|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
450-617 |
9.81e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.26 E-value: 9.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 450 EELARIEAEAMAENVvcAHNELVAQVEKDINASFE--KELLREKEIVDAVEKLAEEAKSELARLRVEKEEETLALERERT 527
Cdd:COG1196 260 AELAELEAELEELRL--ELEELELELEEAQAEEYEllAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 528 SIETEMEALARIRNELEEQLQSLASNKAEMSYEKERFDRLQKQVEDENQEILRLQNELEVERNAL-SIARDWAKDEARRA 606
Cdd:COG1196 338 ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLeELEEAEEALLERLE 417
|
170
....*....|.
gi 42573662 607 REQAKVLEEAR 617
Cdd:COG1196 418 RLEEELEELEE 428
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
451-760 |
7.12e-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: 59.69 E-value: 7.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 451 ELARIEA--EAMAENVVCAHNELVAQVEKDINASFEKELLREKEivDAVEKLAEEAKSELARLR--VEKEEETLA-LERE 525
Cdd:TIGR02168 678 EIEELEEkiEELEEKIAELEKALAELRKELEELEEELEQLRKEL--EELSRQISALRKDLARLEaeVEQLEERIAqLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 526 RTSIETEMEALARIRNELEEQLQSLASNKA-----------EMSYEKERFDRLQKQVEDENQEILRLQNELEVERNALSI 594
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEeleaqieqlkeELKALREALDELRAELTLLNEEAANLRERLESLERRIAA 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 595 ARDWAKDEARRAREQAKVLEEARGRWEKYGLKVivdSDLHEQTTKtestWLN--AGKQNHVEGTMKRAGNLIAKLKKMAK 672
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIESLAAEIEELEELI---EELESELEA----LLNerASLEEALALLRSELEELSEELRELES 908
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 673 DVGEKSREviyliiekisllISALKQQVHGMENKAKDLKIKTKSKAEEVWRQTSLRADEIRNISiVKAKETVEEFKDRVG 752
Cdd:TIGR02168 909 KRSELRRE------------LEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALE-NKIEDDEEEARRRLK 975
|
....*...
gi 42573662 753 KLGEKFKS 760
Cdd:TIGR02168 976 RLENKIKE 983
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
450-746 |
9.26e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.18 E-value: 9.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 450 EELARIEAEAMAenvvCAHNELVAQVEKDinasfEKELLREKEIVDAVEKLAEEAKSELARLRVEKEEETLALERERTSI 529
Cdd:COG1196 220 EELKELEAELLL----LKLRELEAELEEL-----EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 530 ETEMEALARIRNELEEQLQSLASNKAEMSYEKERFDRLQKQVEDENQEILRLQNELEVERNALSIARDWAKDEARRAREQ 609
Cdd:COG1196 291 YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 610 AKVLEEARGRWEkyglkvivdSDLHEQTTKTESTWLNAGKQNHVEGTMKRAGNLIAKLKKMAKDVGEKSREVIYLIIEKI 689
Cdd:COG1196 371 EAELAEAEEELE---------ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE 441
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 42573662 690 SLLISALKQQVhGMENKAKDLKIKTKSKAEEVWRQTSLRADEIRNISIVKAKETVEE 746
Cdd:COG1196 442 EALEEAAEEEA-ELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
439-617 |
3.00e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.25 E-value: 3.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 439 LAIGDAFEVVGEELARIEAEAMAENVVCAHNELVAQVEKDINASFEKELLREKEIVDAVEKLAEEAKSELARLRVEKEEE 518
Cdd:COG1196 277 EELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 519 TLALERERTSIETEMEALARIRNELEEQLQSLASNKAEMSYEKERFDRLQKQVEDENQEILRLQNELEVERNALSIARDW 598
Cdd:COG1196 357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE 436
|
170
....*....|....*....
gi 42573662 599 AKDEARRAREQAKVLEEAR 617
Cdd:COG1196 437 EEEEEEALEEAAEEEAELE 455
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
444-664 |
3.07e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.29 E-value: 3.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 444 AFEVVGEELARIEAEAM-----AENVVCAHNELVAQVEKDinasfEKELLREKEIVDAVEKLAEEAKSELARLRV---EK 515
Cdd:TIGR02168 289 ELYALANEISRLEQQKQilrerLANLERQLEELEAQLEEL-----ESKLDELAEELAELEEKLEELKEELESLEAeleEL 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 516 EEETLALERERTSIETEMEALAR-----------IRNE---LEEQLQSLASNKAEMSYEKE---------RFDRLQKQVE 572
Cdd:TIGR02168 364 EAELEELESRLEELEEQLETLRSkvaqlelqiasLNNEierLEARLERLEDRRERLQQEIEellkkleeaELKELQAELE 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 573 DENQEILRLQNELEVERNALSIARDwAKDEARRAREQAKVlEEARGRWEKYGLKVIVDSdlHEQTTKTESTWLNAGKQNH 652
Cdd:TIGR02168 444 ELEEELEELQEELERLEEALEELRE-ELEEAEQALDAAER-ELAQLQARLDSLERLQEN--LEGFSEGVKALLKNQSGLS 519
|
250
....*....|..
gi 42573662 653 veGTMKRAGNLI 664
Cdd:TIGR02168 520 --GILGVLSELI 529
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
485-757 |
5.47e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.53 E-value: 5.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 485 KELLREKEIVDAVEKL-----AEEAKSELARLRVEKEEETLALERERTSIETEMEALARIRNELEEQLQSLASNK----- 554
Cdd:TIGR02169 214 QALLKEKREYEGYELLkekeaLERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEqlrvk 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 555 ---AEMSYEKERFDRLQKQVEDENQEILRLQNELEVERNAL-SIARDWAKDEARRAREQAKVLEEARGRWEKYGLKVivd 630
Cdd:TIGR02169 294 ekiGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLlAEIEELEREIEEERKRRDKLTEEYAELKEELEDLR--- 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 631 SDLhEQTTKTESTWLNAGKQnhvegtmkragnLIAKLKKMAKDVGEKSREVIYLIIEK--ISLLISALKQQVHGMENKAK 708
Cdd:TIGR02169 371 AEL-EEVDKEFAETRDELKD------------YREKLEKLKREINELKRELDRLQEELqrLSEELADLNAAIAGIEAKIN 437
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 42573662 709 DLKIKTKSKAEEVWRQT----SLRADEIR-NISIVKAKETVEEFKDRVGKLGEK 757
Cdd:TIGR02169 438 ELEEEKEDKALEIKKQEwkleQLAADLSKyEQELYDLKEEYDRVEKELSKLQRE 491
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
484-721 |
1.02e-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: 52.37 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 484 EKELLREKEIVDAVEKLAEEAKSELARLRV-----EKEEETLA----------------LERERTSIETEMEALARIRNE 542
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKeleelEEELEQLRkeleelsrqisalrkdLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 543 LEEQLQSLASNKAEMSYEKERFDRLQKQVEDENQEILRLQNELEVERNALSIARDWAKDEARRAREQAKVLEEARGRWEk 622
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIA- 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 623 ygLKVIVDSDLHEQTTKTEstwlnaGKQNHVEGTMKRAGNLIAKLKKMAKDVgEKSREVIYLIIEKISLLISALKQQVHG 702
Cdd:TIGR02168 835 --ATERRLEDLEEQIEELS------EDIESLAAEIEELEELIEELESELEAL-LNERASLEEALALLRSELEELSEELRE 905
|
250
....*....|....*....
gi 42573662 703 MENKAKDLKIKTKSKAEEV 721
Cdd:TIGR02168 906 LESKRSELRRELEELREKL 924
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
470-620 |
1.41e-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: 51.30 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 470 ELVAQVEKDINASFEKELLREKEIVDAV------EKLAEEAKSELARLRVEKEEetlaLERERTSIETEMEALARIRNEL 543
Cdd:COG4942 108 ELLRALYRLGRQPPLALLLSPEDFLDAVrrlqylKYLAPARREQAEELRADLAE----LAALRAELEAERAELEALLAEL 183
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42573662 544 EEQLQSLASNKAEmsyEKERFDRLQKQVEDENQEILRLQNELEVERNAlsIARDWAKDEARRAREQAKVLEEARGRW 620
Cdd:COG4942 184 EEERAALEALKAE---RQKLLARLEKELAELAAELAELQQEAEELEAL--IARLEAEAAAAAERTPAAGFAALKGKL 255
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
485-754 |
3.07e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 3.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 485 KELLREKEIVDAVEKLAEEAKSELARLRVEKEEetLALERERTSIETEMEALARIRNELEEQLQSLASNKAEMSYEKERF 564
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEE--LREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEEL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 565 DRLQKQVEDENQEILRLQNELEVERNALSIARDW----AKDEARRAREQAKVLEEARGRWEKYGlkvivdSDLHEQTTKT 640
Cdd:COG4717 159 RELEEELEELEAELAELQEELEELLEQLSLATEEelqdLAEELEELQQRLAELEEELEEAQEEL------EELEEELEQL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 641 ESTWLNAGKQNHVE--GTMKRAGNLIAKLKKMAKDVGEKSREVIYLIIEKISLLISALKQQVHGMENKAKDLKIKTKSKA 718
Cdd:COG4717 233 ENELEAAALEERLKeaRLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPA 312
|
250 260 270
....*....|....*....|....*....|....*..
