKEYPVKPFDSVKEDIKKQLLQ-EKQSEVFKKKIEEWKKA 325
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
66-272 |
6.96e-04 |
|
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: 42.31 E-value: 6.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 66 RSRLYVGREKKLAIELSTLIEEkckllekfSIVQKEYESLESSLKDASYE-----KESTEAQSLEAFYE---KLTES-KS 136
Cdd:smart00787 76 KKYISEGRDLFKEIEEETLINN--------PPLFKEYFSASPDVKLLMDKqfqlvKTFARLEAKKMWYEwrmKLLEGlKE 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 137 ELEDEILILEKELKEEKSKHSKQDELMSEISKRIQSLEDESKSLKSQVAEAKttfKIFQMNEERLKIAIKDALSENSQLQ 216
Cdd:smart00787 148 GLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELE---DCDPTELDRAKEKLKKLLQEIMIKV 224
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 217 ESQKQLLQEAEEWREQVNELNKQRMTFEDSKVHVEQVL--CDK--ENQIKSLTERLRKMK 272
Cdd:smart00787 225 KKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLeqCRGftFKEIEKLKEQLKLLQ 284
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
86-497 |
9.84e-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: 9.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 86 EEKCKLLEKfsiVQKEYESLESSLKDaSYEKESTEAQSLEAFYEKLTESKSELEDEILILEKELKEEKSKHSKQDElmsE 165
Cdd:pfam01576 172 EEKAKSLSK---LKNKHEAMISDLEE-RLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEE---E 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 166 ISKRIQSLEDES----------KSLKSQVAEAKTTFKIFQMNEERLKIAIKDALSENSQLQESQKQLL------QEAEEW 229
Cdd:pfam01576 245 LQAALARLEEETaqknnalkkiRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLdttaaqQELRSK 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 230 REQ-VNELnkQRMTFEDSKVHVEQV--LCDKENQ-IKSLTERLRKMKDWTAVL--GEEIADDDNLEWEMKSDSENDAHLD 303
Cdd:pfam01576 325 REQeVTEL--KKALEEETRSHEAQLqeMRQKHTQaLEELTEQLEQAKRNKANLekAKQALESENAELQAELRTLQQAKQD 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 304 NQPKGalkklihaaklraslKTLEGERNQIYTQLSEVDKTKEELTECIKNLQTEQASLQSENTQFENETQKLQQKLKVMT 383
Cdd:pfam01576 403 SEHKR---------------KKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLE 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 384 ELYQENEMILHRkltmEENYRLEKEEKLSKADEKINHAAEELEtyrkRAKDLEEELERTIHSYQGQIISHEKKAHDNWLA 463
Cdd:pfam01576 468 SQLQDTQELLQE----ETRQKLNLSTRLRQLEDERNSLQEQLE----EEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGT 539
|
410 420 430
....*....|....*....|....*....|....
gi 1387233842 464 ARTAERNLNDLRKENAHNRQKLTETEFKIELLEK 497
Cdd:pfam01576 540 LEALEEGKKRLQRELEALTQQLEEKAAAYDKLEK 573
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
72-474 |
1.06e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 72 GREKKLAIELSTLIEEKCKLLEKFSIVQKEYESLESSLKDASYEKESTEAQsleafyekLTESKSELEdeililekelke 151
Cdd:COG4372 17 GLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEE--------LEQARSELE------------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 152 ekskhskqdelmsEISKRIQSLEDESKSLKSQVAEAKTTFKIFQMNEERLKIAIKDALSENSQLQESQKQLLQEAEEwre 231
Cdd:COG4372 77 -------------QLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAE--- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 232 qvnelnkqrmtfedskvhVEQVLCDKENQIKSLTERLRKMKDWTAVLGEEIADDDNLE-----WEMKSDSENDAHLDNQP 306
Cdd:COG4372 141 ------------------LQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEaeqalDELLKEANRNAEKEEEL 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 307 KGALKKLIHAAKLRASLKTLEGERNQIYTQLSEVDKTKEELTECIKNLQTEQASLQSENTQFENETQKLQQKLKVMTELY 386
Cdd:COG4372 203 AEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAA 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 387 QENEMILHRKLTMEENYRLEKEEKLSKADEKINHAAEELETYRKRAKDLEEELERTIHSYQGQIISHEKKAHDNWLAART 466
Cdd:COG4372 283 LELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKG 362
|
....*...
