|
Name |
Accession |
Description |
Interval |
E-value |
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
420-683 |
5.00e-118 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 355.60 E-value: 5.00e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 420 NLESSKQELIDYKQKATRILQSKEKLINSLKEGSGFEGLDSSTASSMELEELRHEKEMQREEIQKLMGQIHQLRSELQDM 499
Cdd:pfam09787 1 NLESAKQELADYKQKAARILQSKEKLIASLKEGSGVEGLDSSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 500 EAQQVNEAESAREQLQDLHDQIAGQKASKQELETELERLKQEFHYIEEDLYRTKNTLQSRIKDRDEEIQKLRNQLTNKTL 579
Cdd:pfam09787 81 EAQQQEEAESSREQLQELEEQLATERSARREAEAELERLQEELRYLEEELRRSKATLQSRIKDREAEIEKLRNQLTSKSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 580 SNSSQSELENRLHQLTETLIQKQTMLESLSTEKNSLVFQLERLEQQMNSASGSSSNGSSINMSGIDNGEGTRLRNVPVLF 659
Cdd:pfam09787 161 SSSSQSELENRLHQLTETLIQKQTMLEALSTEKNSLVLQLERMEQQIKELQGEGSNGTSINMEGISDGEGTRLRNVPGLF 240
|
250 260
....*....|....*....|....
gi 767982138 660 NDTETNLAGMYGKVRKAASSIDQF 683
Cdd:pfam09787 241 SESDSDRAGMYGKVRKAASVIDKF 264
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
227-542 |
8.81e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.97 E-value: 8.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 227 LRLENQLLRNEVQSLNQEMASLLQRSKETQEELNKARARVEKWNADHSKSDRMTRGLRAQVDDLTEAVAAKDSQLAVLKV 306
Cdd:COG1196 216 RELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 307 RLQEADQLLSTRTEALEALQSEKSRIMQDQSEgnslQNQALQTFQERLHEADATLKREQESYKQMQSEFAARLNKVEMER 386
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAE----LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 387 QNLAEAITLAERKYSDEKkrvdELQQQVKLYKLNLESSKQELIDYKQKATRILQSKEKLINSLKegsgfegldsstassm 466
Cdd:COG1196 372 AELAEAEEELEELAEELL----EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA---------------- 431
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767982138 467 ELEELRHEKEMQREEIQKLMGQIHQLRSELQDMEAQQVNEAESAREQLQDLHDQIAgQKASKQELETELERLKQEF 542
Cdd:COG1196 432 ELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELA-EAAARLLLLLEAEADYEGF 506
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
219-570 |
1.03e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 75.09 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 219 GKSHELSNLRLENqllRNEVQSLNQEMASLLQRSKETQEELNKARARVEKWNAdhsksdrMTRGLRAQVDDLTEAVAAKD 298
Cdd:TIGR02168 663 GGSAKTNSSILER---RREIEELEEKIEELEEKIAELEKALAELRKELEELEE-------ELEQLRKELEELSRQISALR 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 299 SQLAVLKVRLQEADQLLSTRTEALEALQSEKsRIMQDQSEGNSLQNQALQTFQERLHEADATLKREQESYKQMQSEFAAR 378
Cdd:TIGR02168 733 KDLARLEAEVEQLEERIAQLSKELTELEAEI-EELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAE 811
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 379 LNKVEMERQNLAEAITLAERKYSDEKKRVDELQQQVKLYKLNLESSKQELIDYKQKATRI---LQSKEKLINSLKEGSGF 455
Cdd:TIGR02168 812 LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELeseLEALLNERASLEEALAL 891
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 456 EGLDSSTASSmELEELRHEKEMQREEIQKLMGQIHQLRSELQDMEAQQVNEAESAREQLQD------------------L 517
Cdd:TIGR02168 892 LRSELEELSE-ELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLtleeaealenkieddeeeA 970
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767982138 518 HDQIAGQKASKQEL-------ETELERLKQEFHYIE---EDLYRTKNTLQSRIKDRDEEIQKL 570
Cdd:TIGR02168 971 RRRLKRLENKIKELgpvnlaaIEEYEELKERYDFLTaqkEDLTEAKETLEEAIEEIDREARER 1033
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
216-540 |
1.09e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 75.09 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 216 NDDGKSHELSNLRLENQLLRNEVQSLNQEMASLLQRSKETQEELNKARARVEKWNADHSKSDRMTRGLRAQVDDLTEAVA 295
Cdd:TIGR02168 219 KAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIS 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 296 AKDSQLAVLKVRLQEADQLLSTRTEALEALQSEKsrimqdqsegnslqnqalqtfqERLHEADATLKREQESYKQMQSEF 375
Cdd:TIGR02168 299 RLEQQKQILRERLANLERQLEELEAQLEELESKL----------------------DELAEELAELEEKLEELKEELESL 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 376 AARLNKVEMERQNLAEAITLAERKYSDEKKRVDELQQQVKLYKLNLESSKQELIDYKQKATRILQSKEKLINSLKEGSGF 455
Cdd:TIGR02168 357 EAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELK 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 456 EGLDSSTASSMELEELRHEKEMQREEIQKLMGQIHQLRSELQDMEAQ------QVNEAESAREQLQDLHDQIAGQKASKQ 529
Cdd:TIGR02168 437 ELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERElaqlqaRLDSLERLQENLEGFSEGVKALLKNQS 516
|
330
....*....|.
gi 767982138 530 ELETELERLKQ 540
Cdd:TIGR02168 517 GLSGILGVLSE 527
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
250-624 |
6.29e-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: 6.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 250 QRSKETQEELNKARARVEKWNADHSKSDRMTRGLRAQVD------DLTEAVaaKDSQLAVLKVRLQEADQLLSTRTEALE 323
Cdd:TIGR02168 172 ERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEkaerykELKAEL--RELELALLVLRLEELREELEELQEELK 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 324 ALQSEKSRImqdqsegnSLQNQALQTFQERLHEADATLKREQESYKQMQSEFAARLNKVEMErqnlaeaitlaERKYSDE 403
Cdd:TIGR02168 250 EAEEELEEL--------TAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQ-----------KQILRER 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 404 KKRVDELQQQVKLYKLNLESSKQELIDYKQKATRILQSKEKLINSLKEgsgfegldsstassmELEELRHEKEMQREEIQ 483
Cdd:TIGR02168 311 LANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEA---------------ELEELEAELEELESRLE 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 484 KLMGQIHQLRSELQDMEAQQV---NEAESAREQLQDLHDQIAGQKASKQELETELERlkQEFHYIEEDLYRTKNTLQSRI 560
Cdd:TIGR02168 376 ELEEQLETLRSKVAQLELQIAslnNEIERLEARLERLEDRRERLQQEIEELLKKLEE--AELKELQAELEELEEELEELQ 453
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767982138 561 KDRDEEIQKLRNQLTNKTLSNSSQSELENRLHQLTETLIQKQTMLESLSTEKNSLVFQLERLEQ 624
Cdd:TIGR02168 454 EELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSG 517
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
284-625 |
1.24e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 68.16 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 284 RAQVDDLTEAVAAKDSQLAVLKVRLQEADQLLSTRTEALEALQSEKSRIMQDQSEGNSlQNQALQTFQERLHEADATLKR 363
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRK-DLARLEAEVEQLEERIAQLSK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 364 EQESYKQMQSEFAARLNKvemERQNLAEAitlaerkysdeKKRVDELQQQVKLYKLNLESSKQELidykqkatrilqske 443
Cdd:TIGR02168 755 ELTELEAEIEELEERLEE---AEEELAEA-----------EAEIEELEAQIEQLKEELKALREAL--------------- 805
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 444 klinslkegsgfegldssTASSMELEELRHEKEMQREEIQKLMGQIHQLRSELQDMEAQqvneAESAREQLQDLHDQIAG 523
Cdd:TIGR02168 806 ------------------DELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ----IEELSEDIESLAAEIEE 863
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 524 QKASKQELETELERLKQEFHYIEEDLYRTKN---TLQSRIKDRDEEIQKLRNQLTNKTLSNSS----QSELENRLHQLTE 596
Cdd:TIGR02168 864 LEELIEELESELEALLNERASLEEALALLRSeleELSEELRELESKRSELRRELEELREKLAQlelrLEGLEVRIDNLQE 943
|
330 340 350
....*....|....*....|....*....|
gi 767982138 597 TLIQK-QTMLESLSTEKNSLVFQLERLEQQ 625
Cdd:TIGR02168 944 RLSEEySLTLEEAEALENKIEDDEEEARRR 973
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
234-588 |
1.57e-11 |
|
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: 67.79 E-value: 1.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 234 LRNEVQSLNQEMASLLqRSKETQEELNKARA--RVEKWNAdhskSDRMTRGLRAQVDDLTEAVAAKDSQLAVLKVRLQEA 311
Cdd:TIGR02169 196 KRQQLERLRREREKAE-RYQALLKEKREYEGyeLLKEKEA----LERQKEAIERQLASLEEELEKLTEEISELEKRLEEI 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 312 DQLLSTRTEALEALQSEKSRimqdqsegnslqnqALQTFQERLHEADATLKREQESYKQMQSEFAARLNKVEMERQNLAE 391
Cdd:TIGR02169 271 EQLLEELNKKIKDLGEEEQL--------------RVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 392 AITLAERKYSDEKKRVDELQQQVKlyklnleSSKQELIDYKQKatriLQSKEKLINSLKEgsgfegldsstassmELEEL 471
Cdd:TIGR02169 337 EIEELEREIEEERKRRDKLTEEYA-------ELKEELEDLRAE----LEEVDKEFAETRD---------------ELKDY 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 472 RHEKEMQREEIQKLMGQIHQLRSELQdmeaqqvneaeSAREQLQDLHDQIAGQKASKQELETELERLKQEFHYIEEDLYR 551
Cdd:TIGR02169 391 REKLEKLKREINELKRELDRLQEELQ-----------RLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQ 459
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 767982138 552 TK---NTLQSRIKDRDEEIQKLRNQLTnktlsnSSQSELE 588
Cdd:TIGR02169 460 LAadlSKYEQELYDLKEEYDRVEKELS------KLQRELA 493
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
219-625 |
2.56e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 66.71 E-value: 2.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 219 GKSHELSNLRL-ENQLLRNEVQSLNQEMASLLQRSKETQEELNKARARVEKWNADHSKSDRMtrglrAQVDDLTEAVAAK 297
Cdd:COG4717 63 GRKPELNLKELkELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKL-----LQLLPLYQELEAL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 298 DSQLAVLKVRLQEADQLLSTRTEALEALQSEKSRIMQDQSEGNSLQNQALQTFQERLHEADATLKREQESYKQMQSEFAA 377
Cdd:COG4717 138 EAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 378 RLNKVEMERQNLAEAITLAERKysDEKKRVDELQQQVKLYK--LNLESSKQELIDYKQKATRILQskekLINSLKEGSGF 455
Cdd:COG4717 218 AQEELEELEEELEQLENELEAA--ALEERLKEARLLLLIAAalLALLGLGGSLLSLILTIAGVLF----LVLGLLALLFL 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 456 EGLDSSTASSMELEELRHEKEMQREEIQKLMGQIHQLRSElQDMEAQQVNEAESAREQLQDLHDQIAG--QKASKQELET 533
Cdd:COG4717 292 LLAREKASLGKEAEELQALPALEELEEEELEELLAALGLP-PDLSPEELLELLDRIEELQELLREAEEleEELQLEELEQ 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 534 ELERLKQEFHYIEEDLYRTKNTLQSRIKDRDEEIQKLRNQLTNKT------LSNSSQSELENRLHQLTETLIQKQTMLES 607
Cdd:COG4717 371 EIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLgeleelLEALDEEELEEELEELEEELEELEEELEE 450
|
410
....*....|....*...
gi 767982138 608 LSTEKNSLVFQLERLEQQ 625
Cdd:COG4717 451 LREELAELEAELEQLEED 468
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
306-616 |
3.62e-11 |
|
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: 66.63 E-value: 3.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 306 VRLQEADQLLSTRtEALEALQSEKSRIMQDQSEGNSLQNQALQTFQErLHEADATLKREQESYKQMQSEFAARLNKVEME 385
Cdd:TIGR02169 668 FSRSEPAELQRLR-ERLEGLKRELSSLQSELRRIENRLDELSQELSD-ASRKIGEIEKEIEQLEQEEEKLKERLEELEED 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 386 RQNLAEAITLAERKYSDEKKRVDELQQQVKLYKLNLESSKQELIDykqkatrilqskeklinslkegsgfEGLDSSTASS 465
Cdd:TIGR02169 746 LSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH-------------------------SRIPEIQAEL 800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 466 MELEELRHEKEMQREEIQKLMGQIHQLRSELQDMEAQQVNEAESAREQLQDLHDQIAGQKASKQELETELERLKQEFHYI 545
Cdd:TIGR02169 801 SKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDL 880
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767982138 546 EEDLYRTKntlqsriKDRDEEIQKLRNQLTNKTLSNSSQSELENRLHQLTETLIQKQTMLESLSTEKNSLV 616
Cdd:TIGR02169 881 ESRLGDLK-------KERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDE 944
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
348-624 |
1.03e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.34 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 348 QTFQERLHEADATLK-REQESYKQMQSEFAARLNKVEMERQNLAEAITLAERKYSDEKKRVDELQQQVKLYKLNLESSKQ 426
Cdd:COG1196 216 RELKEELKELEAELLlLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 427 ELIDYKQKATRILQSKEKLINSLKEgsgfegldsstaSSMELEELRHEKEMQREEIQKLMGQIHQLRSELQDMEAQQVNE 506
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEE------------LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 507 AESAREQLQDLHDQIAGQKASKQELETELERLKQEFHYIEEDLYRTKNTLQSRIKDRDEEIQKLRNQLTNKTLSNSSQSE 586
Cdd:COG1196 364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443
|
250 260 270
....*....|....*....|....*....|....*...