gi 42573662 719 EEVWRQTSLRAD-EIRNISIVKAKETVEEFKDRVGKL 754
Cdd:COG4717 313 LEELEEEELEELlAALGLPPDLSPEELLELLDRIEEL 349
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
451-592 |
1.05e-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: 47.61 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 451 ELARIEAEAMAenvvcaHNELVAQVEKDInASFEKELLREKEIVDAVEKLAEEAKSELA--RLRVEKEEETLAL---ERE 525
Cdd:COG1579 18 ELDRLEHRLKE------LPAELAELEDEL-AALEARLEAAKTELEDLEKEIKRLELEIEevEARIKKYEEQLGNvrnNKE 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42573662 526 RTSIETEMEALARIRNELEEQL-----------QSLASNKAEMSYEKERFDRLQKQVEDENQEILRLQNELEVERNAL 592
Cdd:COG1579 91 YEALQKEIESLKRRISDLEDEIlelmerieeleEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREEL 168
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
450-677 |
1.09e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.37 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 450 EELARIEAEAMAE---NVVCAHNELVAQVEKDINASFEKELLREKEIVDAVEKLAEEAKSELARLRVEkEEETLALERER 526
Cdd:PTZ00121 1561 EEKKKAEEAKKAEedkNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA-EEEKKKVEQLK 1639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 527 TSIETEMEALARIRNELEEQLQSLASNKAEMSYEKERFDRLQKQVEDENQEILRLQNELEVERNALSIARDWAkDEARRA 606
Cdd:PTZ00121 1640 KKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEA-EEKKKA 1718
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42573662 607 REQAKVLEEARGRWEKyglkviVDSDLHEQTTKTESTWLNAGKQNHVEGTMKRAGNLIAKLKKMAKDVGEK 677
Cdd:PTZ00121 1719 EELKKAEEENKIKAEE------AKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE 1783
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
481-622 |
1.45e-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: 47.23 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 481 ASFEKELLREKEIVDAVEKLAEEAKSELARLRVEKEEetlaLERERTSIETEMEALARIRNELEEQLQSLASNKAEMSYE 560
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELED----LEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEALQ 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42573662 561 KErFDRLQKQVEDENQEILRLQNELEVERNALsiardwAKDEARRAREQAKvLEEARGRWEK 622
Cdd:COG1579 96 KE-IESLKRRISDLEDEILELMERIEELEEEL------AELEAELAELEAE-LEEKKAELDE 149
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
440-615 |
1.66e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 440 AIGDAFEVVGEELARIEAEAMAENVVCAHNELvAQVEKDInASFEKELLREKEIVDAVEKLAEEAKSELARLRVEKEE-- 517
Cdd:COG4913 259 ELAERYAAARERLAELEYLRAALRLWFAQRRL-ELLEAEL-EELRAELARLEAELERLEARLDALREELDELEAQIRGng 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 518 -ETLA-LERERTSIETEMEALARIRNELEEQLQSLasnKAEMSYEKERFDRLQKQVEDenqeilrLQNELEVERNALSIA 595
Cdd:COG4913 337 gDRLEqLEREIERLERELEERERRRARLEALLAAL---GLPLPASAEEFAALRAEAAA-------LLEALEEELEALEEA 406
|
170 180
....*....|....*....|
gi 42573662 596 RDWAKDEARRAREQAKVLEE 615
Cdd:COG4913 407 LAEAEAALRDLRRELRELEA 426
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
456-759 |
1.73e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.60 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 456 EAEAMAENVVCAHNeLVAQVEKDINASFEKELLREKEIVDAVEKLAEEAKSELARLRVEKEEETLA-----LERERTSIE 530
Cdd:PTZ00121 1448 EAKKKAEEAKKAEE-AKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKAdeakkAEEAKKADE 1526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 531 TEMEALARIRNEL---EEQLQSLASNKAE---MSYEKERFDRLQKQVEDENQEILRLQNELEVERNALSIARDWAKDEAR 604
Cdd:PTZ00121 1527 AKKAEEAKKADEAkkaEEKKKADELKKAEelkKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKK 1606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 605 RAREQAKVLEEARGRWEKYGLKVIVDSDLHEQTTKTESTWLNAGKQNHVEGTMKRAGnliAKLKKMAKDVGEKSREVIYL 684
Cdd:PTZ00121 1607 MKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKA---AEEAKKAEEDKKKAEEAKKA 1683
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 685 IIEKislliSALKQQVHGMENKAKDLKIKTKSKAEEVWRQTSLR-ADEIRNISIVKAKETVEEFKDRVGKL----GEKFK 759
Cdd:PTZ00121 1684 EEDE-----KKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKkAEEENKIKAEEAKKEAEEDKKKAEEAkkdeEEKKK 1758
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
431-618 |
1.99e-05 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 47.32 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 431 TKAQTAVSLAIGDAFEVVgEELARIEAEAMAENVVCAHNE-LVAQVEKDINasfekELLREKEIVDAVEklaEEAKSELA 509
Cdd:smart00787 105 FSASPDVKLLMDKQFQLV-KTFARLEAKKMWYEWRMKLLEgLKEGLDENLE-----GLKEDYKLLMKEL---ELLNSIKP 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 510 RLRVEKE--EETLALERErtsIETEMEA-----LARIRNELEEQLQSLASNKAEMSYEKERFDRLQKQVEDENQEILRLQ 582
Cdd:smart00787 176 KLRDRKDalEEELRQLKQ---LEDELEDcdpteLDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELN 252
|
170 180 190
....*....|....*....|....*....|....*.
gi 42573662 583 NELEVERNALSIARDWAKDEARRAREQAKVLEEARG 618
Cdd:smart00787 253 TEIAEAEKKLEQCRGFTFKEIEKLKEQLKLLQSLTG 288
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
485-616 |
2.46e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.01 E-value: 2.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 485 KELLREKEIVDAVEKLAEEAKSELARLRVEKEEETLALERER---------TSIETEMEALARIRNELEEQLQSLASNKA 555
Cdd:COG1196 216 RELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEEleaelaeleAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42573662 556 EMSYEKERFDRLQKQVEDENQEILRLQNELEVERNALsiardwAKDEARRAREQAKVLEEA 616
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEEL------EELEEELEELEEELEEAE 350
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
444-617 |
3.50e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.37 E-value: 3.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 444 AFEVVGEELARiEAEAMAENVVCAHNELVAQVEKDINASFEKELLREKEIVDAVEKLAEeAKSELARLRVEKEEETLALE 523
Cdd:TIGR02169 269 EIEQLLEELNK-KIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAK-LEAEIDKLLAEIEELEREIE 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 524 ---RERTSIETEMEALARIRNELEEQLQSL----ASNKAEMSYEKERFDRLQKQVEDENQEILRLQNELEvernALSIAR 596
Cdd:TIGR02169 347 eerKRRDKLTEEYAELKEELEDLRAELEEVdkefAETRDELKDYREKLEKLKREINELKRELDRLQEELQ----RLSEEL 422
|
170 180
....*....|....*....|.