gi 1387233842 467 AERNLNDL 474
Cdd:COG4372 363 AEAGVADG 370
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
86-477 |
1.08e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 42.73 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 86 EEKCKLLEKFSIVQKEYESLESSLK-DASYekesteAQSL-EAFYEKLTESKSELEDEILILEkelkeekskhsKQDELM 163
Cdd:TIGR01612 1190 DEIKKLLNEIAEIEKDKTSLEEVKGiNLSY------GKNLgKLFLEKIDEEKKKSEHMIKAME-----------AYIEDL 1252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 164 SEISKRIQSLEDESKSLKSQVAEAKtTFKIFQMNEERLKIAIKDALSENSQLQESQKQLLQEAEEwREQVNELNKQRMTF 243
Cdd:TIGR01612 1253 DEIKEKSPEIENEMGIEMDIKAEME-TFNISHDDDKDHHIISKKHDENISDIREKSLKIIEDFSE-ESDINDIKKELQKN 1330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 244 -EDSKVH---VEQVLCD--------KENQIKSLterLRKMKDWTAVLGEeiaDDDNLEWEMkSDSEndahldnqpkgalk 311
Cdd:TIGR01612 1331 lLDAQKHnsdINLYLNEianiynilKLNKIKKI---IDEVKEYTKEIEE---NNKNIKDEL-DKSE-------------- 1389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 312 KLIHAAKLRASLKTLegeRNQIYTQLSEVDktkeeLTECIKNLQTEQASLQSE----NTQFENETQklqqklkvmtelYQ 387
Cdd:TIGR01612 1390 KLIKKIKDDINLEEC---KSKIESTLDDKD-----IDECIKKIKELKNHILSEesniDTYFKNADE------------NN 1449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 388 ENEMILHRKLTMEEN-----YRLEKEEKLSKADEKINHAAEELETYR-------KRAKDLE----------EELERTIHS 445
Cdd:TIGR01612 1450 ENVLLLFKNIEMADNksqhiLKIKKDNATNDHDFNINELKEHIDKSKgckdeadKNAKAIEknkelfeqykKDVTELLNK 1529
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1387233842 446 Y---------------QGQIISHEKKAHDNW-LAARTAERNLNDLRKE 477
Cdd:TIGR01612 1530 YsalaiknkfaktkkdSEIIIKEIKDAHKKFiLEAEKSEQKIKEIKKE 1577
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
160-492 |
1.32e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 42.35 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 160 DELMSEISKRiQSLEDESKSLKSQVAEAKTTFKIFQMNEERL-----KIAIKDALSEN--------SQLQESQKQLLQEA 226
Cdd:TIGR01612 1486 NELKEHIDKS-KGCKDEADKNAKAIEKNKELFEQYKKDVTELlnkysALAIKNKFAKTkkdseiiiKEIKDAHKKFILEA 1564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 227 EEWREQVNELNKQRMTFEDSKVH---VEQVLCDKENQIKSLTERLRKMKDWTAVLGEEIADDDNLEWEMKSDSendahLD 303
Cdd:TIGR01612 1565 EKSEQKIKEIKKEKFRIEDDAAKndkSNKAAIDIQLSLENFENKFLKISDIKKKINDCLKETESIEKKISSFS-----ID 1639
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 304 NQPKGALKKLIHAAKLRASLKTLEGERNQIYTQLSEVDKTKEELtECIKNlQTEQASLQSENTQFE--NETQKL-QQKLK 380
Cdd:TIGR01612 1640 SQDTELKENGDNLNSLQEFLESLKDQKKNIEDKKKELDELDSEI-EKIEI-DVDQHKKNYEIGIIEkiKEIAIAnKEEIE 1717
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 381 VMTELYQENEMILHRKLTMEENYRLEKEEKLSKADEKINHAAEE-LETYRKRAKDLE---------EELERTIHSYQGQ- 449
Cdd:TIGR01612 1718 SIKELIEPTIENLISSFNTNDLEGIDPNEKLEEYNTEIGDIYEEfIELYNIIAGCLEtvskepityDEIKNTRINAQNEf 1797
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1387233842 450 --IISHEKKAH---DNwLAARTAERNLNDLRKENAHNRQKLTETEFKI 492
Cdd:TIGR01612 1798 lkIIEIEKKSKsylDD-IEAKEFDRIINHFKKKLDHVNDKFTKEYSKI 1844
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
132-493 |