gi 767982138 587 LENRLHQLTETLIQKQTMLESLSTEKNSLVFQLERLEQ 624
Cdd:COG1196 444 LEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
347-625 |
3.32e-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: 63.54 E-value: 3.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 347 LQTFQERLHEADATLKREQESYKQMQSEFA---ARLNKVEMERQNLAEAITLAERKYSDEKKRVDELQQQVKLYKLNLES 423
Cdd:TIGR02168 234 LEELREELEELQEELKEAEEELEELTAELQeleEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 424 SKQELidyKQKATRILQSKEKLINSLKEgsgfegldsSTASSMELEELRHEKEMQREEIQKLmgqihqlRSELQDMEAQq 503
Cdd:TIGR02168 314 LERQL---EELEAQLEELESKLDELAEE---------LAELEEKLEELKEELESLEAELEEL-------EAELEELESR- 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 504 vneAESAREQLQDLHDQIAGQKASKQELETELERLKQEfhyieedlyrtKNTLQSRIKDRDEEIQKLRNQLTnktlsnss 583
Cdd:TIGR02168 374 ---LEELEEQLETLRSKVAQLELQIASLNNEIERLEAR-----------LERLEDRRERLQQEIEELLKKLE-------- 431
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 767982138 584 qselENRLHQLTETLIQKQTMLESLSTEKNSLVFQLERLEQQ 625
Cdd:TIGR02168 432 ----EAELKELQAELEELEEELEELQEELERLEEALEELREE 469
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
248-625 |
5.16e-10 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 63.05 E-value: 5.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 248 LLQRSKETQEELNKARarvEKWNADHSKSDRMTRGLRAQVD---DLTEAVAAKDSQLAVLK--VRLQEAdqlLSTRTEAL 322
Cdd:COG3096 283 LSERALELRRELFGAR---RQLAEEQYRLVEMARELEELSAresDLEQDYQAASDHLNLVQtaLRQQEK---IERYQEDL 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 323 EALqSEKSRImqdqsegnslQNQALQTFQERLHEADATLKREQESYKQMQSEFAARlnkvemeRQNLAEAITLAeRKYSD 402
Cdd:COG3096 357 EEL-TERLEE----------QEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADY-------QQALDVQQTRA-IQYQQ 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 403 EKKRVDELQQQVKLYKLNLESSKQELIDYKQKA----TRILQSKEKLINSLKEGSGFE-----------GLDSSTASSME 467
Cdd:COG3096 418 AVQALEKARALCGLPDLTPENAEDYLAAFRAKEqqatEEVLELEQKLSVADAARRQFEkayelvckiagEVERSQAWQTA 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 468 LEELRhekemQREEIQKLMGQIHQLRSELQDMEaQQVNEAESAREQLQDLHDQIAGQKASKQELETELERLKQEFHYIEE 547
Cdd:COG3096 498 RELLR-----RYRSQQALAQRLQQLRAQLAELE-QRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEE 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 548 DLyRTKNTLQSRIKDRDEEIQKLRNQLTNK------------TLSNSSQSELENRlHQLTETLiqkQTMLE---SLSTEK 612
Cdd:COG3096 572 QA-AEAVEQRSELRQQLEQLRARIKELAARapawlaaqdaleRLREQSGEALADS-QEVTAAM---QQLLErerEATVER 646
|
410
....*....|...
gi 767982138 613 NSLVFQLERLEQQ 625
Cdd:COG3096 647 DELAARKQALESQ 659
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
223-625 |
1.65e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.47 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 223 ELSNLRLENQLLRNEVQSLNQ--EMASLLQRSKETQEELNKARARVEKWNADHSKS--DRMTRGLRAQVDDLTEAVAAKD 298
Cdd:COG4913 236 DLERAHEALEDAREQIELLEPirELAERYAAARERLAELEYLRAALRLWFAQRRLEllEAELEELRAELARLEAELERLE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 299 SQLAVLKVRLQEA-DQLLSTRTEALEALQSEKSRIMQDQSEgnslQNQALQTFQERLHEADATLKREQESYKQMQSEFAA 377
Cdd:COG4913 316 ARLDALREELDELeAQIRGNGGDRLEQLEREIERLERELEE----RERRRARLEALLAALGLPLPASAEEFAALRAEAAA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 378 RLNKVEMERQNLAEAITLAERKYSDEKKRVDELQQQVKlyklNLESSKQ----------------------------ELI 429
Cdd:COG4913 392 LLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA----SLERRKSniparllalrdalaealgldeaelpfvgELI 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 430 DYKQK---------------ATRILQSKEKL------INSLKEGSG--FEGLDSSTAS---------------------- 464
Cdd:COG4913 468 EVRPEeerwrgaiervlggfALTLLVPPEHYaaalrwVNRLHLRGRlvYERVRTGLPDperprldpdslagkldfkphpf 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 465 ----SMEL------------EEL-RHEKEMQREeiqklmGQIHQLRS--ELQDmeAQQVNEA----ESAREQLQDLHDQI 521
Cdd:COG4913 548 rawlEAELgrrfdyvcvdspEELrRHPRAITRA------GQVKGNGTrhEKDD--RRRIRSRyvlgFDNRAKLAALEAEL 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 522 AGQKASKQELETELERLKQEFHYIEE--DLYRTKNTLQSRIKD---RDEEIQKLRNQLTNKTLSNSSQSELENRLHQLTE 596
Cdd:COG4913 620 AELEEELAEAEERLEALEAELDALQErrEALQRLAEYSWDEIDvasAEREIAELEAELERLDASSDDLAALEEQLEELEA 699
|
490 500
....*....|....*....|....*....
gi 767982138 597 TLIQKQTMLESLSTEKNSLVFQLERLEQQ 625
Cdd:COG4913 700 ELEELEEELDELKGEIGRLEKELEQAEEE 728
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
223-625 |
9.94e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.91 E-value: 9.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 223 ELSNLRLENQLLRNEVQSLNQEMASLLQRSKETQEELNKARARVEkwNADHSKSDRMTRGLRAQVDDLTEAVAAKDSQLA 302
Cdd:TIGR02168 387 KVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE--EAELKELQAELEELEEELEELQEELERLEEALE 464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 303 VLKVRLQEADQLLSTRTEALEALQSEKSRIMQDQSEGNSLQNQALQTFQERLHEAD-----ATLKREQESYKQ-MQSEFA 376
Cdd:TIGR02168 465 ELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGilgvlSELISVDEGYEAaIEAALG 544
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 377 ARLNKVEMERQNLAEAIT-------------LAERKYSDEKKRVDELQQ-----QVKLYKLNLESSKQEL---IDYKQKA 435
Cdd:TIGR02168 545 GRLQAVVVENLNAAKKAIaflkqnelgrvtfLPLDSIKGTEIQGNDREIlknieGFLGVAKDLVKFDPKLrkaLSYLLGG 624
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 436 TRI---LQSKEKLINSLKEGSGFEGLD--------------SSTASSM-----ELEELRHEKEMQREEIQKLMGQIHQLR 493
Cdd:TIGR02168 625 VLVvddLDNALELAKKLRPGYRIVTLDgdlvrpggvitggsAKTNSSIlerrrEIEELEEKIEELEEKIAELEKALAELR 704
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 494 SELQDMEaqqvNEAESAREQLQDLHDQIAGQKASKQELETELERLKQ----------EFHYIEEDLYRTKNTLQSRIKDR 563
Cdd:TIGR02168 705 KELEELE----EELEQLRKELEELSRQISALRKDLARLEAEVEQLEEriaqlskeltELEAEIEELEERLEEAEEELAEA 780
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767982138 564 DEEIQKLRNQLTN----KTLSNSSQSELENRLHQLTETLIQKQTMLESLSTEKNSLVFQLERLEQQ 625
Cdd:TIGR02168 781 EAEIEELEAQIEQlkeeLKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
224-625 |
3.95e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.61 E-value: 3.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 224 LSNLRLENQLLRNEVQSLNQEMASLLQRSKETQEELNKARARVEKWNADHSKSDRMtRGLRAQVDDLT---------EAV 294
Cdd:PRK03918 319 LEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEEL-ERLKKRLTGLTpeklekeleELE 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 295 AAKDS---QLAVLKVRLQEADQLLSTRTEALEALQSEKS------RIMQDQSEGNSLqnqalqtfqERLHEADATLKREQ 365
Cdd:PRK03918 398 KAKEEieeEISKITARIGELKKEIKELKKAIEELKKAKGkcpvcgRELTEEHRKELL---------EEYTAELKRIEKEL 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 366 ESYKQMQSEFAARLNKVEMERQNLAEAITLaeRKYSDEKKRVDElqqqvKLYKLNLESSKQELIDYKQKATRILQSKEKL 445
Cdd:PRK03918 469 KEIEEKERKLRKELRELEKVLKKESELIKL--KELAEQLKELEE-----KLKKYNLEELEKKAEEYEKLKEKLIKLKGEI 541
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 446 INSLKEGSGFEGLDSSTAssmELEELRHEKEMQREEIQKlmgqihqlrsELQDMEAQQVNEAESAREQLQDLHDQIAGQK 525
Cdd:PRK03918 542 KSLKKELEKLEELKKKLA---ELEKKLDELEEELAELLK----------ELEELGFESVEELEERLKELEPFYNEYLELK 608
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 526 ASKQELETELERLK---QEFHYIEEDLYRTKNTLQsRIKDRDEEIQKLRNQLTNKtlsnssqsELENRLHQLTETLIQKQ 602
Cdd:PRK03918 609 DAEKELEREEKELKkleEELDKAFEELAETEKRLE-ELRKELEELEKKYSEEEYE--------ELREEYLELSRELAGLR 679
|
410 420
....*....|....*....|...
gi 767982138 603 TMLESLSTEKNSLVFQLERLEQQ 625
Cdd:PRK03918 680 AELEELEKRREEIKKTLEKLKEE 702
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
232-500 |
1.66e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.92 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 232 QLLRNEVQSLNQEMASLLQRSKETQEELNKARARVEKWN--ADHSKSDRMTRGLRAQVDDLTEAVA---AKDSQLAVLKV 306
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQrlAEYSWDEIDVASAEREIAELEAELErldASSDDLAALEE 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 307 RLQEADQLLSTRTEALEALQSEKSRImqdqsegnslqNQALQTFQERLHEADATLKR-EQESYKQMQSEFAARLNKVEME 385
Cdd:COG4913 693 QLEELEAELEELEEELDELKGEIGRL-----------EKELEQAEEELDELQDRLEAaEDLARLELRALLEERFAAALGD 761
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 386 ------RQNLAEAITLAERKYSDEKKRVDELQQQVK----LYKLNLESSKQELIDYKQKATRILQS-----KEKLINSLK 450
Cdd:COG4913 762 averelRENLEERIDALRARLNRAEEELERAMRAFNrewpAETADLDADLESLPEYLALLDRLEEDglpeyEERFKELLN 841
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 767982138 451 EgsgfegldsstASSMELEELRHEKEMQREEIQKlmgQIHQLRSELQDME 500
Cdd:COG4913 842 E-----------NSIEFVADLLSKLRRAIREIKE---RIDPLNDSLKRIP 877
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
220-608 |
1.69e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.68 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 220 KSHELSNLRLENQLLRNEVQSLNQEmaslLQRSKETQEELNKARARVEKWNADhsksdrmTRGLRAQVDDLTEAVAAKDS 299
Cdd:PRK03918 205 VLREINEISSELPELREELEKLEKE----VKELEELKEEIEELEKELESLEGS-------KRKLEEKIRELEERIEELKK 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 300 QLAVLKVRLQEADQL--LSTRTEALEALQSEKSRIMQDQSEGNSLQNQALQTFQERLHEADAT------LKREQESYKQM 371
Cdd:PRK03918 274 EIEELEEKVKELKELkeKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKeerleeLKKKLKELEKR 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 372 QSEFAARLNKVEMERQNLAEAITLAERKYSDEKKRVDELQQQVKLYKLNLESSKQELIDYKQKATRILQSKEKLINSLKE 451
Cdd:PRK03918 354 LEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKK 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 452 GSGFEGLDSSTASSMELEEL--RHEKEMQR--EEIQKLMGQIHQLRSELQDMEAQQVNEAESAReqLQDLHDQI--AGQK 525
Cdd:PRK03918 434 AKGKCPVCGRELTEEHRKELleEYTAELKRieKELKEIEEKERKLRKELRELEKVLKKESELIK--LKELAEQLkeLEEK 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 526 ASKQELEtELERLKQEFHYIEEDLYRTKNTLqSRIKDRDEEIQKLRNQLTnktlsnssqsELENRLHQLTETLIQKQTML 605
Cdd:PRK03918 512 LKKYNLE-ELEKKAEEYEKLKEKLIKLKGEI-KSLKKELEKLEELKKKLA----------ELEKKLDELEEELAELLKEL 579
|
...
gi 767982138 606 ESL 608
Cdd:PRK03918 580 EEL 582
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
223-574 |
2.16e-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: 54.35 E-value: 2.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 223 ELSNLRLENQLLRNEVQSLNQEMASLLQRSKETQEELNKARARVEK-WNADHSKSDRMTRgLRAQVDDLTEAVaakdsql 301
Cdd:pfam15921 357 ELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRlWDRDTGNSITIDH-LRRELDDRNMEV------- 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 302 avlkvrlqeadqllsTRTEAL-EALQSEKSRIMQDQSEGNSLQNQALqtfqERLHEADATLKREQESYKQMQSEFAAR-- 378
Cdd:pfam15921 429 ---------------QRLEALlKAMKSECQGQMERQMAAIQGKNESL----EKVSSLTAQLESTKEMLRKVVEELTAKkm 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 379 -LNKVEMERQNLAEAITLAERKYSDEKKRVDELQQQVKLYKLNLESSKQELIDYKQKATRI------LQSKEKLINSLKE 451
Cdd:pfam15921 490 tLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECealklqMAEKDKVIEILRQ 569
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 452 G----SGFEGLDSSTASSMELEELRHEKEM--QREEIQKLM-------GQIHQLRSELQDMEAQQVNEAESAREQLQDL- 517
Cdd:pfam15921 570 QienmTQLVGQHGRTAGAMQVEKAQLEKEIndRRLELQEFKilkdkkdAKIRELEARVSDLELEKVKLVNAGSERLRAVk 649
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767982138 518 -----HDQIAGQ-KASKQELET---ELERLKQEFHYIEEDLYRTKNTLQSRIKDRDEEIQKLRNQL 574
Cdd:pfam15921 650 dikqeRDQLLNEvKTSRNELNSlseDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTL 715
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
343-583 |
3.76e-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: 52.84 E-value: 3.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 343 QNQALQTFQERLHEADATLKREQESYKQMQSEfaarLNKVEMERQNLAEAITLAERKYSDEKKRVDELQQQVKLYKLNLE 422
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKE----EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 423 SSKQELIDYKQKATRILQSKEKL--INSLKEGSGFEGLDSSTASSMELEELRHEKEMQREEIQKLMGQIHQLRSELQdme 500
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLgrQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE--- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 501 aQQVNEAESAREQLQDLHDQIAGQKASKQELETELERLKQEFHYIEEDLYRTKNTLQSRIKDRDEEIQKLRNQLTNKTLS 580
Cdd:COG4942 171 -AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
|
...