gi 42573662 597 DWAKDEARRAREQAKVLEEAR 617
Cdd:TIGR02169 423 ADLNAAIAGIEAKINELEEEK 443
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
469-746 |
4.54e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 47.27 E-value: 4.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 469 NELVAQVEKDINASFEKELLREKEIVDAVEKLAEEAKSELArlrvEKEEETLALERERTSIETEMEALARIRNELEEQLQ 548
Cdd:pfam02463 242 LQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKK----LQEEELKLLAKEEEELKSELLKLERRKVDDEEKLK 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 549 SLASN--KAEMSYEKERFDRLQKQVEDENQEILRLQNELEVErnalsiarDWAKDEARRAREQAKVLEEARGRWEkyglk 626
Cdd:pfam02463 318 ESEKEkkKAEKELKKEKEEIEELEKELKELEIKREAEEEEEE--------ELEKLQEKLEQLEEELLAKKKLESE----- 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 627 vivdsdlhEQTTKTESTWLNAGKQNhvegTMKRAGNLIAKLKKMAKDVgEKSREVIYLIIEKISLLISALKQQVHGMENK 706
Cdd:pfam02463 385 --------RLSSAAKLKEEELELKS----EEEKEAQLLLELARQLEDL-LKEEKKEELEILEEEEESIELKQGKLTEEKE 451
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 42573662 707 AKDLKIKTKSKAEEVWRQTSLRADEIRNISIVKAKETVEE 746
Cdd:pfam02463 452 ELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLS 491
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
481-758 |
5.83e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.05 E-value: 5.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 481 ASFEKELLREKEIVDAVEKLAEEAKSELARLRVEKEEETLALERERTSIETEMEALARIRNELEEQLQSLASNKAEMSYE 560
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 561 KERFDRLQKQVEDENQEILRLQ---NELEVERNALSIARDWAKDEARRAREQAKVLEEARGRWEKYgLKVIVDSDLHEQT 637
Cdd:COG4372 107 QEEAEELQEELEELQKERQDLEqqrKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQE-LQALSEAEAEQAL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 638 TKTESTWLNAGKQNHVEGTMKRAGNLIAKLKKMAKDVGEKSREVIYLIIEKISLLISALKQQVHGMENKAKDLKIKTKSK 717
Cdd:COG4372 186 DELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELEL 265
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 42573662 718 AEEVWRQTSLRADEIRNISIVKAKETVEEFKDRVGKLGEKF 758
Cdd:COG4372 266 AILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAA 306
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
475-593 |
7.06e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 7.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 475 VEKDINASFEKELLREKEIVDAVEKLA------EEAKSELARLRV--------EKEEETLALERERTSIETEMEALARIR 540
Cdd:PRK03918 610 AEKELEREEKELKKLEEELDKAFEELAetekrlEELRKELEELEKkyseeeyeELREEYLELSRELAGLRAELEELEKRR 689
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 42573662 541 NELEEQLQSLASNKAEMSYEKERFDRLQK---QVEDENQEILRLQNELevERNALS 593
Cdd:PRK03918 690 EEIKKTLEKLKEELEEREKAKKELEKLEKaleRVEELREKVKKYKALL--KERALS 743
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
451-617 |
7.26e-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: 46.27 E-value: 7.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 451 ELARIEAEAMAENVVCAHNELVAQVEKDINASFEKELLREKEIVDAVEKLAEEAKSElaRLRVEKEEETLALERERTSIE 530
Cdd:pfam17380 379 ELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQR--EVRRLEEERAREMERVRLEEQ 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 531 TEMEALARIRN------------ELEEQLQSLASNKAEMSYEKERFDRLQKQVEDENQEILrLQNELEVERNAlsIARDW 598
Cdd:pfam17380 457 ERQQQVERLRQqeeerkrkklelEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKL-LEKEMEERQKA--IYEEE 533
|
170
....*....|....*....
gi 42573662 599 AKDEARRAREQAKVLEEAR 617
Cdd:pfam17380 534 RRREAEEERRKQQEMEERR 552
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
423-617 |
7.79e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.21 E-value: 7.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 423 LFQPSKAVTKAQTAVSLAIGDAFEVVGEEL---ARIEAEAMAENVvcahneLVAQVEKDINASFEK--ELLREKEIVDAV 497
Cdd:TIGR02169 648 LFEKSGAMTGGSRAPRGGILFSRSEPAELQrlrERLEGLKRELSS------LQSELRRIENRLDELsqELSDASRKIGEI 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 498 EKLAEEAKSELARLR---VEKEEETLALERERTSIETEMEALARIRNELEEQLQSL--ASNKAEMSYEKERFDRLQKQVE 572
Cdd:TIGR02169 722 EKEIEQLEQEEEKLKerlEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLeeALNDLEARLSHSRIPEIQAELS 801
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 42573662 573 DENQEILRLQ---NELEVERNALSIARDWAKDEARRAREQAKVLEEAR 617
Cdd:TIGR02169 802 KLEEEVSRIEarlREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQI 849
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
469-747 |
8.08e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.20 E-value: 8.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 469 NELVAQVEKDINASFEKELLREKEIVDAVEKLaEEAKSELARLRVEKEEetlaLERERTSIETEMealarirNELEEQLQ 548
Cdd:TIGR02168 203 KSLERQAEKAERYKELKAELRELELALLVLRL-EELREELEELQEELKE----AEEELEELTAEL-------QELEEKLE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 549 SLASNKAEMSyekERFDRLQKQVEDENQEILRLQNELEVernalsiardwAKDEARRAREQAKVLEEARGRWEKYglKVI 628
Cdd:TIGR02168 271 ELRLEVSELE---EEIEELQKELYALANEISRLEQQKQI-----------LRERLANLERQLEELEAQLEELESK--LDE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 629 VDSDLHEQTTKTESTwlnagkQNHVEGTMKRAGNLIAKLKKMAKDVGEKSREviyliIEKISLLISALKQQVHGMENKAK 708
Cdd:TIGR02168 335 LAEELAELEEKLEEL------KEELESLEAELEELEAELEELESRLEELEEQ-----LETLRSKVAQLELQIASLNNEIE 403
|
250 260 270
....*....|....*....|....*....|....*....
gi 42573662 709 DLKIKTKSKAEEVWRQTSLRADEIRNISIVKAKETVEEF 747
Cdd:TIGR02168 404 RLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAEL 442
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
451-669 |
1.10e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.70 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 451 ELARIEAEAMAENVVCAHNELVAQVEKDINASFE--KELLREKEIVDAVEKLAEEAKSELARLRVEKEEETLALERERTS 528
Cdd:COG1196 357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEalRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 529 IE----TEMEALARIRNELEEQLQSLASNKAemsyEKERFDRLQKQVEDENQEILRLQNELEVERNALsiardwakDEAR 604
Cdd:COG1196 437 EEeeeeALEEAAEEEAELEEEEEALLELLAE----LLEEAALLEAALAELLEELAEAAARLLLLLEAE--------ADYE 504
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42573662 605 RAREQAKVLEEARGRWEKYGLKVIVDSDLHEQTTKTEsTWLNAGKQNHVEGTMKRAGNLIAKLKK 669
Cdd:COG1196 505 GFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALE-AALAAALQNIVVEDDEVAAAAIEYLKA 568
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
484-612 |
1.40e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 44.96 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 484 EKELLR-EKEIVDAVEKLA-EEAKSELARLRVEKEEETL-ALERERTSIETEMEALARIRNELEEQLQSLAsnkAEMSYE 560
Cdd:PRK09039 52 DSALDRlNSQIAELADLLSlERQGNQDLQDSVANLRASLsAAEAERSRLQALLAELAGAGAAAEGRAGELA---QELDSE 128
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 42573662 561 KERFDRLQKQVEDENQEILRLQNELEVERNALSIArdwakdEARRAREQAKV 612
Cdd:PRK09039 129 KQVSARALAQVELLNQQIAALRRQLAALEAALDAS------EKRDRESQAKI 174
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
388-586 |
1.75e-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: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 388 FLDIDKINPEAWPALIADLSAGEHGITALSF------GRTRLFQPSKAVTKAQTAVSLAIGDAFEVVGEELARIEAEAMA 461
Cdd:COG1196 576 FLPLDKIRARAALAAALARGAIGAAVDLVASdlreadARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEG 655
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 462 ENvvcAHNELVAQVEKDINASFEKELLREKEIVDAVEKLAEEAKSELARLRVEKEEETLALERERTSIETEMEALARIRN 541
Cdd:COG1196 656 GS---AGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEA 732
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 42573662 542 ELEEQLQSLASNKAEMSYEKERFDRLQKQVEDENQEILRLQNELE 586
Cdd:COG1196 733 EREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIE 777
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
363-617 |
1.88e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 363 LSWKMALEFRQLPEADSKKLYQLSGFLDIDKINPEAWPALIADLSAGEhgitalSFGRTRLFQPSKAVTKAQTAVSlaig 442
Cdd:COG4717 285 LLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPP------DLSPEELLELLDRIEELQELLR---- 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 443 dafevvgeELARIEAEAMAENVVCAHNELVAQVEKDINASFEKELLREKEIVDAVEKLaEEAKSELARLrvEKEEETLAL 522
Cdd:COG4717 355 --------EAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEEL-EELEEQLEEL--LGELEELLE 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 523 ERERTSIETEMEALARIRNELEEQLQSL----ASNKAEMSY--EKERFDRLQKQVEDENQEIlrlqNELEVERNALSIAR 596
Cdd:COG4717 424 ALDEEELEEELEELEEELEELEEELEELreelAELEAELEQleEDGELAELLQELEELKAEL----RELAEEWAALKLAL 499
|
250 260
....*....|....*....|...