1.40e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 132 TESKSELEDEILILEKELKEEKSKHSKQDELM--SEISKRIQSL---EDESKSLKSQVAEAKTTFKIFQMNEERLKIAIK 206
Cdd:PTZ00121 1090 DEATEEAFGKAEEAKKTETGKAEEARKAEEAKkkAEDARKAEEArkaEDARKAEEARKAEDAKRVEIARKAEDARKAEEA 1169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 207 DALSENSQLQESQKQL-LQEAEEWR--EQVNELNKQRMTFEDSKVhveqvlcdkenqiksltERLRKMKDWTAVLGEEIA 283
Cdd:PTZ00121 1170 RKAEDAKKAEAARKAEeVRKAEELRkaEDARKAEAARKAEEERKA-----------------EEARKAEDAKKAEAVKKA 1232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 284 DDDNLEWEMKSDSENDAHLDNQPKGALKKLIHAAKLRASLKTLEGERNQIYTQLSEVDKTkEELTECIKNLQTEQASLQS 363
Cdd:PTZ00121 1233 EEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKA-DEAKKAEEKKKADEAKKKA 1311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 364 ENTQFENETQKLQQKLKVMTELYQENEMILHRKLTMEENYRLEKEEKLSKADEKINHAAEELETYRKRAKDLEEELERTI 443
Cdd:PTZ00121 1312 EEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKK 1391
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1387233842 444 HSYQGQIISHEKKAHDNWLAARTAERNLNDLRKENAHNRQKLTETEFKIE 493
Cdd:PTZ00121 1392 KADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAE 1441
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
168-378 |
1.48e-03 |
|
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: 41.34 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 168 KRIQSLEDESKSLKSQVAEAKTTFKIFQMNEErlkiaikdalsenSQLQESQKQLlqeaEEWREQVNELNKQRMTFEDSK 247
Cdd:pfam15905 152 KKMSSLSMELMKLRNKLEAKMKEVMAKQEGME-------------GKLQVTQKNL----EHSKGKVAQLEEKLVSTEKEK 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 248 V----HVEQVLcDKENQIKSLTERLRKMKDWTAVLGEEIAD-DDNLEWEMKSDSENDAHLDNQPKgalkklihaaKLRAS 322
Cdd:pfam15905 215 IeeksETEKLL-EYITELSCVSEQVEKYKLDIAQLEELLKEkNDEIESLKQSLEEKEQELSKQIK----------DLNEK 283
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1387233842 323 LKTLEGERNQIYTQlsevDKTKEEltecikNLQTEQASLQSENTQFENETQKLQQK 378
Cdd:pfam15905 284 CKLLESEKEELLRE----YEEKEQ------TLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
80-487 |
1.58e-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: 41.60 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 80 ELSTLIEEKCKLLEKFSIVQKEYESLES--SLKDASYEKESTEAQSLEAFYEKLTESKSELEDEILILEKELKEEKSKHS 157
Cdd:pfam05622 22 QVSLLQEEKNSLQQENKKLQERLDQLESgdDSGTPGGKKYLLLQKQLEQLQEENFRLETARDDYRIKCEELEKEVLELQH 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 158 KQDELMSeISKRIQSLEDESKSLKSQVaeakttfkifqmneerlkiaikDALSENSQLQESQKQLLQEAEEWREQVNELN 237
Cdd:pfam05622 102 RNEELTS-LAEEAQALKDEMDILRESS----------------------DKVKKLEATVETYKKKLEDLGDLRRQVKLLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 238 KQRMTFEDSKVHVEQVLcDKENQIKSLTERL-RKMKDWTAVLGEEIADDDNLEWEMKsdsendahldnqpkgalkkliha 316
Cdd:pfam05622 159 ERNAEYMQRTLQLEEEL-KKANALRGQLETYkRQVQELHGKLSEESKKADKLEFEYK----------------------- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 317 aKLRASLKTLEGERNQIYTQLSEVDKTKEELtECI----KNLQTEQASLQSENTQFEN---ETQKLQQKLKVMtELYQEN 389