gi 767982138 581 NSS 583
Cdd:COG4942 250 ALK 252
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
218-571 |
5.08e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 5.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 218 DGKSHELSNLRLENQLLRNEVQSLN---------QEMASLLQRSKETQEELNKARARVEKWNADHSKSDRMTRGLRAQVD 288
Cdd:COG4717 98 EELEEELEELEAELEELREELEKLEkllqllplyQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQE 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 289 DLTEAV----AAKDSQLAVLKVRLQEADQLLSTRTEALEALQSEKSRIMQDqsEGNSLQNQALQTFQERLHEADATLK-- 362
Cdd:COG4717 178 ELEELLeqlsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEE--LEQLENELEAAALEERLKEARLLLLia 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 363 ----------REQESYKQMQSEFAA-----------RLNKVEMERQNLAEAITLAERKYSDEKKRVDELQQQVKLYKLNL 421
Cdd:COG4717 256 aallallglgGSLLSLILTIAGVLFlvlgllallflLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLS 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 422 ESSKQELIDYKQKATRILQSKEKLINSLKEGSGFEGLDS--STASSMELEELRhEKEMQREEIQKLMGQIHQLRSELQDM 499
Cdd:COG4717 336 PEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAllAEAGVEDEEELR-AALEQAEEYQELKEELEELEEQLEEL 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 500 -----EAQQVNEAESAREQLQDLHDQIAGQKASKQELETELERLKQEFHYIEED-----LYRTKNTLQSRIKDRDEEIQK 569
Cdd:COG4717 415 lgeleELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDgelaeLLQELEELKAELRELAEEWAA 494
|
..
gi 767982138 570 LR 571
Cdd:COG4717 495 LK 496
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
222-542 |
7.05e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.46 E-value: 7.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 222 HELSNLRLENQLLRNEVQSLNQEMASLLQR-SKETQEELNKARARVEKWNADHSKSDRMTRGLRAQVDDLTEAVAAKDSQ 300
Cdd:COG4717 156 EELRELEEELEELEAELAELQEELEELLEQlSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 301 LAVLKV--RLQEADQLLSTRTEALEALQSEKSRIMQDQSEGN-------------SLQNQALQTFQERLHEADATLKREQ 365
Cdd:COG4717 236 LEAAALeeRLKEARLLLLIAAALLALLGLGGSLLSLILTIAGvlflvlgllallfLLLAREKASLGKEAEELQALPALEE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 366 ESYKQMQSEFAARLNKVEMERQNLAEAI--------TLAERKYSDEKKRVDELQQQVK-LYKLNLESSKQELI------- 429
Cdd:COG4717 316 LEEEELEELLAALGLPPDLSPEELLELLdrieelqeLLREAEELEEELQLEELEQEIAaLLAEAGVEDEEELRaaleqae 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 430 DYKQKATRILQSKEKLINSLKEGSGFEGLDSSTASSMELEELRHEKEMQREEIQKLMGQIHQLRSELQDME-----AQQV 504
Cdd:COG4717 396 EYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEedgelAELL 475
|
330 340 350
....*....|....*....|....*....|....*...
gi 767982138 505 NEAESAREQLQDLHDQIAGQKASKQELETELERLKQEF 542
Cdd:COG4717 476 QELEELKAELRELAEEWAALKLALELLEEAREEYREER 513
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
223-624 |
9.20e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.37 E-value: 9.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 223 ELSNLRLENQLLRNEVQSLNQEMASLLQRSKETQEELNKARARVEKWNADHSKSDRMTRgLRAQVDDLTEAvaakdsqLA 302
Cdd:PRK03918 239 EIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIK-LSEFYEEYLDE-------LR 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 303 VLKVRLQEADQLLSTRTEALEALQSEKSRIMQDQSEGNSLQNQaLQTFQERlHEADATLKREQESYKQMQSEFAAR-LNK 381
Cdd:PRK03918 311 EIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKR-LEELEER-HELYEEAKAKKEELERLKKRLTGLtPEK 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 382 VEMERQNLAEAITLAERKYSDEKKRVDELQQQVKLYKLNL------------------ESSKQELI-DYKQKATRILQSK 442
Cdd:PRK03918 389 LEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIeelkkakgkcpvcgreltEEHRKELLeEYTAELKRIEKEL 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 443 EKLINSLKEgsgfegldsstaSSMELEELRHEKEMQREEI--QKLMGQIHQLRSELQDMEAQQVNEAESAREQLQDLHDQ 520
Cdd:PRK03918 469 KEIEEKERK------------LRKELRELEKVLKKESELIklKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIK 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 521 IAGQKAS-------KQELETELERLKQEFHYIEEDLYRTKNTLQSR----IKDRDEEIQKLRnQLTNKTLS-NSSQSELE 588
Cdd:PRK03918 537 LKGEIKSlkkelekLEELKKKLAELEKKLDELEEELAELLKELEELgfesVEELEERLKELE-PFYNEYLElKDAEKELE 615
|
410 420 430
....*....|....*....|....*....|....*....
gi 767982138 589 ---NRLHQLTETLIQKQTMLESLSTEKNSLVFQLERLEQ 624
Cdd:PRK03918 616 reeKELKKLEEELDKAFEELAETEKRLEELRKELEELEK 654
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
377-551 |
9.77e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 50.31 E-value: 9.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 377 ARLNKVEMERQNLAEAITLAERKYSDEKKRVDELQQQVKlyKLNLESSKQELiDYKQKATRILQSKEKL--INSLKEgsg 454
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELE--DLEKEIKRLEL-EIEEVEARIKKYEEQLgnVRNNKE--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 455 FEGLdsstasSMELEELRHEKEMQREEIQKLMGQIHQLRSELQDMEAQQVNEAESAREQLQDLHDQIAGQKASKQELETE 534
Cdd:COG1579 91 YEAL------QKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
170
....*....|....*..
gi 767982138 535 LERLKQEfhyIEEDLYR 551
Cdd:COG1579 165 REELAAK---IPPELLA 178
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
223-613 |
2.19e-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: 51.17 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 223 ELSNLRLENQLLRNEVQSLNQEMASLLQRSKETQEELNKARARVEKWNADHSKSDRMTRGLRAQVDDLTEAVAAKDSQLA 302
Cdd:TIGR04523 219 QISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEIS 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 303 VLKV-------------------RLQEADQLLSTRTEALEALQSEKSRIMQDQSEGNSlQNQALQTFQERLHEADATLKR 363
Cdd:TIGR04523 299 DLNNqkeqdwnkelkselknqekKLEEIQNQISQNNKIISQLNEQISQLKKELTNSES-ENSEKQRELEEKQNEIEKLKK 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 364 EQESYKQmqsefaarlnkvemERQNLAEAITLAERKYSDEKKRVDELQQQVKLYKLNLESSKQELIDYKQkaTRILQSKE 443
Cdd:TIGR04523 378 ENQSYKQ--------------EIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKE--TIIKNNSE 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 444 klINSLKEgsgfegldSSTASSMELEELRHEKEMQREEIQKLMGQIHQLRSELQDMEAQQV----------NEAESAREQ 513
Cdd:TIGR04523 442 --IKDLTN--------QDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKskekelkklnEEKKELEEK 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 514 LQDLHDQIAGQKASKQELETELERLKQEFHYIEEDLYR-----TKNTLQSRIKDRDEEIQKLRNqltNKTLSNSSQSELE 588
Cdd:TIGR04523 512 VKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKddfelKKENLEKEIDEKNKEIEELKQ---TQKSLKKKQEEKQ 588
|
410 420
....*....|....*....|....*...
gi 767982138 589 NRLHQLTE---TLIQKQTMLESLSTEKN 613
Cdd:TIGR04523 589 ELIDQKEKekkDLIKEIEEKEKKISSLE 616
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
223-430 |
2.49e-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: 50.84 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 223 ELSNLRLENQLLRNEVQSLNQEMASLLQRSKETQEELNKARARVEKWNADHSKSDRMTRGLRAQVDDLTEAVAAKDSQLA 302
Cdd:TIGR02169 820 KLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLR 899
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 303 VLKVRLQEADqllstrtealEALQSEKSRImqdqsegnSLQNQALQTFQERLHEADATLKREQESykqmqSEFAARLNKV 382
Cdd:TIGR02169 900 ELERKIEELE----------AQIEKKRKRL--------SELKAKLEALEEELSEIEDPKGEDEEI-----PEEELSLEDV 956
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 767982138 383 EMERQNLAEAIT-------LAERKYSDEKKRVDELQQqvKLYKLNLESSK-QELID 430
Cdd:TIGR02169 957 QAELQRVEEEIRalepvnmLAIQEYEEVLKRLDELKE--KRAKLEEERKAiLERIE 1010
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
303-539 |
3.08e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 50.40 E-value: 3.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 303 VLKVRLQEADQLLSTRTEALEALQsEKSRIMQD-QSEGNSLQNQALQTFQERLHEadatLKREQESYKQMQSEFAARLNK 381
Cdd:PHA02562 171 LNKDKIRELNQQIQTLDMKIDHIQ-QQIKTYNKnIEEQRKKNGENIARKQNKYDE----LVEEAKTIKAEIEELTDELLN 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 382 VEMERQNLAEAITLAERKYSDEKKRVDELQQQVKLYKLN---------LESSKQELIDYKQKATRILQSKEKLINSLKEG 452
Cdd:PHA02562 246 LVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKGgvcptctqqISEGPDRITKIKDKLKELQHSLEKLDTAIDEL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 453 SgfEGLDSSTASSMELEELRHEKEMQREEIQKLMGQIHQLRSELQDMEAQQVNEAESA---REQLQDLHDQIAGQKASKQ 529
Cdd:PHA02562 326 E--EIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELaklQDELDKIVKTKSELVKEKY 403
|
250
....*....|
gi 767982138 530 ELETELERLK 539
Cdd:PHA02562 404 HRGIVTDLLK 413
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
467-625 |
3.20e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.76 E-value: 3.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 467 ELEELRHEKEMQREEIQKLMGQIHQLRSELQDMEAQqvneAESAREQLQDLHDQIAGQKASKQELETELERLKQEFHYIE 546
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERR----IAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 547 EDL----------------------------YRTKNTLQSRIKDRDEEIQKLRNQLTNKTLSNSSQSELENRLHQLTETL 598
Cdd:COG4942 104 EELaellralyrlgrqpplalllspedfldaVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL 183
|
170 180
....*....|....*....|....*..
gi 767982138 599 IQKQTMLESLSTEKNSLVFQLERLEQQ 625
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAE 210
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
223-624 |
5.72e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.65 E-value: 5.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 223 ELSNLRLENQLLRNEVQSLNQEMASLLQRSKETQEELNKARARVEKWNADhsksdrmTRGLRAQVDDLTEAVAAKDSQLA 302
Cdd:PRK02224 294 ERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEE-------AESLREDADDLEERAEELREEAA 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 303 VLKVRLQEADQLLSTRTEALEALQSEksrimqdqsegnslqnqaLQTFQERLHEADATLKREQESYKQMQSEFAA---RL 379
Cdd:PRK02224 367 ELESELEEAREAVEDRREEIEELEEE------------------IEELRERFGDAPVDLGNAEDFLEELREERDElreRE 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 380 NKVEMERQNLAEAITLAER--------------KYSDEKKRVDELQQQVKLYKLNLESSKQELIDYKQKATRI--LQSKE 443
Cdd:PRK02224 429 AELEATLRTARERVEEAEAlleagkcpecgqpvEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAedLVEAE 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 444 KLINSLKEgsgfegldsstassmeleelrhekemQREEIQKLmgqIHQLRSELQDMEAQqvneAESAREQLQDLHDQIAG 523
Cdd:PRK02224 509 DRIERLEE--------------------------RREDLEEL---IAERRETIEEKRER----AEELRERAAELEAEAEE 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 524 QKASKQELETELERLKQEFHYIEEDLYRTKNTLQS--RIKDRDEEIQKLRNQLtnktlsnssqSELENRLHQLTETLIQK 601
Cdd:PRK02224 556 KREAAAEAEEEAEEAREEVAELNSKLAELKERIESleRIRTLLAAIADAEDEI----------ERLREKREALAELNDER 625
|
410 420
....*....|....*....|....*
gi 767982138 602 QTMLESLSTEKNSLV--FQLERLEQ 624
Cdd:PRK02224 626 RERLAEKRERKRELEaeFDEARIEE 650
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
220-435 |
6.74e-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: 48.99 E-value: 6.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 220 KSHELSNLRLENQLLRNEVQSLNQEMASLLQRSKETQEELNKARARVEKWNADHSKsdrmtrgLRAQVDDLTEAVAAkds 299
Cdd:COG4942 39 LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE-------LRAELEAQKEELAE--- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 300 QLAVL-KVRLQEADQLLSTRTEALEALQSekSRIMQDQSEGNSLQNQALQTFQERLHEADATLKREQESYKQMQSEFAAR 378
Cdd:COG4942 109 LLRALyRLGRQPPLALLLSPEDFLDAVRR--LQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEE 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 767982138 379 LNKVEMERQNLAEAITLAERKYSDEKKRVDELQQQVKLYKLNLESSKQELIDYKQKA 435
Cdd:COG4942 187 RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
218-413 |
7.82e-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: 49.28 E-value: 7.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 218 DGKSHELSNLRLENQLLRNEVQSLNQEMASLLQRSKETQEELNKARARVEKWNADHSKSDRMTRGLRAQVDDLTEAVAAK 297
Cdd:TIGR02168 806 DELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASL 885
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 298 DSQLAVLKVRLQEADqllstrtEALEALQSEKSRIMQDQSEgnslQNQALQTFQERLHEADATLKREQ----ESYKQMQS 373
Cdd:TIGR02168 886 EEALALLRSELEELS-------EELRELESKRSELRRELEE----LREKLAQLELRLEGLEVRIDNLQerlsEEYSLTLE 954
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767982138 374 EFAARLNKVEMERQNLAEAITLAERK--------------YSDEKKRVDELQQQ 413
Cdd:TIGR02168 955 EAEALENKIEDDEEEARRRLKRLENKikelgpvnlaaieeYEELKERYDFLTAQ 1008
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
397-624 |
7.95e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.24 E-value: 7.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 397 ERKYSDEKKRVDELQQQVKLYKLNLESSKQELIDYKQKaTRILQSKEKLINSLKEgsgfegLDSSTASSMELEELRHEKE 476
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQK-NGLVDLSEEAKLLLQQ------LSELESQLAEARAELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 477 MQREEIQKLMGQ-------------IHQLRSELQDMEAQQvneaESAREQLQDLHDQIAGQKASKQELETELERLKQEfh 543
Cdd:COG3206 240 ARLAALRAQLGSgpdalpellqspvIQQLRAQLAELEAEL----AELSARYTPNHPDVIALRAQIAALRAQLQQEAQR-- 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 544 yIEEDLYRTKNTLQSRIKDRDEEIQKLRNQLtnktlsnSSQSELENRLHQLTETLIQKQTMLESLsteknslvfqLERLE 623
Cdd:COG3206 314 -ILASLEAELEALQAREASLQAQLAQLEARL-------AELPELEAELRRLEREVEVARELYESL----------LQRLE 375
|
.