gi 42573662 597 DWAKDEARRARE--QAKVLEEAR 617
Cdd:COG4717 500 ELLEEAREEYREerLPPVLERAS 522
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
494-616 |
2.31e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 494 VDAVEKLAEEAKSELARLRVEKEEetlaLERERTSIETEMEALARIRNELEEQLQSLASNKAEMsyeKERFDRLQKQVED 573
Cdd:COG3883 121 LSALSKIADADADLLEELKADKAE----LEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQ---EALLAQLSAEEAA 193
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 42573662 574 ENQEILRLQNELEVERNALSIARDWAKDEARRAREQAKVLEEA 616
Cdd:COG3883 194 AEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
473-761 |
2.39e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 2.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 473 AQVEKDINA---SFEKELLREKEIVDAVEKLAEEAKSELARLRvEKEEETLALERERTSIETEMEALARIRNELEEQLQS 549
Cdd:PRK03918 168 GEVIKEIKRrieRLEKFIKRTENIEELIKEKEKELEEVLREIN-EISSELPELREELEKLEKEVKELEELKEEIEELEKE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 550 LASNKAEMSYEKERFDRLQKQVEDENQEIlrlqNELEvernalsiardwakdearrarEQAKVLEEARGRWEKY----GL 625
Cdd:PRK03918 247 LESLEGSKRKLEEKIRELEERIEELKKEI----EELE---------------------EKVKELKELKEKAEEYiklsEF 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 626 KVIVDSDLHEqTTKTESTWLNagKQNHVEGTMKRAGNLIAKLKKMAKDVGEKSREviYLIIEKISLLISALKQQVHGMEN 705
Cdd:PRK03918 302 YEEYLDELRE-IEKRLSRLEE--EINGIEERIKELEEKEERLEELKKKLKELEKR--LEELEERHELYEEAKAKKEELER 376
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 706 KAKDLKIKTKSKAEEvwrqtslradEIRNISivKAKETVEE----FKDRVGKLGEKFKSK 761
Cdd:PRK03918 377 LKKRLTGLTPEKLEK----------ELEELE--KAKEEIEEeiskITARIGELKKEIKEL 424
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
331-717 |
2.47e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 44.71 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 331 LISSKLSNNNMPSsessrVTFSPESPLTRQDLLSWKMALEFRQLPEADSKKLYQLSGFLDID---KINPEAWPALIADLS 407
Cdd:pfam05483 246 LIQITEKENKMKD-----LTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKmslQRSMSTQKALEEDLQ 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 408 AGEHGITALSFGRTRLFQPSkavTKAQTAVSLAIGDAFEVVG--EELARIEAEAMAEN----------VVCAHNELVAQV 475
Cdd:pfam05483 321 IATKTICQLTEEKEAQMEEL---NKAKAAHSFVVTEFEATTCslEELLRTEQQRLEKNedqlkiitmeLQKKSSELEEMT 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 476 EKDINASFE----KELLREKEIV----DAVEKLAEEAK---SELARLRVEKEEETLALERERTSIETEMEALARIRNELE 544
Cdd:pfam05483 398 KFKNNKEVEleelKKILAEDEKLldekKQFEKIAEELKgkeQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLK 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 545 EQLQS-------LASNKAEMSYE-------------------------KERFDRLQKQVEDENQEILRLQNELEVERNAL 592
Cdd:pfam05483 478 TELEKeklknieLTAHCDKLLLEnkeltqeasdmtlelkkhqediincKKQEERMLKQIENLEEKEMNLRDELESVREEF 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 593 SIARDWAKDEARRAREQAKVLEEARGRWEKyglkvivdsdlheQTTKTESTWLNAGKQnhVEGTMKRAGNLIAKLKKMAK 672
Cdd:pfam05483 558 IQKGDEVKCKLDKSEENARSIEYEVLKKEK-------------QMKILENKCNNLKKQ--IENKNKNIEELHQENKALKK 622
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 42573662 673 DVGEKSREV-IYLI-IEKISLLISALKQQVHGM-ENKAKDLKIKTKSK 717
Cdd:pfam05483 623 KGSAENKQLnAYEIkVNKLELELASAKQKFEEIiDNYQKEIEDKKISE 670
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
473-759 |
2.77e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 473 AQVEKDINASFEKELLREKEIVDAVEKLAEEAKSELARLRVEKEEETLALERERTSIETEMEALARIRNELEEQLQSLAS 552
Cdd:PTZ00121 1345 AEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAK 1424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 553 NKAEmsyEKERFDRLQKQVEDENQ--EILRLQNELEVERNALSIARDWAK-DEARRAREQAKVLEEARGRWEKYGLKViv 629
Cdd:PTZ00121 1425 KKAE---EKKKADEAKKKAEEAKKadEAKKKAEEAKKAEEAKKKAEEAKKaDEAKKKAEEAKKADEAKKKAEEAKKKA-- 1499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 630 dsdlhEQTTKTESTWLNAGKQNHVEgTMKRAGNLIAKLKKMAKDVGEKSREViyliiEKISLLISAlkQQVHGMENKAkd 709
Cdd:PTZ00121 1500 -----DEAKKAAEAKKKADEAKKAE-EAKKADEAKKAEEAKKADEAKKAEEK-----KKADELKKA--EELKKAEEKK-- 1564
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 42573662 710 lKIKTKSKAEEVWRQTSLRADEIRNISIVKAKETVEEFKDRVGKLGEKFK 759
Cdd:PTZ00121 1565 -KAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK 1613
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
489-615 |
2.77e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.75 E-value: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 489 REKEIVDAVEKLAEEAKSELARLRVEKE-----EETLALERERTSIETEMEALARIRNELEEQLQSLaSNKAEMSYEK-- 561
Cdd:COG1340 134 EEKELVEKIKELEKELEKAKKALEKNEKlkelrAELKELRKEAEEIHKKIKELAEEAQELHEEMIEL-YKEADELRKEad 212
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42573662 562 ---ERFDRLQKQVEDENQEILRLQNELEVERNALSIARDWAKDEARRA-----REQAKVLEE 615
Cdd:COG1340 213 elhKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKekeelEEKAEEIFE 274
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
450-688 |
2.86e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 2.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 450 EELARIEAEAMAENVVCAhnELVAQVEKDINASFEK-ELLR--EKEIVDAVEKLAEEAKSELARLRVEKEEETLALERER 526
Cdd:PTZ00121 1549 DELKKAEELKKAEEKKKA--EEAKKAEEDKNMALRKaEEAKkaEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELK 1626
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 527 TSiETEMEALARIRNELEEQLQSLASNKAEMSYEKERFDRLQKQVEDENQEILRLQNELEVERNALSiARDWAKDEARRA 606
Cdd:PTZ00121 1627 KA-EEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAE-ALKKEAEEAKKA 1704
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 607 REQAKVLEEARGRWEKYGLKVIVDSDLHEQTTKTESTWLNAGKQNHVEGTMKragNLIAKLKKMAKDVGEKSREVIYLII 686
Cdd:PTZ00121 1705 EELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEK---KKIAHLKKEEEKKAEEIRKEKEAVI 1781
|
..
gi 42573662 687 EK 688
Cdd:PTZ00121 1782 EE 1783
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
494-746 |
3.40e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.36 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 494 VDAVEKLAEEAKSELARLRVEKEEetlaLERERTSIETEMEALARIRNELEEQLQSLasnKAEMSYEKERFDRLQKQVed 573
Cdd:COG1340 3 TDELSSSLEELEEKIEELREEIEE----LKEKRDELNEELKELAEKRDELNAQVKEL---REEAQELREKRDELNEKV-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 574 enqeilrlqNELEVERNALSIARDWAKDEARRAREQAKVLEEARGRWEKygLKVIVDSDLHEQTTKTestwLNAGKQNHV 653
Cdd:COG1340 74 ---------KELKEERDELNEKLNELREELDELRKELAELNKAGGSIDK--LRKEIERLEWRQQTEV----LSPEEEKEL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 654 EGTMKRAGNLIAKLKKMAkdvgEKSREVIYLI--IEKISLLISALKQQVHGMENKA---KDLKIKTKSKAEEVWRQtslr 728
Cdd:COG1340 139 VEKIKELEKELEKAKKAL----EKNEKLKELRaeLKELRKEAEEIHKKIKELAEEAqelHEEMIELYKEADELRKE---- 210
|
250
....*....|....*...