Cdd:pfam05622 215 -KLEEKLEALQKEKERLIIERDTLRETNEEL-RCAqlqqAELSQADALLSPSSDPGDNlaaEIMPAEIREKLI-RLQHEN 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 390 EMIlhrKLTMEENYRlEKEEKLSKADEKINHAAEELETYRKRAKDLEEELERTIHSYQGQIISHEKKAHDNWLAARTAER 469
Cdd:pfam05622 292 KML---RLGQEGSYR-ERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQGSKAEDSSLLKQKLEE 367
|
410
....*....|....*...
gi 1387233842 470 NLNDLRKENAhNRQKLTE 487
Cdd:pfam05622 368 HLEKLHEAQS-ELQKKKE 384
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
308-474 |
1.61e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 41.20 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 308 GALKKLIHAAKLRASLKTLEGERNQIY----TQLSEVDKTKEELTECIKNLqteqaslqsenTQFENETQKLQQKLkvmt 383
Cdd:cd22656 94 AEILELIDDLADATDDEELEEAKKTIKalldDLLKEAKKYQDKAAKVVDKL-----------TDFENQTEKDQTAL---- 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 384 elyQENEMILHRKLTMEENyrLEKEEKLSKADEKInhaAEELETYRKRAKDLEEELERTIHSYQGQiISHEKKAHDNWLA 463
Cdd:cd22656 159 ---ETLEKALKDLLTDEGG--AIARKEIKDLQKEL---EKLNEEYAAKLKAKIDELKALIADDEAK-LAAALRLIADLTA 229
|
170
....*....|.
gi 1387233842 464 ARTAERNLNDL 474
Cdd:cd22656 230 ADTDLDNLLAL 240
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
163-376 |
1.63e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.92 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 163 MSEISK-RIQSLEDESKSLKSQVAEAKTTFKIFQMNEERLKIAIKDALSEnsqLQESQKQLLQEAEEWREQVNELNKQrm 241
Cdd:PHA02562 168 MDKLNKdKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIAR---KQNKYDELVEEAKTIKAEIEELTDE-- 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 242 tfedskvhveqvLCDKENQIKSLTERLRKMKDWTAVLGEEIaddDNLEWEMKSDSEND------AHLDNQPKgalkkliH 315
Cdd:PHA02562 243 ------------LLNLVMDIEDPSAALNKLNTAAAKIKSKI---EQFQKVIKMYEKGGvcptctQQISEGPD-------R 300
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387233842 316 AAKLRASLKTLEGERNQIYTQLSEVDKTKEELTECIKNLQTEQASLQSENTQF----------ENETQKLQ 376
Cdd:PHA02562 301 ITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLitlvdkakkvKAAIEELQ 371
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
80-283 |
1.94e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 80 ELSTLIEEKCKLLEKFSIVQKEYESLESSLKDASYEKESTEAQsLEAFYEKLTESKSELedeililekelkeekskhskq 159
Cdd:COG3883 24 ELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAE-IDKLQAEIAEAEAEI--------------------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 160 DELMSEISKRIQSL--EDESKSLKSQVAEAKTTFKIFQmNEERLKIAIKDALSENSQLQESQKQLLQEAEEWREQVNELN 237
Cdd:COG3883 82 EERREELGERARALyrSGGSVSYLDVLLGSESFSDFLD-RLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1387233842 238 KQRMTFEDSKVHVEQVLCDKENQIKSLTERLRKMKDWTAVLGEEIA 283
Cdd:COG3883 161 ALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELA 206
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
99-322 |
4.08e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.13 E-value: 4.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 99 QKEYESLESSLKDASYEKESTEAQsleafYEKLTESKSELEDEILILEKELKEEKSKHSKQDELMSEISKRIQSLEDESK 178