gi 767982138 624 Q 624
Cdd:COG3206 376 E 376
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
168-469 |
8.27e-06 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 49.13 E-value: 8.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 168 IKTIEENSFGSQTHEAASNSDSSHEGQEESSKENVSSNAACPDHTPTPNDDGKSHELSNLRLENQLLRNEVQSLNQEMAS 247
Cdd:PLN02939 172 INILEMRLSETDARIKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 248 LlqrsKETQEelnkaraRVEKWNADHSKSDRMTRGLRAQVDDLTEAVaakdSQLAVLKVrlqeadQLLSTRTEALEALqs 327
Cdd:PLN02939 252 V----AETEE-------RVFKLEKERSLLDASLRELESKFIVAQEDV----SKLSPLQY------DCWWEKVENLQDL-- 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 328 eksrimqdqsegnslqnqaLQTFQERLHEADATLKREQESYKqmqsefaarlnKVEMERQNLAEAITlaeRKYSDEKkrV 407
Cdd:PLN02939 309 -------------------LDRATNQVEKAALVLDQNQDLRD-----------KVDKLEASLKEANV---SKFSSYK--V 353
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767982138 408 DELQQQVKLYKLNLESSKQELIDYKQKATRILQSKEKLINSLKEGSGFEGLDSStASSMELE 469
Cdd:PLN02939 354 ELLQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQDTLSKLKEESKKRSLEHP-ADDMPSE 414
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
223-420 |
1.09e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.86 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 223 ELSNLRLENQLLrnevqSLNQEMASLLQRSKETQEELNKARARVEKWNADHSKSDRMTRGLRAQVDDLTE--AVAAKDSQ 300
Cdd:COG3206 197 ALEEFRQKNGLV-----DLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQspVIQQLRAQ 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 301 LAVLKVRLQEADQLLSTRTEALEALQSEKSRIMQDQSEGNSLQNQALQTFQERLHEADATLKREQESYKQMqsefAARLN 380
Cdd:COG3206 272 LAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEAR----LAELP 347
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 767982138 381 KVEMERQNLAEAITLAERKYSDEKKRVDELQQQVKLYKLN 420
Cdd:COG3206 348 ELEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGN 387
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
284-538 |
1.24e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 48.66 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 284 RAQVDDLTEAVAAKDSQLAVL-------KVRLQEADQLLSTRTEALEALQSEKS------RIMQDQSEGNSLQNQALQTF 350
Cdd:pfam10174 323 KQHIEVLKESLTAKEQRAAILqtevdalRLRLEEKESFLNKKTKQLQDLTEEKStlageiRDLKDMLDVKERKINVLQKK 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 351 QERLHEAdatlKREQEsyKQMqSEFAARLNKVEMERQNLAEAITLAERKYSDEKKRVDELQQQVKL----YKLNLESSKQ 426
Cdd:pfam10174 403 IENLQEQ----LRDKD--KQL-AGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQRERedreRLEELESLKK 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 427 ELIDYKQKAT---RILQSKEKLINSLKEGSgfegldSSTASSM-----ELEELRHEKEMQREEIQKLMGQIHQlrselqd 498
Cdd:pfam10174 476 ENKDLKEKVSalqPELTEKESSLIDLKEHA------SSLASSGlkkdsKLKSLEIAVEQKKEECSKLENQLKK------- 542
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 767982138 499 meAQQVNEAESARE----QLQDLHDQIAGQKASKQELETELERL 538
Cdd:pfam10174 543 --AHNAEEAVRTNPeindRIRLLEQEVARYKEESGKAQAEVERL 584
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
220-621 |
1.32e-05 |
|
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: 48.48 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 220 KSHELSNLRLENQLLRNEVQSLNQEMASLLQRSKETQEELNKAR---ARVEKWNADHSKSDRMTRGLRAQVDDLTEAVAA 296
Cdd:TIGR04523 150 KEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKnklLKLELLLSNLKKKIQKNKSLESQISELKKQNNQ 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 297 KDSQLAVLKVRLQEADQLLSTRTEALEALQSEKSRIMQDQSEGNSLQNQALQTFQErLHEADATLKREQESYKQMQSEfa 376
Cdd:TIGR04523 230 LKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKE-LEKQLNQLKSEISDLNNQKEQ-- 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 377 ARLNKVEMERQNLAEAITLAERKYSDEKKRVDELQQQVKlyklNLESSKQELIDYKQKATRILQSKEKLINSLKEGSGfE 456
Cdd:TIGR04523 307 DWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQIS----QLKKELTNSESENSEKQRELEEKQNEIEKLKKENQ-S 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 457 GLDSSTASSMELEELRHEKEMQREEIQKLMGQIHQLRSELQDMEAQQVN---EAESAREQLQDLHDQIAGQKASKQELET 533
Cdd:TIGR04523 382 YKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERlkeTIIKNNSEIKDLTNQDSVKELIIKNLDN 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 534 ELERLKQEFHYIEEDLYRTKNTLQSRIKDRDEEIQKLrNQLTNKTlsnssqSELENRLHQLTE---TLIQKQTMLESLST 610
Cdd:TIGR04523 462 TRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKEL-KKLNEEK------KELEEKVKDLTKkisSLKEKIEKLESEKK 534
|
410
....*....|.
gi 767982138 611 EKNSLVFQLER 621
Cdd:TIGR04523 535 EKESKISDLED 545
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
283-517 |
1.42e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.47 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 283 LRAQVDDLTEAVAAKDSQLAVLKVRLQEADQllstrteALEALQsEKSRIMQDQSEGNSLQNQaLQTFQERLHEADATLK 362
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEA-------ALEEFR-QKNGLVDLSEEAKLLLQQ-LSELESQLAEARAELA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 363 REQESYKQMQSEFAARLNKVEM-----ERQNLAEAITLAERKYSDEKKRVDELQQQVKLYKLNLESSKQELidyKQKATR 437
Cdd:COG3206 237 EAEARLAALRAQLGSGPDALPEllqspVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQL---QQEAQR 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 438 ILQSKEKLINSLKEgsgfegldsstassmELEELRHEKEMQREEIQKLMgqihQLRSELQDMEaqqvNEAESAREQLQDL 517
Cdd:COG3206 314 ILASLEAELEALQA---------------REASLQAQLAQLEARLAELP----ELEAELRRLE----REVEVARELYESL 370
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
253-625 |
2.19e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.21 E-value: 2.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 253 KETQEELNKARARVEKWNADHSKSDRMTRGLRAQVD-DLTEAVAAKDSQLAVLKVRLQEADQLLSTRTEALEALQSEKSR 331
Cdd:PTZ00121 1384 KKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKaDEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAK 1463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 332 IMQDQSEgnslQNQALQTFQERLHEADATLKREQESYKQmqsefAARLNKVEMERQNLAEAITLAERKYSDEKKRVDELQ 411
Cdd:PTZ00121 1464 KKAEEAK----KADEAKKKAEEAKKADEAKKKAEEAKKK-----ADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAK 1534
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 412 QQVKLYKLNLESSKQELidYKQKATRILQSKEKLINSLKEGSGFEGLDSSTASSMELEELRHEKEMQREEIQKLMGQIHQ 491
Cdd:PTZ00121 1535 KADEAKKAEEKKKADEL--KKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEA 1612
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 492 LRSELQDMEAQQVNEAESAREQLQDLHDQIAGQKASKQELETELE----RLKQEFHYIEEDlyrtkntlqsriKDRDEEI 567
Cdd:PTZ00121 1613 KKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEenkiKAAEEAKKAEED------------KKKAEEA 1680
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 767982138 568 QKLRNQLTNKTLSNSSQSELENRLHQLTETLIQKQTMLESLSTEKNSLVFQLERLEQQ 625
Cdd:PTZ00121 1681 KKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKE 1738
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
360-625 |
2.38e-05 |
|
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: 47.71 E-value: 2.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 360 TLKREQESYKQMQSEFAARLNKVEMERQNLAEAITLAERKYSDEKKRVDELQQQVKLYKLNLESSKQELIDYKQKATR-- 437
Cdd:TIGR04523 121 KLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKle 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 438 ----ILQSKEKLINSL-KEGSGFEGLDSSTASSmeLEELRHEKEMQREEIQKLMGQIHQLRSELQDMEAQ---QVNEAES 509
Cdd:TIGR04523 201 lllsNLKKKIQKNKSLeSQISELKKQNNQLKDN--IEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQlseKQKELEQ 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 510 AREQLQDLHDQIagqkaskQELETELERLKQEfhyIEEDLyrtKNTLQSRIKDRDEEIQKLRNQLTNktlSNSSQSELEN 589
Cdd:TIGR04523 279 NNKKIKELEKQL-------NQLKSEISDLNNQ---KEQDW---NKELKSELKNQEKKLEEIQNQISQ---NNKIISQLNE 342
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 767982138 590 RLHQL--------------TETLIQKQTMLESLSTEKNSLVFQLERLEQQ 625
Cdd:TIGR04523 343 QISQLkkeltnsesensekQRELEEKQNEIEKLKKENQSYKQEIKNLESQ 392
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
223-580 |
2.43e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 223 ELSNLRLENQLLRNEVQSLNQEMASLLQRSKETQ---EELNKARARVEKWNADHSKSDR--MTRGLRAQVDDLTEAVAAK 297
Cdd:PRK03918 392 ELEELEKAKEEIEEEISKITARIGELKKEIKELKkaiEELKKAKGKCPVCGRELTEEHRkeLLEEYTAELKRIEKELKEI 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 298 DSQLAVLKVRLQEADQLLS---------TRTEALEALQSEKSRIMQDQSEGNSLQNQALQTFQERLHEADATLKREQESY 368
Cdd:PRK03918 472 EEKERKLRKELRELEKVLKkeseliklkELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKL 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 369 KQMQSEFAARLNKVEMERQNLAEAIT-LAERKYSDEKKRVDELQQQVKLYK--LNLESSKQELidykqkatrilQSKEKL 445
Cdd:PRK03918 552 EELKKKLAELEKKLDELEEELAELLKeLEELGFESVEELEERLKELEPFYNeyLELKDAEKEL-----------EREEKE 620
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 446 INSLKEgsgfegldsstassmELEELRHEKEMQREEIQKLMGQIHQLRSELQDMEAQQV-NEAESAREQLQDLHDQIAGQ 524
Cdd:PRK03918 621 LKKLEE---------------ELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELrEEYLELSRELAGLRAELEEL 685
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 767982138 525 KASKQELETELERLKQEFHYIEEDLYRTK--NTLQSRIKDRDEEIQKLRNQLTNKTLS 580
Cdd:PRK03918 686 EKRREEIKKTLEKLKEELEEREKAKKELEklEKALERVEELREKVKKYKALLKERALS 743
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
239-449 |
2.49e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.70 E-value: 2.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 239 QSLNQEMASLLQRSKETQEELNKARARVEKWNADHS--KSDRMTRGLRAQVDDLTEAVAAKDSQLAVLKVRLQEADQLLS 316
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 317 TRTEALEALQSEKSRIMQDQSEGNSLQNqaLQTFQERLHEADATLKREQESYKQMQSEFAARLNKVEMERQNLAEAItla 396
Cdd:COG3206 244 ALRAQLGSGPDALPELLQSPVIQQLRAQ--LAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASL--- 318
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 767982138 397 ERKYSDEKKRVDELQQQVKLYKLNLESSKQELIDYKQkATRILQSKEKLINSL 449
Cdd:COG3206 319 EAELEALQAREASLQAQLAQLEARLAELPELEAELRR-LEREVEVARELYESL 370
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
232-612 |
2.66e-05 |
|
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: 47.20 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 232 QLLRNEVQSLNQEMASLLQRSKETQEELNKARarvEKWNADHSKSDRMTRGLRAQVDDLTEAVAAKDSQLAVLKVRLQEA 311
Cdd:pfam07888 30 ELLQNRLEECLQERAELLQAQEAANRQREKEK---ERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 312 DQLLSTRTEALEALQSEKS----RIMQDQSEGNSLQNQA------LQTFQERLHEADATLKREQESYKQMQSEfaarLNK 381
Cdd:pfam07888 107 SASSEELSEEKDALLAQRAaheaRIRELEEDIKTLTQRVlereteLERMKERAKKAGAQRKEEEAERKQLQAK----LQQ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 382 VEMERQNLAEAITLAERKYSDEKKRVDELQQQVKLYKLNLESSKQELIDYKQKATRILQSKEKLINSLKEGSGFEGLDSS 461
Cdd:pfam07888 183 TEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSS 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 462 TASSMEleelRHEKEMQREEIQ--KLMGQIHQLRSELQDMEAQQVNEAESAREQLQDLHDQIAGQKASKQELETELERLK 539
Cdd:pfam07888 263 MAAQRD----RTQAELHQARLQaaQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEER 338
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767982138 540 QEFHYIEEDLYRTKNTLQSRIKDRDEEIQKLRNQLtnktlsNSSQSELENRLHQLTETLI---QKQTMLESLSTEK 612
Cdd:pfam07888 339 MEREKLEVELGREKDCNRVQLSESRRELQELKASL------RVAQKEKEQLQAEKQELLEyirQLEQRLETVADAK 408
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
332-615 |
3.14e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 47.43 E-value: 3.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 332 IMQDQSEGNSLQNQAL--QTFQERLHEADATLKREQESYKQM-------------QSEFAARLNKVEMERQNLAEAITLA 396
Cdd:pfam17380 277 IVQHQKAVSERQQQEKfeKMEQERLRQEKEEKAREVERRRKLeeaekarqaemdrQAAIYAEQERMAMERERELERIRQE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 397 ERKYSDEKKRVDELQQQV----KLYKLNLE-SSKQELIDYKQKATRilqsKEKLINSLKEGSGFEGLDSSTASSMELEEL 471
Cdd:pfam17380 357 ERKRELERIRQEEIAMEIsrmrELERLQMErQQKNERVRQELEAAR----KVKILEEERQRKIQQQKVEMEQIRAEQEEA 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 472 RhEKEMQR--EEIQKLMGQIHQLRSELQ-DMEAQQVNEAESAREQLQDLHDQIAGQKASKQE---LETELERLKQEFhyI 545
Cdd:pfam17380 433 R-QREVRRleEERAREMERVRLEEQERQqQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRrkiLEKELEERKQAM--I 509
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767982138 546 EEDlyRTKNTLQSRIKDRDEEI-QKLRNQLTNKTLSNSSQSELENRLHQLTETLIQKQTMLESLSTEKNSL 615
Cdd:pfam17380 510 EEE--RKRKLLEKEMEERQKAIyEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMM 578
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
343-625 |
4.42e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.87 E-value: 4.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 343 QNQALQTFQERLHEADATLKREQESYKQMQSEFAarlnkvemerqNLAEAITLAERK---YSDEKKRVDELQQQVKLYKL 419
Cdd:PRK04863 367 QNEVVEEADEQQEENEARAEAAEEEVDELKSQLA-----------DYQQALDVQQTRaiqYQQAVQALERAKQLCGLPDL 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 420 NLESSKQELIDYKQKA----TRILQSKEKLINSLKEGSGFE-----------GLDSSTASSMELEELRhekemQREEIQK 484
Cdd:PRK04863 436 TADNAEDWLEEFQAKEqeatEELLSLEQKLSVAQAAHSQFEqayqlvrkiagEVSRSEAWDVARELLR-----RLREQRH 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 485 LMGQIHQLRSELQDMEaQQVNEAESAREQLQDLHDQIAGQKASKQELETELERLKQEFHYIEEDLyRTKNTLQSRIKDRD 564
Cdd:PRK04863 511 LAEQLQQLRMRLSELE-QRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESV-SEARERRMALRQQL 588
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767982138 565 EEIQKLRNQLTNK------------TLSNSSQSELENRlHQLTETLIQKQTMLESLSTEKNSLVFQLERLEQQ 625
Cdd:PRK04863 589 EQLQARIQRLAARapawlaaqdalaRLREQSGEEFEDS-QDVTEYMQQLLERERELTVERDELAARKQALDEE 660
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
233-451 |
4.65e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.30 E-value: 4.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 233 LLRNEVQSLNQEMASLLQRSKETQEELNKARARVEKWNADHSKSDRMTRGLRAQVDDLTEAVAAKDSQLAVLKVRLQEAD 312
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 313 QLLSTRTEALEALQSEKSRIMQDQSEGNSLQNQALQTFQERLHEADATLKREQESYKQMQS---EFAARLNKVEMERQNL 389
Cdd:COG4942 90 KEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREqaeELRADLAELAALRAEL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767982138 390 AEAITLAERKYSDEKKRVDELQQQVKLYKLNLESSKQELIDYKQKATRILQSKEKLINSLKE 451
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
237-409 |
4.88e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.30 E-value: 4.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 237 EVQSLNQEMASLLQRSKETQEELNKARARVEKWNADHSKsdrmtrgLRAQVDDLTEAVAAKDSQLAVLKVRLQEA-DQLL 315
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEA-------AKTELEDLEKEIKRLELEIEEVEARIKKYeEQLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 316 STRTE-ALEALQSEksriMQDQSEGNSLQNQALQTFQERLHEADATLKREQESYKQMQSEFAARLNKVEMERQNLAEAIT 394
Cdd:COG1579 84 NVRNNkEYEALQKE----IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELE 159
|
170
....*....|....*
gi 767982138 395 LAERKYSDEKKRVDE 409
Cdd:COG1579 160 ELEAEREELAAKIPP 174
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
239-495 |
5.26e-05 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 46.22 E-value: 5.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 239 QSLNQEMASLLQRSKETQEELNKARARVEKWNADHsksDRmtrgLRAQVDDLTEA--VAAKDSQLAVLKVRLQEADQLLS 316
Cdd:COG0497 154 EELLEEYREAYRAWRALKKELEELRADEAERAREL---DL----LRFQLEELEAAalQPGEEEELEEERRRLSNAEKLRE 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 317 TRTEALEALqseksrimqDQSEGNSLQ--NQALQTFqERLHEADATLK----REQESYKQMQ---SEFAARLNKVEMERQ 387
Cdd:COG0497 227 ALQEALEAL---------SGGEGGALDllGQALRAL-ERLAEYDPSLAelaeRLESALIELEeaaSELRRYLDSLEFDPE 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 388 NLAEAITlaerkysdekkRVDELQQQVKLYKLNLEsskqELIDYKQKAtrilqsKEKLinslkegsgfEGLDSSTAssmE 467
Cdd:COG0497 297 RLEEVEE-----------RLALLRRLARKYGVTVE----ELLAYAEEL------RAEL----------AELENSDE---R 342
|
250 260
....*....|....*....|....*...