gi 42573662 729 ADEIRNiSIVKAKETVEE 746
Cdd:COG1340 211 ADELHK-EIVEAQEKADE 227
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
450-718 |
3.78e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 3.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 450 EELARIEAE--AMAENVVCAHNELVaQVEKDINAsfEKELLREKEIVDAVEKLAEEAKS-------ELARLRVEKEEETL 520
Cdd:PRK03918 459 AELKRIEKElkEIEEKERKLRKELR-ELEKVLKK--ESELIKLKELAEQLKELEEKLKKynleeleKKAEEYEKLKEKLI 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 521 ALERERTSIETEMEALARIRN---ELEEQLQSLASNKAEMSYEKERF--------DRLQKQVEDENQEILRLQN---ELE 586
Cdd:PRK03918 536 KLKGEIKSLKKELEKLEELKKklaELEKKLDELEEELAELLKELEELgfesveelEERLKELEPFYNEYLELKDaekELE 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 587 VERNALSIARDWAKDEARRAREQAKVLEEARGRWEKygLKVIVDSDLHEQTTK--TESTWLNAGKQNHVEGTMKRAGNLI 664
Cdd:PRK03918 616 REEKELKKLEEELDKAFEELAETEKRLEELRKELEE--LEKKYSEEEYEELREeyLELSRELAGLRAELEELEKRREEIK 693
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 42573662 665 AKLKKMAKDVGEKSREviyliIEKISLLISALKqQVHGMENKAKDLKIKTKSKA 718
Cdd:PRK03918 694 KTLEKLKEELEEREKA-----KKELEKLEKALE-RVEELREKVKKYKALLKERA 741
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
450-619 |
3.88e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 43.96 E-value: 3.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 450 EELARIEAEAMAENVVCAHNELVAQVEKDINasfekellrEKEIVDAVEKLAEEakselaRLRVEKEEETLALERERTSI 529
Cdd:pfam17380 255 EYTVRYNGQTMTENEFLNQLLHIVQHQKAVS---------ERQQQEKFEKMEQE------RLRQEKEEKAREVERRRKLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 530 ETEMEALArirnELEEQlQSLASNKAEMSYEKER-FDRLQKqvEDENQEILRLQNE---LEVER----NALSIARDWAKD 601
Cdd:pfam17380 320 EAEKARQA----EMDRQ-AAIYAEQERMAMEREReLERIRQ--EERKRELERIRQEeiaMEISRmrelERLQMERQQKNE 392
|
170 180
....*....|....*....|.
gi 42573662 602 EARRAREQA---KVLEEARGR 619
Cdd:pfam17380 393 RVRQELEAArkvKILEEERQR 413
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
415-618 |
3.94e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.85 E-value: 3.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 415 ALSFGRTRLFQPSKAVTKAQTAVS--------LAIGDAFEVVGEELARIEAE-AMAENVVCAHNELVAQVEKDINASFEK 485
Cdd:COG3206 176 ALEFLEEQLPELRKELEEAEAALEefrqknglVDLSEEAKLLLQQLSELESQlAEARAELAEAEARLAALRAQLGSGPDA 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 486 --ELLREKEIVDAVEKLAEeAKSELARLRV---EKEEETLALERERTSIETEMEA-LARIRNELEEQLQSLASNKAEMSY 559
Cdd:COG3206 256 lpELLQSPVIQQLRAQLAE-LEAELAELSArytPNHPDVIALRAQIAALRAQLQQeAQRILASLEAELEALQAREASLQA 334
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 42573662 560 EKERFDRLQKQVEDENQEILRLQNELEVERNALsiardwakDEARRAREQAKVLEEARG 618
Cdd:COG3206 335 QLAQLEARLAELPELEAELRRLEREVEVARELY--------ESLLQRLEEARLAEALTV 385
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
509-669 |
4.50e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 4.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 509 ARLRVEKEEETLALERERTSIETEMEALARIRNELEEQLQSLAsNKAEMSYEKERFDRLQKQVEDENQEILRLQN----- 583
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQ-RLAEYSWDEIDVASAEREIAELEAELERLDAssddl 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 584 -ELEVERNALSIARDWAKDEARRAREQAKVLEEARGRWE------KYGLKVIVDSDLHEQTTKTESTWLNAGKQNHVEGT 656
Cdd:COG4913 688 aALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEeeldelQDRLEAAEDLARLELRALLEERFAAALGDAVEREL 767
|
170
....*....|...
gi 42573662 657 MKRAGNLIAKLKK 669
Cdd:COG4913 768 RENLEERIDALRA 780
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
440-635 |
4.81e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 4.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 440 AIGDAFEVVGEELARIEAEAMAENVVCAHNELVAQVEKDInasfeKELLREKEIVDAVEKLAEEAKSELARLRVEKEEet 519
Cdd:COG4913 638 AELDALQERREALQRLAEYSWDEIDVASAEREIAELEAEL-----ERLDASSDDLAALEEQLEELEAELEELEEELDE-- 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 520 laLERERTSIETEMEALARIRNELEEQLQSLASN-------------KAEMSYEKER--FDRLQKQVEDENQEILRLQNE 584
Cdd:COG4913 711 --LKGEIGRLEKELEQAEEELDELQDRLEAAEDLarlelralleerfAAALGDAVERelRENLEERIDALRARLNRAEEE 788
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 42573662 585 LEVERNAlsIARDWaKDEARRAREQAKVLEEARGRwekygLKVIVDSDLHE 635
Cdd:COG4913 789 LERAMRA--FNREW-PAETADLDADLESLPEYLAL-----LDRLEEDGLPE 831
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
440-732 |
5.41e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 43.41 E-value: 5.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 440 AIGDAFEVVGEELARIEAEAMAENVVCAH--NELVAQVEKDINASfeKELLREKEIVDAVEKLAEEAKSELARLRVEKEE 517
Cdd:COG5185 250 QTSDKLEKLVEQNTDLRLEKLGENAESSKrlNENANNLIKQFENT--KEKIAEYTKSIDIKKATESLEEQLAAAEAEQEL 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 518 ETLALERErTSIETEMEALARIRNELEEQLQSLASNKAEMSYEkERFDRLQKQVEDENQEILRLQNELEVE-RNALSIAR 596
Cdd:COG5185 328 EESKRETE-TGIQNLTAEIEQGQESLTENLEAIKEEIENIVGE-VELSKSSEELDSFKDTIESTKESLDEIpQNQRGYAQ 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 597 DWAKDEARRAREQAKVLEEARGRWEKYGLKVIVDSD----LHEQTTKTESTWLNAGKQNHVEGTMKRAGNLIAKLKKMAK 672
Cdd:COG5185 406 EILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKllneLISELNKVMREADEESQSRLEEAYDEINRSVRSKKEDLNE 485
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42573662 673 DVGEKSREVIYL------IIEKISLLISALKQQVHGMENKAKDLKIKTKSkAEEVWRQTSLRADEI 732
Cdd:COG5185 486 ELTQIESRVSTLkatlekLRAKLERQLEGVRSKLDQVAESLKDFMRARGY-AHILALENLIPASEL 550
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
489-618 |
5.52e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 43.50 E-value: 5.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 489 REKEIVDAVEKLA---EEAKSELA----RLRVEKEEETLALERERTSIETEMEALARIRNELE-EQLQslASNKAEMSye 560
Cdd:PRK10929 131 RAREISDSLSQLPqqqTEARRQLNeierRLQTLGTPNTPLAQAQLTALQAESAALKALVDELElAQLS--ANNRQELA-- 206
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 42573662 561 KERFDRLQKQVEdenqeilRLQNELEVERNALSIARdwaKDEARRAREQAKVLEEARG 618
Cdd:PRK10929 207 RLRSELAKKRSQ-------QLDAYLQALRNQLNSQR---QREAERALESTELLAEQSG 254
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
481-746 |
5.80e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.51 E-value: 5.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 481 ASFEKELLREKEIVDAVEKLAEEAKSELARLRVEKEEetlaLERERTSIETEMEALARIRNELEEQLQ-------SLASN 553
Cdd:TIGR02168 242 EELQEELKEAEEELEELTAELQELEEKLEELRLEVSE----LEEEIEELQKELYALANEISRLEQQKQilrerlaNLERQ 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 554 KAEMSYEKERFDRLQKQVEDENQEILRLQNELEVERNALSIARDWAKDEARRAREQAKVLEEArgrWEKYGLKVIvdsDL 633
Cdd:TIGR02168 318 LEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ---LETLRSKVA---QL 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 634 HEQTTKTESTWLNAGKQnhVEGTMKRAGNLIAKLKKMAKDVGEKSREviyLIIEKISLLISALKQQVHGMENKAKDLKIK 713
Cdd:TIGR02168 392 ELQIASLNNEIERLEAR--LERLEDRRERLQQEIEELLKKLEEAELK---ELQAELEELEEELEELQEELERLEEALEEL 466
|
250 260 270
....*....|....*....|....*....|...