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKE-----EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 179 SLKSQVAE-AKTTFKIFQMNEERLKIA---IKDALSENSQLQESQKQLLQEAEEWREQVNELNKQRMTFEDSKVHVEQVL 254
Cdd:COG4942 101 AQKEELAElLRALYRLGRQPPLALLLSpedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387233842 255 CDKENQIKSLTERLRKMKDWTAVLGEEIADDDNLEWEMKSDSENdahLDNQPKGALKKLIHAAKLRAS 322
Cdd:COG4942 181 AELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE---LEALIARLEAEAAAAAERTPA 245
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
160-497 |
4.68e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.20 E-value: 4.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 160 DELMSEISKRIQSLEDESKSLKSQ-------VAEAKTTFKIFQmneerlkiaiKDALSENSQLQESQKQL---LQEAEEW 229
Cdd:PRK04778 111 ESLLDLIEEDIEQILEELQELLESeeknreeVEQLKDLYRELR----------KSLLANRFSFGPALDELekqLENLEEE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 230 REQVNELNKQ------RMTFEDSKVHVEQ------------VLCDKE--NQIKSLTERLRKMKDWTAVLgeeiaDDDNLE 289
Cdd:PRK04778 181 FSQFVELTESgdyveaREILDQLEEELAAleqimeeipellKELQTElpDQLQELKAGYRELVEEGYHL-----DHLDIE 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 290 WEMKSdsendahLDNQPKGALKKL--IHAAKLRASLKTLEGERNQIYTQLS-------EVDKTKEELTECIKNLQTEqas 360
Cdd:PRK04778 256 KEIQD-------LKEQIDENLALLeeLDLDEAEEKNEEIQERIDQLYDILErevkarkYVEKNSDTLPDFLEHAKEQ--- 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 361 lqseNTQFENETQKLQQKlkvmtelYQENEmilhrklTMEENYR-LEKEekLSKADEKINHAAEELETYRKRAKDLEEEL 439
Cdd:PRK04778 326 ----NKELKEEIDRVKQS-------YTLNE-------SELESVRqLEKQ--LESLEKQYDEITERIAEQEIAYSELQEEL 385
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387233842 440 ER------TIHSYQGQIISHekkahdnwlaartaernLNDLRKENAHNRQKLTETEFKIE----LLEK 497
Cdd:PRK04778 386 EEilkqleEIEKEQEKLSEM-----------------LQGLRKDELEAREKLERYRNKLHeikrYLEK 436
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
154-487 |
5.62e-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: 40.16 E-value: 5.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 154 SKHSKQDELMSEISKRIQSLEDESKSLKSQV-------AEAKTTFKIFQMNEERLKIAIKDALSENSQLQESQKQLLQEA 226
Cdd:pfam01576 19 ERQQKAESELKELEKKHQQLCEEKNALQEQLqaetelcAEAEEMRARLAARKQELEEILHELESRLEEEEERSQQLQNEK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 227 EEWREQVNELNKQRMTFEDS--KVHVEQVLCdkENQIKSLTERLRKMKDWTAVLGEEIADDDNLEWEMKSD-SENDAHLD 303
Cdd:pfam01576 99 KKMQQHIQDLEEQLDEEEAArqKLQLEKVTT--EAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNlAEEEEKAK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 304 NQPKGALKKLIHAAKLRASLKTLEGERNQIYTQLSEVDKTKEELTECIKNLQTEQASLQSENTQFENETQKLQQKLKvmT 383
Cdd:pfam01576 177 SLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLE--E 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 384 ELYQENEmiLHRKLTMEENYRLEKEEKL-------SKADEKINHAAEELETYRkraKDLEEELERT-----IHSYQGQII 451
Cdd:pfam01576 255 ETAQKNN--ALKKIRELEAQISELQEDLeseraarNKAEKQRRDLGEELEALK---TELEDTLDTTaaqqeLRSKREQEV 329
|
330 340 350
....*....|....*....|....*....|....*.