gi 767982138 468 LEELRHEKEMQREEIQKLMGQIHQLRSE 495
Cdd:COG0497 343 LEELEAELAEAEAELLEAAEKLSAARKK 370
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
479-575 |
6.61e-05 |
|
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.
Pssm-ID: 463295 [Multi-domain] Cd Length: 151 Bit Score: 43.46 E-value: 6.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 479 REEIQKLMGQIHQLRSELQdmeaQQVNEAESAREQLQDLHDQIAGQKASKQELETELERLKQEFHYIEEDLYRTKNTLQS 558
Cdd:pfam11559 51 LEFRESLNETIRTLEAEIE----RLQSKIERLKTQLEDLERELALLQAKERQLEKKLKTLEQKLKNEKEELQRLKNALQQ 126
|
90 100
....*....|....*....|....
gi 767982138 559 R-------IKDRDEEIQKLRNQLT 575
Cdd:pfam11559 127 IktqfaheVKKRDREIEKLKERLA 150
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
376-602 |
7.02e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.53 E-value: 7.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 376 AARLNKVEMERQNLAEAITLAERKYSDEKKRVDELQQQVKLYKLNLESSKQELIDYKQKatriLQSKEKLINSLKEgsgf 455
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQE----LAALEAELAELEK---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 456 egldsstassmELEELRHEKEMQREEIQKLMGQIHQLRSELQDM---EAQQVNEAESAREQLQDLH----DQIAGQKASK 528
Cdd:COG4942 91 -----------EIAELRAELEAQKEELAELLRALYRLGRQPPLAlllSPEDFLDAVRRLQYLKYLAparrEQAEELRADL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767982138 529 QELET---ELERLKQEFHYIEEDLYRTKNTLQSRIKDRDEEIQKLRNQLTNKTLSNSSQSELENRLHQLTETLIQKQ 602
Cdd:COG4942 160 AELAAlraELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
329-584 |
7.66e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.78 E-value: 7.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 329 KSRIMQDQSEGNSLQNQaLQTFQERLheadATLKREQESYKQMQSEFAARLNKVEMERQNLAEAItlaerkysdeKKRVD 408
Cdd:PHA02562 173 KDKIRELNQQIQTLDMK-IDHIQQQI----KTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTI----------KAEIE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 409 ELQQQVKLYKLNLESSKQELIDYKQKATRIlQSKEKLINslKEGSGFEGLDSSTASSMELEElrhekemQREEIQKLMGQ 488
Cdd:PHA02562 238 ELTDELLNLVMDIEDPSAALNKLNTAAAKI-KSKIEQFQ--KVIKMYEKGGVCPTCTQQISE-------GPDRITKIKDK 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 489 IHQLrselqdmeAQQVNEAESAREQLQDLHDQIAGQKASKQELETELERLKQEFHYIEEDLYRTK---NTLQSRIKDRDE 565
Cdd:PHA02562 308 LKEL--------QHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKaaiEELQAEFVDNAE 379
|
250 260
....*....|....*....|.
gi 767982138 566 EIQKLRNQL--TNKTLSNSSQ 584
Cdd:PHA02562 380 ELAKLQDELdkIVKTKSELVK 400
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
223-495 |
1.46e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.44 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 223 ELSNLRLENQLLRNEVQSLNQEMASLLQRSKETQEELNKARARVEKWNADHSKS-----DRMTRGLRAQVDDLTEAVAAK 297
Cdd:TIGR02169 738 RLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSripeiQAELSKLEEEVSRIEARLREI 817
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 298 DSQLAVLKVRLQEADQLLSTRTEALEALQSEKSRIMQDQSEGNsLQNQALQTFQERLHEADATLKREQESYKQMQSEFAA 377
Cdd:TIGR02169 818 EQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLN-GKKEELEEELEELEAALRDLESRLGDLKKERDELEA 896
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 378 RLNKVEMERQNLAEAITLAERKYSDEKKRVDELQQQVKLYKLNLESSKQE------LIDYKQKATRILQSKEKL--INSL 449
Cdd:TIGR02169 897 QLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIpeeelsLEDVQAELQRVEEEIRALepVNML 976
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 767982138 450 KEgsgfEGLDSSTASSMELEELRHEKEMQREEIQKLMGQIHQLRSE 495
Cdd:TIGR02169 977 AI----QEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKRE 1018
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
223-570 |
1.50e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.31 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 223 ELSNLRLENQLLRNEVQSLNQEMASLLQRSKETQEELNKARARVEKWNADHSKSDRMTRGLRAQVDDLTEAVAAKDSQLA 302
Cdd:COG1196 387 ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 303 VLKVRLQEADQLLSTRTEALEALQSEKSRI--MQDQSEGNS--------------------------------LQNQALQ 348
Cdd:COG1196 467 ELLEEAALLEAALAELLEELAEAAARLLLLleAEADYEGFLegvkaalllaglrglagavavligveaayeaaLEAALAA 546
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 349 TFQERLHEADATLKREQESYKQMQSEFAARLNKVEMERQNLAEAITL------------AERKYSDEKKRVDELQQQVKL 416
Cdd:COG1196 547 ALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALArgaigaavdlvaSDLREADARYYVLGDTLLGRT 626
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 417 YKLNLESSKQELIDYKQKATRILQSKEKLINSLKEGSGFEGLDSSTASSMELEELRHEKEMQREEIQKLMGQIHQLRSEL 496
Cdd:COG1196 627 LVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEE 706
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767982138 497 QDMEAQQVNEAESAREQLQDLHDQIAGQKASKQELETELERLKQEFHYIEEDLYRTKnTLQSRIKDRDEEIQKL 570
Cdd:COG1196 707 RELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLE-ELERELERLEREIEAL 779
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
223-570 |
1.69e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.93 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 223 ELSNLRLENQLLRNEVQSLNQEMASLLQRSKETQEELNKARARVEKWNADHSKSDRMTRGLRAQVDDLTEAVAAKDSQLA 302
Cdd:COG1196 415 RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 303 VLKVRLQEADQLL-STRTEALEALQSEKSRIMQDQSEGNSLQNQALQTF-----QERLHEADATLKREQESYKQMQSEFA 376
Cdd:COG1196 495 LLLEAEADYEGFLeGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAAlaaalQNIVVEDDEVAAAAIEYLKAAKAGRA 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 377 ARLNKVEMERQNLAEAITL------------AERKYSDEKKRVDELQQQVKLYKLNLESSKQELIDYKQKATRILQSKEK 444
Cdd:COG1196 575 TFLPLDKIRARAALAAALArgaigaavdlvaSDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGE 654
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 445 LINSLKEGSGFEGLDSSTASSMELEELR-------------HEKEMQREEIQKLMGQIHQLRSELQDMEAQQVNEAESAR 511
Cdd:COG1196 655 GGSAGGSLTGGSRRELLAALLEAEAELEelaerlaeeelelEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAER 734
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 512 EQLQDLHDQIAGQ-----------KASKQELETELERLKQ--------------EFHYIEE----------DLYRTKNTL 556
Cdd:COG1196 735 EELLEELLEEEELleeealeelpePPDLEELERELERLEReiealgpvnllaieEYEELEErydflseqreDLEEARETL 814
|
410
....*....|....
gi 767982138 557 QSRIKDRDEEIQKL 570
Cdd:COG1196 815 EEAIEEIDRETRER 828
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
459-625 |
2.29e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.75 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 459 DSSTASSMELEELRHEKEMQREEIQKLMGQIHQLRSELQDMEAQQvneaESAREQLQDLHDQIAGQKASKQELETELERL 538
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKR----DELNAQVKELREEAQELREKRDELNEKVKEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 539 KQEfhyieedlyrtKNTLQSRIKDRDEEIQKLRNQLTNKTLSNSSQSELENRLHQLTETLiqkQTmlESLSTEK-NSLVF 617
Cdd:COG1340 77 KEE-----------RDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQ---QT--EVLSPEEeKELVE 140
|
....*...
gi 767982138 618 QLERLEQQ 625
Cdd:COG1340 141 KIKELEKE 148
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
223-469 |
3.57e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 3.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 223 ELSNLRLENQLLRNEVQSLNQEMASLLQRSKETQEELNKARARVEKwnadhsksdrmtrgLRAQVDDLTEAVAAKDSQLA 302
Cdd:COG3883 24 ELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDK--------------LQAEIAEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 303 VLKVRLQEADQLLSTRTEALEAlqseksrimqdQSEGNSLQN-QALQTFQERLHEADATLKREQESYKQMQSEFAARLNK 381
Cdd:COG3883 90 ERARALYRSGGSVSYLDVLLGS-----------ESFSDFLDRlSALSKIADADADLLEELKADKAELEAKKAELEAKLAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 382 VEMERQNLAEAITLAERKYSDEKKRVDELQQQVKLYKLNLESSKQELIDYKQKATRILQSKEKLINSLKEGSGFEGLDSS 461
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238
|
....*...