gi 42573662 714 TKSKAEEVWRQTSLRADEIRNISIVKAKETVEE 746
Cdd:TIGR02168 467 REELEEAEQALDAAERELAQLQARLDSLERLQE 499
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
456-616 |
6.16e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 6.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 456 EAEAMAENVVcahnelvAQVEKDINASFEKELLREKEivdAVEKLAEEAKSELARLRVE--KEEETLaLERERTsIETEM 533
Cdd:PRK12704 35 EAEEEAKRIL-------EEAKKEAEAIKKEALLEAKE---EIHKLRNEFEKELRERRNElqKLEKRL-LQKEEN-LDRKL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 534 EALARIRNELEEQLQSLASNKAEMSYEKERFDRLQKQVEDENQEILRLQNElEVERNALSIARDWAKDEA----RRAREQ 609
Cdd:PRK12704 103 ELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAE-EAKEILLEKVEEEARHEAavliKEIEEE 181
|
....*..
gi 42573662 610 AKvlEEA 616
Cdd:PRK12704 182 AK--EEA 186
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
472-547 |
7.05e-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: 7.05e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42573662 472 VAQVEKDInASFEKELLREKEIVDAVEKLAEEAKSELARLRVEKEEETLALERERTSIETEMEALARIRNELEEQL 547
Cdd:COG1579 98 IESLKRRI-SDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
470-760 |
1.01e-03 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 42.69 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 470 ELVAQVEKDINASFE---KELLREKEIVDAVEKLAEEAKSelaRLRVEKEEE----------TLALERERTSIETEMEAL 536
Cdd:NF033838 114 ELTSKTKKELDAAFEqfkKDTLEPGKKVAEATKKVEEAEK---KAKDQKEEDrrnyptntykTLELEIAESDVEVKKAEL 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 537 ARIRNELEEQLQSLASNKAEMSYEKERFD--RLQK------QVEDENQEILRLQNELEVERNALSIARDWAKDEARRARE 608
Cdd:NF033838 191 ELVKEEAKEPRDEEKIKQAKAKVESKKAEatRLEKiktdreKAEEEAKRRADAKLKEAVEKNVATSEQDKPKRRAKRGVL 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 609 QAKVLEEARGRWEKYGlkvivDSDLHEQTTKTEStwLNAGKQnhvegtMKRAGNLIAKLKKMAKDVGEKSRE----VIYL 684
Cdd:NF033838 271 GEPATPDKKENDAKSS-----DSSVGEETLPSPS--LKPEKK------VAEAEKKVEEAKKKAKDQKEEDRRnyptNTYK 337
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42573662 685 IIEkisllisalkqqvhgMENKAKDLKIKtKSKAEEVWRQtslrADEIRNISIVK-AKETVEEFKDRVGKLgEKFKS 760
Cdd:NF033838 338 TLE---------------LEIAESDVKVK-EAELELVKEE----AKEPRNEEKIKqAKAKVESKKAEATRL-EKIKT 393
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
440-617 |
1.03e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.72 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 440 AIGDAFEVVGE-ELARIEAEAMAENVVCAHNELVAQVEKdinasfEKELLREKEIVDAVEKLAEEAKSelarlRVEKEEE 518
Cdd:PRK02224 469 TIEEDRERVEElEAELEDLEEEVEEVEERLERAEDLVEA------EDRIERLEERREDLEELIAERRE-----TIEEKRE 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 519 TLALERER-TSIETEME----ALARIRNELEEQLQSLASNKAEMSYEKERFDRLQK------QVEDENQEILRLQNELE- 586
Cdd:PRK02224 538 RAEELRERaAELEAEAEekreAAAEAEEEAEEAREEVAELNSKLAELKERIESLERirtllaAIADAEDEIERLREKREa 617
|
170 180 190
....*....|....*....|....*....|..
gi 42573662 587 -VERNALSiaRDWAKDEARRAREQAKVLEEAR 617
Cdd:PRK02224 618 lAELNDER--RERLAEKRERKRELEAEFDEAR 647
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
484-761 |
1.17e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 42.65 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 484 EKELLREKEIVDAVEKLAEEAKSELARLRVEKEEETLALERERTSIETEMEALARI---------------RNELEEQLQ 548
Cdd:pfam02463 172 KEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLyldylklneeridllQELLRDEQE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 549 SLASNKAEMSYEKERFDRLQKQVEDENQEI---LRLQNELEVERNALSIARDWAKDEARRAREQAKVLEEARGRWEKYGL 625
Cdd:pfam02463 252 EIESSKQEIEKEEEKLAQVLKENKEEEKEKklqEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 626 KVIVDSDlHEQTTKTESTWLNAGKQNHVEGTMKRAGNLIAKLKKMAKDVGEKSR------EVIYLIIEKISLLISALKQQ 699
Cdd:pfam02463 332 KEKEEIE-ELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESErlssaaKLKEEELELKSEEEKEAQLL 410
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42573662 700 VHGMENKAKDLKIKTKSKAEEVWRQTSLRADEIRNISIVKAKETVEEFKDRVGKLGEKFKSK 761
Cdd:pfam02463 411 LELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSED 472
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
498-621 |
1.37e-03 |
|
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
Pssm-ID: 464788 [Multi-domain] Cd Length: 211 Bit Score: 40.80 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 498 EKLAEEAKSELARLRVEKEEETLALERER----TSIETEMEAlarIRNELEEQLQSLASNKAEMSYEKERfdRLQKQVED 573
Cdd:pfam15665 66 ERMKRQALTEFEQYKRRVEERELKAEAEHrqrvVELSREVEE---AKRAFEEKLESFEQLQAQFEQEKRK--ALEELRAK 140
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 42573662 574 ENQEILRLQNELEVERNalsiarDWAKDEARRAREQAKVLEEARGRWE 621
Cdd:pfam15665 141 HRQEIQELLTTQRAQSA------SSLAEQEKLEELHKAELESLRKEVE 182
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
468-703 |
1.59e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 42.27 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 468 HNELVAQVEKDINASFEKELLREKEIVDAVEKLAEEAKSELARLRVEKEEETLALERERTsIETEMEALARIRNELEEQL 547
Cdd:pfam02463 311 DDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQ-LEEELLAKKKLESERLSSA 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 548 QSLASNKAEMSYEKERFDRLQKQVEDENQEIL-RLQNELEVERNALSIARDWAKDEARRAREQAKVLEEARGRWEKYGLK 626
Cdd:pfam02463 390 AKLKEEELELKSEEEKEAQLLLELARQLEDLLkEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKK 469
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42573662 627 VIVDSDLHEQTTKTESTWLNAGKQNHVEGTMKRAGNLIAKLKKMAKDVGEKSREVIYLIIEKISLLISALKQQVHGM 703
Cdd:pfam02463 470 SEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAIS 546
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
488-618 |
1.85e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 488 LREKEIVDAVEKlAEEAKSELARLRVEKEEETLALERERTSIETEMEALARIrNELEEQLQSLASNKAEmsyEKERFDRL 567
Cdd:PRK02224 461 VEGSPHVETIEE-DRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRI-ERLEERREDLEELIAE---RRETIEEK 535
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 42573662 568 QKQVEDENQEILRLQNELEVERNALSIARDwakdEARRAREQAKVLEEARG 618
Cdd:PRK02224 536 RERAEELRERAAELEAEAEEKREAAAEAEE----EAEEAREEVAELNSKLA 582
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
467-556 |
1.97e-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: 41.29 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 467 AHNELVAQVEKDIN--ASFEKELLREKEIVDAVEKLAEEAKSELARLRVEKEEETLALERERTSIETEMEALARIRNELE 544
Cdd:COG4942 147 ARREQAEELRADLAelAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226
|
90
....*....|..