gi 1387233842 452 SHEKKAHDNwlAARTAERNLNDLRKENAHNRQKLTE 487
Cdd:pfam01576 330 TELKKALEE--ETRSHEAQLQEMRQKHTQALEELTE 363
|
|
| BAR |
cd07307 |
The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects ... |
309-443 |
6.11e-03 |
|
The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects membrane curvature; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions including organelle biogenesis, membrane trafficking or remodeling, and cell division and migration. Mutations in BAR containing proteins have been linked to diseases and their inactivation in cells leads to altered membrane dynamics. A BAR domain with an additional N-terminal amphipathic helix (an N-BAR) can drive membrane curvature. These N-BAR domains are found in amphiphysins and endophilins, among others. BAR domains are also frequently found alongside domains that determine lipid specificity, such as the Pleckstrin Homology (PH) and Phox Homology (PX) domains which are present in beta centaurins (ACAPs and ASAPs) and sorting nexins, respectively. A FES-CIP4 Homology (FCH) domain together with a coiled coil region is called the F-BAR domain and is present in Pombe/Cdc15 homology (PCH) family proteins, which include Fes/Fes tyrosine kinases, PACSIN or syndapin, CIP4-like proteins, and srGAPs, among others. The Inverse (I)-BAR or IRSp53/MIM homology Domain (IMD) is found in multi-domain proteins, such as IRSp53 and MIM, that act as scaffolding proteins and transducers of a variety of signaling pathways that link membrane dynamics and the underlying actin cytoskeleton. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. The I-BAR domain induces membrane protrusions in the opposite direction compared to classical BAR and F-BAR domains, which produce membrane invaginations. BAR domains that also serve as protein interaction domains include those of arfaptin and OPHN1-like proteins, among others, which bind to Rac and Rho GAP domains, respectively.
Pssm-ID: 153271 [Multi-domain] Cd Length: 194 Bit Score: 38.58 E-value: 6.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 309 ALKKLIHAAKLRAslkTLEGERNQIYTQLSEV---------DKTKEELTECIKNLQTEQASLQSENTQFENETQK----- 374
Cdd:cd07307 8 LLKKLIKDTKKLL---DSLKELPAAAEKLSEAlqelgkelpDLSNTDLGEALEKFGKIQKELEEFRDQLEQKLENkviep 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387233842 375 LQQKLKVMTELYQENEMILHRKLTMEENYRlEKEEKLSKA---DEKINHAAEELETYRKRAKDLEEELERTI 443
Cdd:cd07307 85 LKEYLKKDLKEIKKRRKKLDKARLDYDAAR-EKLKKLRKKkkdSSKLAEAEEELQEAKEKYEELREELIEDL 155
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
228-385 |
7.22e-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: 39.23 E-value: 7.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 228 EWREQVNE-----LNKQRMTFEDSKvhveQVLCDKENQIKSLTERLRKMKDwtaVLGEEIADDDNLEWEMKSDSENDAhl 302
Cdd:smart00787 136 EWRMKLLEglkegLDENLEGLKEDY----KLLMKELELLNSIKPKLRDRKD---ALEEELRQLKQLEDELEDCDPTEL-- 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 303 dnqpkgalkklihaAKLRASLKTLEGE-------RNQIYTQLSEVDKTKEELTECIKNLQTEQASLQS---ENTQFEN-E 371
Cdd:smart00787 207 --------------DRAKEKLKKLLQEimikvkkLEELEEELQELESKIEDLTNKKSELNTEIAEAEKkleQCRGFTFkE 272
|
170
....*....|....