gi 767982138 462 TASSMELE 469
Cdd:COG3883 239 AAAAAASA 246
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
321-577 |
3.61e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 43.89 E-value: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 321 ALEALQSEKSRIMQD--QSEGNSLQNQ-----ALQTFQERLHEADATLKREQEsYKQMQSEFAaRLNKvEMERQNLAEAi 393
Cdd:PRK10929 17 AYAATAPDEKQITQEleQAKAAKTPAQaeiveALQSALNWLEERKGSLERAKQ-YQQVIDNFP-KLSA-ELRQQLNNER- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 394 tlAERKYSDEKKRVDELQQQVklyklnLESSKQELIDYKQkatrilqskeklinslkegsgfegldsstassmeleeLRH 473
Cdd:PRK10929 93 --DEPRSVPPNMSTDALEQEI------LQVSSQLLEKSRQ-------------------------------------AQQ 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 474 EKEMQREeIQKLMGQIHQLRSELQdmeaQQVNEAES------------AREQLQDLHDQIAGQKASKQELEteLERL--- 538
Cdd:PRK10929 128 EQDRARE-ISDSLSQLPQQQTEAR----RQLNEIERrlqtlgtpntplAQAQLTALQAESAALKALVDELE--LAQLsan 200
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 767982138 539 -KQEFHYIEEDLYrtkntlQSRIKDRDEEIQKLRNQLTNK 577
Cdd:PRK10929 201 nRQELARLRSELA------KKRSQQLDAYLQALRNQLNSQ 234
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
344-541 |
4.17e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.47 E-value: 4.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 344 NQALQTFQERlheadaTLKREQESYKQMQSEFAARLNKVemeRQNLAEAitlaERKYSD--EKKRVDELQQQVKLYKLNL 421
Cdd:COG3206 155 NALAEAYLEQ------NLELRREEARKALEFLEEQLPEL---RKELEEA----EAALEEfrQKNGLVDLSEEAKLLLQQL 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 422 ESSKQELIDYKQKATRILQSKEKLINSLKEGSGFEGLDSSTASSMELEELRHEKEMQREE-----------IQKLMGQIH 490
Cdd:COG3206 222 SELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAElsarytpnhpdVIALRAQIA 301
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 767982138 491 QLRSELQDMEAQQV----NEAESAREQLQDLHDQIAGQKASKQEL---ETELERLKQE 541
Cdd:COG3206 302 ALRAQLQQEAQRILasleAELEALQAREASLQAQLAQLEARLAELpelEAELRRLERE 359
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
244-583 |
5.28e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 5.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 244 EMASLLQRSKETQEELNKARARVEKWNADHSKSDRMTRGLRA-QVDDLTEAVAAKDSQLAVLKVRLQEADQLlstrTEAL 322
Cdd:PTZ00121 1480 EEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAkKADEAKKAEEAKKADEAKKAEEKKKADEL----KKAE 1555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 323 EALQSEKSRIMQDQSEGNSLQNQALQTFQERLHEADATLKREQESYKQMQSEFAARLNKVEMERQNLAEAitlaeRKYSD 402
Cdd:PTZ00121 1556 ELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEEL-----KKAEE 1630
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 403 EKKRVDELQQQVKLYKLNLESSKQELIDYKQKATRILQSKEKLINSLKEGSGFEGLDSSTASSMELEElrhEKEMQREEI 482
Cdd:PTZ00121 1631 EKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEA---EEAKKAEEL 1707
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 483 QKLMGQIHQLRSELQDMEAQQVNEAESAREQLQDLHDQIAGQKASKQELETELERLKQEFHYIEEDLYRTKNTLQSRIKD 562
Cdd:PTZ00121 1708 KKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDE 1787
|
330 340
....*....|....*....|.
gi 767982138 563 RDEEIQKLRNQLTNKTLSNSS 583
Cdd:PTZ00121 1788 EDEKRRMEVDKKIKDIFDNFA 1808
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
232-519 |
6.20e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.18 E-value: 6.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 232 QLLRNEVQSLNQ-------EMASLLQRSKETQEELNKARARVEKWNADHSKSDRMTRGLRAQVDDL----TEAVAAKDSQ 300
Cdd:pfam15921 565 EILRQQIENMTQlvgqhgrTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLelekVKLVNAGSER 644
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 301 LAVLKVRLQEADQLLstrtealealqsekSRIMQDQSEGNSLQNQ---ALQTFQERLHEADATLKREQESYKQMQSEFAA 377
Cdd:pfam15921 645 LRAVKDIKQERDQLL--------------NEVKTSRNELNSLSEDyevLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQ 710
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 378 RLNKVEMERQNLAEAITLA---ERKYSDEKKRVDELQQQVKLYKLNLESSKQELIDYKQKATRILQSKEKLINSLKEGSG 454
Cdd:pfam15921 711 TRNTLKSMEGSDGHAMKVAmgmQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAG 790
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767982138 455 fegldsstassmELEELRHEKEMQREEIQKLmgQIHQLRSELQDMEAQ---QVNEAESAREQLQDLHD 519
Cdd:pfam15921 791 ------------ELEVLRSQERRLKEKVANM--EVALDKASLQFAECQdiiQRQEQESVRLKLQHTLD 844
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
411-573 |
7.33e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.83 E-value: 7.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 411 QQQVKLYKL-NLESSKQELIDYKQKATRILQSKEKLINSLKegsgfeglDSSTASSMELEELRHEKEMQREEIQKLMGQI 489
Cdd:COG1579 4 EDLRALLDLqELDSELDRLEHRLKELPAELAELEDELAALE--------ARLEAAKTELEDLEKEIKRLELEIEEVEARI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 490 HQLRSELQ------DMEAQQvNEAESAREQLQDLHDQIAGQKASKQELETELERLKQEFHYIEEDLYRTKNTLQSRIKDR 563
Cdd:COG1579 76 KKYEEQLGnvrnnkEYEALQ-KEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAEL 154
|
170
....*....|
gi 767982138 564 DEEIQKLRNQ 573
Cdd:COG1579 155 EAELEELEAE 164
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
404-616 |
7.41e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.69 E-value: 7.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 404 KKRVDELQQQVKLYKLNLESSKQELIDYKqkatrilqskeKLINSLKEGSGfegldsstassmeleELRHEKEMQREEIQ 483
Cdd:PHA02562 173 KDKIRELNQQIQTLDMKIDHIQQQIKTYN-----------KNIEEQRKKNG---------------ENIARKQNKYDELV 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 484 KLMGQIHQLRSELQDMEAQQVNEAESAREQLQDLHDQIAGQKAskqeletELERLKQEFHYIEEDlyRTKNTLQSRIKDR 563
Cdd:PHA02562 227 EEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKS-------KIEQFQKVIKMYEKG--GVCPTCTQQISEG 297
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 767982138 564 DEEIQKLRNQLTNKTLS----NSSQSELENRLHQLTETLIQKQTMLESLSTEKNSLV 616
Cdd:PHA02562 298 PDRITKIKDKLKELQHSleklDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLI 354
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
223-622 |
7.43e-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: 7.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 223 ELSNLRLENQLLRNEVQSLNQEMASLLQRSKETQEELNKARARVEKWNADHSKSDRMTRGLRAQVDDLTEAVAAKDSQLA 302
Cdd:pfam01576 518 QLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVS 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 303 VLKVRLQEADQLLSTRTEALEALQSEKSRIMQDQSEGNSLQ---NQALQTFQERLHEADATLKREQESYKQ-MQSEFAAR 378
Cdd:pfam01576 598 NLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRAlslARALEEALEAKEELERTNKQLRAEMEDlVSSKDDVG 677
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 379 LNKVEMERQNLAeaitlAERKYSDEKKRVDELQ---QQVKLYKLNLESSKQELidyKQKATRILQSKEKlinslkegsgf 455
Cdd:pfam01576 678 KNVHELERSKRA-----LEQQVEEMKTQLEELEdelQATEDAKLRLEVNMQAL---KAQFERDLQARDE----------- 738
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 456 EGLDSSTASSMELEELRHEKEMQREEIQKLMGQIHQLRSELQDMEAQqVNEAESARE-----------QLQDLHDQIAGQ 524
Cdd:pfam01576 739 QGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQ-IDAANKGREeavkqlkklqaQMKDLQRELEEA 817
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 525 KASKQEL-------ETELERLKQEFHYIEEDLYRTKNTLQSRIKDRDEEIQKLRNQLTNKTLSNSSQSELENRLHQLTET 597
Cdd:pfam01576 818 RASRDEIlaqskesEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEE 897
|
410 420
....*....|....*....|....*
gi 767982138 598 LIQKQTMLESLSTEKNSLVFQLERL 622
Cdd:pfam01576 898 LEEEQSNTELLNDRLRKSTLQVEQL 922
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
512-624 |
7.95e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.98 E-value: 7.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 512 EQLQDLHDQIAGQKASKQELETELERLKQefhyIE------EDLYRTKNTLQSRIKDRDEEIQKLRNQL---TNKTLSNS 582
Cdd:PRK11281 46 DALNKQKLLEAEDKLVQQDLEQTLALLDK----IDrqkeetEQLKQQLAQAPAKLRQAQAELEALKDDNdeeTRETLSTL 121
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 767982138 583 SQSELENRlhqLTETLIQKQTMLESLSTEKNSLVFQLERLEQ 624
Cdd:PRK11281 122 SLRQLESR---LAQTLDQLQNAQNDLAEYNSQLVSLQTQPER 160
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
462-605 |
9.02e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.76 E-value: 9.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 462 TASSMeleeLRHEKEMQREEIQKLMGQIHQLRSELQDMEAQQvneAESAREQLQDLHDQIAgqkaskqELETELERLKQE 541
Cdd:COG0542 397 EAAAR----VRMEIDSKPEELDELERRLEQLEIEKEALKKEQ---DEASFERLAELRDELA-------ELEEELEALKAR 462
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767982138 542 FHyiEEdlyrtkntlqsriKDRDEEIQKLRNQLTNKtlsNSSQSELENRLHQLTETLIQKQTML 605
Cdd:COG0542 463 WE--AE-------------KELIEEIQELKEELEQR---YGKIPELEKELAELEEELAELAPLL 508
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
235-615 |
9.13e-04 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 42.53 E-value: 9.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 235 RNEVQSLNQEMASLLQRSkeTQEELNKARA---------RVEKWNADHsksDRMTRGLRAQVDDLTEAVAAKDSQLAVLK 305
Cdd:pfam06160 9 YKEIDELEERKNELMNLP--VQEELSKVKKlnltgetqeKFEEWRKKW---DDIVTKSLPDIEELLFEAEELNDKYRFKK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 306 VR--LQEADQLLSTRTEALEALQSEKSRIMqDQSEGNSLQNQALQtfqERLHEADATLKREQESYKQMQSEFAARLNKVE 383
Cdd:pfam06160 84 AKkaLDEIEELLDDIEEDIKQILEELDELL-ESEEKNREEVEELK---DKYRELRKTLLANRFSYGPAIDELEKQLAEIE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 384 merQNLAEAITLAER-KYSDEKKRVDELQQQVKlyklNLESSKQELIDYKQKATRILQSKeklINSLKEGsgfegLDSST 462
Cdd:pfam06160 160 ---EEFSQFEELTESgDYLEAREVLEKLEEETD----ALEELMEDIPPLYEELKTELPDQ---LEELKEG-----YREME 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 463 ASSMELEELRHEKEMQ--REEIQKLMGQIHQLRSElqdmEAQQVNEAESAR-EQLQD------------------LHDQI 521
Cdd:pfam06160 225 EEGYALEHLNVDKEIQqlEEQLEENLALLENLELD----EAEEALEEIEERiDQLYDllekevdakkyveknlpeIEDYL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 522 AGQKASKQELETELERLKQEFHYIEEDLYRTKNtLQSRIKDRDEEIQKLRNQLTNKTlsnSSQSELENRLHQLTETLIQK 601
Cdd:pfam06160 301 EHAEEQNKELKEELERVQQSYTLNENELERVRG-LEKQLEELEKRYDEIVERLEEKE---VAYSELQEELEEILEQLEEI 376
|
410
....*....|....
gi 767982138 602 QTMLESLSTEKNSL 615
Cdd:pfam06160 377 EEEQEEFKESLQSL 390
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
312-624 |
9.26e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.80 E-value: 9.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 312 DQLLSTRTEaLEALQSEKSRIMQDQSEGNSLQNQALQTFQERLHEADATL-KREQESYKQMQSEFaarlNKVEMERQNLA 390
Cdd:pfam15921 145 NQLQNTVHE-LEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILvDFEEASGKKIYEHD----SMSTMHFRSLG 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 391 EAITLAERKYSDE----KKRVDELQQQVKLYKLNLESSKQELIDYKQ-KATRILQSKEKLINSLKE-GSGFEGLDSSTAS 464
Cdd:pfam15921 220 SAISKILRELDTEisylKGRIFPVEDQLEALKSESQNKIELLLQQHQdRIEQLISEHEVEITGLTEkASSARSQANSIQS 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 465 SMEL--EELRHEKEMQREEIQKLMGQIHQLRSELQDMEAQQVNEAESAREQLQDLHDQIAGQKASKQELETELERLKQEF 542
Cdd:pfam15921 300 QLEIiqEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQL 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 543 HYIEEDLYRTKNTL------QSRIKDRDE----EIQKLRNQLTNKTLS--------NSSQSELENRLHQLTETLIQKQTM 604
Cdd:pfam15921 380 QKLLADLHKREKELslekeqNKRLWDRDTgnsiTIDHLRRELDDRNMEvqrleallKAMKSECQGQMERQMAAIQGKNES 459
|
330 340
....*....|....*....|
gi 767982138 605 LESLSteknSLVFQLERLEQ 624
Cdd:pfam15921 460 LEKVS----SLTAQLESTKE 475
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
277-620 |
1.01e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.50 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 277 DRMTRGLRAQVDDLTEAVAAKDSQLAVLKVRLQEADQLLSTRTEALEALQ---SEKSRIMQDQSEGNSLQNQALQTFQER 353
Cdd:pfam10174 393 ERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEealSEKERIIERLKEQREREDRERLEELES 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 354 LHEADATLKREQESYKQMQSEFAARLNKVEMERQNLAEAITLAERKYSD-----EKKRVDELQQQVKLYK---------- 418
Cdd:pfam10174 473 LKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSleiavEQKKEECSKLENQLKKahnaeeavrt 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 419 -----LNLESSKQELIDYKQKATRILQSKEKLINSLKEGSGFEGLDSSTASSMELEELRHEKEMQREEIQKLMGQihqlr 493
Cdd:pfam10174 553 npeinDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQ----- 627
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 494 selQDMEAQQVNEAESAREQLQDLHDQIAGQKASkqELETELERLKQEFHYIEEDLYRTKNTLQSrikdRDEEIQKLRNQ 573
Cdd:pfam10174 628 ---QEMKKKGAQLLEEARRREDNLADNSQQLQLE--ELMGALEKTRQELDATKARLSSTQQSLAE----KDGHLTNLRAE 698
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 767982138 574 ltnktlsnssqselenRLHQLTETLIQKQTMLESLSTEKNSLVFQLE 620
Cdd:pfam10174 699 ----------------RRKQLEEILEMKQEALLAAISEKDANIALLE 729
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
234-625 |
1.02e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.47 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 234 LRNEVQSLNQEMASLLQRSKETQEELNKARARVEkwnADHSKSDRMTRGLRAQVDDLTEAVAAKDSQLAVLKVRLQEADQ 313
Cdd:pfam01576 181 LKNKHEAMISDLEERLKKEEKGRQELEKAKRKLE---GESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETA 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 314 LLSTRTEALEALQSEKSRIMQDQSEGNSLQNQALQT---FQERLHEADATLKREQESYKQMQSEFAARLNKVEMERQNLA 390
Cdd:pfam01576 258 QKNNALKKIRELEAQISELQEDLESERAARNKAEKQrrdLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 391 EAITLAERKYSDEKKR----VDELQQQV---KLYKLNLESSKQELidykQKATRILQSKEKLINSLKEGSGfEGLDSSTA 463
Cdd:pfam01576 338 EETRSHEAQLQEMRQKhtqaLEELTEQLeqaKRNKANLEKAKQAL----ESENAELQAELRTLQQAKQDSE-HKRKKLEG 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 464 SSMELEELRHEKEMQREEIQKlmgQIHQLRSELQDMEAqQVNEAESAREQLQDLHDQIAGQKASKQELETELERLKQEFH 543
Cdd:pfam01576 413 QLQELQARLSESERQRAELAE---KLSKLQSELESVSS-LLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLS 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 544 YIEEDLYRTKNTLQSRIKDRDEEIQKLRNQLTNktlSNSSQSELENRLHQLTETLIQKQTMLESLSTEKNSLVFQLERLE 623
Cdd:pfam01576 489 TRLRQLEDERNSLQEQLEEEEEAKRNVERQLST---LQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKA 565
|
..