gi 42573662 545 EQLQSLASNKAE 556
Cdd:COG4942 227 ALIARLEAEAAA 238
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
463-586 |
2.14e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 41.64 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 463 NVVCAHNELVAQVEKDINASFEKELLREKEIVDAVEKLAEEAKsELARLRVEKEEETLAL-ERERTSIETEMEALARIRN 541
Cdd:pfam15921 295 NSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAK-RMYEDKIEELEKQLVLaNSELTEARTERDQFSQESG 373
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42573662 542 ELEEQLQSLASN----KAEMSYEKER--------------FDRLQKQVEDENQEILRLQNELE 586
Cdd:pfam15921 374 NLDDQLQKLLADlhkrEKELSLEKEQnkrlwdrdtgnsitIDHLRRELDDRNMEVQRLEALLK 436
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
480-600 |
2.31e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.49 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 480 NASFEKELLREKEIVDAVEKLAEEAKSELARLRVEKEEETLALERER-----------TSIETEMEALARIRNELEEQLQ 548
Cdd:TIGR00618 161 KSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTlctpcmpdtyhERKQVLEKELKHLREALQQTQQ 240
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 42573662 549 SLA--SNKAEMSYEKERFDRLQKQVEDENQEILRLQNELEVERNALSIARDWAK 600
Cdd:TIGR00618 241 SHAylTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAP 294
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
473-617 |
2.53e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 473 AQVEKDINASFEKELLREKEIVDAVEKLAEEAKsELARLRvekeeetLALERERTSIETemeaLARIRnELEEQLQSLAS 552
Cdd:COG4913 203 FKPIGDLDDFVREYMLEEPDTFEAADALVEHFD-DLERAH-------EALEDAREQIEL----LEPIR-ELAERYAAARE 269
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42573662 553 NKAEMSYEKERFD--RLQKQVEDENQEILRLQNELEVERNALSIARDwakdEARRAREQAKVLEEAR 617
Cdd:COG4913 270 RLAELEYLRAALRlwFAQRRLELLEAELEELRAELARLEAELERLEA----RLDALREELDELEAQI 332
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
467-708 |
2.82e-03 |
|
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: 41.21 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 467 AHNELVAQVEKDInASFEKELL--------REKEIVDAVEKLAEEAK-------SELARLRVEKEEETLALERERTSI-- 529
Cdd:TIGR02169 234 ALERQKEAIERQL-ASLEEELEklteeiseLEKRLEEIEQLLEELNKkikdlgeEEQLRVKEKIGELEAEIASLERSIae 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 530 -ETEMEALARIRNELEEQLQSLASNKAEMSYEKE----RFDRLQKQVEDENQEILRLQNELEVERNALSIARDWAKDEAR 604
Cdd:TIGR02169 313 kERELEDAEERLAKLEAEIDKLLAEIEELEREIEeerkRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYRE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 605 R-----------AREQAKVLEEARGRWEKYglkvivdSDLHEQTTKTEstwlnaGKQNHVEGTMKRAGNLIA----KLKK 669
Cdd:TIGR02169 393 KleklkreinelKRELDRLQEELQRLSEEL-------ADLNAAIAGIE------AKINELEEEKEDKALEIKkqewKLEQ 459
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 42573662 670 MAKDVgEKSREVIYLIIEKISLL---ISALKQQVHGMENKAK 708
Cdd:TIGR02169 460 LAADL-SKYEQELYDLKEEYDRVekeLSKLQRELAEAEAQAR 500
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
481-622 |
2.85e-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: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 481 ASFEKELLREKEIVDAVEKLAEEAKSELARLRVEK-------------------EEETLALERERTSIET---EMEALAR 538
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERRealqrlaeyswdeidvasaEREIAELEAELERLDAssdDLAALEE 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 539 IRNELEEQLQSLASNKAEMSYEKErfdRLQKQVEDENQEILRLQNELEVERNALSIARDWAKDEARRAREQAKVLEEARG 618
Cdd:COG4913 693 QLEELEAELEELEEELDELKGEIG---RLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRE 769
|
....
gi 42573662 619 RWEK 622
Cdd:COG4913 770 NLEE 773
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
450-761 |
2.99e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 2.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 450 EELARIEAEAMAENVVCAHNELVAQVEKDINASFEKELLREKEivdAVEKLAEEAKSElARLRVEKEEETLALERERTSI 529
Cdd:PTZ00121 1197 EDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDA---EEAKKAEEERNN-EEIRKFEEARMAHFARRQAAI 1272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 530 ETEMEALARIRNELEEQLQSLASNKAE----------MSYEKERFDRLQKQVEDENQEILRLQNELEVERNALSIAR--- 596
Cdd:PTZ00121 1273 KAEEARKADELKKAEEKKKADEAKKAEekkkadeakkKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKaea 1352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 597 DWAKDEARRAREQAKV----LEEARGRWEKYGLKVIVDSDLHEQTTKTESTWLNAGKQNHVEGTMKRAGNLIAKL--KKM 670
Cdd:PTZ00121 1353 EAAADEAEAAEEKAEAaekkKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAeeKKK 1432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 671 AKDVGEKSREviyliiekisllisalkqqvhgmENKAKDLKIKT--KSKAEEVWRqtslRADEIRNISIVKAKETVEEFK 748
Cdd:PTZ00121 1433 ADEAKKKAEE-----------------------AKKADEAKKKAeeAKKAEEAKK----KAEEAKKADEAKKKAEEAKKA 1485
|
330
....*....|...
gi 42573662 749 DRVGKLGEKFKSK 761
Cdd:PTZ00121 1486 DEAKKKAEEAKKK 1498
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
472-746 |
3.10e-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: 41.19 E-value: 3.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 472 VAQVEKDINASFEKELLREK---EIVDAVEKLAEEAKSELARLRVEKEEETLALERERTSIETEMEALARIRNELEEQLQ 548
Cdd:TIGR00606 264 IMKLDNEIKALKSRKKQMEKdnsELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKT 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 549 SLASNKAEMSYEKerfDRLQKQVEDENQEILRLQNELEVE------------RNALSIARDWAKDEARRAREQAKVLEEA 616
Cdd:TIGR00606 344 ELLVEQGRLQLQA---DRHQEHIRARDSLIQSLATRLELDgfergpfserqiKNFHTLVIERQEDEAKTAAQLCADLQSK 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 617 RGRWEKYGLKVIVDSDLHEQTTKTESTWLNAgKQNHVEGTMKRAGNLIAKLKKMAKDVGEKSREVIYLIIEKISLLISAL 696
Cdd:TIGR00606 421 ERLKQEQADEIRDEKKGLGRTIELKKEILEK-KQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETL 499
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 42573662 697 KQQVHGMENKAKDLKIKTKSKAEEVWRQTSLRADEIRNISIVKAKETVEE 746
Cdd:TIGR00606 500 KKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDE 549
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
501-592 |
3.40e-03 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 37.98 E-value: 3.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 501 AEEAKSELARLRVEKEEETLALERERTSIETEMEALARIRNELEEQLQSLASNKAEMsyeKERFDRLQKQVEDENQEILR 580
Cdd:pfam20492 32 SEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEEKEQLEAELAEA---QEEIARLEEEVERKEEEARR 108
|
90
....*....|..
gi 42573662 581 LQNELEVERNAL 592
Cdd:pfam20492 109 LQEELEEAREEE 120
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
484-761 |
3.88e-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: 3.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 484 EKELLREKEIVDAVEKLAEEAKSELARLRVEKEEETLAL--------ERERTSIETEMEALARIRNELEEQLQSLASNKA 555
Cdd:TIGR04523 273 QKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKElkselknqEKKLEEIQNQISQNNKIISQLNEQISQLKKELT 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 556 EMSYEKErfdRLQKQVEDENQEILRLQNE----------LEVERNALSIARDWAKDEARRAREQAKVLEEARGRWEKYgl 625
Cdd:TIGR04523 353 NSESENS---EKQRELEEKQNEIEKLKKEnqsykqeiknLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKE-- 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 626 kvivDSDLHEQTTKTESTWLNAGKQNHVegtmkragnliakLKKMAKDVgEKSREVIYLIIEKISLLISALKQQvhgMEN 705
Cdd:TIGR04523 428 ----IERLKETIIKNNSEIKDLTNQDSV-------------KELIIKNL-DNTRESLETQLKVLSRSINKIKQN---LEQ 486
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 42573662 706 KAKDLKIKTKsKAEEVWRQTSLRADEIRNIS--IVKAKETVEEFKDRVGKLGEKFKSK 761
Cdd:TIGR04523 487 KQKELKSKEK-ELKKLNEEKKELEEKVKDLTkkISSLKEKIEKLESEKKEKESKISDL 543
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
467-617 |
4.47e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.13 E-value: 4.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 467 AHNELVAQVEKDIN------ASFEKELLREKEIVDAVEKLAEEAKSELARLRVEKEEETLALERERTSIETEMEALARIR 540
Cdd:COG4942 38 ELEKELAALKKEEKallkqlAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLG 117
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42573662 541 NELEEQLQSLASNKAEMSYEKERFDRLQKQVEDENQEILRLQNELEVERNALSIARDWAKDEARRAREQAKVLEEAR 617
Cdd:COG4942 118 RQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALK 194
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
444-622 |
5.54e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.41 E-value: 5.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 444 AFEVVGEELARIEAEAMAEnVVCAHNELVAQVEKDINASFEKELLREKEIVDAVEKLA--EEAKSELARLR--VEKEEET 519
Cdd:PRK02224 188 SLDQLKAQIEEKEEKDLHE-RLNGLESELAELDEEIERYEEQREQARETRDEADEVLEehEERREELETLEaeIEDLRET 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 520 LA-LERERTSIETEMEALARIRNELEEQLQSLASNKAEMSYEKERFDRLQKQVEDENQEilrLQNELEVERNALSIAR-- 596
Cdd:PRK02224 267 IAeTEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEE---LRDRLEECRVAAQAHNee 343
|
170 180
....*....|....*....|....*..