gi 1387233842 372 TQKLQQKLKVMTEL 385
Cdd:smart00787 273 IEKLKEQLKLLQSL 286
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
195-388 |
9.59e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 39.23 E-value: 9.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 195 QMNEERLKIAIKDALSENSQLQESQKQLLQEAEEWREQVNELNKQRMTF---EDSKVHVEQVLcDKENQIKSLTERLRKM 271
Cdd:COG3206 160 AYLEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVdlsEEAKLLLQQLS-ELESQLAEARAELAEA 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 272 KDWTAVLGEEIADDDNLEWEMKSDSENDAhLDNQPKGALKKLihaAKLRASL-------KTLEGERNQIYTQL-SEVDKT 343
Cdd:COG3206 239 EARLAALRAQLGSGPDALPELLQSPVIQQ-LRAQLAELEAEL---AELSARYtpnhpdvIALRAQIAALRAQLqQEAQRI 314
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1387233842 344 KEELTECIKNLQTEQASLQSENTQFENETQKLQQKLKVMTELYQE 388
Cdd:COG3206 315 LASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLERE 359
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
69-422 |
9.82e-03 |
|
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: 39.11 E-value: 9.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 69 LYVGREKKLAIELSTLIEEKCKLLEKFSIVQKEYESLESSLKDA--SYEKESTEAQS-LEAFYEKLTESKSELEDEILIL 145
Cdd:pfam07888 24 LVVPRAELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDreQWERQRRELESrVAELKEELRQSREKHEELEEKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 146 EKELKEEKSKHSKQDELM---SEISKRIQSLEDESKSLKSQVAEAKTTFKIFQMNEERLKIAIKDALSENSQLqesQKQL 222
Cdd:pfam07888 104 KELSASSEELSEEKDALLaqrAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQL---QAKL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 223 LQEAEEWREQVNELNKQRMTFEDSKVHVEQV------LCDKEN--------------QIKSLTERLRKMKDWTAVLGEEI 282
Cdd:pfam07888 181 QQTEEELRSLSKEFQELRNSLAQRDTQVLQLqdtittLTQKLTtahrkeaenealleELRSLQERLNASERKVEGLGEEL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 283 AD----DDNLEWEMKSDSENDAHLDNQPKGALKKL----IHAAKLRASL-KTLEGERNQIYTQLSEVDKT----KEELTE 349
Cdd:pfam07888 261 SSmaaqRDRTQAELHQARLQAAQLTLQLADASLALregrARWAQERETLqQSAEADKDRIEKLSAELQRLeerlQEERME 340
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1387233842 350 CIKnLQTEQASLQSENTQFENETQKLQQKLKVMTELYQ-ENEMILHRKLTMEEnYRLEKEEKLSK-ADEKINHAA 422
Cdd:pfam07888 341 REK-LEVELGREKDCNRVQLSESRRELQELKASLRVAQkEKEQLQAEKQELLE-YIRQLEQRLETvADAKWSEAA 413
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
188-441 |
9.84e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.37 E-value: 9.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 188 KTTFKIF--QMNEERLKIAIKDALSENSQLQESQKQLLQEAEEWREQVNELNKQRMTFEDSKVHVEQVLCDKENQIKSLT 265
Cdd:COG4717 36 KSTLLAFirAMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 266 ERLRKmkdwtavlgeeiadddnlewemksdsendahldnqpkgaLKKLIHAAKLRASLKTLEGERNQIYTQLSEVDKTKE 345
Cdd:COG4717 116 EELEK---------------------------------------LEKLLQLLPLYQELEALEAELAELPERLEELEERLE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387233842 346 EltecIKNLQTEQASLQSENTQFENETQKLQQKLKVMTELYQEnemilhrklTMEENYRlEKEEKLSKADEKINHAAEEL 425
Cdd:COG4717 157 E----LRELEEELEELEAELAELQEELEELLEQLSLATEEELQ---------DLAEELE-ELQQRLAELEEELEEAQEEL 222
|
250
....*....|....*.
gi 1387233842 426 ETYRKRAKDLEEELER 441
Cdd:COG4717 223 EELEEELEQLENELEA 238
|
|
| |