gi 767982138 624 QQ 625
Cdd:pfam01576 566 AA 567
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
308-625 |
1.04e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 42.65 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 308 LQEADQLLSTRTEaLEALQSEKSRIMQDQSEGNSLQNQALQTFQERLHEADATLKREQESYKQMQSEFAARLNKveMERQ 387
Cdd:TIGR00618 183 LMEFAKKKSLHGK-AELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQ--LKKQ 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 388 NLAEAITLAERKYSDEKKRVDELQQQVKL--YKLNLESSKQELIDYKQKATRILQSKEKLINSLKegSGFEGLDSSTASS 465
Cdd:TIGR00618 260 QLLKQLRARIEELRAQEAVLEETQERINRarKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRA--KLLMKRAAHVKQQ 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 466 MELEELRH-EKEMQREEIqkLMGQIHQLRSELQDMEAQQVNEAESAREQLQDLHDQIAGQKASKQELETE------LERL 538
Cdd:TIGR00618 338 SSIEEQRRlLQTLHSQEI--HIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILqreqatIDTR 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 539 KQEFHYIEEDLYRTKNTLQSRIKDRDEEIQKLRNQLTNKTLSNSSQSELENRLHQLTETLIQKQTMLESLSTEKNSLVFQ 618
Cdd:TIGR00618 416 TSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLAR 495
|
....*..
gi 767982138 619 LERLEQQ 625
Cdd:TIGR00618 496 LLELQEE 502
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
278-615 |
1.20e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 278 RMTRGLRAQVDDLTEAVAAKDSqlAVLKVRLQEADQLLSTRTEALEALQSEKsrimqdqsegnslqnqalQTFQERLHEA 357
Cdd:PRK02224 180 RVLSDQRGSLDQLKAQIEEKEE--KDLHERLNGLESELAELDEEIERYEEQR------------------EQARETRDEA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 358 DATLkreqESYKQMQSEfaarLNKVEMERQNLAEAITLAERKYSDEKKRVDELQQQVklykLNLESSkqelidykqkatr 437
Cdd:PRK02224 240 DEVL----EEHEERREE----LETLEAEIEDLRETIAETEREREELAEEVRDLRERL----EELEEE------------- 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 438 ilqskeklINSLKEGSGFEGLDSSTASSmELEELRHEKEMQREEIQklmgqihQLRSELQDMEaqqvNEAESAREQLQDL 517
Cdd:PRK02224 295 --------RDDLLAEAGLDDADAEAVEA-RREELEDRDEELRDRLE-------ECRVAAQAHN----EEAESLREDADDL 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 518 hdqiagqkaskqelETELERLKQEFHYIEEDLYRTKNTL---QSRIKDRDEEIQKLRNQLTNktlSNSSQSELENRLHQL 594
Cdd:PRK02224 355 --------------EERAEELREEAAELESELEEAREAVedrREEIEELEEEIEELRERFGD---APVDLGNAEDFLEEL 417
|
330 340
....*....|....*....|....*
gi 767982138 595 TET---LIQKQTMLE-SLSTEKNSL 615
Cdd:PRK02224 418 REErdeLREREAELEaTLRTARERV 442
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
376-608 |
1.42e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 376 AARLNKVEMERQNLAEAITLAERKYSDEKKRVDELQQQVKLYKlNLESSKQELIDYKQKATRILQSKEKLinslkegsgf 455
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQ-RLAEYSWDEIDVASAEREIAELEAEL---------- 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 456 EGLDsstASSMELEELRHekemqreeiqklmgQIHQLRSELQDmeaqqvneaesAREQLQDLHDQIAGQKASKQELETEL 535
Cdd:COG4913 678 ERLD---ASSDDLAALEE--------------QLEELEAELEE-----------LEEELDELKGEIGRLEKELEQAEEEL 729
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767982138 536 ERLKQEFHYIEEDlyrtkntlqsRIKDRDEEIQKLRNQLTNKTLSNSSQSELENRLHQLTETLIQKQTMLESL 608
Cdd:COG4913 730 DELQDRLEAAEDL----------ARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERA 792
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
247-576 |
1.45e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 41.81 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 247 SLLQRSKETQEELNKARAR-VEKWNADHSKSDRMTRGLRAQVDDltEAVAAKDSQLAvlkvRLQEADQLLSTRTEAL-EA 324
Cdd:PLN02939 63 SKLQSNTDENGQLENTSLRtVMELPQKSTSSDDDHNRASMQRDE--AIAAIDNEQQT----NSKDGEQLSDFQLEDLvGM 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 325 LQS-EKSRIMQDQSEGNSLQN--------QALQ----TFQERLHEADATLKREQesykqmQSEFAARLNKVEME--RQNL 389
Cdd:PLN02939 137 IQNaEKNILLLNQARLQALEDlekiltekEALQgkinILEMRLSETDARIKLAA------QEKIHVEILEEQLEklRNEL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 390 AEAITLAERKYSDEKKRVDELQQQVKLYKLNLESSKQELIDYKQKATRILQ-SKEK--LINSLKEgsgfegLDSSTASSM 466
Cdd:PLN02939 211 LIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAETEERVFKlEKERslLDASLRE------LESKFIVAQ 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 467 E----LEELRHEKEMQR-EEIQKLMgqihqlrselqDMEAQQVNEAESAREQLQDLHDQIAGQKASKQELET------EL 535
Cdd:PLN02939 285 EdvskLSPLQYDCWWEKvENLQDLL-----------DRATNQVEKAALVLDQNQDLRDKVDKLEASLKEANVskfssyKV 353
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 767982138 536 ERLKQEFHYIEEDLYRTKNTLQSRIKDRDEEIQKLRNQLTN 576
Cdd:PLN02939 354 ELLQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQDTLSK 394
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
478-625 |
1.55e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 478 QREEIQKLMGQIHQLRSELQDMEAQQVNEAESAREQLQDLHDQIAGQKASKQELETELERLKQEFHYIEE-----DLYRT 552
Cdd:COG4717 54 EADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKllqllPLYQE 133
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767982138 553 KNTLQSRIKDRDEEIQKLRNQLTNKTLSNSSQSELENRLHQLTETLIQKQTMLeSLSTEK--NSLVFQLERLEQQ 625
Cdd:COG4717 134 LEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQL-SLATEEelQDLAEELEELQQR 207
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
439-622 |
1.75e-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: 41.16 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 439 LQSKE-------KLINSLKEG--SGFEGLDSSTASSM-ELEELRHEKEMQREEIQKLMGQIHQLRSELQDMEAQQVNEAE 508
Cdd:smart00787 128 LEAKKmwyewrmKLLEGLKEGldENLEGLKEDYKLLMkELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELD 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 509 SAREQLQDLHDQIAGQKASKQELETELERLKQEfhyIEEdlyrtKNTLQSRIKDRDEEIQKLRNQltNKTLSNSSQSELE 588
Cdd:smart00787 208 RAKEKLKKLLQEIMIKVKKLEELEEELQELESK---IED-----LTNKKSELNTEIAEAEKKLEQ--CRGFTFKEIEKLK 277
|
170 180 190
....*....|....*....|....*....|....
gi 767982138 589 NRLHQLtetliQKQTMLESLSTEKNSLVFQLERL 622
Cdd:smart00787 278 EQLKLL-----QSLTGWKITKLSGNTLSMTYDRE 306
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
366-623 |
2.82e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.77 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 366 ESYKQMQSEFAARLNKVEMERQNLAEAITLAERKYSDEKKRVDELQQQVKLYKLNLESSKQELIDYKQ---KATRILQSK 442
Cdd:TIGR04523 207 KKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKeleQNNKKIKEL 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 443 EKLINSLK------EGSGFEGLDSSTASSME-----LEELRHEKEMQREEIQKLMGQIHQLRSELQDMEAQQV---NEAE 508
Cdd:TIGR04523 287 EKQLNQLKseisdlNNQKEQDWNKELKSELKnqekkLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSekqRELE 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 509 SAREQLQDLHDQIAGQKASKQELETELERLKQEFHYIEEDlyrtKNTLQSRIKDRDEEIQKLRNQLTN-KTLSNSSQSEL 587
Cdd:TIGR04523 367 EKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKL----NQQKDEQIKKLQQEKELLEKEIERlKETIIKNNSEI 442
|
250 260 270
....*....|....*....|....*....|....*.
gi 767982138 588 ENrlhqLTETLIQKQTMLESLSTEKNSLVFQLERLE 623
Cdd:TIGR04523 443 KD----LTNQDSVKELIIKNLDNTRESLETQLKVLS 474
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
284-568 |
3.04e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 284 RAQVDDLTEAVAAKDSQLAVLKVRLQEADQLLSTRTEALEALQSEKSRIMQDQSegnslqnqaLQTFQERLHEADATLKR 363
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEID---------VASAEREIAELEAELER 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 364 EQESYKQMQsEFAARLNKVEMERQNLAEAITLAERKYSDEKKRVDELQQQVKLYKLNLESskqelIDYKQKATRILQSKE 443
Cdd:COG4913 680 LDASSDDLA-ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA-----AEDLARLELRALLEE 753
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 444 KLINSLKEGSGFEGLDSSTASSMELEELRHEKEmqrEEIQKLMGQIHQL-RSELQDMEAqqvnEAESAREqLQDLHDQIA 522
Cdd:COG4913 754 RFAAALGDAVERELRENLEERIDALRARLNRAE---EELERAMRAFNREwPAETADLDA----DLESLPE-YLALLDRLE 825
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 767982138 523 gqkaskqelETELERLKQEF-HYIEEDLYRTKNTLQSRIKDRDEEIQ 568
Cdd:COG4913 826 ---------EDGLPEYEERFkELLNENSIEFVADLLSKLRRAIREIK 863
|
|
| pepcterm_ChnLen |
TIGR03007 |
polysaccharide chain length determinant protein, PEP-CTERM locus subfamily; Members of this ... |
398-608 |
3.13e-03 |
|
polysaccharide chain length determinant protein, PEP-CTERM locus subfamily; Members of this protein family belong to the family of polysaccharide chain length determinant proteins (pfam02706). All are found in species that encode the PEP-CTERM/exosortase system predicted to act in protein sorting in a number of Gram-negative bacteria, and are found near the epsH homolog that is the putative exosortase gene. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
Pssm-ID: 274386 [Multi-domain] Cd Length: 498 Bit Score: 40.80 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 398 RKYSDEKKRVdeLQQQVKLYKLNLESSKQELIDYKQKATRILQskeklinslkegsgfeglDSSTASSMELEELRHEKEM 477
Cdd:TIGR03007 156 RQDSDSAQRF--IDEQIKTYEKKLEAAENRLKAFKQENGGILP------------------DQEGDYYSEISEAQEELEA 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 478 QREEIQKLMGQIHQLRSELQDMEAQQVNEAESA----REQLQDLHDQIAGQKASKQELETELERLKQEFHYIEEDL---Y 550
Cdd:TIGR03007 216 ARLELNEAIAQRDALKRQLGGEEPVLLAGSSVAnselDGRIEALEKQLDALRLRYTDKHPDVIATKREIAQLEEQKeeeG 295
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 767982138 551 RTKNTLQSRIKDRDEEIQKLRNQLTNKTLSNSSqseLENRLHQLTETLIQKQTMLESL 608
Cdd:TIGR03007 296 SAKNGGPERGEIANPVYQQLQIELAEAEAEIAS---LEARVAELTARIERLESLLRTI 350
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
222-541 |
3.42e-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: 40.65 E-value: 3.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 222 HELSNLRLENQLLRNEVQSLNQEMASLLQRSKETQ---EELNKARARVEKWNADHSKSdrmTRGLRAQVDDLTEAVAAKD 298
Cdd:pfam07888 73 RQRRELESRVAELKEELRQSREKHEELEEKYKELSassEELSEEKDALLAQRAAHEAR---IRELEEDIKTLTQRVLERE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 299 SQLAVLKvrlQEADQLLSTRTEALEALQSEKSRIMQDQSEGNSLqNQALQTFQERLHEADATLKREQESYKQMQSEFAAR 378
Cdd:pfam07888 150 TELERMK---ERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSL-SKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTA 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 379 LNKVEMERQNLAEAITLAERKYSDEKKrVDELQQQVKLYKLNLESSKQELIDYKQKATRILQSKEKLINSLKEGSG-FEG 457
Cdd:pfam07888 226 HRKEAENEALLEELRSLQERLNASERK-VEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRArWAQ 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 458 LDSSTASSMELEELRHEKemQREEIQKLMGQIHQLRSELQDMEAQQVNEAESAREQLQDLHDQIAGQKASKQELETELER 537
Cdd:pfam07888 305 ERETLQQSAEADKDRIEK--LSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQ 382
|
....
gi 767982138 538 LKQE 541
Cdd:pfam07888 383 LQAE 386
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
359-616 |
3.93e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 40.49 E-value: 3.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 359 ATLKREQESYKQMQSEFAARLNKVEMERQNLAEAITLAERKYSDEKKRVDELQQQVKLYKLNL---ESSKQELIDYKQKA 435
Cdd:pfam05557 2 AELIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREaeaEEALREQAELNRLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 436 TRILQSKEKLINSlKEGSGFEGLDSSTASSMELEELRHEKEMQREEIQKLMGQIHQLRSELqDMEAQQVNEAESAREQLQ 515
Cdd:pfam05557 82 KKYLEALNKKLNE-KESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERL-DLLKAKASEAEQLRQNLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 516 DLHDQIAGQKASKQELETEL---ERLKQEFHYIEEDLYRTKnTLQSRIKDRDEEIQKLRNQLTNKTLSNSSQSELENRLH 592
Cdd:pfam05557 160 KQQSSLAEAEQRIKELEFEIqsqEQDSEIVKNSKSELARIP-ELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLE 238
|
250 260
....*....|....*....|....*..