gi 42573662 597 -DWAKDEARRAREQAKVLEEARGRWEK 622
Cdd:PRK02224 344 aESLREDADDLEERAEELREEAAELES 370
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
509-602 |
6.84e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 40.06 E-value: 6.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 509 ARLRVE---KEEETLALERERTSIETEMEALARIRN--------ELEEQLQSLASNKAEMSY----EKERFDRLQK---Q 570
Cdd:COG0542 400 ARVRMEidsKPEELDELERRLEQLEIEKEALKKEQDeasferlaELRDELAELEEELEALKArweaEKELIEEIQElkeE 479
|
90 100 110
....*....|....*....|....*....|..
gi 42573662 571 VEDENQEILRLQNELEVERNALSIARDWAKDE 602
Cdd:COG0542 480 LEQRYGKIPELEKELAELEEELAELAPLLREE 511
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
480-622 |
7.66e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.64 E-value: 7.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 480 NASFEKELLREkEIVDAVEKLAE-EAKSELARLRVEKEEETLA-------------------LERERTSIETEMEALARI 539
Cdd:PRK02224 409 NAEDFLEELRE-ERDELREREAElEATLRTARERVEEAEALLEagkcpecgqpvegsphvetIEEDRERVEELEAELEDL 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 540 RNELEEQLQSLASNKAEMSYEKeRFDRLQKQVEDENQEILRLQNELEVERNALSIARDWAKDEARRAREQAKVLEEARGR 619
Cdd:PRK02224 488 EEEVEEVEERLERAEDLVEAED-RIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEE 566
|
...
gi 42573662 620 WEK 622
Cdd:PRK02224 567 AEE 569
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
484-758 |
7.79e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.66 E-value: 7.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 484 EKELLREKEIVDAVEKLAEEAKSELARLRVEKEEET------------------LALERERTSIETEMEALARIRNELEE 545
Cdd:PRK03918 347 LKELEKRLEELEERHELYEEAKAKKEELERLKKRLTgltpeklekeleelekakEEIEEEISKITARIGELKKEIKELKK 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 546 QLQSLASNK-------AEMSYE-----KERFDRLQKQVEDENQEILRLQNELEVERNALSIARDWAKdEARRAREQAKVL 613
Cdd:PRK03918 427 AIEELKKAKgkcpvcgRELTEEhrkelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKES-ELIKLKELAEQL 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 614 EEARGRWEKYGLKVIVDSDLHEQTTKTESTWLNaGKQNHVEGTMKRAGNLIAKLKKMAKDVGEKSREVIYLIIEKISLLI 693
Cdd:PRK03918 506 KELEEKLKKYNLEELEKKAEEYEKLKEKLIKLK-GEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGF 584
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42573662 694 SALKQqvhgMENKAKDLK------IKTKSKAEEVWRQTSLRADEIRNIS-----IVKAKETVEEFKDRVGKLGEKF 758
Cdd:PRK03918 585 ESVEE----LEERLKELEpfyneyLELKDAEKELEREEKELKKLEEELDkafeeLAETEKRLEELRKELEELEKKY 656
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
484-604 |
7.93e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 39.55 E-value: 7.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 484 EKELLREKEiVDAVEKLAEEAKSELARLRVEKEEETL-ALERERTSIETE-MEALARIRNELEEQLQSLASNKAEMSyEK 561
Cdd:pfam15709 397 EEERQRQEE-EERKQRLQLQAAQERARQQQEEFRRKLqELQRKKQQEEAErAEAEKQRQKELEMQLAEEQKRLMEMA-EE 474
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 42573662 562 ERFDRLQKQVEDENQEIL----RLQNELEVERNALSIARDWAKDEAR 604
Cdd:pfam15709 475 ERLEYQRQKQEAEEKARLeaeeRRQKEEEAARLALEEAMKQAQEQAR 521
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
484-620 |
9.28e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.51 E-value: 9.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 484 EKELLREKEIVDA---VEKLAEEAKSELARLRV-EKEEETLALERERTSIETEMEALARIRNELEEQLQSLASNKAEMSY 559
Cdd:COG4913 241 HEALEDAREQIELlepIRELAERYAAARERLAElEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDA 320
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42573662 560 EKERFDRLQKQ--------VEDENQEILRLQNELEVERNALSIARDWAKDEARRAREQAKVLEEARGRW 620
Cdd:COG4913 321 LREELDELEAQirgnggdrLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEA 389
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
450-610 |
9.30e-03 |
|
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: 39.34 E-value: 9.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 450 EELARIEAEAMAENVVCAHNELVAQVEKDINASFEKELLREKEIVDAVEKLAEEAKsELARLRVEKEEET-----LALER 524
Cdd:pfam17380 435 REVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAE-EQRRKILEKELEErkqamIEEER 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 525 ERTSIETEMEAlaRIRNELEEQLQSLASNKAEMSYEKERFDRLQKQVEDENQEILRLQnELEVERNALsiaRDWAKDEAR 604
Cdd:pfam17380 514 KRKLLEKEMEE--RQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLE-AMEREREMM---RQIVESEKA 587
|
....*.
gi 42573662 605 RAREQA 610
Cdd:pfam17380 588 RAEYEA 593
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
502-623 |
9.54e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 39.24 E-value: 9.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 502 EEAKSELARLRVEKEEETLALERERtsietEMEalarirnELEEQLQSLASNKAEMSYEKERFDRLQKQVEDENQE---- 577
Cdd:pfam05667 311 EAPAATSSPPTKVETEEELQQQREE-----ELE-------ELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEElkeq 378
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 42573662 578 ILRLQNELEVERNALSIARDwakDEARRAREQAKV------LEEARGRWEKY 623
Cdd:pfam05667 379 NEELEKQYKVKKKTLDLLPD---AEENIAKLQALVdasaqrLVELAGQWEKH 427
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
467-749 |
9.56e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 39.46 E-value: 9.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 467 AHNELVAQVEKDINASFEKE-----LLREKEIVDAVEKLAEEaksELARLRVEKEEETLALERERTSIETEMEALARIRN 541
Cdd:COG2433 347 AYKNKFERVEKKVPPDVDRDevkarVIRGLSIEEALEELIEK---ELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVE 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 542 ELEEQLQSL----ASNKAEMSYEKERFDRLQKQVEDE----------NQEILRLQNELEVERNALsiardwakDEARRAR 607
Cdd:COG2433 424 RLEAEVEELeaelEEKDERIERLERELSEARSEERREirkdreisrlDREIERLERELEEERERI--------EELKRKL 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 608 EQAKVLEEARGRWEKYGLKVIvdsdlhEQTTKTEstwlnagkqnhvegtmkragnliakLKKMAKDVGEKSREVIYLiie 687
Cdd:COG2433 496 ERLKELWKLEHSGELVPVKVV------EKFTKEA-------------------------IRRLEEEYGLKEGDVVYL--- 541
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42573662 688 kisllisalkQQVHGMENKAKDLKIKTKSKAEEVWRQTSLRADEI---RNISIVKAKE-TVEEFKD 749
Cdd:COG2433 542 ----------RDASGAGRSTAELLAEAGPRAVIVPGELSEAADEVlfeEGIPVLPAEDvTIQEVDD 597
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
486-611 |
9.95e-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: 9.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573662 486 ELLREKEivdAVEKLAEEAKSELARLRVEKEEETLALERERTSIETEMEALARIRNELEEQLQSLASNKAEMSYEKerfD 565
Cdd:pfam07888 45 ELLQAQE---AANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEK---D 118
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 42573662 566 RLQKQVEDENQEILrlqnELEVERNALSIARDWAKDEARRAREQAK 611
Cdd:pfam07888 119 ALLAQRAAHEARIR----ELEEDIKTLTQRVLERETELERMKERAK 160
|
|
| |