gi 767982138 593 QL---TETLIQKQTMLESLSTEKNSLV 616
Cdd:pfam05557 239 REekyREEAATLELEKEKLEQELQSWV 265
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
345-623 |
4.61e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.42 E-value: 4.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 345 QALQTFQERLHEADATLKreqesYKQMQSEFAARLNKVEMERQNLAEAITLAERKYSDEKKRVDELQQQVKLYKLNLESS 424
Cdd:TIGR00606 193 QVRQTQGQKVQEHQMELK-----YLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKL 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 425 KQELIDYKQKATRILQSKEKLinSLKEGSGFEGLDSstassmELEELRH-------EKEMQREEIQKLMGQIHQLRSELQ 497
Cdd:TIGR00606 268 DNEIKALKSRKKQMEKDNSEL--ELKMEKVFQGTDE------QLNDLYHnhqrtvrEKERELVDCQRELEKLNKERRLLN 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 498 DMEAQQVNEAESAREQLQDLHDQIAGQKASKQELETELERLKQEFH-YIEEDLYRTKNTLQSRIKDRDEEIQKLRNQLTN 576
Cdd:TIGR00606 340 QEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGpFSERQIKNFHTLVIERQEDEAKTAAQLCADLQS 419
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 767982138 577 K-TLSNSSQSELENRLHQLTETLIQKQTMLESLSTEKNSLVFQLERLE 623
Cdd:TIGR00606 420 KeRLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLE 467
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
356-613 |
5.51e-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: 40.42 E-value: 5.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 356 EADATLK---REQESYKQMQSEFAARLNKV-EMERQNlaeaiTLAERKySDEKKRVDELQQQVKLYKLNLESSKQELIDY 431
Cdd:TIGR01612 1501 EADKNAKaieKNKELFEQYKKDVTELLNKYsALAIKN-----KFAKTK-KDSEIIIKEIKDAHKKFILEAEKSEQKIKEI 1574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 432 KQKATRILQSKEKLINSLKEGSGFE-GLDSSTASSMELEELRHEKEMQREEIQKLMGQIHQLRSELQDMEaqqVNEAESA 510
Cdd:TIGR01612 1575 KKEKFRIEDDAAKNDKSNKAAIDIQlSLENFENKFLKISDIKKKINDCLKETESIEKKISSFSIDSQDTE---LKENGDN 1651
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 511 REQLQDLHDQIAGQKASKQELETELERLKQEFHYIEEDLYRTKNTLQSRIKDRDEEIQKlrnqlTNKTLSNSSQSELENR 590
Cdd:TIGR01612 1652 LNSLQEFLESLKDQKKNIEDKKKELDELDSEIEKIEIDVDQHKKNYEIGIIEKIKEIAI-----ANKEEIESIKELIEPT 1726
|
250 260 270
....*....|....*....|....*....|
gi 767982138 591 LHQLTETL-------IQKQTMLESLSTEKN 613
Cdd:TIGR01612 1727 IENLISSFntndlegIDPNEKLEEYNTEIG 1756
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
522-625 |
5.52e-03 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 38.37 E-value: 5.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 522 AGQKASKQELETELERLKQEfhyiEEDLYRTKNTLQSRIKDRDEEIQKLRNQLTNKTLSNSSQ----SELENRLHQLTET 597
Cdd:pfam08614 46 SPQSASIQSLEQLLAQLREE----LAELYRSRGELAQRLVDLNEELQELEKKLREDERRLAALeaerAQLEEKLKDREEE 121
|
90 100
....*....|....*....|....*...
gi 767982138 598 LIQKQTMLESLSTEKNSLVFQLERLEQQ 625
Cdd:pfam08614 122 LREKRKLNQDLQDELVALQLQLNMAEEK 149
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
284-625 |
6.53e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.03 E-value: 6.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 284 RAQVDDLTEAVAAKDSQLAVLKVRLQEADQLLSTRTEALEALQSEKSRIMQDQSEGNSLQNQALQTFQ---ERLHEADAT 360
Cdd:TIGR00606 230 EAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQgtdEQLNDLYHN 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 361 LKREQESYKQMQSEFAARLNKVEMERQNLAEAITLAERKYSDEKKRVDELQQQVKLYKLNLESSKQEL-IDYKQKATRIL 439
Cdd:TIGR00606 310 HQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLeLDGFERGPFSE 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 440 QSKEKLINSLKEGSGFEG--LDSSTASSMELEELRHEKEMQREEIQKLMGQIHQLRSELQDMEAQQVNEAESAREQLQDL 517
Cdd:TIGR00606 390 RQIKNFHTLVIERQEDEAktAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGS 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 518 HDQI---------AGQKASKQELETELERLKQEFHYIEE---DLYRTKNTLQSRIK--------------------DRDE 565
Cdd:TIGR00606 470 SDRIleldqelrkAERELSKAEKNSLTETLKKEVKSLQNekaDLDRKLRKLDQEMEqlnhhtttrtqmemltkdkmDKDE 549
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767982138 566 EIQKLRNQ-----------LTNKTLSNSSQSELENRLHQLTETLIQKQTMLESLSTEKNSLVFQLERLEQQ 625
Cdd:TIGR00606 550 QIRKIKSRhsdeltsllgyFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQ 620
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
471-574 |
6.82e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 39.18 E-value: 6.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 471 LRHEKEMQREEIQKLMGQIHQL-------RSELQDMEAQ------QVNEAESAREQLQDLHDQIAGQKASKQELETELER 537
Cdd:PRK09039 44 LSREISGKDSALDRLNSQIAELadllsleRQGNQDLQDSvanlraSLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQ 123
|
90 100 110
....*....|....*....|....*....|....*...
gi 767982138 538 -LKQEFHYIEEDLyrtkntlqSRIKDRDEEIQKLRNQL 574
Cdd:PRK09039 124 eLDSEKQVSARAL--------AQVELLNQQIAALRRQL 153
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
221-551 |
6.96e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 39.95 E-value: 6.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 221 SHELSNLRLENQLLRNEVQSLNQEMASLLQRSKETQEELNKARARVEKWNADHSKSDRMTRGLRAQVDDLTEaVAAKDSQ 300
Cdd:TIGR00618 583 KEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLT-LTQERVR 661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 301 LAVLKVRLQEAdQLLSTRTEALEALQSEKSRIMQDQSEgnslqnqaLQTFQERLHEADATLKREQESYKQMQSEFAARLN 380
Cdd:TIGR00618 662 EHALSIRVLPK-ELLASRQLALQKMQSEKEQLTYWKEM--------LAQCQTLLRELETHIEEYDREFNEIENASSSLGS 732
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 381 KVEMERQNLAEAITLAERKYSDEKKRVDELQQQVKLYKLNLESSKQELIDYKQKATRILQSKEKLINSLKEgsgfegldS 460
Cdd:TIGR00618 733 DLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKT--------L 804
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 461 STASSMELEELRHEKEMQREEIQKLMGQIHQLRSELQDMEAQQVNEAESAREQLQDLhDQIAGQKASKQELETELERLKQ 540
Cdd:TIGR00618 805 EAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQL-AQLTQEQAKIIQLSDKLNGINQ 883
|
330
....*....|.
gi 767982138 541 EFHYIEEDLYR 551
Cdd:TIGR00618 884 IKIQFDGDALI 894
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
289-615 |
7.15e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 39.89 E-value: 7.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 289 DLTEAVAAKDSQLAVLKVRLQEADQLLSTRTEALEALQSEKSRIMQDQSEGNSL---------QNQALQTFQERLHEADA 359
Cdd:PRK11281 70 ALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETLSTLSLrqlesrlaqTLDQLQNAQNDLAEYNS 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 360 TLKREQESYKQMQSEFAARLNKVEMERQNLAEAitlaerkySDEKKRVDELQQQvklyKLNLESSKQEL-IDYKQKAtri 438
Cdd:PRK11281 150 QLVSLQTQPERAQAALYANSQRLQQIRNLLKGG--------KVGGKALRPSQRV----LLQAEQALLNAqNDLQRKS--- 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 439 LQSKEKLINSLKEgsgfegldsstassmELEELRHEKEMQREEIQKLMGQIHQLR---SELQDMEAQQVNEAESARE--- 512
Cdd:PRK11281 215 LEGNTQLQDLLQK---------------QRDYLTARIQRLEHQLQLLQEAINSKRltlSEKTVQEAQSQDEAARIQAnpl 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 513 ---------QL-QDLHDQI-AGQKASKQELETE--LERLKQEFHYIEED-------------LYRTKNTLQS-------- 558
Cdd:PRK11281 280 vaqeleinlQLsQRLLKATeKLNTLTQQNLRVKnwLDRLTQSERNIKEQisvlkgslllsriLYQQQQALPSadliegla 359
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767982138 559 -RIKD-RDE--EIQKLRNQLTN-----KTLSNSSQSELENRLH-QLTETLIQKQTMLESLSTEKNSL 615
Cdd:PRK11281 360 dRIADlRLEqfEINQQRDALFQpdayiDKLEAGHKSEVTDEVRdALLQLLDERRELLDQLNKQLNNQ 426
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
238-605 |
7.42e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 39.65 E-value: 7.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 238 VQSLNQEM----ASLLQRSKETQEELNKARArvekwnadhsKSDRMTrglraqvddlteavaakdsqlavlkvrlqeadQ 313
Cdd:PRK10929 104 TDALEQEIlqvsSQLLEKSRQAQQEQDRARE----------ISDSLS--------------------------------Q 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 314 LLSTRTEALEALqSEKSRIMQDQSEGNSLQNQAlqtfQERLHEADATLKReqesykqmqsefaARLNKVEME------RQ 387
Cdd:PRK10929 142 LPQQQTEARRQL-NEIERRLQTLGTPNTPLAQA----QLTALQAESAALK-------------ALVDELELAqlsannRQ 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 388 NLAeaitlaeRKYSD-EKKRVDELQQQVKLYKLNLESSKQelidykQKATRILQSKEKlinsLKEGSGfeGLDSSTASSM 466
Cdd:PRK10929 204 ELA-------RLRSElAKKRSQQLDAYLQALRNQLNSQRQ------REAERALESTEL----LAEQSG--DLPKSIVAQF 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 467 EL-EELRHEKEMQREEIQKLMGQIHQLRSELqdmeaQQVNEAESA-REQLQ----------DLHDQIA--GQKASKQELE 532
Cdd:PRK10929 265 KInRELSQALNQQAQRMDLIASQQRQAASQT-----LQVRQALNTlREQSQwlgvsnalgeALRAQVArlPEMPKPQQLD 339
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767982138 533 TELERLK-QEFHYieEDLYRTKNTLQSRIKDRDEEIQKLRNQLTNKTLSNssQSELENRLHQLTETLIQKQTML 605
Cdd:PRK10929 340 TEMAQLRvQRLRY--EDLLNKQPQLRQIRQADGQPLTAEQNRILDAQLRT--QRELLNSLLSGGDTLILELTKL 409
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
467-623 |
8.19e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.66 E-value: 8.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 467 ELEELRHEKEMQREEIQKLMGQIHQLRSELQDMEAQQvNEAESAREQLQDLHDQIAGQKASKQELETELERLKQEFHYIE 546
Cdd:PRK03918 201 ELEEVLREINEISSELPELREELEKLEKEVKELEELK-EEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELE 279
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767982138 547 EDLYRTKntlqsRIKDRDEEIQKLRNQLTNKTLSNSSQSELENRLHQLTETLIQKQTMLESLSTEKNSLVFQLERLE 623
Cdd:PRK03918 280 EKVKELK-----ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELE 351
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
501-600 |
8.30e-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: 38.98 E-value: 8.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 501 AQQVNEAESAREQLQDLHDQIAGQKASKQELETELERLKQEFHYIEEDLyrtkNTLQSRIKDRDEEIQKLRNQLTNKtls 580
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRI----AALARRIRALEQELAALEAELAEL--- 88
|
90 100
....*....|....*....|
gi 767982138 581 NSSQSELENRLHQLTETLIQ 600
Cdd:COG4942 89 EKEIAELRAELEAQKEELAE 108
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
474-679 |
8.70e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.04 E-value: 8.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 474 EKEMQREEIQKLMGQIHQLRSELQDMEAQqvneAESAREQLQDLHDQIAGQKASKQELETELERLKQEFHYIEEDL---- 549
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAE----LEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELgera 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 550 ---YRTKNTLQ---------------------SRIKDRD----EEIQKLRNQLTNKTLSNSS--------QSELENRLHQ 593
Cdd:COG3883 93 ralYRSGGSVSyldvllgsesfsdfldrlsalSKIADADadllEELKADKAELEAKKAELEAklaelealKAELEAAKAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 594 LTETLIQKQTMLESLSTEKNSLVFQLERLEQQMNSASGSSSNGSSINMSGIDNGEGTRLRNVPVLFNDTETNLAGMYGKV 673
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAA 252
|
....*.
gi 767982138 674 RKAASS 679
Cdd:COG3883 253 GAAGAA 258
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
423-591 |
8.79e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.38 E-value: 8.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 423 SSKQELIDYKQKATRILQSKEKlinslkegsgfegldsstassmELEELRHEKEMQREEiqklmgQIHQLRSELQdmeaq 502
Cdd:PRK12704 28 IAEAKIKEAEEEAKRILEEAKK----------------------EAEAIKKEALLEAKE------EIHKLRNEFE----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 503 qvNEAESAREQLQDLHDQIAGQKAS-KQELEtELERLKQEFHYIEEDLYRTKNTLQSRIKDRDEEIQKLRNQLTNktLSN 581
Cdd:PRK12704 75 --KELRERRNELQKLEKRLLQKEENlDRKLE-LLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELER--ISG 149
|
170
....*....|
gi 767982138 582 SSQSELENRL 591
Cdd:PRK12704 150 LTAEEAKEIL 159
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
221-510 |
9.63e-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: 9.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 221 SHELSNLRLENQLLRNEVQSLNQEMASLLQRSKETQEELNKARARVEKWNADHSKSDRMTRGLRAQVDDLTEAVAAKDSQ 300
Cdd:pfam07888 114 SEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKE 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 301 LAVLKVRLQEADQLLSTRTEALEALQSEKSRIMQDQSEGNSLQNQaLQTFQERLHEAD---ATLKREQESYKQMQSEFAA 377
Cdd:pfam07888 194 FQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEE-LRSLQERLNASErkvEGLGEELSSMAAQRDRTQA 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982138 378 RLNKVEMERQN----LAEA-ITLAERKYSDEKKRvDELQQQVKLYKLNLESSKQELidykQKATRILQSKEKLINSLKEG 452
Cdd:pfam07888 273 ELHQARLQAAQltlqLADAsLALREGRARWAQER-ETLQQSAEADKDRIEKLSAEL----QRLEERLQEERMEREKLEVE 347
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767982138 453 SGFE---GLDSSTASSMELEELR-------HEKEMQREEIQKLMGQIHQLRSELQDMEAQQVNEAESA 510
Cdd:pfam07888 348 LGREkdcNRVQLSESRRELQELKaslrvaqKEKEQLQAEKQELLEYIRQLEQRLETVADAKWSEAALT 415
|
|
| |
